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1: NP_005414. trefoil factor 2 ...[gi:4885629] Links  


LOCUS       TFF2                     129 aa            linear   PRI 01-NOV-2000
DEFINITION  trefoil factor 2 (spasmolytic protein 1); spasmolytic protein 1;
            trefoil factor 2, SML1, human spasmolytic polypeptide (SP) [Homo
            sapiens].
ACCESSION   NP_005414
VERSION     NP_005414.1  GI:4885629
DBSOURCE    REFSEQ: accession NM_005423.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 129)
  AUTHORS   Tomasetto,C., Rio,M.C., Gautier,C., Wolf,C., Hareuveni,M.,
            Chambon,P. and Lathe,R.
  TITLE     hSP, the domain-duplicated homolog of pS2 protein, is co-expressed
            with pS2 in stomach but not in breast carcinoma
  JOURNAL   EMBO J. 9 (2), 407-414 (1990)
  MEDLINE   90151615
   PUBMED   2303034
REFERENCE   2  (residues 1 to 129)
  AUTHORS   Tomasetto,C., Rockel,N., Mattei,M.G., Fujita,R. and Rio,M.C.
  TITLE     The gene encoding the human spasmolytic protein (SML1/hSP) is in
            21q 22.3, physically linked to the homologous breast cancer marker
            gene BCEI/pS2
  JOURNAL   Genomics 13 (4), 1328-1330 (1992)
  MEDLINE   92372037
   PUBMED   1505966
REFERENCE   3  (residues 1 to 129)
  AUTHORS   Gott,P., Beck,S., Machado,J.C., Carneiro,F., Schmitt,H. and Blin,N.
  TITLE     Human trefoil peptides: genomic structure in 21q22.3 and
            coordinated expression
  JOURNAL   Eur. J. Hum. Genet. 4 (6), 308-315 (1996)
  MEDLINE   97196773
   PUBMED   9043862
REFERENCE   4  (residues 1 to 129)
  AUTHORS   Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS,
            Toyoda A, Ishii K, Totoki Y, Choi DK, Soeda E, Ohki M, Takagi T,
            Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J,
            Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M
            and Schudy A.
  TITLE     The DNA sequence of human chromosome 21
  JOURNAL   Nature 405 (6784), 311-319 (2000)
  MEDLINE   20289799
   PUBMED   10830953
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U47292.1.
            Summary: Members of the trefoil family are characterized by having
            at least one copy of the trefoil motif, a 40-amino acid domain that
            contains three conserved disulfides. They are stable secretory
            proteins expressed in gastrointestinal mucosa. Their functions are
            not defined, but they may protect the mucosa from insults,
            stabilize the mucus layer and affect healing of the epithelium.
            TFF2, which is expressed in the gastric mucosa, has also been
            studied because of its expression in human tumors. The TFF2 gene
            consists of 4 exons, with exons 2 and 3 each encoding a trefoil
            domain. The TFF1, TFF2, and TFF3 genes are located within a 55 kb
            region, suggesting they evolved from a common ancestor by
            duplication.
FEATURES             Location/Qualifiers
     source          1..129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..129
                     /product="trefoil factor 2 (spasmolytic protein 1)"
                     /note="spasmolytic protein 1; trefoil factor 2, SML1,
                     human spasmolytic polypeptide (SP)"
     Region          33..72
                     /region_name="Trefoil (P-type) domain"
                     /note="trefoil"
                     /db_xref="CDD:pfam00088"
     Region          35..72
                     /region_name="P or trefoil or TFF domain"
                     /note="P"
                     /db_xref="CDD:P"
     Region          79..124
                     /region_name="P or trefoil or TFF domain"
                     /note="P"
                     /db_xref="CDD:P"
     Region          80..121
                     /region_name="Trefoil (P-type) domain"
                     /note="trefoil"
                     /db_xref="CDD:pfam00088"
     CDS             1..129
                     /gene="TFF2"
                     /coded_by="NM_005423.1:1..390"
                     /db_xref="LocusID:7032"
                     /db_xref="MIM:182590"
ORIGIN      
        1 mgrrdaqlla allvlglcal agsekpspcq csrlsphnrt ncgfpgitsd qcfdngccfd
       61 ssvtgvpwcf hplpkqesdq cvmevsdrrn cgypgispee casrkccfsn fifevpwcff
      121 pksvedchy
//



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1: NP_003348. secretoglobin, fa...[gi:4507809] Links  


LOCUS       SCGB1A1                   91 aa            linear   PRI 27-AUG-2002
DEFINITION  secretoglobin, family 1A, member 1 (uteroglobin); Uteroglobin
            (Clara-cell specific 10-kD protein); secretoglobin, family 1A,
            member 1; uteroglobin [Homo sapiens].
ACCESSION   NP_003348
VERSION     NP_003348.1  GI:4507809
DBSOURCE    REFSEQ: accession NM_003357.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 91)
  AUTHORS   Singh,G., Katyal,S.L., Brown,W.E., Phillips,S., Kennedy,A.L.,
            Anthony,J. and Squeglia,N.
  TITLE     Amino-acid and cDNA nucleotide sequences of human Clara cell 10 kDa
            protein
  JOURNAL   Biochim. Biophys. Acta 950 (3), 329-337 (1988)
  MEDLINE   89000784
   PUBMED   3167058
REFERENCE   2  (residues 1 to 91)
  AUTHORS   Wolf,M., Klug,J., Hackenberg,R., Gessler,M., Grzeschik,K.H.,
            Beato,M. and Suske,G.
  TITLE     Human CC10, the homologue of rabbit uteroglobin: genomic cloning,
            chromosomal localization and expression in endometrial cell lines
  JOURNAL   Hum. Mol. Genet. 1 (6), 371-378 (1992)
  MEDLINE   93250776
   PUBMED   1284526
REFERENCE   3  (residues 1 to 91)
  AUTHORS   Hay,J.G., Danel,C., Chu,C.S. and Crystal,R.G.
  TITLE     Human CC10 gene expression in airway epithelium and subchromosomal
            locus suggest linkage to airway disease
  JOURNAL   Am. J. Physiol. 268 (4 Pt 1), L565-L575 (1995)
  MEDLINE   95250987
   PUBMED   7733299
REFERENCE   4  (residues 1 to 91)
  AUTHORS   Zhang,Z., Zimonjic,D.B., Popescu,N.C., Wang,N., Gerhard,D.S.,
            Stone,E.M., Arbour,N.C., De Vries,H.G., Scheffer,H., Gerritsen,J.,
            Colle'e,J.M., Ten Kate,L.P. and Mukherjee,A.B.
  TITLE     Human uteroglobin gene: structure, subchromosomal localization, and
            polymorphism
  JOURNAL   DNA Cell Biol. 16 (1), 73-83 (1997)
  MEDLINE   97174312
   PUBMED   9022046
REFERENCE   5  (residues 1 to 91)
  AUTHORS   Muller-Schottle,F., Classen-Linke,I., Alfer,J., Krusche,C.,
            Beier-Hellwig,K., Sterzik,K. and Beier,H.M.
  TITLE     Expression of uteroglobin in the human endometrium
  JOURNAL   Mol. Hum. Reprod. 5 (12), 1155-1161 (1999)
  MEDLINE   20054915
   PUBMED   10587371
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC004481.1.
FEATURES             Location/Qualifiers
     source          1..91
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q12.3-q13.1"
                     /clone="MGC:10583 IMAGE:3688615"
                     /tissue_type="Pancreas, adenocarcinoma"
                     /clone_lib="NIH_MGC_39"
                     /lab_host="DH10B-R"
                     /note="Vector: pOTB7"
     Protein         1..91
                     /product="secretoglobin, family 1A, member 1
                     (uteroglobin)"
                     /note="Uteroglobin (Clara-cell specific 10-kD protein);
                     secretoglobin, family 1A, member 1; uteroglobin"
     Region          1..90
                     /region_name="pfam01099, Uteroglobin, Uteroglobin family.
                     Uteroglobin is a homodimer of two identical 70 amino acid
                     polypeptides linked by two disulphide bridges. The precise
                     role of uteroglobin has still to be elucidated"
     Region          22..90
                     /region_name="smart00096, UTG, Uteroglobin"
     variation       56
                     /allele="R"
                     /allele="G"
                     /db_xref="dbSNP:1802634"
     variation       68
                     /allele="A"
                     /allele="T"
                     /db_xref="dbSNP:1802632"
     CDS             1..91
                     /gene="SCGB1A1"
                     /coded_by="NM_003357.2:55..330"
                     /db_xref="LocusID:7356"
                     /db_xref="MIM:192020"
ORIGIN      
        1 mklavtltlv tlalccssas aeicpsfqrv ietllmdtps syeaamelfs pdqdmreaga
       61 qlkklvdtlp qkpresiikl mekiaqsslc n
//



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1: NP_057667. palate, lung and ...[gi:7706119] Links  


LOCUS       PLUNC                    256 aa            linear   PRI 19-FEB-2002
DEFINITION  palate, lung and nasal epithelium carcinoma associated protein
            precursor; Nasopharyngeal carcinoma-related protein; tracheal
            epithelium enriched protein [Homo sapiens].
ACCESSION   NP_057667
VERSION     NP_057667.1  GI:7706119
DBSOURCE    REFSEQ: accession NM_016583.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Bingle,C.D. and Bingle,L.
  TITLE     Characterisation of the human plunc gene, a gene product with an
            upper airways and nasopharyngeal restricted expression pattern
  JOURNAL   Biochim. Biophys. Acta 1493 (3), 363-367 (2000)
  MEDLINE   20472055
   PUBMED   11018263
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Iwao,K., Watanabe,T., Fujiwara,Y., Takami,K., Kodama,K.,
            Higashiyama,M., Yokouchi,H., Ozaki,K., Monden,M. and Tanigami,A.
  TITLE     Isolation of a novel human lung-specific gene, LUNX, a potential
            molecular marker for detection of micrometastasis in non-small-cell
            lung cancer
  JOURNAL   Int. J. Cancer 91 (4), 433-437 (2001)
  MEDLINE   21150203
   PUBMED   11251963
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Lindahl,M., Stahlbom,B. and Tagesson,C.
  TITLE     Identification of a new potential airway irritation marker, palate
            lung nasal epithelial clone protein, in human nasal lavage fluid
            with two-dimensional electrophoresis and matrix-assisted laser
            desorption/ionization-time of flight
  JOURNAL   Electrophoresis 22 (9), 1795-1800 (2001)
  MEDLINE   21317946
   PUBMED   11425234
REFERENCE   4  (residues 1 to 256)
  AUTHORS   Ghafouri,B., Stahlbom,B., Tagesson,C. and Lindahl,M.
  TITLE     Newly identified proteins in human nasal lavage fluid from
            non-smokers and smokers using two-dimensional gel electrophoresis
            and peptide mass fingerprinting
  JOURNAL   Proteomics 2 (1), 112-120 (2002)
  MEDLINE   21648993
   PUBMED   11788998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012549.1.
            Summary: This gene is the human homolog of murine plunc, and like
            the mouse gene, is specifically expressed in the upper airways and
            nasopharyngeal regions. The exact biological function of this gene
            is not known, however, it has been suggested to be involved in
            inflammatory responses to irritants in the upper airways. It may
            also serve as a potential molecular marker for detection of
            micrometastasis in non-small-cell lung cancer. Multiple transcript
            variants resulting from alternative splicing in the 3' UTR have
            been detected, but the full-length nature of only two is known.
            Transcript Variant: This variant (1) utilizes exon 9, and has a
            shorter 3' UTR compared to transcript variant 2. Both variants
            encode the same protein.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.2"
                     /clone="MGC:13372 IMAGE:4246419"
                     /clone_lib="NIH_MGC_81"
     Protein         1..256
                     /product="palate, lung and nasal epithelium carcinoma
                     associated protein precursor"
                     /note="Nasopharyngeal carcinoma-related protein; tracheal
                     epithelium enriched protein"
     sig_peptide     1..19
     mat_peptide     20..256
                     /product="palate, lung and nasal epithelium carcinoma
                     associated protein"
     CDS             1..256
                     /gene="PLUNC"
                     /coded_by="NM_016583.2:72..842"
                     /db_xref="LocusID:51297"
ORIGIN      
        1 mfqtgglivf ygllaqtmaq fgglpvpldq tlplnvnpal plsptglags ltnalsngll
       61 sggllgilen lplldilkpg ggtsggllgg llgkvtsvip glnniidikv tdpqllelgl
      121 vqspdghrly vtiplgiklq vntplvgasl lrlavkldit aeilavrdkq erihlvlgdc
      181 thspgslqis lldglgplpi qglldsltgi lnkvlpelvq gnvcplvnev lrglditlvh
      241 divnmlihgl qfvikv
//



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1: NP_001440. four and a half L...[gi:21361122] Links  


LOCUS       FHL1                     280 aa            linear   PRI 10-JUN-2002
DEFINITION  four and a half LIM domains 1; Four-and-a-half LIM domains 1 [Homo
            sapiens].
ACCESSION   NP_001440
VERSION     NP_001440.2  GI:21361122
DBSOURCE    REFSEQ: accession NM_001449.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 280)
  AUTHORS   Strausberg,R.
  TITLE     Homo sapiens four and a half LIM domains 1 (FHL1), mRNA
  JOURNAL   Unpublished (2001)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC010998.1.
            On Jun 10, 2002 this sequence version replaced gi:4503721.
FEATURES             Location/Qualifiers
     source          1..280
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq26"
                     /clone="MGC:15297 IMAGE:4039973"
                     /tissue_type="Lung, large cell carcinoma"
                     /clone_lib="NIH_MGC_18"
                     /lab_host="DH10B-R"
                     /note="Vector: pOTB7"
     Protein         1..280
                     /product="four and a half LIM domains 1"
                     /note="Four-and-a-half LIM domains 1"
     Region          40..92
                     /region_name="LIM domain"
                     /note="LIM"
                     /db_xref="CDD:pfam00412"
     Region          40..92
                     /region_name="Zinc-binding domain present in Lin-11,
                     Isl-1, Mec-3."
                     /note="LIM"
                     /db_xref="CDD:smart00132"
     Region          100..153
                     /region_name="Zinc-binding domain present in Lin-11,
                     Isl-1, Mec-3."
                     /note="LIM"
                     /db_xref="CDD:smart00132"
     Region          101..159
                     /region_name="LIM domain"
                     /note="LIM"
                     /db_xref="CDD:pfam00412"
     Region          162..213
                     /region_name="LIM domain"
                     /note="LIM"
                     /db_xref="CDD:pfam00412"
     Region          162..212
                     /region_name="Zinc-binding domain present in Lin-11,
                     Isl-1, Mec-3."
                     /note="LIM"
                     /db_xref="CDD:smart00132"
     Region          220..276
                     /region_name="Zinc-binding domain present in Lin-11,
                     Isl-1, Mec-3."
                     /note="LIM"
                     /db_xref="CDD:smart00132"
     CDS             1..280
                     /gene="FHL1"
                     /coded_by="NM_001449.2:218..1060"
                     /db_xref="LocusID:2273"
                     /db_xref="MIM:300163"
ORIGIN      
        1 maekfdchyc rdplqgkkyv qkdghhcclk cfdkfcantc vecrkpigad skevhyknrf
       61 whdtcfrcak clhplanetf vakdnkilcn kcttredspk ckgcfkaiva gdqnveykgt
      121 vwhkdcftcs nckqvigtgs ffpkgedfyc vtchetkfak hcvkcnkait sggityqdqp
      181 whadcfvcvt cskklagqrf tavedqyycv dcyknfvakk cagcknpitg fgkgssvvay
      241 egqswhdycf hckkcsvnla nkrfvfhqeq vycpdcakkl 
//



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1: NP_003636. solute carrier fa...[gi:4503653] Links  


LOCUS       SLC27A2                  620 aa            linear   PRI 18-SEP-2002
DEFINITION  solute carrier family 27 (fatty acid transporter), member 2; very
            long-chain fatty-acid-coenzyme A ligase 1; very-long-chain acyl-CoA
            synthetase [Homo sapiens].
ACCESSION   NP_003636
VERSION     NP_003636.1  GI:4503653
DBSOURCE    REFSEQ: accession NM_003645.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 620)
  AUTHORS   Hirsch,D., Stahl,A. and Lodish,H.F.
  TITLE     A family of fatty acid transporters conserved from mycobacterium to
            man
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 95 (15), 8625-8629 (1998)
  MEDLINE   98337965
   PUBMED   9671728
REFERENCE   2  (residues 1 to 620)
  AUTHORS   Wakui,K., Aoyama,T., Uchiyama,A., Hashimoto,T. and Fukushima,Y.
  TITLE     Assignment of human fatty-acid-coenzyme A ligase, very long-chain 1
            gene (FACVL1) to human chromosome band 15q21.2 by fluorescence in
            situ hybridization
  JOURNAL   Cytogenet. Cell Genet. 81 (3-4), 292-293 (1998)
  MEDLINE   98399873
   PUBMED   9730624
REFERENCE   3  (residues 1 to 620)
  AUTHORS   Steinberg,S.J., Wang,S.J., Kim,D.G., Mihalik,S.J. and Watkins,P.A.
  TITLE     Human very-long-chain acyl-CoA synthetase: cloning, topography, and
            relevance to branched-chain fatty acid metabolism
  JOURNAL   Biochem. Biophys. Res. Commun. 257 (2), 615-621 (1999)
  MEDLINE   99216327
   PUBMED   10198260
REFERENCE   4  (residues 1 to 620)
  AUTHORS   Watkins,P.A., Pevsner,J. and Steinberg,S.J.
  TITLE     Human very long-chain acyl-CoA synthetase and two human homologs:
            initial characterization and relationship to fatty acid transport
            protein
  JOURNAL   Prostaglandins Leukot. Essent. Fatty Acids 60 (5-6), 323-328 (1999)
  MEDLINE   99397717
   PUBMED   10471116
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D88308.1.
            Summary: The protein encoded by this gene is an isozyme of
            long-chain fatty-acid-coenzyme A ligase family. Although differing
            in substrate specificity, subcellular localization, and tissue
            distribution, all isozymes of this family convert free long-chain
            fatty acids into fatty acyl-CoA esters, and thereby play a key role
            in lipid biosynthesis and fatty acid degradation. This isozyme
            activates long-chain, branched-chain and very-long-chain fatty
            acids containing 22 or more carbons to their CoA derivatives. It is
            expressed primarily in liver and kidney, and is present in both
            endoplasmic reticulum and peroxisomes but not in mitochondria. Its
            decreased peroxisomal enzyme activity is in part responsible for
            the biochemical pathology in X-linked adrenoleukodystrophy.
FEATURES             Location/Qualifiers
     source          1..620
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21.2"
     Protein         1..620
                     /product="solute carrier family 27 (fatty acid
                     transporter), member 2"
                     /EC_number="6.2.1.-"
                     /note="very long-chain fatty-acid-coenzyme A ligase 1;
                     very-long-chain acyl-CoA synthetase"
     Region          1..21
                     /region_name="transmembrane region"
     Region          80..512
                     /region_name="pfam00501, AMP-binding, AMP-binding enzyme"
     Region          107..127
                     /region_name="transmembrane region"
     Region          226..234
                     /region_name="ATP binding domain"
     Region          262..282
                     /region_name="transmembrane region"
     CDS             1..620
                     /gene="SLC27A2"
                     /coded_by="NM_003645.2:204..2066"
                     /db_xref="LocusID:11001"
                     /db_xref="MIM:603247"
ORIGIN      
        1 mlsaiytvla gllflpllvn lccpyffqdi gyflkvaavg rrvrsygqrr partilrafl
       61 ekarqtphkp fllfrdetlt yaqvdrrsnq varalhdhlg lrqgdcvall mgnepayvwl
      121 wlglvklgca maclnynira ksllhcfqcc gakvllvspe lqaaveeilp slkkddvsiy
      181 yvsrtsntdg idsfldkvde vstepipesw rsevtfstpa lyiytsgttg lpkaamithq
      241 riwygtgltf vsglkaddvi yitlpfyhsa alligihgci vagatlalrt kfsasqfwdd
      301 crkynvtviq yigellrylc nspqkpndrd hkvrlalgng lrgdvwrqfv krfgdiciye
      361 fyaategnig fmnyarkvga vgrvnylqkk iitydlikyd vekdepvrde ngycvrvpkg
      421 evgllvckit qltpfngyag akaqtekkkl rdvfkkgdly fnsgdllmvd henfiyfhdr
      481 vgdtfrwkge nvattevadt vglvdfvqev nvygvhvpdh egrigmasik mkenhefdgk
      541 klfqhiadyl psyarprflr iqdtieitgt fkhrkmtlve egfnpavikd alyflddtak
      601 myvpmtediy naisaktlkl 
//



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1: NP_000229. potassium voltage...[gi:4557729] Links  


LOCUS       KCNH2                   1159 aa            linear   PRI 31-OCT-2000
DEFINITION  potassium voltage-gated channel, subfamily H, member 2 [Homo
            sapiens].
ACCESSION   NP_000229
VERSION     NP_000229.1  GI:4557729
DBSOURCE    REFSEQ: accession NM_000238.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1159)
  AUTHORS   Warmke,J.W. and Ganetzky,B.
  TITLE     A family of potassium channel genes related to eag in Drosophila
            and mammals
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 91 (8), 3438-3442 (1994)
  MEDLINE   94211879
   PUBMED   8159766
REFERENCE   2  (residues 1 to 1159)
  AUTHORS   Jiang C, Atkinson D, Towbin JA, Splawski I, Lehmann MH, Li H,
            Timothy K, Taggart RT, Schwartz PJ, Vincent GM et al.
  TITLE     Two long QT syndrome loci map to chromosomes 3 and 7 with evidence
            for further heterogeneity
  JOURNAL   Nat. Genet. 8 (2), 141-147 (1994)
  MEDLINE   95144170
   PUBMED   7842012
REFERENCE   3  (residues 1 to 1159)
  AUTHORS   Vincent,G.M.
  TITLE     The molecular genetics of the long QT syndrome: genes causing
            fainting and sudden death
  JOURNAL   Annu. Rev. Med. 49, 263-274 (1998)
  MEDLINE   98170000
   PUBMED   9509262
REFERENCE   4  (residues 1 to 1159)
  AUTHORS   Ackerman,M.J.
  TITLE     The long QT syndrome: ion channel diseases of the heart
  JOURNAL   Mayo Clin. Proc. 73 (3), 250-269 (1998)
  MEDLINE   98172776
   PUBMED   9511785
REFERENCE   5  (residues 1 to 1159)
  AUTHORS   Taglialatela,M., Castaldo,P., Pannaccione,A., Giorgio,G. and
            Annunziato,L.
  TITLE     Human ether-a-gogo related gene (HERG) K+ channels as
            pharmacological targets: present and future implications
  JOURNAL   Biochem. Pharmacol. 55 (11), 1741-1746 (1998)
  MEDLINE   98378093
   PUBMED   9714291
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U04270.1.
            Summary: KCNH2 encodes a human homologue of the Drosophila
            melanogaster eag gene, a potassium channel protein.  Along with
            five other human genes, mutations in KCNH2 that result in loss of
            function or dominant negative function cause long QT syndrome.
FEATURES             Location/Qualifiers
     source          1..1159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q35-q36"
                     /clone="pBII+HH1, pBII+HH10, pBHH10-4.5"
                     /sex="female"
                     /tissue_type="hippocampus"
                     /clone_lib="Stratagene Number 936205 Human hippocampus
                     cDNA library"
                     /dev_stage="2 year old"
     Protein         1..1159
                     /product="potassium voltage-gated channel, subfamily H,
                     member 2"
                     /note="human eag related potassium channel"
     variation       41
                     /allele="V"
                     /allele="G"
                     /db_xref="dbSNP:731506"
     Region          94..135
                     /region_name="PAC motif"
                     /note="PAC"
                     /db_xref="CDD:pfam00785"
     Region          94..134
                     /region_name="Motif C-terminal to PAS motifs (likely to
                     contribute to PAS structural domain)"
                     /note="PAC"
                     /db_xref="CDD:PAC"
     Region          540..728
                     /region_name="Transmembrane region cyclic Nucleotide Gated
                     Channel"
                     /note="CNG_membrane"
                     /db_xref="CDD:pfam00914"
     Region          742..860
                     /region_name="Cyclic nucleotide-monophosphate binding
                     domain"
                     /note="cNMP"
                     /db_xref="CDD:cNMP"
     Region          760..847
                     /region_name="Cyclic nucleotide-binding domain"
                     /note="cNMP_binding"
                     /db_xref="CDD:pfam00027"
     variation       897
                     /allele="K"
                     /allele="T"
                     /db_xref="dbSNP:1805123"
     CDS             1..1159
                     /gene="KCNH2"
                     /coded_by="NM_000238.1:184..3663"
                     /db_xref="LocusID:3757"
                     /db_xref="MIM:152427"
ORIGIN      
        1 mpvrrghvap qntfldtiir kfegqsrkfi ianarvenca viycndgfce lcgysraevm
       61 qrpctcdflh gprtqrraaa qiaqallgae erkveiafyr kdgscflclv dvvpvknedg
      121 avimfilnfe vvmekdmvgs pahdtnhrgp ptswlapgra ktfrlklpal laltaressv
      181 rsggaggaga pgavvvdvdl tpaapssesl aldevtamdn hvaglgpaee rralvgpgsp
      241 prsapgqlps prahslnpda sgsscslart rsrescasvr rassaddiea mragvlpppp
      301 rhastgamhp lrsgllnsts dsdlvryrti skipqitlnf vdlkgdpfla sptsdreiia
      361 pkikerthnv tekvtqvlsl gadvlpeykl qaprihrwti lhyspfkavw dwlilllviy
      421 tavftpysaa fllketeegp patecgyacq plavvdlivd imfivdilin frttyvnane
      481 evvshpgria vhyfkgwfli dmvaaipfdl lifgsgseel igllktarll rlvrvarkld
      541 ryseygaavl fllmctfali ahwlaciwya ignmeqphmd srigwlhnlg dqigkpynss
      601 glggpsikdk yvtalyftfs sltsvgfgnv spntnsekif sicvmligsl myasifgnvs
      661 aiiqrlysgt aryhtqmlrv refirfhqip nplrqrleey fqhawsytng idmnavlkgf
      721 peclqadicl hlnrsllqhc kpfrgatkgc lralamkfkt thappgdtlv hagdlltaly
      781 fisrgsieil rgdvvvailg kndifgepln lyarpgksng dvraltycdl hkihrddlle
      841 vldmypefsd hfwssleitf nlrdtnmipg spgstelegg fsrqrkrkls frrrtdkdte
      901 qpgevsalgp gragagpssr grpggpwges pssgpsspes sedegpgrss splrlvpfss
      961 prppgeppgg eplmedceks sdtcnplsga fsgvsnifsf wgdsrgrqyq elprcpaptp
     1021 sllniplssp grrprgdves rldalqrqln rletrlsadm atvlqllqrq mtlvppaysa
     1081 vttpgpgpts tspllpvspl ptltldslsq vsqfmaceel ppgapelpqe gptrrlslpg
     1141 qlgaltsqpl hrhgsdpgs
//



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1: NP_001704. betaine-homocyste...[gi:4502407] Links  


LOCUS       BHMT                     406 aa            linear   PRI 31-OCT-2000
DEFINITION  betaine-homocysteine methyltransferase [Homo sapiens].
ACCESSION   NP_001704
VERSION     NP_001704.1  GI:4502407
DBSOURCE    REFSEQ: accession NM_001713.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Garrow,T.A.
  TITLE     Purification, kinetic properties, and cDNA cloning of mammalian
            betaine-homocysteine methyltransferase
  JOURNAL   J. Biol. Chem. 271 (37), 22831-22838 (1996)
  MEDLINE   96394355
   PUBMED   8798461
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Park,E.I. and Garrow,T.A.
  TITLE     Interaction between dietary methionine and methyl donor intake on
            rat liver betaine-homocysteine methyltransferase gene expression
            and organization of the human gene
  JOURNAL   J. Biol. Chem. 274 (12), 7816-7824 (1999)
  MEDLINE   99175153
   PUBMED   10075673
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U50929.1.
            Summary: Betaine-homocysteine methyltransferase is a cytosolic
            enzyme that catalyzes the conversion of betaine and homocysteine to
            dimethylglycine and methionine, respectively. Defects in BHMT could
            lead to hyperhomocyst(e)inemia,but such a defect has not yet been
            observed.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.1-q15"
                     /tissue_type="liver"
     Protein         1..406
                     /product="betaine-homocysteine methyltransferase"
                     /EC_number="2.1.1.5"
                     /function="betaine-dependent methylation of homocysteine"
     CDS             1..406
                     /gene="BHMT"
                     /coded_by="NM_001713.1:27..1247"
                     /db_xref="LocusID:635"
                     /db_xref="MIM:602888"
ORIGIN      
        1 mppvggkkak kgilerlnag eivigdggfv falekrgyvk agpwtpeaav ehpeavrqlh
       61 reflragsnv mqtftfyase dklenrgnyv lekisgqevn eaacdiarqv adegdalvag
      121 gvsqtpsyls cksetevkkv flqqlevfmk knvdfliaey fehveeavwa vetliasgkp
      181 vaatmcigpe gdlhgvppge cavrlvkaga siigvnchfd ptislktvkl mkegleaaql
      241 kahlmsqpla yhtpdcnkqg fidlpefpfg leprvatrwd iqkyareayn lgvryiggcc
      301 gfepyhirai aeelapergf lppasekhgs wgsgldmhtk pwvrararke ywenlriasg
      361 rpynpsmskp dgwgvtkgta elmqqkeatt eqqlkelfek qkfksq
//



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1: NP_005359. myoglobin [Homo s...[gi:4885477] Links  


LOCUS       MB                       154 aa            linear   PRI 27-AUG-2002
DEFINITION  myoglobin [Homo sapiens].
ACCESSION   NP_005359
VERSION     NP_005359.1  GI:4885477
DBSOURCE    REFSEQ: accession NM_005368.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 154)
  AUTHORS   Herrera,A.E. and Lehmann,H.
  TITLE     Primary structure of human myoglobin
  JOURNAL   Nature New Biol. 232 (31), 149-152 (1971)
  MEDLINE   71291923
   PUBMED   5285572
REFERENCE   2  (residues 1 to 154)
  AUTHORS   Weller,P., Jeffreys,A.J., Wilson,V. and Blanchetot,A.
  TITLE     Organization of the human myoglobin gene
  JOURNAL   EMBO J. 3 (2), 439-446 (1984)
  MEDLINE   84182508
   PUBMED   6571704
REFERENCE   3  (residues 1 to 154)
  AUTHORS   Jeffreys,A.J., Wilson,V., Blanchetot,A., Weller,P., Geurts van
            Kessel,A., Spurr,N., Solomon,E. and Goodfellow,P.
  TITLE     The human myoglobin gene: a third dispersed globin locus in the
            human genome
  JOURNAL   Nucleic Acids Res. 12 (7), 3235-3243 (1984)
  MEDLINE   84193192
   PUBMED   6326055
REFERENCE   4  (residues 1 to 154)
  AUTHORS   Akaboshi,E.
  TITLE     Cloning of the human myoglobin gene
  JOURNAL   Gene 33 (3), 241-249 (1985)
  MEDLINE   85232026
   PUBMED   2989088
REFERENCE   5  (residues 1 to 154)
  AUTHORS   Suzuki,T. and Imai,K.
  TITLE     Evolution of myoglobin
  JOURNAL   Cell Mol. Life Sci. 54 (9), 979-1004 (1998)
  MEDLINE   99007752
   PUBMED   9791540
REFERENCE   6  (residues 1 to 154)
  AUTHORS   Witting,P.K., Douglas,D.J. and Mauk,A.G.
  TITLE     Reaction of human myoglobin and H2O2. Involvement of a thiyl
            radical produced at cysteine 110
  JOURNAL   J. Biol. Chem. 275 (27), 20391-20398 (2000)
  MEDLINE   20347119
   PUBMED   10779502
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X00371.1, X00372.1 and
            X00373.1.
            Summary: The human myoglobin gene is 10.4 kb long and has a three
            exon/two intron structure with long non-coding regions. It encodes
            the protein myoglobin, which is a haemoprotein contributing to
            intracellular oxygen storage and transcellular facilitated
            diffusion of oxygen. Myoglobin is a member of the globin
            superfamily and present in skeletal and cardiac muscle.
FEATURES             Location/Qualifiers
     source          1..154
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.1"
     Protein         1..154
                     /product="myoglobin"
     Region          4..148
                     /region_name="pfam00042, globin, Globin"
     CDS             1..154
                     /gene="MB"
                     /coded_by="NM_005368.1:71..535"
                     /db_xref="LocusID:4151"
                     /db_xref="MIM:160000"
ORIGIN      
        1 mglsdgewql vlnvwgkvea dipghgqevl irlfkghpet lekfdkfkhl ksedemkase
       61 dlkkhgatvl talggilkkk ghheaeikpl aqshatkhki pvkylefise ciiqvlqskh
      121 pgdfgadaqg amnkalelfr kdmasnykel gfqg
//



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1: NP_005114. nuclear receptor ...[gi:4826980] Links  


LOCUS       NR1H4                    472 aa            linear   PRI 27-AUG-2002
DEFINITION  nuclear receptor subfamily 1, group H, member 4 [Homo sapiens].
ACCESSION   NP_005114
VERSION     NP_005114.1  GI:4826980
DBSOURCE    REFSEQ: accession NM_005123.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 472)
  AUTHORS   Forman,B.M., Goode,E., Chen,J., Oro,A.E., Bradley,D.J.,
            Perlmann,T., Noonan,D.J., Burka,L.T., McMorris,T., Lamph,W.W. et
            al.
  TITLE     Identification of a nuclear receptor that is activated by farnesol
            metabolites
  JOURNAL   Cell 81 (5), 687-693 (1995)
  MEDLINE   95292336
   PUBMED   7774010
REFERENCE   2  (residues 1 to 472)
  AUTHORS   Zavacki,A.M., Lehmann,J.M., Seol,W., Willson,T.M., Kliewer,S.A. and
            Moore,D.D.
  TITLE     Activation of the orphan receptor RIP14 by retinoids
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 94 (15), 7909-7914 (1997)
  MEDLINE   97368291
   PUBMED   9223286
REFERENCE   3  (residues 1 to 472)
  AUTHORS   Makishima,M., Okamoto,A.Y., Repa,J.J., Tu,H., Learned,R.M., Luk,A.,
            Hull,M.V., Lustig,K.D., Mangelsdorf,D.J. and Shan,B.
  TITLE     Identification of a nuclear receptor for bile acids
  JOURNAL   Science 284 (5418), 1362-1365 (1999)
  MEDLINE   99269275
   PUBMED   10334992
REFERENCE   4  (residues 1 to 472)
  AUTHORS   Parks,D.J., Blanchard,S.G., Bledsoe,R.K., Chandra,G., Consler,T.G.,
            Kliewer,S.A., Stimmel,J.B., Willson,T.M., Zavacki,A.M., Moore,D.D.
            and Lehmann,J.M.
  TITLE     Bile acids: natural ligands for an orphan nuclear receptor
  JOURNAL   Science 284 (5418), 1365-1368 (1999)
  MEDLINE   99269276
   PUBMED   10334993
REFERENCE   5  (residues 1 to 472)
  AUTHORS   Papetti,M., Wood,N., Lohmar,P.D. and Bowman,M.R.
  TITLE     The Identification of the cDNA Coding for HRR-1, a Novel Human
            Farnesol Receptor
  JOURNAL   Unpublished
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U68233.1.
FEATURES             Location/Qualifiers
     source          1..472
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23.1"
     Protein         1..472
                     /product="nuclear receptor subfamily 1, group H, member 4"
     Region          124..195
                     /region_name="smart00399, ZnF_C4, c4 zinc finger in
                     nuclear hormone receptors"
     Region          125..200
                     /region_name="pfam00105, zf-C4, Zinc finger, C4 type (two
                     domains). In nearly all cases, this is the DNA binding
                     domain of a nuclear hormone receptor. The alignment
                     contains two Zinc finger domains that are too dissimilar
                     to be aligned with each other"
     Region          289..442
                     /region_name="smart00430, HOLI, Ligand binding domain of
                     hormone receptors"
     Region          292..469
                     /region_name="pfam00104, hormone_rec, Ligand-binding
                     domain of nuclear hormone receptor. This all helical
                     domain is involved in binding the hormone in these
                     receptors"
     CDS             1..472
                     /gene="NR1H4"
                     /coded_by="NM_005123.1:354..1772"
                     /note="FXR; retinoid receptor"
                     /db_xref="LocusID:9971"
                     /db_xref="MIM:603826"
ORIGIN      
        1 mgskmnlieh shlpttdefs fsenlfgvlt eqvagplgqn levepysqys nvqfpqvqpq
       61 issssyysnl gfypqqpeew yspgiyelrr mpaetlyqge tevaempvtk kprmgasagr
      121 ikgdelcvvc gdrasgyhyn altcegckgf frrsitknav ykcknggncv mdmymrrkcq
      181 ecrlrkckem gmlaecllte iqckskrlrk nvkqhadqtv nedsegrdlr qvtsttkscr
      241 ekteltpdqq tllhfimdsy nkqrmpqeit nkilkeefsa eenfliltem atnhvqvlve
      301 ftkklpgfqt ldhedqiall kgsaveamfl rsaeifnkkl psghsdllee rirnsgisde
      361 yitpmfsfyk sigelkmtqe eyalltaivi lspdrqyikd reaveklqep lldvlqklck
      421 ihqpenpqhf acllgrltel rtfnhhhaem lmswrvndhk ftpllceiwd vq
//



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1: NP_001967. enolase 3; enolas...[gi:4503573] Links  


LOCUS       ENO3                     434 aa            linear   PRI 31-OCT-2001
DEFINITION  enolase 3; enolase-3, beta, muscle; muscle specific enolase; beta
            enolase; skeletal muscle enolase; 2-phospho-D-glycerate hydrolyase
            [Homo sapiens].
ACCESSION   NP_001967
VERSION     NP_001967.1  GI:4503573
DBSOURCE    REFSEQ: accession NM_001976.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 434)
  AUTHORS   Peshavaria,M., Hinks,L.J. and Day,I.N.
  TITLE     Structure of human muscle (beta) enolase mRNA and protein deduced
            from a genomic clone
  JOURNAL   Nucleic Acids Res. 17 (21), 8862 (1989)
  MEDLINE   90067857
   PUBMED   2587223
REFERENCE   2  (residues 1 to 434)
  AUTHORS   Cali,L., Feo,S., Oliva,D. and Giallongo,A.
  TITLE     Nucleotide sequence of a cDNA encoding the human muscle-specific
            enolase (MSE)
  JOURNAL   Nucleic Acids Res. 18 (7), 1893 (1990)
  MEDLINE   90245587
   PUBMED   2336366
REFERENCE   3  (residues 1 to 434)
  AUTHORS   Giallongo,A., Venturella,S., Oliva,D., Barbieri,G., Rubino,P. and
            Feo,S.
  TITLE     Structural features of the human gene for muscle-specific enolase.
            Differential splicing in the 5'-untranslated sequence generates two
            forms of mRNA
  JOURNAL   Eur. J. Biochem. 214 (2), 367-374 (1993)
  MEDLINE   93292497
   PUBMED   8513787
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X51957.1 and X56832.1.
            Summary: This gene encodes one of the three enolase isoenzymes
            found in mammals. This isoenzyme, a homodimer, is found in skeletal
            muscle cells in the adult. A switch from alpha enolase to beta
            enolase occurs in muscle tissue during development in rodents.
            Mutations in this gene can be associated with metabolic myopathies
            that may result from decreased stability of the enzyme. Two
            transcripts have been identified for this gene that differ only in
            their 5' UTR.
            Transcript Variant: This variant (1) is the longer, less abundant
            transcript that differs from variant 2 by containing a complete
            first exon.
FEATURES             Location/Qualifiers
     source          1..434
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17pter-p11"
     Protein         1..434
                     /product="enolase 3"
                     /EC_number="4.2.1.11"
                     /note="enolase-3, beta, muscle; muscle specific enolase;
                     beta enolase; skeletal muscle enolase;
                     2-phospho-D-glycerate hydrolyase"
     Region          2..432
                     /region_name="Enol-ase"
                     /note="enolase"
                     /db_xref="CDD:pfam00113"
     CDS             1..434
                     /gene="ENO3"
                     /coded_by="NM_001976.2:109..1413"
                     /db_xref="LocusID:2027"
                     /db_xref="MIM:131370"
ORIGIN      
        1 mamqkifare ildsrgnptv evdlhtakgr fraavpsgas tgiyealelr dgdkgrylgk
       61 gvlkavenin ntlgpallqk klsvadqekv dkfmieldgt enkskfgana ilgvslavck
      121 agaaekgvpl yrhiadlagn pdlilpvpaf nvinggshag nklamqefmi lpvgassfke
      181 amrigaevyh hlkgvikaky gkdatnvgde ggfapnilen nealellkta iqaagypdkv
      241 vigmdvaase fyrngkydld fkspddparh itgeklgely ksfiknypvv siedpfdqdd
      301 watwtsflsg vniqivgddl tvtnpkriaq avekkacncl llkvnqigsv tesiqackla
      361 qsngwgvmvs hrsgetedtf iadlvvglct gqiktgapcr serlakynql mrieealgdk
      421 aifagrkfrn pkak
//



Revised: July 5, 2002.
 
 


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1: NP_002344. tumor-associated ...[gi:4505057] Links  


LOCUS       TACSTD2                  323 aa            linear   PRI 27-AUG-2002
DEFINITION  tumor-associated calcium signal transducer 2 precursor; membrane
            component, chromosome 1, surface marker 1 (40kD glycoprotein,
            identified by monoclonal antibody GA733); epithelial glycoprotein-1
            [Homo sapiens].
ACCESSION   NP_002344
VERSION     NP_002344.1  GI:4505057
DBSOURCE    REFSEQ: accession NM_002353.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 323)
  AUTHORS   Linnenbach,A.J., Wojcierowski,J., Wu,S.A., Pyrc,J.J., Ross,A.H.,
            Dietzschold,B., Speicher,D. and Koprowski,H.
  TITLE     Sequence investigation of the major gastrointestinal
            tumor-associated antigen gene family, GA733
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 86 (1), 27-31 (1989)
  MEDLINE   89098896
   PUBMED   2911574
REFERENCE   2  (residues 1 to 323)
  AUTHORS   Linnenbach,A.J., Seng,B.A., Wu,S., Robbins,S., Scollon,M.,
            Pyrc,J.J., Druck,T. and Huebner,K.
  TITLE     Retroposition in a family of carcinoma-associated antigen genes
  JOURNAL   Mol. Cell. Biol. 13 (3), 1507-1515 (1993)
  MEDLINE   93180797
   PUBMED   8382772
REFERENCE   3  (residues 1 to 323)
  AUTHORS   Fornaro,M., Dell'Arciprete,R., Stella,M., Bucci,C., Nutini,M.,
            Capri,M.G. and Alberti,S.
  TITLE     Cloning of the gene encoding Trop-2, a cell-surface glycoprotein
            expressed by human carcinomas
  JOURNAL   Int. J. Cancer 62 (5), 610-618 (1995)
  MEDLINE   95394524
   PUBMED   7665234
REFERENCE   4  (residues 1 to 323)
  AUTHORS   Dryden,D.T., Cooper,L.P., Thorpe,P.H. and Byron,O.
  TITLE     The in vitro assembly of the EcoKI type I DNA
            restriction/modification enzyme and its in vivo implications
  JOURNAL   Biochemistry 36 (5), 1065-1076 (1997)
  MEDLINE   97185715
   PUBMED   9033396
REFERENCE   5  (residues 1 to 323)
  AUTHORS   Ripani,E., Sacchetti,A., Corda,D. and Alberti,S.
  TITLE     Human Trop-2 is a tumor-associated calcium signal transducer
  JOURNAL   Int. J. Cancer 76 (5), 671-676 (1998)
  MEDLINE   98272255
   PUBMED   9610724
REFERENCE   6  (residues 1 to 323)
  AUTHORS   Tsujikawa,M., Kurahashi,H., Tanaka,T., Nishida,K., Shimomura,Y.,
            Tano,Y. and Nakamura,Y.
  TITLE     Identification of the gene responsible for gelatinous drop-like
            corneal dystrophy
  JOURNAL   Nat. Genet. 21 (4), 420-423 (1999)
  MEDLINE   99206613
   PUBMED   10192395
REFERENCE   7  (residues 1 to 323)
  AUTHORS   Nakamura,T., Nishida,K., Dota,A., Adachi,W., Yamamoto,S., Maeda,N.,
            Okada,M. and Kinoshita,S.
  TITLE     Gelatino-lattice corneal dystrophy: clinical features and
            mutational analysis
  JOURNAL   Am. J. Ophthalmol. 129 (5), 665-666 (2000)
  MEDLINE   20304354
   PUBMED   10844062
REFERENCE   8  (residues 1 to 323)
  AUTHORS   Kinoshita,S., Nishida,K., Dota,A., Inatomi,T., Koizumi,N.,
            Elliott,A., Lewis,D., Quantock,A. and Fullwood,N.
  TITLE     Epithelial barrier function and ultrastructure of gelatinous
            drop-like corneal dystrophy
  JOURNAL   Cornea 19 (4), 551-555 (2000)
  MEDLINE   20382520
   PUBMED   10928776
REFERENCE   9  (residues 1 to 323)
  AUTHORS   Ha,N.T., Fujiki,K., Hotta,Y., Nakayasu,K. and Kanai,A.
  TITLE     Q118X mutation of M1S1 gene caused gelatinous drop-like corneal
            dystrophy: the P501T of BIGH3 gene found in a family with
            gelatinous drop-like corneal dystrophy
  JOURNAL   Am. J. Ophthalmol. 130 (1), 119-120 (2000)
  MEDLINE   20460624
   PUBMED   11004271
REFERENCE   10 (residues 1 to 323)
  AUTHORS   Tsujikawa,M., Tsujikawa,K., Maeda,N., Watanabe,H., Inoue,Y.,
            Mashima,Y., Shimomura,Y. and Tano,Y.
  TITLE     Rapid detection of M1S1 mutations by the protein truncation test
  JOURNAL   Invest. Ophthalmol. Vis. Sci. 41 (9), 2466-2468 (2000)
  MEDLINE   20391334
   PUBMED   10937555
REFERENCE   11 (residues 1 to 323)
  AUTHORS   Calabrese,G., Crescenzi,C., Morizio,E., Palka,G., Guerra,E. and
            Alberti,S.
  TITLE     Assignment of TACSTD1 (alias TROP1, M4S1) to human chromosome 2p21
            and refinement of mapping of TACSTD2 (alias TROP2, M1S1) to human
            chromosome 1p32 by in situ hybridization
  JOURNAL   Cytogenet. Cell Genet. 92 (1-2), 164-165 (2001)
  MEDLINE   21203566
   PUBMED   11306819
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X77753.1.
            Summary: This intronless gene encodes a carcinoma-associated
            antigen defined by the monoclonal antibody GA733. This antigen is a
            member of a family including at least two type I membrane proteins.
            It transduces an intracellular calcium signal and acts as a cell
            surface receptor. Mutations of this gene result in gelatinous
            drop-like corneal dystrophy, an autosomal recessive disorder
            characterized by severe corneal amyloidosis leading to blindness.
FEATURES             Location/Qualifiers
     source          1..323
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p32-p31"
     Protein         1..323
                     /product="tumor-associated calcium signal transducer 2
                     precursor"
                     /note="membrane component, chromosome 1, surface marker 1
                     (40kD glycoprotein, identified by monoclonal antibody
                     GA733); epithelial glycoprotein-1"
     sig_peptide     1..26
     mat_peptide     27..323
                     /product="tumor-associated calcium signal transducer 2"
     Region          27..274
                     /region_name="extracellular domain"
     Region          73..145
                     /region_name="pfam00086, thyroglobulin_1, Thyroglobulin
                     type-1 repeat. Thyroglobulin type 1 repeats are thought to
                     be involved in the control of proteolytic degradation. The
                     domain usually contains six conserved cysteines. These
                     form three disulphide bridges. Cysteines 1 pairs with 2, 3
                     with 4 and 5 with 6"
     Region          106..147
                     /region_name="smart00211, TY, Thyroglobulin type I
                     repeats; The N-terminal region of human thyroglobulin
                     contains 11 type-1 repeats TY repeats are proposed to be
                     inhibitors of cysteine proteases and binding partners of
                     heparin"
     Region          275..297
                     /region_name="transmembrane domain"
     Region          298..323
                     /region_name="cytoplasmic domain"
     CDS             1..323
                     /gene="TACSTD2"
                     /coded_by="NM_002353.1:616..1587"
                     /db_xref="LocusID:4070"
                     /db_xref="MIM:137290"
ORIGIN      
        1 margpglapp plrlpllllv laavtghtaa qdnctcptnk mtvcspdgpg grcqcralgs
       61 gmavdcstlt skclllkarm sapknartlv rpsehalvdn dglydpdcdp egrfkarqcn
      121 qtsvcwcvns vgvrrtdkgd lslrcdelvr thhilidlrh rptagafnhs dldaelrrlf
      181 reryrlhpkf vaavhyeqpt iqielrqnts qkaagevdig daayyferdi kgeslfqgrg
      241 gldlrvrgep lqvertliyy ldeippkfsm krltagliav ivvvvvalva gmavlvitnr
      301 rksgkykkve ikelgelrke psl
//



Revised: July 5, 2002.
 
 


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1: NP_001801. centromere protei...[gi:21735415] Links  


LOCUS       CENPB                    599 aa            linear   PRI 07-SEP-2002
DEFINITION  centromere protein B; centromere protein B (80kD); centromere
            autoantigen B [Homo sapiens].
ACCESSION   NP_001801
VERSION     NP_001801.1  GI:21735415
DBSOURCE    REFSEQ: accession NM_001810.3
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Earnshaw,W.C., Sullivan,K.F., Machlin,P.S., Cooke,C.A.,
            Kaiser,D.A., Pollard,T.D., Rothfield,N.F. and Cleveland,D.W.
  TITLE     Molecular cloning of cDNA for CENP-B, the major human centromere
            autoantigen
  JOURNAL   J. Cell Biol. 104 (4), 817-829 (1987)
  MEDLINE   87166180
   PUBMED   2435739
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Sullivan,K.F. and Glass,C.A.
  TITLE     CENP-B is a highly conserved mammalian centromere protein with
            homology to the helix-loop-helix family of proteins
  JOURNAL   Chromosoma 100 (6), 360-370 (1991)
  MEDLINE   91372020
   PUBMED   1893793
REFERENCE   3  (residues 1 to 599)
  AUTHORS   Yoda,K., Kitagawa,K., Masumoto,H., Muro,Y. and Okazaki,T.
  TITLE     A human centromere protein, CENP-B, has a DNA binding domain
            containing four potential alpha helices at the NH2 terminus, which
            is separable from dimerizing activity
  JOURNAL   J. Cell Biol. 119 (6), 1413-1427 (1992)
  MEDLINE   93107144
   PUBMED   1469042
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Sugimoto,K., Yata,H. and Himeno,M.
  TITLE     Mapping of the human CENP-B gene to chromosome 20 and the CENP-C
            gene to chromosome 12 by a rapid cycle DNA amplification procedure
  JOURNAL   Genomics 17 (1), 240-242 (1993)
  MEDLINE   94010896
   PUBMED   8406460
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Seki,N., Saito,T., Kitagawa,K., Masumoto,H., Okazaki,T. and
            Hori,T.A.
  TITLE     Mapping of the human centromere protein B gene (CENPB) to
            chromosome 20p13 by fluorescence in situ hybridization
  JOURNAL   Genomics 24 (1), 187-188 (1994)
  MEDLINE   95203879
   PUBMED   7896278
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Kitagawa,K., Masumoto,H., Ikeda,M. and Okazaki,T.
  TITLE     Analysis of protein-DNA and protein-protein interactions of
            centromere protein B (CENP-B) and properties of the DNA-CENP-B
            complex in the cell cycle
  JOURNAL   Mol. Cell. Biol. 15 (3), 1602-1612 (1995)
  MEDLINE   95166245
   PUBMED   7862152
REFERENCE   7  (residues 1 to 599)
  AUTHORS   Ando,S., Yang,H., Nozaki,N., Okazaki,T. and Yoda,K.
  TITLE     CENP-A, -B, and -C chromatin complex that contains the I-type
            alpha-satellite array constitutes the prekinetochore in HeLa cells
  JOURNAL   Mol. Cell. Biol. 22 (7), 2229-2241 (2002)
  MEDLINE   21881955
   PUBMED   11884609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109804.41.
            Summary: This gene product is a highly conserved protein associated
            with the centromere. It is a DNA-binding protein containing a
            helix-loop-helix DNA binding motif at the N-terminus, and a
            dimerization domain at the C-terminus. The DNA binding domain
            recognizes and binds a 17-bp sequence (CENP-B box) in the
            centromeric satellite DNA. This protein is proposed to play an
            important role in the assembly of specific centromere structures in
            interphase nuclei and on mitotic chromosomes. It is also considered
            a major centromere autoantigen recognized by sera from patients
            with anti-centromere antibodies.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
                     /cell_type="peripheral lymphocytes"
                     /clone_lib="lambda EMBL 3 genomic"
     Protein         1..599
                     /product="centromere protein B"
                     /note="centromere protein B (80kD); centromere autoantigen
                     B"
     Region          3..134
                     /region_name="pfam03221, Transposase_Tc5, Tc5 transposase"
     Region          74..135
                     /region_name="smart00674, CENPB, Putative DNA-binding
                     domain in centromere protein B, mouse jerky and
                     transposases"
     Region          204..391
                     /region_name="pfam03184, CENP-B, CENP-B protein.
                     Centromere Protein B (CENP-B) is a DNA-binding protein
                     localized to the centromere. Within the N-terminal 125
                     residues, there is a DNA-binding domain, which binds to a
                     corresponding 17bp CENP-B box sequence. In the C-terminal
                     59 residues, CENP-B has a dimerization domain. CENP-B
                     dimers either bind two separate DNA molecules or
                     alternatively, they may bind two CENP-B boxes on one DNA
                     molecule, with the intervening stretch of DNA forming a
                     loop structure. The CENP-B DNA-binding domain consists of
                     two repeating units, RP1 and RP2. RP1 has been shown to
                     consist of four helices in a helix- turn-helix structure"
     CDS             1..599
                     /gene="CENPB"
                     /coded_by="NM_001810.3:1..1800"
                     /db_xref="LocusID:1059"
                     /db_xref="MIM:117140"
ORIGIN      
        1 mgpkrrqltf reksriiqev eenpdlrkge iarrfnipps tlstilknkr ailaserkyg
       61 vastcrktnk lspydklegl liawfqqira aglpvkgiil kekalriaee lgmddftasn
      121 gwldrfrrrh gvvscsgvar ararnaaprt paapaspaav psegsggstt gwrareeqpp
      181 svaegyasqd vfsatetslw ydflpdqaag lcggdgrprq atqrlsvllc anadgseklp
      241 plvagksakp ragqaglpcd ytanskggvt tqalakylka ldtrmaaesr rvlllagrla
      301 aqsldtsglr hvqlaffppg tvhplergvv qqvkghyrqa mllkamaale gqdpsglqlg
      361 ltealhfvaa awqavepsdi aacfreagfg ggpnatitts lksegeeeee eeeeeeeeeg
      421 egeeeeeege eeeeeggege elgeeeevee egdvdsdeee eedeessseg leaedwaqgv
      481 veaggsfgay gaqeeaqcpt lhfleggeds dsdseeedde eeddededdd ddeedgdevp
      541 vpsfgeamay famvkrylts fpiddrvqsh ilhlehdlvh vtrknharqa gvrglghqs
//



Revised: July 5, 2002.
 
 


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1: NP_004311. ATPase, Ca++ tran...[gi:10835220] Links  


LOCUS       ATP2A1                   994 aa            linear   PRI 31-AUG-2001
DEFINITION  ATPase, Ca++ transporting, fast twitch 1 [Homo sapiens].
ACCESSION   NP_004311
VERSION     NP_004311.1  GI:10835220
DBSOURCE    REFSEQ: accession NM_004320.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 994)
  AUTHORS   Callen,D.F., Baker,E., Lane,S., Nancarrow,J., Thompson,A.,
            Whitmore,S.A., MacLennan,D.H., Berger,R., Cherif,D., Jarvela,I. et
            al.
  TITLE     Regional mapping of the Batten disease locus (CLN3) to human
            chromosome 16p12
  JOURNAL   Am. J. Hum. Genet. 49 (6), 1372-1377 (1991)
  MEDLINE   92081784
   PUBMED   1746562
REFERENCE   2  (residues 1 to 994)
  AUTHORS   Zhang,Y., Fujii,J., Phillips,M.S., Chen,H.S., Karpati,G., Yee,W.C.,
            Schrank,B., Cornblath,D.R., Boylan,K.B. and MacLennan,D.H.
  TITLE     Characterization of cDNA and genomic DNA encoding SERCA1, the
            Ca(2+)-ATPase of human fast-twitch skeletal muscle sarcoplasmic
            reticulum, and its elimination as a candidate gene for Brody
            disease
  JOURNAL   Genomics 30 (3), 415-424 (1995)
  MEDLINE   96423024
   PUBMED   8825625
REFERENCE   3  (residues 1 to 994)
  AUTHORS   Odermatt,A., Taschner,P.E., Khanna,V.K., Busch,H.F., Karpati,G.,
            Jablecki,C.K., Breuning,M.H. and MacLennan,D.H.
  TITLE     Mutations in the gene-encoding SERCA1, the fast-twitch skeletal
            muscle sarcoplasmic reticulum Ca2+ ATPase, are associated with
            Brody disease
  JOURNAL   Nat. Genet. 14 (2), 191-194 (1996)
  MEDLINE   96438858
   PUBMED   8841193
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U96781.1.
FEATURES             Location/Qualifiers
     source          1..994
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p12.1"
     Protein         1..994
                     /product="ATPase, Ca++ transporting, fast twitch 1"
     Region          3..77
                     /region_name="Cation transporter/ATPase"
                     /note="Cation_ATPase_N"
                     /db_xref="CDD:pfam00690"
     Region          101..341
                     /region_name="E1-E2 ATPase"
                     /note="E1-E2_ATPase"
                     /db_xref="CDD:pfam00122"
     Region          550..724
                     /region_name="haloacid dehalogenase-like hydrolase"
                     /note="Hydrolase"
                     /db_xref="CDD:pfam00702"
     Region          818..993
                     /region_name="Cation transporting ATPase"
                     /note="Cation_ATPase_C"
                     /db_xref="CDD:pfam00689"
     CDS             1..994
                     /gene="ATP2A1"
                     /coded_by="NM_004320.1:1..2985"
                     /note="SERCA1b"
                     /db_xref="LocusID:487"
                     /db_xref="MIM:108730"
ORIGIN      
        1 meaahaktte eclayfgvse ttgltpdqvk rnlekyglne lpaeegktlw elvieqfedl
       61 lvrilllaac isfvlawfee geetitafve pfvillilia naivgvwqer naenaiealk
      121 eyepemgkvy radrksvqri kardivpgdi vevavgdkvp adirilaiks ttlrvdqsil
      181 tgesvsvikh tepvpdprav nqdkknmlfs gtniaagkal givattgvgt eigkirdqma
      241 ateqdktplq qkldefgeql skvislicva vwlinighfn dpvhggswfr gaiyyfkiav
      301 alavaaipeg lpavittcla lgtrrmakkn aivrslpsve tlgctsvics dktgtlttnq
      361 msvckmfiid kvdgdiclln efsitgstya pegevlkndk pvrpgqydgl velaticalc
      421 ndssldfnea kgvyekvgea tetalttlve kmnvfntdvr slskverana cnsvirqlmk
      481 keftlefsrd rksmsvycsp akssraavgn kmfvkgapeg vidrcnyvrv gttrvpltgp
      541 vkekimavik ewgtgrdtlr clalatrdtp pkreemvldd sarfleyetd ltfvgvvgml
      601 dpprkevtgs iqlcrdagir vimitgdnkg taiaicrrig ifgeneevad raytgrefdd
      661 lplaeqreac rraccfarve pshkskivey lqsydeitam tgdgvndapa lkkaeigiam
      721 gsgtavakta semvladdnf stivaaveeg raiynnmkqf irylissnvg evvcifltaa
      781 lglpealipv qllwvnlvtd glpatalgfn ppdldimdrp prspkeplis gwlffrymai
      841 ggyvgaatvg aaawwflyae dgphvnysql thfmqctedn thfegidcev feapepmtma
      901 lsvlvtiemc nalnslsenq sllrmppwvn iwllgsicls mslhflilyv dplpmifklr
      961 aldltqwlmv lkislpvigl deilkfvarn yleg
//



Revised: July 5, 2002.
 
 


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1: NP_002951. S100 calcium-bind...[gi:4506763] Links  


LOCUS       S100A3                   101 aa            linear   PRI 20-DEC-2001
DEFINITION  S100 calcium-binding protein A3 [Homo sapiens].
ACCESSION   NP_002951
VERSION     NP_002951.1  GI:4506763
DBSOURCE    REFSEQ: accession NM_002960.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 101)
  AUTHORS   Engelkamp,D., Schafer,B.W., Mattei,M.G., Erne,P. and Heizmann,C.W.
  TITLE     Six S100 genes are clustered on human chromosome 1q21:
            identification of two genes coding for the two previously
            unreported calcium-binding proteins S100D and S100E
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 90 (14), 6547-6551 (1993)
  MEDLINE   93342029
   PUBMED   8341667
REFERENCE   2  (residues 1 to 101)
  AUTHORS   Schafer,B.W., Wicki,R., Engelkamp,D., Mattei,M.G. and Heizmann,C.W.
  TITLE     Isolation of a YAC clone covering a cluster of nine S100 genes on
            human chromosome 1q21: rationale for a new nomenclature of the S100
            calcium-binding protein family
  JOURNAL   Genomics 25 (3), 638-643 (1995)
  MEDLINE   95278932
   PUBMED   7759097
REFERENCE   3  (residues 1 to 101)
  AUTHORS   Schafer,B.W. and Heizmann,C.W.
  TITLE     The S100 family of EF-hand calcium-binding proteins: functions and
            pathology
  JOURNAL   Trends Biochem. Sci. 21 (4), 134-140 (1996)
  MEDLINE   96273192
   PUBMED   8701470
REFERENCE   4  (residues 1 to 101)
  AUTHORS   Kizawa,K., Uchiwa,H. and Murakami,U.
  TITLE     Highly-expressed S100A3, a calcium-binding protein, in human hair
            cuticle
  JOURNAL   Biochim. Biophys. Acta 1312 (2), 94-98 (1996)
  MEDLINE   96271430
   PUBMED   8672544
REFERENCE   5  (residues 1 to 101)
  AUTHORS   Groves,P., Finn,B.E., Kuznicki,J. and Forsen,S.
  TITLE     A model for target protein binding to calcium-activated S100 dimers
  JOURNAL   FEBS Lett. 421 (3), 175-179 (1998)
  MEDLINE   98127819
   PUBMED   9468301
REFERENCE   6  (residues 1 to 101)
  AUTHORS   Ridinger,K., Ilg,E.C., Niggli,F.K., Heizmann,C.W. and Schafer,B.W.
  TITLE     Clustered organization of S100 genes in human and mouse
  JOURNAL   Biochim. Biophys. Acta 1448 (2), 254-263 (1998)
  MEDLINE   99117144
   PUBMED   9920416
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z18948.1.
            Summary: The protein encoded by this gene is a member of the S100
            family of proteins containing 2 EF-hand calcium-binding motifs.
            S100 proteins are localized in the cytoplasm and/or nucleus of a
            wide range of cells, and involved in the regulation of a number of
            cellular processes such as cell cycle progression and
            differentiation. S100 genes include at least 13 members which are
            located as a cluster on chromosome 1q21. This protein has the
            highest content of cysteines of all S100 proteins, has a high
            affinity for Zinc, and is highly expressed in human hair cuticle.
            The precise function of this protein is unknown.
FEATURES             Location/Qualifiers
     source          1..101
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..101
                     /product="S100 calcium-binding protein A3"
     Region          5..27
                     /region_name="S-100/ICaBP type calcium binding domain. The
                     S-100 domain is a subfamily of the EF-hand calcium binding
                     proteins"
                     /note="S_100"
                     /db_xref="CDD:pfam01023"
     Region          20..33
                     /region_name="Calcium binding region"
     Region          63..74
                     /region_name="Calcium binding region"
     CDS             1..101
                     /gene="S100A3"
                     /coded_by="NM_002960.1:84..389"
                     /db_xref="LocusID:6274"
                     /db_xref="MIM:176992"
ORIGIN      
        1 marpleqava aivctfqeya grcgdkyklc qaelkellqk elatwtptef recdynkfms
       61 vldtnkdcev dfveyvrsla clclycheyf kdcpseppcs q
//



Revised: July 5, 2002.
 
 


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1: NP_001714. bullous pemphigoi...[gi:4502443] Links  


LOCUS       BPAG1                   2649 aa            linear   PRI 07-SEP-2002
DEFINITION  bullous pemphigoid antigen 1 isoform 1e precursor; bullous
            pemphigoid antigen 1; bullous pemphigoid antigen 1 (230/240kD);
            dystonin; hemidesmosomal plaque protein [Homo sapiens].
ACCESSION   NP_001714
VERSION     NP_001714.1  GI:4502443
DBSOURCE    REFSEQ: accession NM_001723.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2649)
  AUTHORS   Stanley,J.R., Tanaka,T., Mueller,S., Klaus-Kovtun,V. and Roop,D.
  TITLE     Isolation of complementary DNA for bullous pemphigoid antigen by
            use of patients' autoantibodies
  JOURNAL   J. Clin. Invest. 82 (6), 1864-1870 (1988)
  MEDLINE   89067122
   PUBMED   2461961
REFERENCE   2  (residues 1 to 2649)
  AUTHORS   Owaribe,K., Kartenbeck,J., Stumpp,S., Magin,T.M., Krieg,T.,
            Diaz,L.A. and Franke,W.W.
  TITLE     The hemidesmosomal plaque. I. Characterization of a major
            constituent protein as a differentiation marker for certain forms
            of epithelia
  JOURNAL   Differentiation 45 (3), 207-220 (1990)
  MEDLINE   91216368
   PUBMED   2090522
REFERENCE   3  (residues 1 to 2649)
  AUTHORS   Sawamura,D., Nomura,K., Sugita,Y., Mattei,M.G., Chu,M.L.,
            Knowlton,R. and Uitto,J.
  TITLE     Bullous pemphigoid antigen (BPAG1): cDNA cloning and mapping of the
            gene to the short arm of human chromosome 6
  JOURNAL   Genomics 8 (4), 722-726 (1990)
  MEDLINE   91115331
   PUBMED   2276744
REFERENCE   4  (residues 1 to 2649)
  AUTHORS   Tanaka,T., Parry,D.A., Klaus-Kovtun,V., Steinert,P.M. and
            Stanley,J.R.
  TITLE     Comparison of molecularly cloned bullous pemphigoid antigen to
            desmoplakin I confirms that they define a new family of cell
            adhesion junction plaque proteins
  JOURNAL   J. Biol. Chem. 266 (19), 12555-12559 (1991)
  MEDLINE   91286285
   PUBMED   1712022
REFERENCE   5  (residues 1 to 2649)
  AUTHORS   Sawamura,D., Li,K., Chu,M.L. and Uitto,J.
  TITLE     Human bullous pemphigoid antigen (BPAG1). Amino acid sequences
            deduced from cloned cDNAs predict biologically important peptide
            segments and protein domains
  JOURNAL   J. Biol. Chem. 266 (27), 17784-17790 (1991)
  MEDLINE   92011493
   PUBMED   1717441
REFERENCE   6  (sites)
  AUTHORS   Elgart,G.W. and Stanley,J.R.
  TITLE     Cloning of the 5' mRNA for the 230-kD bullous pemphigoid antigen by
            rapid amplification of cDNA ends
  JOURNAL   J. Invest. Dermatol. 101 (2), 244-246 (1993)
  MEDLINE   93346806
   PUBMED   8345227
REFERENCE   7  (residues 1 to 2649)
  AUTHORS   Tamai,K., Sawamura,D., Do,H.C., Tamai,Y., Li,K. and Uitto,J.
  TITLE     The human 230-kD bullous pemphigoid antigen gene (BPAG1).
            Exon-intron organization and identification of regulatory tissue
            specific elements in the promoter region
  JOURNAL   J. Clin. Invest. 92 (2), 814-822 (1993)
  MEDLINE   93352829
   PUBMED   8349819
REFERENCE   8  (residues 1 to 2649)
  AUTHORS   Hopkinson,S.B. and Jones,J.C.
  TITLE     Identification of a second protein product of the gene encoding a
            human epidermal autoantigen
  JOURNAL   Biochem. J. 300 (Pt 3), 851-857 (1994)
  MEDLINE   94280413
   PUBMED   8010969
REFERENCE   9  (residues 1 to 2649)
  AUTHORS   Brown,A., Dalpe,G., Mathieu,M. and Kothary,R.
  TITLE     Cloning and characterization of the neural isoforms of human
            dystonin
  JOURNAL   Genomics 29 (3), 777-780 (1995)
  MEDLINE   96121394
   PUBMED   8575775
REFERENCE   10 (residues 1 to 2649)
  AUTHORS   Yang,Y., Bauer,C., Strasser,G., Wollman,R., Julien,J.P. and
            Fuchs,E.
  TITLE     Integrators of the cytoskeleton that stabilize microtubules
  JOURNAL   Cell 98 (2), 229-238 (1999)
  MEDLINE   99354988
   PUBMED   10428034
REFERENCE   11 (residues 1 to 2649)
  AUTHORS   Okumura,M., Yamakawa,H., Ohara,O. and Owaribe,K.
  TITLE     Novel alternative splicings of BPAG1 (bullous pemphigoid antigen 1)
            including the domain structure closely related to MACF (microtubule
            actin cross-linking factor)
  JOURNAL   J. Biol. Chem. 277 (8), 6682-6687 (2002)
  MEDLINE   21839111
   PUBMED   11751855
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L11690.1 and M69225.1.
            Summary: This gene encodes two proteins, dystonin and bullous
            pemphigoid antigen 1 (BPAG1), both members of the plakin protein
            family of adhesion junction plaque proteins. Dystonin is expressed
            in neural and muscle tissue, anchoring neural intermediate
            filaments to the actin cytoskeleton. Mice defective for this
            protein have sensory neurodegeneration. Three dystonin isoforms
            have been identified but the transcripts for these isoforms have
            not been completely characterized. The 3' exons of the dystonin
            transcripts are identical to some of the 5' exons of the BPAG1
            transcripts. BPAG1 is expressed in epithelial tissue, anchoring
            keratin-containing intermediate filaments to hemidesmosomes. In the
            blistering disease bullous pemphigoid, autoantibodies are generated
            against this protein. Four BPAG1 isoforms have been identified but
            complete transcripts have been determined for only three isoforms.
            Transcript Variant: This variant (1e) is the shortest transcript,
            sharing all but two of its exons with variant 1eA; the last two
            exons are unique to variant 1e. Isoform 1e is the shortest isoform
            and the C-terminal half of isoform 1e is distinct from that of
            isoform 1eA.
FEATURES             Location/Qualifiers
     source          1..2649
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p12-p11"
     Protein         1..2649
                     /product="bullous pemphigoid antigen 1 isoform 1e
                     precursor"
                     /note="isoform 1e is encoded by transcript variant 1e;
                     bullous pemphigoid antigen 1; bullous pemphigoid antigen 1
                     (230/240kD); dystonin; hemidesmosomal plaque protein"
     sig_peptide     1..43
     variation       33
                     /allele="S"
                     /allele="L"
                     /db_xref="dbSNP:1024196"
     mat_peptide     44..2649
                     /product="bullous pemphigoid antigen 1, isoform 1e"
     Region          282..373
                     /region_name="smart00150, SPEC, Spectrin repeats"
     Region          375..477
                     /region_name="pfam00435, spectrin, Spectrin repeat.
                     Spectrin repeats are found in several proteins involved in
                     cytoskeletal structure. These include spectrin,
                     alpha-actinin and dystrophin. The sequence repeat used in
                     this family is taken from the structural repeat in
                     reference. The spectrin repeat forms a three helix bundle.
                     The second helix is interrupted by proline in some
                     sequences. The repeats are defined by a characteristic
                     tryptophan (W) residue at position 17 in helix A and a
                     leucine (L) at 2 residues from the carboxyl end of helix
                     C"
     Region          376..476
                     /region_name="smart00150, SPEC, Spectrin repeats"
     Region          1011..1666
                     /region_name="pfam01576, Myosin_tail, Myosin tail. The
                     myosin molecule is a multi-subunit complex made up of two
                     heavy chains and four light chains it is a fundamental
                     contractile protein found in all eukaryote cell types.
                     This family consists of the coiled-coil myosin heavy chain
                     tail region. The coiled-coil is composed of the tail from
                     two molecules of myosin. These can then assemble into the
                     macromolecular thick filament. The coiled-coil region
                     provides the structural backbone the thick filament"
     Region          1108..1697
                     /region_name="pfam01576, Myosin_tail, Myosin tail. The
                     myosin molecule is a multi-subunit complex made up of two
                     heavy chains and four light chains it is a fundamental
                     contractile protein found in all eukaryote cell types.
                     This family consists of the coiled-coil myosin heavy chain
                     tail region. The coiled-coil is composed of the tail from
                     two molecules of myosin. These can then assemble into the
                     macromolecular thick filament. The coiled-coil region
                     provides the structural backbone the thick filament"
     Region          1132..1698
                     /region_name="pfam01576, Myosin_tail, Myosin tail. The
                     myosin molecule is a multi-subunit complex made up of two
                     heavy chains and four light chains it is a fundamental
                     contractile protein found in all eukaryote cell types.
                     This family consists of the coiled-coil myosin heavy chain
                     tail region. The coiled-coil is composed of the tail from
                     two molecules of myosin. These can then assemble into the
                     macromolecular thick filament. The coiled-coil region
                     provides the structural backbone the thick filament"
     Region          1141..1474
                     /region_name="pfam00038, filament, Intermediate filament
                     protein"
     Region          1340..1516
                     /region_name="pfam00038, filament, Intermediate filament
                     protein"
     Region          1350..1698
                     /region_name="pfam01576, Myosin_tail, Myosin tail. The
                     myosin molecule is a multi-subunit complex made up of two
                     heavy chains and four light chains it is a fundamental
                     contractile protein found in all eukaryote cell types.
                     This family consists of the coiled-coil myosin heavy chain
                     tail region. The coiled-coil is composed of the tail from
                     two molecules of myosin. These can then assemble into the
                     macromolecular thick filament. The coiled-coil region
                     provides the structural backbone the thick filament"
     Region          1353..1559
                     /region_name="pfam00769, ERM, Ezrin/radixin/moesin family.
                     This family of proteins contain a band 4.1 domain
                     (pfam00373), at their amino terminus. This family
                     represents the rest of these proteins"
     Region          1359..1528
                     /region_name="pfam00769, ERM, Ezrin/radixin/moesin family.
                     This family of proteins contain a band 4.1 domain
                     (pfam00373), at their amino terminus. This family
                     represents the rest of these proteins"
     Region          1370..1662
                     /region_name="pfam01576, Myosin_tail, Myosin tail. The
                     myosin molecule is a multi-subunit complex made up of two
                     heavy chains and four light chains it is a fundamental
                     contractile protein found in all eukaryote cell types.
                     This family consists of the coiled-coil myosin heavy chain
                     tail region. The coiled-coil is composed of the tail from
                     two molecules of myosin. These can then assemble into the
                     macromolecular thick filament. The coiled-coil region
                     provides the structural backbone the thick filament"
     Region          1412..1671
                     /region_name="pfam00038, filament, Intermediate filament
                     protein"
     Region          1501..1697
                     /region_name="pfam00769, ERM, Ezrin/radixin/moesin family.
                     This family of proteins contain a band 4.1 domain
                     (pfam00373), at their amino terminus. This family
                     represents the rest of these proteins"
     Region          2170..2212
                     /region_name="pfam00681, Plectin, Plectin repeat. This
                     family includes repeats from plectin, desmoplakin,
                     envoplakin and bullous pemphigoid antigen"
     Region          2170..2205
                     /region_name="smart00250, PLEC, Plectin repeat"
     Region          2242..2286
                     /region_name="pfam00681, Plectin, Plectin repeat. This
                     family includes repeats from plectin, desmoplakin,
                     envoplakin and bullous pemphigoid antigen"
     Region          2242..2275
                     /region_name="smart00250, PLEC, Plectin repeat"
     Region          2439..2483
                     /region_name="pfam00681, Plectin, Plectin repeat. This
                     family includes repeats from plectin, desmoplakin,
                     envoplakin and bullous pemphigoid antigen"
     Region          2477..2521
                     /region_name="pfam00681, Plectin, Plectin repeat. This
                     family includes repeats from plectin, desmoplakin,
                     envoplakin and bullous pemphigoid antigen"
     Region          2477..2514
                     /region_name="smart00250, PLEC, Plectin repeat"
     Region          2515..2552
                     /region_name="smart00250, PLEC, Plectin repeat"
     Region          2553..2596
                     /region_name="pfam00681, Plectin, Plectin repeat. This
                     family includes repeats from plectin, desmoplakin,
                     envoplakin and bullous pemphigoid antigen"
     Region          2553..2586
                     /region_name="smart00250, PLEC, Plectin repeat"
     CDS             1..2649
                     /gene="BPAG1"
                     /coded_by="NM_001723.2:103..8052"
                     /db_xref="LocusID:667"
                     /db_xref="MIM:113810"
ORIGIN      
        1 mhsssysyrs sdsvfsntts trtsldsnen lllvhcgptl inscisfgse sfdghrleml
       61 qqianrvqrd svicedklil agnalqsdsk rlesgvqfqn eaeiagyile cenllrqhvi
      121 dvqilidgky yqadqlvqrv aklrdeimal rnecssvysk griltteqtk lmisgitqsl
      181 nsgfaqtlhp sltsgltqsl tpsltsssmt sglssgmtsr ltpsvtpayt pgfpsglvpn
      241 fssgvepnsl qtlklmqirk pllksslldq nlteeeinmk fvqdllnwvd emqvqldrte
      301 wgsdlpsves hlenhknvhr aieefesslk eakiseiqmt aplkltyaek lhrlesqyak
      361 llntsrnqer hldtlhnfvs ratneliwln ekeeeevayd wserntniar kkdyhaelmr
      421 eldqkeenik svqeiaeqll lenhparlti eayraamqtq wswilqlcqc veqhikenta
      481 yfeffndake atdylrnlkd aiqrkyscdr sssihkledl vqesmeekee llqykstian
      541 lmgkaktiiq lkprnsdcpl ktsipikaic dyrqieitiy kddecvlann shrakwkvis
      601 ptgneamvps vcftvpppnk eavdlanrie qqyqnvltlw heshinmksv vswhylinei
      661 drirasnvas iktmlpgehq qvlsnlqsrf edfledsqes qvfsgsditq lekevnvckq
      721 yyqellksae reeqeesvyn lyisevrnir lrlencedrl irqirtpler ddlhesvfri
      781 teqeklkkel erlkddlgti tnkceeffsq aaasssvptl rselnvvlqn mnqvysmsst
      841 yidklktvnl vlkntqaaea lvklyetklc eeeaviadkn nienlistlk qwrsevdekr
      901 qvfhaledel qkakaisdem fktykerdld fdwhkekadq lverwqnvhv qidnrlrdle
      961 gigkslkyyr dtyhplddwi qqvettqrki qenqpenskt latqlnqqkm lvseiemkqs
     1021 kmdecqkyae qysatvkdye lqtmtyramv dsqqkspvkr rrmqssadli iqefmdlrtr
     1081 ytalvtlmtq yikfagdslk rleeeeikrc ketsehgays dllqrqkatv lenskltgki
     1141 selermvael kkqksrveee lpkvreaaen elrkqqrnve dislqkirae seakqyrrel
     1201 etivrekeaa erelervrql tieaeakraa veenllnfrn qleentftrr tledhlkrkd
     1261 lslndleqqk nklmeelrrk rdneeellkl ikqmekdlaf qkqvaekqlk ekqkielear
     1321 rkiteiqytc renalpvcpi tqatscravt glqqehdkqk aeelkqqvde ltaanrkaeq
     1381 dmreltyeln alqlektsse ekarllkdkl detnntlrcl klelerkdqa ekgysqqlre
     1441 lgrqlnqttg kaeeamqeas dlkkikrnyq leleslnhek gklqrevdri trahavaekn
     1501 iqhlnsqihs frdekelerl qicqrksdhl keqfeksheq llqnikaeke nndkiqrlne
     1561 eleksnecae mlkqkveelt rqnnetklmm qriqaeseni vlekqtiqqr cealkiqadg
     1621 fkdqlrstne hlhkqtkteq dfqrkikcle edlaksqnlv sefkqkcdqq niiiqntkke
     1681 vrnlnaelna skeekrrgeq kvqlqqaqvq elnnrlkkvq delhlktiee qmthrkmvlf
     1741 qeesgkfkqs aeefrkkmek lmeskviten disgirldfv slqqensraq enaklcetni
     1801 kelerqlqqy reqmqqgqhm eanhyqkcqk ledeliaqkr evenlkqkmd qqikehehql
     1861 vllqceiqkk stakdctfkp dfemtvkecq hsgelssrnt ghlhptprsp llrwtqepqp
     1921 leekwqhrvv eqipkevqfq ppgaplekek sqqcyseyfs qtstelqitf detnpitrls
     1981 eiekirdqal nnsrppvryq dnacemelvk vltpleiakn kqydmhtevt tlkqeknpvp
     2041 saeewmlegc rasgglkkgd flkkglepet fqnfdgdhac svrddefkfq glrhtvtarq
     2101 lveaklldmr tieqlrlglk tveevqktln kfltkatsia glylestkek isfasaaeri
     2161 iidkmvalaf leaqaatgfi idpisgqtys vedavlkgvv dpefrirlle aekaavgysy
     2221 ssktlsvfqa menrmldrqk gkhileaqia sggvidpvrg irvppeialq qgllnnailq
     2281 flhepssntr vfpnpnnkqa lyysellrmc vfdvesqcfl fpfgernisn lnvkkthris
     2341 vvdtktgsel tvyeafqrnl ieksiylels gqqyqwkeam ffesyghssh mltdtktglh
     2401 fnineaieqg tidkalvkky qeglitltel adsllsrlvp kkdlhspvag ywltasgeri
     2461 svlkasrrnl vdritalrcl eaqvstggii dpltgkkyrv aealhrglvd egfaqqlrqc
     2521 elvitgighp itnkmmsvve avnaniinke mgirclefqy ltggliepqv hsrlsieeal
     2581 qvgiidvlia tklkdqksyv rniicpqtkr kltykealek adfdfhtglk llevseplmt
     2641 gisslyyss
//



Revised: July 5, 2002.
 
 


Disclaimer | Write to the Help Desk
NCBI | NLM | NIH 

 

Oct 21 2002 11:56:56 

BLinkBLinkRelated SequencesRelated SequencesDomain RelativesDomain RelativesDomainsDomainsMap ViewerMap ViewerNucleotideNucleotideOMIMOMIMPubMedPubMedSNPSNPTaxonomyTaxonomyLinkOutLinkOutHelpHelp  



&&&&&&&


    
 
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   Search PubMed Protein Nucleotide PopSet Taxonomy Genome OMIM Structure Domains GEO Books Books2 MapViewDr TestDb UniSTS CDD SNP Journals UniGene  for        
 
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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_004763. P311 protein [Hom...[gi:4758866] Links  


LOCUS       P311                      68 aa            linear   PRI 14-MAY-2002
DEFINITION  P311 protein [Homo sapiens].
ACCESSION   NP_004763
VERSION     NP_004763.1  GI:4758866
DBSOURCE    REFSEQ: accession NM_004772.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Studler,J.M., Glowinski,J. and Levi-Strauss,M.
  TITLE     An abundant mRNA of the embryonic brain persists at a high level in
            cerebellum, hippocampus and olfactory bulb during adulthood
  JOURNAL   Eur. J. Neurosci. 5 (6), 614-623 (1993)
  MEDLINE   94084289
   PUBMED   8261136
COMMENT     PREDICTED REFSEQ: The mRNA record is supported by experimental
            evidence; however, the coding sequence is predicted. The reference
            sequence was derived from U30521.1.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q21.3"
                     /sex="female"
                     /tissue_type="cerebellum"
                     /dev_stage="2 year-old"
     Protein         1..68
                     /product="P311 protein"
     CDS             1..68
                     /gene="P311"
                     /coded_by="NM_004772.1:203..409"
                     /note="putative"
                     /db_xref="LocusID:9315"
ORIGIN      
        1 mvyypelfvw vsqepfpnkd megrlpkgrl pvpkevnrkk ndetnaaslt plgsselrsp
       61 risylhff
//



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1: NP_000561. Fc fragment of Ig...[gi:10835139] Links  


LOCUS       FCGR3B                   233 aa            linear   PRI 31-OCT-2000
DEFINITION  Fc fragment of IgG, low affinity IIIb, receptor for (CD16) [Homo
            sapiens].
ACCESSION   NP_000561
VERSION     NP_000561.1  GI:10835139
DBSOURCE    REFSEQ: accession NM_000570.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 233)
  AUTHORS   Ravetch,J.V. and Perussia,B.
  TITLE     Alternative membrane forms of Fc gamma RIII(CD16) on human natural
            killer cells and neutrophils. Cell type-specific expression of two
            genes that differ in single nucleotide substitutions
  JOURNAL   J. Exp. Med. 170 (2), 481-497 (1989)
  MEDLINE   89328325
   PUBMED   2526846
REFERENCE   2  (residues 1 to 233)
  AUTHORS   Qiu,W.Q., de Bruin,D., Brownstein,B.H., Pearse,R. and Ravetch,J.V.
  TITLE     Organization of the human and mouse low-affinity Fc gamma R genes:
            duplication and recombination
  JOURNAL   Science 248 (4956), 732-735 (1990)
  MEDLINE   90239570
   PUBMED   2139735
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X16863.1.
FEATURES             Location/Qualifiers
     source          1..233
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23"
                     /cell_line="primary-peripheral blood granulocytes"
                     /note="Allele: NA-2"
     Protein         1..233
                     /product="Fc fragment of IgG, low affinity IIIb, receptor
                     for (CD16)"
     Region          38..92
                     /region_name="Immunoglobulin"
                     /note="IG"
                     /db_xref="CDD:IG"
     CDS             1..233
                     /gene="FCGR3B"
                     /coded_by="NM_000570.1:34..735"
                     /note="(AA 1-233)"
                     /db_xref="LocusID:2215"
ORIGIN      
        1 mwqlllptal lllvsagmrt edlpkavvfl epqwysvlek dsvtlkcqga yspednstqw
       61 fhneslissq assyfidaat vndsgeyrcq tnlstlsdpv qlevhigwll lqaprwvfke
      121 edpihlrchs wkntalhkvt ylqngkdrky fhhnsdfhip katlkdsgsy fcrglvgskn
      181 vssetvniti tqglavstis sfsppgyqvs fclvmvllfa vdtglyfsvk tni
//



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1: NP_005075. phospholipase A2,...[gi:4826884] Links  


LOCUS       PLA2G7                   441 aa            linear   PRI 01-NOV-2000
DEFINITION  phospholipase A2, group VII (platelet-activating factor
            acetylhydrolase, plasma); Platelet-activating factor
            acetylhydrolase [Homo sapiens].
ACCESSION   NP_005075
VERSION     NP_005075.1  GI:4826884
DBSOURCE    REFSEQ: accession NM_005084.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 441)
  AUTHORS   Tjoelker,L.W., Wilder,C., Eberhardt,C., Stafforini,D.M.,
            Dietsch,G., Schimpf,B., Hooper,S., Trong,H., Cousens,L.S.,
            Zimmerman,G.A., Yamada,Y., McIntyre,T.M., Prescott,S.M. and
            Gray,P.W.
  TITLE     Anti-inflammatory properties of a platelet-activating factor
            acetylhydrolase
  JOURNAL   Nature 374 (6522), 549-553 (1995)
  MEDLINE   95214779
   PUBMED   7700381
REFERENCE   2  (residues 1 to 441)
  AUTHORS   Tew,D.G., Southan,C., Rice,S.Q., Lawrence,M.P., Li,H., Boyd,H.F.,
            Moores,K., Gloger,I.S. and Macphee,C.H.
  TITLE     Purification, properties, sequencing, and cloning of a
            lipoprotein-associated, serine-dependent phospholipase involved in
            the oxidative modification of low-density lipoproteins
  JOURNAL   Arterioscler. Thromb. Vasc. Biol. 16 (4), 591-599 (1996)
  MEDLINE   96197208
   PUBMED   8624782
REFERENCE   3  (residues 1 to 441)
  AUTHORS   Hiramoto,M., Yoshida,H., Imaizumi,T., Yoshimizu,N. and Satoh,K.
  TITLE     A mutation in plasma platelet-activating factor acetylhydrolase
            (Val279-->Phe) is a genetic risk factor for stroke
  JOURNAL   Stroke 28 (12), 2417-2420 (1997)
  MEDLINE   98074100
   PUBMED   9412624
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U20157.1.
FEATURES             Location/Qualifiers
     source          1..441
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.2-p12"
                     /clone="sAH 406-3"
                     /cell_type="macrophage"
                     /tissue_type="myeloid"
                     /clone_lib="in vitro differentiated macrophage cDNA
                     library"
     Protein         1..441
                     /product="phospholipase A2, group VII (platelet-activating
                     factor acetylhydrolase, plasma)"
                     /note="Platelet-activating factor acetylhydrolase"
     variation       92
                     /allele="H"
                     /allele="R"
                     /db_xref="dbSNP:1805017"
     variation       198
                     /allele="I"
                     /allele="T"
                     /db_xref="dbSNP:1805018"
     Region          250..430
                     /region_name="alpha/beta hydrolase fold"
                     /note="abhydrolase"
                     /db_xref="CDD:pfam00561"
     variation       379
                     /allele="A"
                     /allele="V"
                     /db_xref="dbSNP:1051931"
     CDS             1..441
                     /gene="PLA2G7"
                     /coded_by="NM_005084.1:162..1487"
                     /db_xref="LocusID:7941"
                     /db_xref="MIM:601690"
ORIGIN      
        1 mvppklhvlf clcgclavvy pfdwqyinpv ahmkssawvn kiqvlmaaas fgqtkiprgn
       61 gpysvgctdl mfdhtnkgtf lrlyypsqdn drldtlwipn keyfwglskf lgthwlmgni
      121 lrllfgsmtt panwnsplrp gekyplvvfs hglgafrtly saigidlash gfivaavehr
      181 drsasatyyf kdqsaaeigd kswlylrtlk qeeethirne qvrqrakecs qalslildid
      241 hgkpvknald lkfdmeqlkd sidrekiavi ghsfggatvi qtlsedqrfr cgialdawmf
      301 plgdevysri pqplffinse yfqypaniik mkkcyspdke rkmitirgsv hqnfadftfa
      361 tgkiighmlk lkgdidsnva idlsnkasla flqkhlglhk dfdqwdclie gddenlipgt
      421 ninttnqhim lqnssgieky n
//



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1: NP_000551. CD53 antigen; leu...[gi:10834972] Links  


LOCUS       CD53                     219 aa            linear   PRI 27-AUG-2002
DEFINITION  CD53 antigen; leukocyte surface antigen CD53; antigen MOX44
            identified by monoclonal antibody MRC-OX44; CD53 glycoprotein; cell
            surface antigen; transmembrane glycoprotein; CD53 tetraspan antigen
            [Homo sapiens].
ACCESSION   NP_000551
VERSION     NP_000551.1  GI:10834972
DBSOURCE    REFSEQ: accession NM_000560.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Angelisova,P., Vlcek,C., Stefanova,I., Lipoldova,M. and Horejsi,V.
  TITLE     The human leucocyte surface antigen CD53 is a protein structurally
            similar to the CD37 and MRC OX-44 antigens
  JOURNAL   Immunogenetics 32 (4), 281-285 (1990)
  MEDLINE   91055810
   PUBMED   1700763
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Amiot,M.
  TITLE     Identification and analysis of cDNA clones encoding CD53. A
            pan-leukocyte antigen related to membrane transport proteins
  JOURNAL   J. Immunol. 145 (12), 4322-4325 (1990)
  MEDLINE   91079522
   PUBMED   2258620
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Horejsi,V. and Vlcek,C.
  TITLE     Novel structurally distinct family of leucocyte surface
            glycoproteins including CD9, CD37, CD53 and CD63
  JOURNAL   FEBS Lett. 288 (1-2), 1-4 (1991)
  MEDLINE   91348240
   PUBMED   1879540
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Gonzalez,M.E., Pardo-Manuel de Villena,F., Fernandez-Ruiz,E.,
            Rodriguez de Cordoba,S. and Lazo,P.A.
  TITLE     The human CD53 gene, coding for a four transmembrane domain
            protein, maps to chromosomal region 1p13
  JOURNAL   Genomics 18 (3), 725-728 (1993)
  MEDLINE   94140382
   PUBMED   8307585
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Korinek,V. and Horejsi,V.
  TITLE     Genomic structure of the human CD53 gene
  JOURNAL   Immunogenetics 38 (4), 272-279 (1993)
  MEDLINE   93307785
   PUBMED   8319976
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Taguchi,T., Bellacosa,A., Zhou,J.Y., Gilbert,D.J., Lazo,P.A.,
            Copeland,N.G., Jenkins,N.A., Tsichlis,P.N. and Testa,J.R.
  TITLE     Chromosomal localization of the Ox-44 (CD53) leukocyte antigen gene
            in man and rodents
  JOURNAL   Cytogenet. Cell Genet. 64 (3-4), 217-221 (1993)
  MEDLINE   94007965
   PUBMED   8404042
REFERENCE   7  (residues 1 to 219)
  AUTHORS   Virtaneva,K.I., Angelisova,P., Baumruker,T., Horejsi,V.,
            Nevanlinna,H. and Schroder,J.
  TITLE     The genes for CD37, CD53, and R2, all members of a novel gene
            family, are located on different chromosomes
  JOURNAL   Immunogenetics 37 (6), 461-465 (1993)
  MEDLINE   93170894
   PUBMED   8436422
REFERENCE   8  (residues 1 to 219)
  AUTHORS   Serru,V., Le Naour,F., Billard,M., Azorsa,D.O., Lanza,F.,
            Boucheix,C. and Rubinstein,E.
  TITLE     Selective tetraspan-integrin complexes (CD81/alpha4beta1,
            CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting
            tetraspan interactions
  JOURNAL   Biochem. J. 340 (Pt 1), 103-111 (1999)
  MEDLINE   99247901
   PUBMED   10229664
REFERENCE   9  (residues 1 to 219)
  AUTHORS   Hernandez-Torres,J., Yunta,M. and Lazo,P.A.
  TITLE     Differential cooperation between regulatory sequences required for
            human CD53 gene expression
  JOURNAL   J. Biol. Chem. 276 (38), 35405-35413 (2001)
  MEDLINE   21443707
   PUBMED   11443129
REFERENCE   10 (residues 1 to 219)
  AUTHORS   Berditchevski,F.
  TITLE     Complexes of tetraspanins with integrins: more than meets the eye
  JOURNAL   J. Cell. Sci. 114 (Pt 23), 4143-4151 (2001)
  MEDLINE   21601835
   PUBMED   11739647
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M37033.1, L11670.1 and
            L11671.1.
            Summary: The protein encoded by this gene is a member of the
            transmembrane 4 superfamily, also known as the tetraspanin family.
            Most of these members are cell-surface proteins that are
            characterized by the presence of four hydrophobic domains. The
            proteins mediate signal transduction events that play a role in the
            regulation of cell development, activation, growth and motility.
            This encoded protein is a cell surface glycoprotein that is known
            to complex with integrins. It contributes to the transduction of
            CD2-generated signals in T cells and natural killer cells and has
            been suggested to play a role in growth regulation. Familial
            deficiency of this gene has been linked to an immunodeficiency
            associated with recurrent infectious diseases caused by bacteria,
            fungi and viruses.
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p13"
     Protein         1..219
                     /product="CD53 antigen"
                     /note="leukocyte surface antigen CD53; antigen MOX44
                     identified by monoclonal antibody MRC-OX44; CD53
                     glycoprotein; cell surface antigen; transmembrane
                     glycoprotein; CD53 tetraspan antigen"
     Region          10..210
                     /region_name="pfam00335, transmembrane4, Tetraspanin
                     family"
     CDS             1..219
                     /gene="CD53"
                     /coded_by="NM_000560.2:116..775"
                     /db_xref="LocusID:963"
                     /db_xref="MIM:151525"
ORIGIN      
        1 mgmsslkllk yvlfffnllf wicgccilgf giyllihnnf gvlfhnlpsl tlgnvfvivg
       61 siimvvaflg cmgsikenkc llmsffilll iillaevtla illfvyeqkl neyvakgltd
      121 sihryhsdns tkaawdsiqs flqccgingt sdwtsgppas cpsdrkvegc yakarlwfhs
      181 nflyigiiti cvcvievlgm sfaltlncqi dktsqtigl
//



Revised: July 5, 2002.
 
 


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1: NP_000868. interleukin 1 rec...[gi:4504659] Links  


LOCUS       IL1R1                    569 aa            linear   PRI 31-OCT-2000
DEFINITION  interleukin 1 receptor, type I [Homo sapiens].
ACCESSION   NP_000868
VERSION     NP_000868.1  GI:4504659
DBSOURCE    REFSEQ: accession NM_000877.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 569)
  AUTHORS   Sims,J.E., Acres,R.B., Grubin,C.E., McMahan,C.J., Wignall,J.M.,
            March,C.J. and Dower,S.K.
  TITLE     Cloning the interleukin 1 receptor from human T cells
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 86 (22), 8946-8950 (1989)
  MEDLINE   90046906
   PUBMED   2530587
REFERENCE   2  (residues 1 to 569)
  AUTHORS   Chua AO and Gubler U.
  TITLE     Sequence of the cDNA for the human fibroblast type interleukin-1
            receptor
  JOURNAL   Nucleic Acids Res. 17 (23), 10114 (1989)
  MEDLINE   90098789
   PUBMED   2532321
REFERENCE   3  (residues 1 to 569)
  AUTHORS   Copeland NG, Silan CM, Kingsley DM, Jenkins NA, Cannizzaro LA,
            Croce CM, Huebner K and Sims JE.
  TITLE     Chromosomal location of murine and human IL-1 receptor genes
  JOURNAL   Genomics 9 (1), 44-50 (1991)
  MEDLINE   91169515
   PUBMED   1672292
REFERENCE   4  (residues 1 to 569)
  AUTHORS   McMahan CJ, Slack JL, Mosley B, Cosman D, Lupton SD, Brunton LL,
            Grubin CE, Wignall JM, Jenkins NA, Brannan CI et al.
  TITLE     A novel IL-1 receptor, cloned from B cells by mammalian expression,
            is expressed in many cell types
  JOURNAL   EMBO J. 10 (10), 2821-2832 (1991)
  MEDLINE   92007725
   PUBMED   1833184
REFERENCE   5  (residues 1 to 569)
  AUTHORS   Dale M and Nicklin MJ.
  TITLE     Interleukin-1 receptor cluster: gene organization of IL1R2, IL1R1,
            IL1RL2 (IL-1Rrp2), IL1RL1 (T1/ST2), and IL18R1 (IL-1Rrp) on human
            chromosome 2q
  JOURNAL   Genomics 57 (1), 177-179 (1999)
  MEDLINE   99208678
   PUBMED   10191101
REFERENCE   6  (residues 1 to 569)
  AUTHORS   Sims,J.E., Grubin,C.E. and McMahan,C.J.
  JOURNAL   Unpublished
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M27492.1.
FEATURES             Location/Qualifiers
     source          1..569
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q12"
     Protein         1..569
                     /product="interleukin 1 receptor, type I"
     sig_peptide     1..17
                     /gene="IL1R1"
     mat_peptide     18..569
                     /gene="IL1R1"
                     /product="interleukin 1 receptor, type I"
     Region          44..101
                     /region_name="Immunoglobulin"
                     /note="IG"
                     /db_xref="CDD:IG"
     Region          151..199
                     /region_name="Immunoglobulin"
                     /note="IG"
                     /db_xref="CDD:IG"
     Region          385..511
                     /region_name="Toll - interleukin 1 - resistance"
                     /note="TIR"
                     /db_xref="CDD:TIR"
     Region          387..540
                     /region_name="TIR domain"
                     /note="TIR"
                     /db_xref="CDD:pfam01582"
     CDS             1..569
                     /gene="IL1R1"
                     /coded_by="NM_000877.1:83..1792"
                     /db_xref="LocusID:3554"
                     /db_xref="MIM:147810"
ORIGIN      
        1 mkvllrlicf iallisslea dkckereeki ilvssaneid vrpcplnpne hkgtitwykd
       61 dsktpvsteq asrihqhkek lwfvpakved sghyycvvrn ssyclrikis akfvenepnl
      121 cynaqaifkq klpvagdggl vcpymeffkn ennelpklqw ykdckpllld nihfsgvkdr
      181 livmnvaekh rgnytchasy tylgkqypit rviefitlee nkptrpvivs panetmevdl
      241 gsqiqlicnv tgqlsdiayw kwngsvided dpvlgedyys venpankrrs tlitvlnise
      301 iesrfykhpf tcfaknthgi daayiqliyp vtnfqkhmig icvtltviiv csvfiykifk
      361 idivlwyrds cydflpikas dgktydayil ypktvgegst sdcdifvfkv lpevlekqcg
      421 yklfiygrdd yvgedivevi nenvkksrrl iiilvretsg fswlggssee qiamynalvq
      481 dgikvvllel ekiqdyekmp esikfikqkh gairwsgdft qgpqsaktrf wknvryhmpv
      541 qrrspsskhq llspatkekl qreahvplg
//



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1: NP_000409. interleukin 4 rec...[gi:4557669] Links  


LOCUS       IL4R                     825 aa            linear   PRI 31-OCT-2000
DEFINITION  interleukin 4 receptor precursor; CD124 [Homo sapiens].
ACCESSION   NP_000409
VERSION     NP_000409.1  GI:4557669
DBSOURCE    REFSEQ: accession NM_000418.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Idzerda,R.L., March,C.J., Mosley,B., Lyman,S.D., Bos,T.V.,
            Gimpel,S.D., Din,W.S., Grabstein,K.H., Widmer,M.B., Park,L.S.,
            Cosman,D. and Beckmann,M.P.
  TITLE     Human interleukin 4 receptor confers biological responsiveness and
            defines a novel receptor superfamily
  JOURNAL   J. Exp. Med. 171 (3), 861-873 (1990)
  MEDLINE   90171849
   PUBMED   2307934
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Pritchard MA, Baker E, Whitmore SA, Sutherland GR, Idzerda RL, Park
            LS, Cosman D, Jenkins NA, Gilbert DJ, Copeland NG et al.
  TITLE     The interleukin-4 receptor gene (IL4R) maps to 16p11.2-16p12.1 in
            human and to the distal region of mouse chromosome 7
  JOURNAL   Genomics 10 (3), 801-806 (1991)
  MEDLINE   91365391
   PUBMED   1679753
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J,
            Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y,
            Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC and
            Adams MD.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
  MEDLINE   99425270
   PUBMED   10493829
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X52425.1.
            Summary:  IL4R when complexed with the common gamma chain (IL2RG)
            serves as the high-affinity interleukin 4 (IL4) receptor.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2-12.1"
                     /cell_type="T cell, tissue=peripheral blood, clone=T22-8"
     Proprotein      1..825
                     /note="CD124"
     sig_peptide     1..25
     mat_peptide     26..825
                     /product="interleukin 4 receptor"
     variation       75
                     /allele="I"
                     /allele="V"
                     /db_xref="dbSNP:3024558"
     Region          123..213
                     /region_name="Fibronectin type III domain"
                     /note="fn3"
                     /db_xref="CDD:pfam00041"
     variation       400
                     /allele="A"
                     /allele="E"
                     /db_xref="dbSNP:1805011"
     variation       431
                     /allele="R"
                     /allele="C"
                     /db_xref="dbSNP:1805012"
     variation       436
                     /allele="S"
                     /allele="L"
                     /db_xref="dbSNP:1805013"
     variation       503
                     /allele="P"
                     /allele="S"
                     /db_xref="dbSNP:1805015"
     variation       576
                     /allele="Q"
                     /allele="R"
                     /db_xref="dbSNP:1801275"
     variation       579
                     /allele="I"
                     /allele="V"
                     /db_xref="dbSNP:3024677"
     variation       675
                     /allele="P"
                     /allele="S"
                     /db_xref="dbSNP:3024678"
     variation       752
                     /allele="A"
                     /allele="S"
                     /db_xref="dbSNP:1805016"
     CDS             1..825
                     /gene="IL4R"
                     /coded_by="NM_000418.1:176..2653"
                     /db_xref="LocusID:3566"
                     /db_xref="MIM:147781"
ORIGIN      
        1 mgwlcsgllf pvsclvllqv assgnmkvlq eptcvsdyms istcewkmng ptncstelrl
       61 lyqlvfllse ahtcipenng gagcvchllm ddvvsadnyt ldlwagqqll wkgsfkpseh
      121 vkprapgnlt vhtnvsdtll ltwsnpyppd nylynhltya vniwsendpa dfriynvtyl
      181 epslriaast lksgisyrar vrawaqcynt twsewspstk whnsyrepfe qhlllgvsvs
      241 civilavcll cyvsitkikk ewwdqipnpa rsrlvaiiiq daqgsqwekr srgqepakcp
      301 hwkncltkll pcflehnmkr dedphkaake mpfqgsgksa wcpveisktv lwpesisvvr
      361 cvelfeapve ceeeeeveee kgsfcaspes srddfqegre givarltesl fldllgeeng
      421 gfcqqdmges cllppsgsts ahmpwdefps agpkeappwg keqplhleps ppasptqspd
      481 nltctetplv iagnpayrsf snslsqspcp relgpdplla rhleevepem pcvpqlsept
      541 tvpqpepetw eqilrrnvlq hgaaaapvsa ptsgyqefvh aveqggtqas avvglgppge
      601 agykafssll assavspekc gfgassgeeg ykpfqdlipg cpgdpapvpv plftfgldre
      661 pprspqsshl pssspehlgl epgekvedmp kpplpqeqat dplvdslgsg ivysaltchl
      721 cghlkqchgq edggqtpvma spccgcccgd rssppttplr apdpspggvp leaslcpasl
      781 apsgiseksk ssssfhpapg naqsssqtpk ivnfvsvgpt ymrvs
//



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1: NP_001242. CD68 antigen; Mac...[gi:4557435] Links  


LOCUS       CD68                     354 aa            linear   PRI 31-OCT-2000
DEFINITION  CD68 antigen; Macrophage antigen CD68 (microsialin) [Homo sapiens].
ACCESSION   NP_001242
VERSION     NP_001242.1  GI:4557435
DBSOURCE    REFSEQ: accession NM_001251.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 354)
  AUTHORS   Holness,C.L. and Simmons,D.L.
  TITLE     Molecular cloning of CD68, a human macrophage marker related to
            lysosomal glycoproteins
  JOURNAL   Blood 81 (6), 1607-1613 (1993)
  MEDLINE   93200523
   PUBMED   7680921
REFERENCE   2  (residues 1 to 354)
  AUTHORS   Jones,E., Quinn,C.M., See,C.G., Montgomery,D.S., Ford,M.J.,
            Kolble,K., Gordon,S. and Greaves,D.R.
  TITLE     The linked human elongation initiation factor 4A1 (EIF4A1) and CD68
            genes map to chromosome 17p13
  JOURNAL   Genomics 53 (2), 248-250 (1998)
  MEDLINE   99009345
   PUBMED   9790779
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from S57235.1.
            Summary: CD68 is a 110-kD transmembrane glycoprotein that is highly
            expressed by human monocytes and tissue macrophages.  It is a type
            I integral membrane protein with a heavily glycosylated
            extracellular domain.
FEATURES             Location/Qualifiers
     source          1..354
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17p13"
                     /cell_line="promonocyte cell line U937"
     Protein         1..354
                     /product="CD68 antigen"
                     /note="Macrophage antigen CD68 (microsialin)"
     Region          85..354
                     /region_name="Lysosome-associated membrane glycoprotein
                     (Lamp)"
                     /note="Lamp"
                     /db_xref="CDD:pfam01299"
     CDS             1..354
                     /gene="CD68"
                     /coded_by="NM_001251.1:16..1080"
                     /db_xref="LocusID:968"
                     /db_xref="MIM:153634"
ORIGIN      
        1 mrlavlfsga llgllaaqgt gndcphkksa tllpsftvtp tvtestgtts hrttkshktt
       61 thrttttgtt shgpttathn ptttshgnvt vhptsnstat sqgpstaths pattshgnat
      121 vhptsnstat spgftssahp eppppspsps ptsketigdy twtngsqpcv hlqaqiqirv
      181 myttqgggea wgisvlnpnk tkvqgscega hphlllsfpy ghlsfgfmqd lqqkvvylsy
      241 maveynvsfp haakwtfsaq naslrdlqap lgqsfscsns siilspavhl dllslrlqaa
      301 qlphtgvfgq sfscpsdrsi llpliiglil lgllalvlia fciirrrpsa yqal
//



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1: NP_000638. chemokine (C-C mo...[gi:4502633] Links  


LOCUS       CCR2                     374 aa            linear   PRI 06-SEP-2001
DEFINITION  chemokine (C-C motif) receptor 2, isoform A; chemokine (C-C)
            receptor 2; monocyte chemoattractant protein 1 receptor; monocyte
            chemotactic protein 1 receptor [Homo sapiens].
ACCESSION   NP_000638
VERSION     NP_000638.1  GI:4502633
DBSOURCE    REFSEQ: accession NM_000647.3
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 374)
  AUTHORS   Charo,I.F., Myers,S.J., Herman,A., Franci,C., Connolly,A.J. and
            Coughlin,S.R.
  TITLE     Molecular cloning and functional expression of two monocyte
            chemoattractant protein 1 receptors reveals alternative splicing of
            the carboxyl-terminal tails
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 91 (7), 2752-2756 (1994)
  MEDLINE   94195821
   PUBMED   8146186
REFERENCE   2  (residues 1 to 374)
  AUTHORS   Yamagami,S., Tokuda,Y., Ishii,K., Tanaka,H. and Endo,N.
  TITLE     cDNA cloning and functional expression of a human monocyte
            chemoattractant protein 1 receptor
  JOURNAL   Biochem. Biophys. Res. Commun. 202 (2), 1156-1162 (1994)
  MEDLINE   94324942
   PUBMED   8048929
REFERENCE   3  (residues 1 to 374)
  AUTHORS   Combadiere,C., Ahuja,S.K., Van Damme,J., Tiffany,H.L., Gao,J.L. and
            Murphy,P.M.
  TITLE     Monocyte chemoattractant protein-3 is a functional ligand for CC
            chemokine receptors 1 and 2B
  JOURNAL   J. Biol. Chem. 270 (50), 29671-29675 (1995)
  MEDLINE   96102011
   PUBMED   8530354
REFERENCE   4  (residues 1 to 374)
  AUTHORS   Samson,M., Soularue,P., Vassart,G. and Parmentier,M.
  TITLE     The genes encoding the human CC-chemokine receptors CC-CKR1 to
            CC-CKR5 (CMKBR1-CMKBR5) are clustered in the p21.3-p24 region of
            chromosome 3
  JOURNAL   Genomics 36 (3), 522-526 (1996)
  MEDLINE   97038695
   PUBMED   8884276
REFERENCE   5  (residues 1 to 374)
  AUTHORS   Wong,L.M., Myers,S.J., Tsou,C.L., Gosling,J., Arai,H. and
            Charo,I.F.
  TITLE     Organization and differential expression of the human monocyte
            chemoattractant protein 1 receptor gene. Evidence for the role of
            the carboxyl-terminal tail in receptor trafficking
  JOURNAL   J. Biol. Chem. 272 (2), 1038-1045 (1997)
  MEDLINE   97150864
   PUBMED   8995400
REFERENCE   6  (residues 1 to 374)
  AUTHORS   Frade,J.M., Mellado,M., del Real,G., Gutierrez-Ramos,J.C., Lind,P.
            and Martinez-A,C.
  TITLE     Characterization of the CCR2 chemokine receptor: functional CCR2
            receptor expression in B cells
  JOURNAL   J. Immunol. 159 (11), 5576-5584 (1997)
  MEDLINE   98208279
   PUBMED   9548499
REFERENCE   7  (residues 1 to 374)
  AUTHORS   Mellado,M., Rodriguez-Frade,J.M., Aragay,A., del Real,G.,
            Martin,A.M., Vila-Coro,A.J., Serrano,A., Mayor,F. Jr. and
            Martinez-A,C.
  TITLE     The chemokine monocyte chemotactic protein 1 triggers Janus kinase
            2 activation and tyrosine phosphorylation of the CCR2B receptor
  JOURNAL   J. Immunol. 161 (2), 805-813 (1998)
  MEDLINE   98334032
   PUBMED   9670957
REFERENCE   8  (residues 1 to 374)
  AUTHORS   McManus,C.M., Weidenheim,K., Woodman,S.E., Nunez,J.,
            Hesselgesser,J., Nath,A. and Berman,J.W.
  TITLE     Chemokine and chemokine-receptor expression in human glial
            elements: induction by the HIV protein, Tat, and chemokine
            autoregulation
  JOURNAL   Am. J. Pathol. 156 (4), 1441-1453 (2000)
  MEDLINE   20216651
   PUBMED   10751368
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U03882.1.
            Summary: This gene encodes two isoforms of a receptor for monocyte
            chemoattractant protein-1, a chemokine which specifically mediates
            monocyte chemotaxis. Monocyte chemoattractant protein-1 is involved
            in monocyte infiltration in inflammatory diseases such as
            rheumatoid arthritis as well as in the inflammatory response
            against tumors. The receptors encoded by this gene mediate
            agonist-dependent calcium mobilization and inhibition of adenylyl
            cyclase. This gene is located in the chemokine receptor gene
            cluster region. Two alternatively spliced transcript variants are
            expressed by the gene.
            Transcript Variant: This variant (A) encodes the cytoplasmic
            isoform. It is alternatively spliced in the coding region resulting
            in a frameshift and use of a downstream stop codon, compared to
            variant B. Isoform A has distinct C-terminus and is 14 amino acids
            longer than isoform B.
FEATURES             Location/Qualifiers
     source          1..374
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21"
     Protein         1..374
                     /product="chemokine (C-C motif) receptor 2, isoform A"
                     /note="isoform A is encoded by transcript variant A;
                     chemokine (C-C) receptor 2; monocyte chemoattractant
                     protein 1 receptor; monocyte chemotactic protein 1
                     receptor"
     variation       64
                     /allele="I"
                     /allele="V"
                     /db_xref="dbSNP:1799864"
     Region          77..305
                     /region_name="7 transmembrane receptor (rhodopsin family)"
                     /note="7tm_1"
                     /db_xref="CDD:pfam00001"
     CDS             1..374
                     /gene="CCR2"
                     /coded_by="NM_000647.3:81..1205"
                     /db_xref="LocusID:1231"
                     /db_xref="MIM:601267"
ORIGIN      
        1 mlstsrsrfi rntnesgeev ttffdydyga pchkfdvkqi gaqllpplys lvfifgfvgn
       61 mlvvlilinc kklkcltdiy llnlaisdll flitlplwah saanewvfgn amcklftgly
      121 higyfggiff iilltidryl aivhavfalk artvtfgvvt svitwlvavf asvpgiiftk
      181 cqkedsvyvc gpyfprgwnn fhtimrnilg lvlpllimvi cysgilktll rcrnekkrhr
      241 avrviftimi vyflfwtpyn ivillntfqe ffglsncest sqldqatqvt etlgmthcci
      301 npiiyafvge kfrslfhial gcriaplqkp vcggpgvrpg knvkvttqgl ldgrgkgksi
      361 grapeaslqd kega
//



Revised: July 5, 2002.
 
 


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1: NP_055025. ecotropic viral i...[gi:7657075] Links  


LOCUS       EVI2A                    232 aa            linear   PRI 25-JUL-2002
DEFINITION  ecotropic viral integration site 2A [Homo sapiens].
ACCESSION   NP_055025
VERSION     NP_055025.1  GI:7657075
DBSOURCE    REFSEQ: accession NM_014210.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 232)
  AUTHORS   Wallace,M.R., Marchuk,D.A., Andersen,L.B., Letcher,R., Odeh,H.M.,
            Saulino,A.M., Fountain,J.W., Brereton,A., Nicholson,J.,
            Mitchell,A.L. et al.
  TITLE     Type 1 neurofibromatosis gene: identification of a large transcript
            disrupted in three NF1 patients
  JOURNAL   Science 249 (4965), 181-186 (1990)
  MEDLINE   90319792
   PUBMED   2134734
REFERENCE   2  (residues 1 to 232)
  AUTHORS   O'Connell,P., Viskochil,D., Buchberg,A.M., Fountain,J.,
            Cawthon,R.M., Culver,M., Stevens,J., Rich,D.C., Ledbetter,D.H.,
            Wallace,M. et al.
  TITLE     The human homolog of murine Evi-2 lies between two von
            Recklinghausen neurofibromatosis translocations
  JOURNAL   Genomics 7 (4), 547-554 (1990)
  MEDLINE   90353952
   PUBMED   2117565
REFERENCE   3  (residues 1 to 232)
  AUTHORS   Cawthon,R.M., O'Connell,P., Buchberg,A.M., Viskochil,D.,
            Weiss,R.B., Culver,M., Stevens,J., Jenkins,N.A., Copeland,N.G. and
            White,R.
  TITLE     Identification and characterization of transcripts from the
            neurofibromatosis 1 region: the sequence and genomic structure of
            EVI2 and mapping of other transcripts
  JOURNAL   Genomics 7 (4), 555-565 (1990)
  MEDLINE   90353953
   PUBMED   2117566
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M55267.1.
FEATURES             Location/Qualifiers
     source          1..232
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
                     /cell_type="lymphoblast"
     Protein         1..232
                     /product="ecotropic viral integration site 2A"
     sig_peptide     <1..26
                     /gene="EVI2A"
                     /note="G00-125-191"
     mat_peptide     27..>232
                     /gene="EVI2A"
                     /product="ecotropic viral integration site 2A"
                     /note="G00-125-191"
     CDS             1..232
                     /gene="EVI2A"
                     /coded_by="NM_014210.1:220..918"
                     /db_xref="LocusID:2123"
                     /db_xref="MIM:158380"
ORIGIN      
        1 mehtghylhl aflmttvfsl spgtkanytr lwanstsswd sviqnktgrn qnenintnpi
       61 tpevdykgns tnmpetshiv altskseqel yipsvvsnsp stvqsients kshgeifkkd
      121 vcaennnnma mlicliiiav lflictflfl stvvlankvs slrrskqvgk rqprsngdfl
      181 asglwpaesd twkrtkqltg pnlvmqstgv ltatrerkde egtekltnkq ig
//



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1: NP_000582. CD14 antigen prec...[gi:4557417] Links  


LOCUS       CD14                     375 aa            linear   PRI 27-AUG-2002
DEFINITION  CD14 antigen precursor [Homo sapiens].
ACCESSION   NP_000582
VERSION     NP_000582.1  GI:4557417
DBSOURCE    REFSEQ: accession NM_000591.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 375)
  AUTHORS   Ferrero,E. and Goyert,S.M.
  TITLE     Nucleotide sequence of the gene encoding the monocyte
            differentiation antigen, CD14
  JOURNAL   Nucleic Acids Res. 16 (9), 4173 (1988)
  MEDLINE   88234022
   PUBMED   2453848
REFERENCE   2  (residues 1 to 375)
  AUTHORS   Simmons,D.L., Tan,S., Tenen,D.G., Nicholson-Weller,A. and Seed,B.
  TITLE     Monocyte antigen CD14 is a phospholipid anchored membrane protein
  JOURNAL   Blood 73 (1), 284-289 (1989)
  MEDLINE   89088540
   PUBMED   2462937
REFERENCE   3  (residues 1 to 375)
  AUTHORS   Setoguchi,M., Nasu,N., Yoshida,S., Higuchi,Y., Akizuki,S. and
            Yamamoto,S.
  TITLE     Mouse and human CD14 (myeloid cell-specific leucine-rich
            glycoprotein) primary structure deduced from cDNA clones
  JOURNAL   Biochim. Biophys. Acta 1008 (2), 213-222 (1989)
  MEDLINE   89287330
   PUBMED   2472171
REFERENCE   4  (residues 1 to 375)
  AUTHORS   Gupta,D., Kirkland,T.N., Viriyakosol,S. and Dziarski,R.
  TITLE     CD14 is a cell-activating receptor for bacterial peptidoglycan
  JOURNAL   J. Biol. Chem. 271 (38), 23310-23316 (1996)
  MEDLINE   96394425
   PUBMED   8798531
REFERENCE   5  (residues 1 to 375)
  AUTHORS   Devitt,A., Moffatt,O.D., Raykundalia,C., Capra,J.D., Simmons,D.L.
            and Gregory,C.D.
  TITLE     Human CD14 mediates recognition and phagocytosis of apoptotic cells
  JOURNAL   Nature 392 (6675), 505-509 (1998)
  MEDLINE   98208033
   PUBMED   9548256
REFERENCE   6  (residues 1 to 375)
  AUTHORS   Mahlknecht,U., Bucala,R., Hoelzer,D. and Verdin,E.
  TITLE     High resolution physical mapping of human HDAC3, a potential tumor
            suppressor gene in the 5q31 region
  JOURNAL   Cytogenet. Cell Genet. 86 (3-4), 237-239 (1999)
  MEDLINE   20044614
   PUBMED   10575214
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X13334.1.
            Summary: CD14 is a surface protein preferentially expressed on
            monocytes/macrophages.  It binds lipopolysaccharide binding protein
            and recently has been shown to bind apoptotic cells.
FEATURES             Location/Qualifiers
     source          1..375
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31.1"
     Protein         1..375
                     /product="CD14 antigen precursor"
     sig_peptide     1..19
     mat_peptide     20..375
                     /product="CD14 antigen, mature peptide"
     CDS             1..375
                     /gene="CD14"
                     /coded_by="NM_000591.1:120..1247"
                     /db_xref="LocusID:929"
                     /db_xref="MIM:158120"
ORIGIN      
        1 merascllll llplvhvsat tpepceldde dfrcvcnfse pqpdwseafq cvsaveveih
       61 agglnlepfl krvdadadpr qyadtvkalr vrrltvgaaq vpaqllvgal rvlaysrlke
      121 ltledlkitg tmpplpleat glalsslrlr nvswatgrsw laelqqwlkp glkvlsiaqa
      181 hspafsceqv rafpaltsld lsdnpglger glmaalcphk fpaiqnlalr ntgmetptgv
      241 caalaaagvq phsldlshns lratvnpsap rcmwssalns lnlsfagleq vpkglpaklr
      301 vldlscnrln rapqpdelpe vdnltldgnp flvpgtalph egsmnsgvvp acarstlsvg
      361 vsgtlvllqg argfa
//



Revised: July 5, 2002.
 
 


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1: NP_000409. interleukin 4 rec...[gi:4557669] Links  


LOCUS       IL4R                     825 aa            linear   PRI 31-OCT-2000
DEFINITION  interleukin 4 receptor precursor; CD124 [Homo sapiens].
ACCESSION   NP_000409
VERSION     NP_000409.1  GI:4557669
DBSOURCE    REFSEQ: accession NM_000418.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 825)
  AUTHORS   Idzerda,R.L., March,C.J., Mosley,B., Lyman,S.D., Bos,T.V.,
            Gimpel,S.D., Din,W.S., Grabstein,K.H., Widmer,M.B., Park,L.S.,
            Cosman,D. and Beckmann,M.P.
  TITLE     Human interleukin 4 receptor confers biological responsiveness and
            defines a novel receptor superfamily
  JOURNAL   J. Exp. Med. 171 (3), 861-873 (1990)
  MEDLINE   90171849
   PUBMED   2307934
REFERENCE   2  (residues 1 to 825)
  AUTHORS   Pritchard MA, Baker E, Whitmore SA, Sutherland GR, Idzerda RL, Park
            LS, Cosman D, Jenkins NA, Gilbert DJ, Copeland NG et al.
  TITLE     The interleukin-4 receptor gene (IL4R) maps to 16p11.2-16p12.1 in
            human and to the distal region of mouse chromosome 7
  JOURNAL   Genomics 10 (3), 801-806 (1991)
  MEDLINE   91365391
   PUBMED   1679753
REFERENCE   3  (residues 1 to 825)
  AUTHORS   Loftus BJ, Kim UJ, Sneddon VP, Kalush F, Brandon R, Fuhrmann J,
            Mason T, Crosby ML, Barnstead M, Cronin L, Deslattes Mays A, Cao Y,
            Xu RX, Kang HL, Mitchell S, Eichler EE, Harris PC, Venter JC and
            Adams MD.
  TITLE     Genome duplications and other features in 12 Mb of DNA sequence
            from human chromosome 16p and 16q
  JOURNAL   Genomics 60 (3), 295-308 (1999)
  MEDLINE   99425270
   PUBMED   10493829
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X52425.1.
            Summary:  IL4R when complexed with the common gamma chain (IL2RG)
            serves as the high-affinity interleukin 4 (IL4) receptor.
FEATURES             Location/Qualifiers
     source          1..825
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p11.2-12.1"
                     /cell_type="T cell, tissue=peripheral blood, clone=T22-8"
     Proprotein      1..825
                     /note="CD124"
     sig_peptide     1..25
     mat_peptide     26..825
                     /product="interleukin 4 receptor"
     variation       75
                     /allele="I"
                     /allele="V"
                     /db_xref="dbSNP:3024558"
     Region          123..213
                     /region_name="Fibronectin type III domain"
                     /note="fn3"
                     /db_xref="CDD:pfam00041"
     variation       400
                     /allele="A"
                     /allele="E"
                     /db_xref="dbSNP:1805011"
     variation       431
                     /allele="R"
                     /allele="C"
                     /db_xref="dbSNP:1805012"
     variation       436
                     /allele="S"
                     /allele="L"
                     /db_xref="dbSNP:1805013"
     variation       503
                     /allele="P"
                     /allele="S"
                     /db_xref="dbSNP:1805015"
     variation       576
                     /allele="Q"
                     /allele="R"
                     /db_xref="dbSNP:1801275"
     variation       579
                     /allele="I"
                     /allele="V"
                     /db_xref="dbSNP:3024677"
     variation       675
                     /allele="P"
                     /allele="S"
                     /db_xref="dbSNP:3024678"
     variation       752
                     /allele="A"
                     /allele="S"
                     /db_xref="dbSNP:1805016"
     CDS             1..825
                     /gene="IL4R"
                     /coded_by="NM_000418.1:176..2653"
                     /db_xref="LocusID:3566"
                     /db_xref="MIM:147781"
ORIGIN      
        1 mgwlcsgllf pvsclvllqv assgnmkvlq eptcvsdyms istcewkmng ptncstelrl
       61 lyqlvfllse ahtcipenng gagcvchllm ddvvsadnyt ldlwagqqll wkgsfkpseh
      121 vkprapgnlt vhtnvsdtll ltwsnpyppd nylynhltya vniwsendpa dfriynvtyl
      181 epslriaast lksgisyrar vrawaqcynt twsewspstk whnsyrepfe qhlllgvsvs
      241 civilavcll cyvsitkikk ewwdqipnpa rsrlvaiiiq daqgsqwekr srgqepakcp
      301 hwkncltkll pcflehnmkr dedphkaake mpfqgsgksa wcpveisktv lwpesisvvr
      361 cvelfeapve ceeeeeveee kgsfcaspes srddfqegre givarltesl fldllgeeng
      421 gfcqqdmges cllppsgsts ahmpwdefps agpkeappwg keqplhleps ppasptqspd
      481 nltctetplv iagnpayrsf snslsqspcp relgpdplla rhleevepem pcvpqlsept
      541 tvpqpepetw eqilrrnvlq hgaaaapvsa ptsgyqefvh aveqggtqas avvglgppge
      601 agykafssll assavspekc gfgassgeeg ykpfqdlipg cpgdpapvpv plftfgldre
      661 pprspqsshl pssspehlgl epgekvedmp kpplpqeqat dplvdslgsg ivysaltchl
      721 cghlkqchgq edggqtpvma spccgcccgd rssppttplr apdpspggvp leaslcpasl
      781 apsgiseksk ssssfhpapg naqsssqtpk ivnfvsvgpt ymrvs
//



Revised: July 5, 2002.
 
 


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1: NP_000202. integrin beta cha...[gi:4557886] Links  


LOCUS       ITGB2                    769 aa            linear   PRI 31-OCT-2000
DEFINITION  integrin beta chain, beta 2 precursor; cell surface adhesion
            glycoprotein (LFA-1/CR3/P150,959 beta subunit precursor); Integrin,
            beta-2 (antigen CD18 (p95), lymphocyte function-associated [Homo
            sapiens].
ACCESSION   NP_000202
VERSION     NP_000202.1  GI:4557886
DBSOURCE    REFSEQ: accession NM_000211.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 769)
  AUTHORS   Kishimoto,T.K., O'Connor,K., Lee,A., Roberts,T.M. and Springer,T.A.
  TITLE     Cloning of the beta subunit of the leukocyte adhesion proteins:
            homology to an extracellular matrix receptor defines a novel
            supergene family
  JOURNAL   Cell 48 (4), 681-690 (1987)
  MEDLINE   87131080
   PUBMED   3028646
REFERENCE   2  (residues 1 to 769)
  AUTHORS   Law SK, Gagnon J, Hildreth JE, Wells CE, Willis AC and Wong AJ.
  TITLE     The primary structure of the beta-subunit of the cell surface
            adhesion glycoproteins LFA-1, CR3 and p150,95 and its relationship
            to the fibronectin receptor
  JOURNAL   EMBO J. 6 (4), 915-919 (1987)
  MEDLINE   87246525
   PUBMED   2954816
REFERENCE   3  (residues 1 to 769)
  AUTHORS   Solomon,E., Palmer,R.W., Hing,S. and Law,S.K.
  TITLE     Regional localization of CD18, the beta-subunit of the cell surface
            adhesion molecule LFA-1, on human chromosome 21 by in situ
            hybridization
  JOURNAL   Ann. Hum. Genet. 52 (Pt 2), 123-128 (1988)
  MEDLINE   89245796
   PUBMED   3073708
REFERENCE   4  (residues 1 to 769)
  AUTHORS   Weitzman JB, Wells CE, Wright AH, Clark PA and Law SK.
  TITLE     The gene organisation of the human beta 2 integrin subunit (CD18)
  JOURNAL   FEBS Lett. 294 (1-2), 97-103 (1991)
  MEDLINE   92077153
   PUBMED   1683838
REFERENCE   5  (residues 1 to 769)
  AUTHORS   Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS,
            Toyoda A, Ishii K, Totoki Y, Choi DK, Soeda E, Ohki M, Takagi T,
            Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J,
            Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M
            and Schudy A.
  TITLE     The DNA sequence of human chromosome 21. The chromosome 21 mapping
            and sequencing consortium
  JOURNAL   Nature 405 (6784), 311-319 (2000)
  MEDLINE   20289799
   PUBMED   10830953
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M15395.1.
            Summary: The ITGB2 protein product is the integrin beta chain beta
            2. Integrins are integral cell-surface proteins composed of an
            alpha chain and a beta chain.  A given chain may combine with
            multiple partners resulting in different integrins.  For example,
            beta 2 combines with the alpha L chain to form the integrin LFA-1,
            and combines with the alpha M chain to form the integrin Mac-1.
            Integrins are known to participate in cell adhesion as well as
            cell-surface mediated signalling.
FEATURES             Location/Qualifiers
     source          1..769
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..769
                     /product="integrin beta chain, beta 2 precursor"
                     /note="cell surface adhesion glycoprotein
                     (LFA-1/CR3/P150,959 beta subunit precursor); Integrin,
                     beta-2 (antigen CD18 (p95), lymphocyte
                     function-associated"
     sig_peptide     1..22
     mat_peptide     23..769
                     /product="integrin beta chain, beta 2"
     Region          32..447
                     /region_name="Integrin beta subunits (N-terminal portion
                     of extracellular region)"
                     /note="INB"
                     /db_xref="CDD:INB"
     Region          32..447
                     /region_name="Integrins"
                     /note="integrin_B"
                     /db_xref="CDD:pfam00362"
     CDS             1..769
                     /gene="ITGB2"
                     /coded_by="NM_000211.1:73..2382"
                     /db_xref="LocusID:3689"
                     /db_xref="MIM:600065"
ORIGIN      
        1 mlglrpplla lvgllslgcv lsqectkfkv sscreciesg pgctwcqkln ftgpgdpdsi
       61 rcdtrpqllm rgcaaddimd ptslaetqed hnggqkqlsp qkvtlylrpg qaaafnvtfr
      121 rakgypidly ylmdlsysml ddlrnvkklg gdllralnei tesgrigfgs fvdktvlpfv
      181 nthpdklrnp cpnkekecqp pfafrhvlkl tnnsnqfqte vgkqlisgnl dapeggldam
      241 mqvaacpeei gwrnvtrllv fatddgfhfa gdgklgailt pndgrchled nlykrsnefd
      301 ypsvgqlahk laenniqpif avtsrmvkty eklteiipks avgelsedss nvvhliknay
      361 nklssrvfld hnalpdtlkv tydsfcsngv thrnqprgdc dgvqinvpit fqvkvtatec
      421 iqeqsfvira lgftdivtvq vlpqcecrcr dqsrdrslch gkgflecgic rcdtgyigkn
      481 cecqtqgrss qelegscrkd nnsiicsglg dcvcgqclch tsdvpgkliy gqycecdtin
      541 ceryngqvcg gpgrglcfcg kcrchpgfeg sacqcertte gclnprrvec sgrgrcrcnv
      601 cechsgyqlp lcqecpgcps pcgkyiscae clkfekgpfg kncsaacpgl qlsnnpvkgr
      661 tckerdsegc wvaytleqqd gmdryliyvd esrecvagpn iaaivggtva givligilll
      721 viwkalihls dlreyrrfek eklksqwnnd nplfksattt vmnpkfaes
//



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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_077294. immunoglobulin-li...[gi:13324690] Links  


LOCUS       ILT8                     464 aa            linear   PRI 14-MAR-2001
DEFINITION  immunoglobulin-like transcript 8 [Homo sapiens].
ACCESSION   NP_077294
VERSION     NP_077294.1  GI:13324690
DBSOURCE    REFSEQ: accession NM_024318.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Wende H, Volz A and Ziegler A.
  TITLE     Extensive gene duplications and a large inversion characterize the
            human leukocyte receptor cluster
  JOURNAL   Immunogenetics 51 (8-9), 703-713 (2000)
  MEDLINE   20395290
   PUBMED   10941842
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Colonna,M.
  TITLE     Immunoglobulin-like transcript 8
  JOURNAL   Unpublished
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF041262.1.
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.4"
                     /clone="3"
                     /cell_type="leukocyte"
     Protein         1..464
                     /product="immunoglobulin-like transcript 8"
                     /function="activating receptor"
     CDS             1..464
                     /gene="ILT8"
                     /coded_by="NM_024318.1:1..1395"
                     /db_xref="LocusID:79168"
ORIGIN      
        1 mtpiltvlic lglslgprth vqagpfpkpt lwaepgsvis wgspvtiwcq gsleaqeyrl
       61 dkegspepwd rnnplepknk arfsipsite hhagryrchy yssagwseps dalelvmtga
      121 yskptlsalp spvvasggnm tlqcgsqkgy hqfvlmkege hqlprtldsq qlhsggfqal
      181 fpvgpvnpsh rwrftcyyyy mntprvwshp sdpleilpsg vsrkpslltl qgpvlapgqs
      241 ltlqcgsdvg ydrfvlykeg erdflqrpgq qpqaglsqan ftlgpvspsh ggqyrcygah
      301 nlssewsaps dplnilmagq iydtvslsaq pgptvasgen vtllcqswwq fdtflltkeg
      361 aahpplrlrs mygahkyqae fpmspvtsah agtyrcygsy ssnphllsfp seplelmvsa
      421 shakdytven lirmgmaglv lvflgillfe aqhsqrnpqd aarr
//



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1: NP_001805. cathepsin C isofo...[gi:4503141] Links  


LOCUS       CTSC                     463 aa            linear   PRI 29-AUG-2002
DEFINITION  cathepsin C isoform a preproprotein; dipeptidyl-peptidase I;
            dipeptidyl transferase; cathepsin J [Homo sapiens].
ACCESSION   NP_001805
VERSION     NP_001805.1  GI:4503141
DBSOURCE    REFSEQ: accession NM_001814.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Paris,A., Strukelj,B., Pungercar,J., Renko,M., Dolenc,I. and
            Turk,V.
  TITLE     Molecular cloning and sequence analysis of human preprocathepsin C
  JOURNAL   FEBS Lett. 369 (2-3), 326-330 (1995)
  MEDLINE   95377428
   PUBMED   7649281
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Rao,N.V., Rao,G.V. and Hoidal,J.R.
  TITLE     Human dipeptidyl-peptidase I. Gene characterization, localization,
            and expression
  JOURNAL   J. Biol. Chem. 272 (15), 10260-10265 (1997)
  MEDLINE   97248590
   PUBMED   9092576
REFERENCE   3  (residues 1 to 463)
  AUTHORS   Fischer,J., Blanchet-Bardon,C., Prud'homme,J.F., Pavek,S.,
            Steijlen,P.M., Dubertret,L. and Weissenbach,J.
  TITLE     Mapping of Papillon-Lefevre syndrome to the chromosome 11q14 region
  JOURNAL   Eur. J. Hum. Genet. 5 (3), 156-160 (1997)
  MEDLINE   97417366
   PUBMED   9272739
REFERENCE   4  (residues 1 to 463)
  AUTHORS   Suzuki,Y., Ishihara,D., Sasaki,M., Nakagawa,H., Hata,H.,
            Tsunoda,T., Watanabe,M., Komatsu,T., Ota,T., Isogai,T., Suyama,A.
            and Sugano,S.
  TITLE     Statistical analysis of the 5' untranslated region of human mRNA
            using 'Oligo-Capped' cDNA libraries
  JOURNAL   Genomics 64 (3), 286-297 (2000)
  MEDLINE   20221373
   PUBMED   10756096
REFERENCE   5  (residues 1 to 463)
  AUTHORS   Allende,L.M., Garcia-Perez,M.A., Moreno,A., Corell,A., Carasol,M.,
            Martinez-Canut,P. and Arnaiz-Villena,A.
  TITLE     Cathepsin C gene: First compound heterozygous patient with
            Papillon-Lefevre syndrome and a novel symptomless mutation
  JOURNAL   Hum. Mutat. 17 (2), 152-153 (2001)
  MEDLINE   21113227
   PUBMED   11180601
REFERENCE   6  (residues 1 to 463)
  AUTHORS   Turk,D., Janjic,V., Stern,I., Podobnik,M., Lamba,D., Dahl,S.W.,
            Lauritzen,C., Pedersen,J., Turk,V. and Turk,B.
  TITLE     Structure of human dipeptidyl peptidase I (cathepsin C): exclusion
            domain added to an endopeptidase framework creates the machine for
            activation of granular serine proteases
  JOURNAL   EMBO J. 20 (23), 6570-6582 (2001)
  MEDLINE   21583324
   PUBMED   11726493
REFERENCE   7  (residues 1 to 463)
  AUTHORS   Matsui,K., Yuyama,N., Akaiwa,M., Yoshida,N.L., Maeda,M., Sugita,Y.
            and Izuhara,K.
  TITLE     Identification of an alternative splicing variant of cathepsin
            C/dipeptidyl-peptidase I
  JOURNAL   Gene 293 (1-2), 1-7 (2002)
  MEDLINE   22133301
   PUBMED   12137938
REFERENCE   8  (residues 1 to 463)
  AUTHORS   Tran,T.V., Ellis,K.A., Kam,C.M., Hudig,D. and Powers,J.C.
  TITLE     Dipeptidyl peptidase I: importance of progranzyme activation
            sequences, other dipeptide sequences, and the N-terminal amino
            group of synthetic substrates for enzyme activity
  JOURNAL   Arch. Biochem. Biophys. 403 (2), 160-170 (2002)
  MEDLINE   22135248
   PUBMED   12139965
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X87212.1 and AU076460.1.
            Summary: The protein encoded by this gene, a member of the
            peptidase C1 family, is a lysosomal cysteine proteinase that
            appears to be a central coordinator for activation of many serine
            proteinases in immune/inflammatory cells. It is composed of a dimer
            of disulfide-linked heavy and light chains, both produced from a
            single protein precursor. It requires chloride ions for activity
            and can degrade glucagon. Defects in the encoded protein have been
            shown to be a cause of Papillon-Lefevre syndrome, an autosomal
            recessive disorder characterized by palmoplantar keratosis and
            periodontitis. Two transcript variants encoding different isoforms
            have been found for this gene.
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (a).
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q14.1-q14.3"
     Protein         1..463
                     /product="cathepsin C isoform a preproprotein"
                     /EC_number="3.4.14.1"
                     /note="isoform a is encoded by transcript variant 1;
                     dipeptidyl-peptidase I; dipeptidyl transferase; cathepsin
                     J"
     sig_peptide     1..24
     Proprotein      25..463
     Region          231..458
                     /region_name="pfam00112, Peptidase_C1, Papain family
                     cysteine protease"
     Region          231..456
                     /region_name="smart00645, Pept_C1, Papain family cysteine
                     protease"
     mat_peptide     231..394
                     /product="cathepsin C light chain"
     mat_peptide     395..463
                     /product="cathepsin C heavy chain"
     Region          402..439
                     /region_name="pfam03051, Pept_C1-like, Peptidase C1-like
                     family. This family is closely related to the Peptidase_C1
                     family pfam00112, containing several prokaryotic and
                     eukaryotic aminopeptidases and bleomycin hydrolases"
     CDS             1..463
                     /gene="CTSC"
                     /coded_by="NM_001814.2:99..1490"
                     /db_xref="LocusID:1075"
                     /db_xref="MIM:602365"
ORIGIN      
        1 mgagpsllla alllllsgdg avrcdtpanc tyldllgtwv fqvgssgsqr dvncsvmgpq
       61 ekkvvvylqk ldtayddlgn sghftiiynq gfeivlndyk wfaffkykee gskvttycne
      121 tmtgwvhdvl grnwacftgk kvgtasenvy vntahlknsq ekysnrlyky dhnfvkaina
      181 iqkswtatty meyetltlgd mirrsgghsr kiprpkpapl taeiqqkilh lptswdwrnv
      241 hginfvspvr nqascgscys fasmgmlear iriltnnsqt pilspqevvs csqyaqgceg
      301 gfpyliagky aqdfglveea cfpytgtdsp ckmkedcfry ysseyhyvgg fyggcnealm
      361 klelvhhgpm avafevyddf lhykkgiyhh tglrdpfnpf eltnhavllv gygtdsasgm
      421 dywivknswg tgwgengyfr irrgtdecai esiavaatpi pkl
//



Revised: July 5, 2002.
 
 


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1: NP_005979. small proline-ric...[gi:5174693] Links  


LOCUS       SPRR2A                    72 aa            linear   PRI 01-NOV-2000
DEFINITION  small proline-rich protein 2A [Homo sapiens].
ACCESSION   NP_005979
VERSION     NP_005979.1  GI:5174693
DBSOURCE    REFSEQ: accession NM_005988.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 72)
  AUTHORS   Gibbs,S., Lohman,F., Teubel,W., van de Putte,P. and Backendorf,C.
  TITLE     Characterization of the human spr2 promoter: induction after UV
            irradiation or TPA treatment and regulation during differentiation
            of cultured primary keratinocytes
  JOURNAL   Nucleic Acids Res. 18 (15), 4401-4407 (1990)
  MEDLINE   90356372
   PUBMED   2388825
REFERENCE   2  (residues 1 to 72)
  AUTHORS   Gibbs,S., Fijneman,R., Wiegant,J., van Kessel,A.G., van De Putte,P.
            and Backendorf,C.
  TITLE     Molecular characterization and evolution of the SPRR family of
            keratinocyte differentiation markers encoding small proline-rich
            proteins
  JOURNAL   Genomics 16 (3), 630-637 (1993)
  MEDLINE   93315153
   PUBMED   8325635
REFERENCE   3  (residues 1 to 72)
  AUTHORS   Fischer,D.F., Gibbs,S., van De Putte,P. and Backendorf,C.
  TITLE     Interdependent transcription control elements regulate the
            expression of the SPRR2A gene during keratinocyte terminal
            differentiation
  JOURNAL   Mol. Cell. Biol. 16 (10), 5365-5374 (1996)
  MEDLINE   96413286
   PUBMED   8816448
REFERENCE   4  (residues 1 to 72)
  AUTHORS   Fischer,D.F., van Drunen,C.M., Winkler,G.S., van de Putte,P. and
            Backendorf,C.
  TITLE     Involvement of a nuclear matrix association region in the
            regulation of the SPRR2A keratinocyte terminal differentiation
            marker
  JOURNAL   Nucleic Acids Res. 26 (23), 5288-5294 (1998)
  MEDLINE   99045591
   PUBMED   9826750
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X53064.1.
FEATURES             Location/Qualifiers
     source          1..72
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21-q22"
                     /tissue_type="blood"
                     /clone_lib="EMBL3"
     Protein         1..72
                     /product="small proline-rich protein 2A"
     CDS             1..72
                     /gene="SPRR2A"
                     /coded_by="NM_005988.1:1..219"
                     /note="cornified envelope precursor; contains 3 internal
                     nonapeptide repeats; head and tail domains are substrates
                     for transglutaminase-mediated cross-linking"
                     /db_xref="LocusID:6700"
                     /db_xref="MIM:182267"
ORIGIN      
        1 msyqqqqckq pcqpppvcpt pkcpepcppp kcpepcpppk cpqpcppqqc qqkyppvtps
       61 ppcqskyppk sk
//



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1: NP_000401. hemochromatosis p...[gi:4504377] Links  


LOCUS       HFE                      348 aa            linear   PRI 21-MAY-2002
DEFINITION  hemochromatosis protein isoform 1 precursor; hereditary
            haemochromatosis protein [Homo sapiens].
ACCESSION   NP_000401
VERSION     NP_000401.1  GI:4504377
DBSOURCE    REFSEQ: accession NM_000410.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 348)
  AUTHORS   Edwards,C.Q., Griffen,L.M., Dadone,M.M., Skolnick,M.H. and
            Kushner,J.P.
  TITLE     Mapping the locus for hereditary hemochromatosis: localization
            between HLA-B and HLA-A
  JOURNAL   Am. J. Hum. Genet. 38 (6), 805-811 (1986)
  MEDLINE   86265593
   PUBMED   3460331
REFERENCE   2  (residues 1 to 348)
  AUTHORS   Geraghty,D.E., Koller,B.H., Pei,J. and Hansen,J.A.
  TITLE     Examination of four HLA class I pseudogenes. Common events in the
            evolution of HLA genes and pseudogenes
  JOURNAL   J. Immunol. 149 (6), 1947-1956 (1992)
  MEDLINE   92388662
   PUBMED   1517564
REFERENCE   3  (residues 1 to 348)
  AUTHORS   Feder,J.N., Gnirke,A., Thomas,W., Tsuchihashi,Z., Ruddy,D.A.,
            Basava,A., Dormishian,F., Domingo,R. Jr., Ellis,M.C., Fullan,A.,
            Hinton,L.M., Jones,N.L., Kimmel,B.E., Kronmal,G.S., Lauer,P.,
            Lee,V.K., Loeb,D.B., Mapa,F.A., McClelland,E., Meyer,N.C.,
            Mintier,G.A., Moeller,N., Moore,T., Morikang,E., Prass,C.E.,
            Quintana,L., Starnes,S.M., Schatzman,R.C., Brunke,K.J.,
            Drayna,D.T., Risch,N.J., Bacon,B.R. and Wolff,R.K.
  TITLE     A novel MHC class I-like gene is mutated in patients with
            hereditary haemochromatosis
  JOURNAL   Nat. Genet. 13 (4), 399-408 (1996)
  MEDLINE   96331279
   PUBMED   8696333
REFERENCE   4  (residues 1 to 348)
  AUTHORS   Albig,W., Drabent,B., Burmester,N., Bode,C. and Doenecke,D.
  TITLE     The haemochromatosis candidate gene HFE (HLA-H) of man and mouse is
            located in syntenic regions within the histone gene cluster
  JOURNAL   J. Cell. Biochem. 69 (2), 117-126 (1998)
  MEDLINE   98208340
   PUBMED   9548560
REFERENCE   5  (residues 1 to 348)
  AUTHORS   Roy,C.N., Penny,D.M., Feder,J.N. and Enns,C.A.
  TITLE     The hereditary hemochromatosis protein, HFE, specifically regulates
            transferrin-mediated iron uptake in HeLa cells
  JOURNAL   J. Biol. Chem. 274 (13), 9022-9028 (1999)
  MEDLINE   99185134
   PUBMED   10085150
REFERENCE   6  (residues 1 to 348)
  AUTHORS   Rhodes,D.A. and Trowsdale,J.
  TITLE     Alternate splice variants of the hemochromatosis gene Hfe
  JOURNAL   Immunogenetics 49 (4), 357-359 (1999)
  MEDLINE   99180629
   PUBMED   10079302
REFERENCE   7  (residues 1 to 348)
  AUTHORS   Bennett,M.J., Lebron,J.A. and Bjorkman,P.J.
  TITLE     Crystal structure of the hereditary haemochromatosis protein HFE
            complexed with transferrin receptor
  JOURNAL   Nature 403 (6765), 46-53 (2000)
  MEDLINE   20102284
   PUBMED   10638746
REFERENCE   8  (residues 1 to 348)
  AUTHORS   Thenie,A., Orhant,M., Gicquel,I., Fergelot,P., Le Gall,J.Y.,
            David,V. and Mosser,J.
  TITLE     The HFE gene undergoes alternate splicing processes
  JOURNAL   Blood Cells Mol. Dis. 26 (2), 155-162 (2000)
  MEDLINE   20448010
   PUBMED   11001625
REFERENCE   9  (residues 1 to 348)
  AUTHORS   Sanchez,M., Bruguera,M., Rodes,J. and Oliva,R.
  TITLE     Complete characterization of the 3' region of the human and mouse
            hereditary hemochromatosis HFE gene and detection of novel splicing
            forms
  JOURNAL   Blood Cells Mol. Dis. 27 (1), 35-43 (2001)
  MEDLINE   21257661
   PUBMED   11358357
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U60319.1.
            Summary: The protein encoded by this gene is a membrane protein
            that is similar to MHC class I-type proteins and associates with
            beta2-microglobulin (beta2M). It is thought that this protein
            functions to regulate iron absorption by regulating the interaction
            of the transferrin receptor with transferrin. The iron storage
            disorder, hereditary haemochromatosis, is a recessive genetic
            disorder that results from defects in this gene. At least eleven
            alternatively spliced variants have been described for this gene.
            Additional variants have been found but their full length nature
            has not been determined.
            Transcript Variant: This variant (1) encodes the longest isoform.
FEATURES             Location/Qualifiers
     source          1..348
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.3"
     Protein         1..348
                     /product="hemochromatosis protein isoform 1 precursor"
                     /note="isoform 1 is encoded by transcript variant 1;
                     hereditary haemochromatosis protein"
     sig_peptide     1..22
     mat_peptide     23..348
                     /product="hemochromatosis protein isoform 1"
     Region          27..202
                     /region_name="Class I Histocompatibility antigen, domains
                     alpha 1 and 2"
                     /note="MHC_I"
                     /db_xref="CDD:pfam00129"
     variation       35
                     /allele="T"
                     /allele="M"
                     /db_xref="dbSNP:2242956"
     variation       63
                     /allele="H"
                     /allele="D"
                     /db_xref="dbSNP:1799945"
     Region          223..292
                     /region_name="Immunoglobulin C-Type"
                     /note="IGc1"
                     /db_xref="CDD:smart00407"
     Region          223..284
                     /region_name="Immunoglobulin domain"
                     /note="ig"
                     /db_xref="CDD:pfam00047"
     CDS             1..348
                     /gene="HFE"
                     /coded_by="NM_000410.2:222..1268"
                     /db_xref="LocusID:3077"
                     /db_xref="MIM:235200"
ORIGIN      
        1 mgprarpall llmllqtavl qgrllrshsl hylfmgaseq dlglslfeal gyvddqlfvf
       61 ydhesrrvep rtpwvssris sqmwlqlsqs lkgwdhmftv dfwtimenhn hskeshtlqv
      121 ilgcemqedn stegywkygy dgqdhlefcp dtldwraaep rawptklewe rhkirarqnr
      181 aylerdcpaq lqqllelgrg vldqqvpplv kvthhvtssv ttlrcralny ypqnitmkwl
      241 kdkqpmdake fepkdvlpng dgtyqgwitl avppgeeqry tcqvehpgld qpliviweps
      301 psgtlvigvi sgiavfvvil figilfiilr krqgsrgamg hyvlaere
//



Revised: July 5, 2002.
 
 


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1: NP_057193. angiopoietin-like...[gi:21536396] Links  


LOCUS       ANGPTL4                  406 aa            linear   PRI 21-JUN-2002
DEFINITION  angiopoietin-like 4 protein; hepatic angiopoietin-related protein;
            PPARG angiopoietin related protein; fasting-induced adipose factor;
            hepatic fibrinogen/angiopoietin-related protein [Homo sapiens].
ACCESSION   NP_057193
VERSION     NP_057193.2  GI:21536396
DBSOURCE    REFSEQ: accession NM_016109.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Kim,I., Kim,H.G., Kim,H., Kim,H.H., Park,S.K., Uhm,C.S., Lee,Z.H.
            and Koh,G.Y.
  TITLE     Hepatic expression, synthesis and secretion of a novel
            fibrinogen/angiopoietin-related protein that prevents
            endothelial-cell apoptosis
  JOURNAL   Biochem. J. 346 Pt 3, 603-610 (2000)
  MEDLINE   20164042
   PUBMED   10698685
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Yoon,J.C., Chickering,T.W., Rosen,E.D., Dussault,B., Qin,Y.,
            Soukas,A., Friedman,J.M., Holmes,W.E. and Spiegelman,B.M.
  TITLE     Peroxisome proliferator-activated receptor gamma target gene
            encoding a novel angiopoietin-related protein associated with
            adipose differentiation
  JOURNAL   Mol. Cell. Biol. 20 (14), 5343-5349 (2000)
  MEDLINE   20325357
   PUBMED   10866690
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Zhu,H., Li,J., Qin,W., Yang,Y., He,X., Wan,D. and Gu,J.
  TITLE     Cloning of a novel gene, ANGPTL4 and the functional study in
            angiogenesis
  JOURNAL   Chung-Hua I Hsueh Tsa Chih 82 (2), 94-99 (2002)
  MEDLINE   21951180
   PUBMED   11953136
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF153606.1, BG424907.1 and
            AF202636.1.
            On Jun 21, 2002 this sequence version replaced gi:7705829.
            Summary: Peroxisome proliferator-activated receptor gamma is a
            nuclear receptor which regulates adipose differentiation and
            glucose homeostasis. It acts through ligand-dependent
            transcriptional activation of target genes. This gene is one of the
            targets of peroxisome proliferator-activated receptor gamma and
            encodes an angiopoietin-like secreted glycoprotein. This gene also
            has been referred to as ANGPTL2, although a different gene exists
            with that same designation. Two transcript variants encoding the
            same protein have been found for this gene.
            Transcript Variant: This variant (2) differs only in the 3' UTR as
            compared to variant 1.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..406
                     /product="angiopoietin-like 4 protein"
                     /note="hepatic angiopoietin-related protein; PPARG
                     angiopoietin related protein; fasting-induced adipose
                     factor; hepatic fibrinogen/angiopoietin-related protein"
     Region          184..400
                     /region_name="smart00186, FBG, Fibrinogen-related domains
                     (FReDs); Domain present at the C-termini of fibrinogen
                     beta and gamma chains, and a variety of fibrinogen-related
                     proteins, including tenascin and Drosophila scabrous"
     Region          185..399
                     /region_name="pfam00147, fibrinogen_C, Fibrinogen beta and
                     gamma chains, C-terminal globular domain"
     CDS             1..406
                     /gene="ANGPTL4"
                     /coded_by="NM_016109.2:196..1416"
                     /db_xref="LocusID:51129"
                     /db_xref="MIM:605910"
ORIGIN      
        1 msgaptagaa lmlcaatavl lsaqggpvqs ksprfaswde mnvlahgllq lgqglrehae
       61 rtrsqlsale rrlsacgsac qgtegstdlp lapesrvdpe vlhslqtqlk aqnsriqqlf
      121 hkvaqqqrhl ekqhlriqhl qsqfglldhk hldhevakpa rrkrlpemaq pvdpahnvsr
      181 lhrlprdcqe lfqvgerqsg lfeiqpqgsp pflvnckmts dggwtviqrr hdgsvdfnrp
      241 weaykagfgd phgefwlgle kvhsitgdrn srlavqlrdw dgnaellqfs vhlggedtay
      301 slqltapvag qlgattvpps glsvpfstwd qdhdlrrdkn cakslsggww fgtcshsnln
      361 gqyfrsipqq rqklkkgifw ktwrgryypl qattmliqpm aaeaas
//



Revised: July 5, 2002.
 
 


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1: NP_002308. lysyl oxidase pre...[gi:20149540] Links  


LOCUS       LOX                      417 aa            linear   PRI 27-AUG-2002
DEFINITION  lysyl oxidase preproprotein; protein-lysine 6-oxidase [Homo
            sapiens].
ACCESSION   NP_002308
VERSION     NP_002308.2  GI:20149540
DBSOURCE    REFSEQ: accession NM_002317.3
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 417)
  AUTHORS   Kuivaniemi,H., Savolainen,E.R. and Kivirikko,K.I.
  TITLE     Human placental lysyl oxidase. Purification, partial
            characterization, and preparation of two specific antisera to the
            enzyme
  JOURNAL   J. Biol. Chem. 259 (11), 6996-7002 (1984)
  MEDLINE   84212548
   PUBMED   6144680
REFERENCE   2  (residues 1 to 417)
  AUTHORS   Hamalainen,E.R., Jones,T.A., Sheer,D., Taskinen,K., Pihlajaniemi,T.
            and Kivirikko,K.I.
  TITLE     Molecular cloning of human lysyl oxidase and assignment of the gene
            to chromosome 5q23.3-31.2
  JOURNAL   Genomics 11 (3), 508-516 (1991)
  MEDLINE   92128932
   PUBMED   1685472
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Mariani,T.J., Trackman,P.C., Kagan,H.M., Eddy,R.L., Shows,T.B.,
            Boyd,C.D. and Deak,S.B.
  TITLE     The complete derived amino acid sequence of human lysyl oxidase and
            assignment of the gene to chromosome 5 (extensive sequence homology
            with the murine ras recision gene)
  JOURNAL   Matrix 12 (3), 242-248 (1992)
  MEDLINE   93024096
   PUBMED   1357535
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Svinarich,D.M., Twomey,T.A., Macauley,S.P., Krebs,C.J., Yang,T.P.
            and Krawetz,S.A.
  TITLE     Characterization of the human lysyl oxidase gene locus
  JOURNAL   J. Biol. Chem. 267 (20), 14382-14387 (1992)
  MEDLINE   92332554
   PUBMED   1352776
REFERENCE   5  (residues 1 to 417)
  AUTHORS   Csiszar,K., Mariani,T.J., Gosin,J.S., Deak,S.B. and Boyd,C.D.
  TITLE     A restriction fragment length polymorphism results in a
            nonconservative amino acid substitution encoded within the first
            exon of the human lysyl oxidase gene
  JOURNAL   Genomics 16 (2), 401-406 (1993)
  MEDLINE   93300514
   PUBMED   8100215
REFERENCE   6  (residues 1 to 417)
  AUTHORS   Hamalainen,E.R., Kemppainen,R., Pihlajaniemi,T. and Kivirikko,K.I.
  TITLE     Structure of the human lysyl oxidase gene
  JOURNAL   Genomics 17 (3), 544-548 (1993)
  MEDLINE   94063892
   PUBMED   7902322
REFERENCE   7  (residues 1 to 417)
  AUTHORS   Contente,S., Kenyon,K., Sriraman,P., Subramanyan,S. and
            Friedman,R.M.
  TITLE     Epigenetic inhibition of lysyl oxidase transcription after
            transformation by ras oncogene
  JOURNAL   Mol. Cell. Biochem. 194 (1-2), 79-91 (1999)
  MEDLINE   99318011
   PUBMED   10391127
REFERENCE   8  (residues 1 to 417)
  AUTHORS   Martins,R.P., Ujfalusi,A.A., Csiszar,K. and Krawetz,S.A.
  TITLE     Characterization of the region encompassing the human lysyl oxidase
            locus
  JOURNAL   DNA Seq. 12 (4), 215-227 (2001)
  MEDLINE   21913078
   PUBMED   11916256
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF039291.1 and AF039290.1.
            On Apr 15, 2002 this sequence version replaced gi:4505009.
            Summary: The protein encoded by this gene is an extracellular
            copper enzyme that initiates the crosslinking of collagens and
            elastin. The enzyme catalyzes oxidative deamination of the
            epsilon-amino group in certain lysine and hydroxylysine residues of
            collagens and lysine residues of elastin. In addition to
            crosslinking extracellular matrix proteins, the encoded protein may
            have a role in tumor suppression.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.2"
     Protein         1..417
                     /product="lysyl oxidase preproprotein"
                     /EC_number="1.4.3.13"
                     /note="protein-lysine 6-oxidase"
     sig_peptide     1..21
     Proprotein      22..417
     variation       137
                     /allele="P"
                     /allele="A"
                     /db_xref="dbSNP:2914604"
     variation       158
                     /allele="Q"
                     /allele="R"
                     /db_xref="dbSNP:1800449"
     mat_peptide     169..417
                     /product="lysyl oxidase"
     Region          213..417
                     /region_name="pfam01186, Lysyl_oxidase, Lysyl oxidase"
     variation       273
                     /allele="E"
                     /allele="G"
                     /db_xref="dbSNP:2434980"
     CDS             1..417
                     /gene="LOX"
                     /coded_by="NM_002317.3:274..1527"
                     /db_xref="LocusID:4015"
                     /db_xref="MIM:153455"
ORIGIN      
        1 mrfawtvlll gplqlcalvh cappaagqqq ppreppaapg awrqqiqwen ngqvfsllsl
       61 gsqyqpqrrr dpgaavpgaa nasaqqprtp illirdnrta aartrtagss gvtagrprpt
      121 arhwfqagys tsrareagas raenqtapge vpalsnlrpp srvdgmvgdd pynpykysdd
      181 npyynyydty erprpggryr pgygtgyfqy glpdlvadpy yiqastyvqk msmynlrcaa
      241 eenclastay radvrdydhr vllrfpqrvk nqgtsdflps rpryswewhs chqhyhsmde
      301 fshydlldan tqrrvaeghk asfcledtsc dygyhrrfac tahtqglspg cydtygadid
      361 cqwiditdvk pgnyilkvsv npsylvpesd ytnnvvrcdi rytghhayas gctispy
//



Revised: July 5, 2002.
 
 


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1: NP_000519. mannosidase, alph...[gi:10834968] Links  


LOCUS       MAN2B1                  1010 aa            linear   PRI 18-AUG-2002
DEFINITION  mannosidase, alpha, class 2B, member 1; mannosidase, alpha B,
            lysosomal [Homo sapiens].
ACCESSION   NP_000519
VERSION     NP_000519.1  GI:10834968
DBSOURCE    REFSEQ: accession NM_000528.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1010)
  AUTHORS   Nebes,V.L. and Schmidt,M.C.
  TITLE     Human lysosomal alpha-mannosidase: isolation and nucleotide
            sequence of the full-length cDNA
  JOURNAL   Biochem. Biophys. Res. Commun. 200 (1), 239-245 (1994)
  MEDLINE   94220092
   PUBMED   8166692
REFERENCE   2  (residues 1 to 1010)
  AUTHORS   Emiliani,C., Martino,S., Stirling,J.L., Maras,B. and Orlacchio,A.
  TITLE     Partial sequence of the purified protein confirms the identity of
            cDNA coding for human lysosomal alpha-mannosidase B
  JOURNAL   Biochem. J. 305 (Pt 2), 363-366 (1995)
  MEDLINE   95134211
   PUBMED   7832746
REFERENCE   3  (residues 1 to 1010)
  AUTHORS   Liao,Y.F., Lal,A. and Moremen,K.W.
  TITLE     Cloning, expression, purification, and characterization of the
            human broad specificity lysosomal acid alpha-mannosidase
  JOURNAL   J. Biol. Chem. 271 (45), 28348-28358 (1996)
  MEDLINE   97067056
   PUBMED   8910458
REFERENCE   4  (residues 1 to 1010)
  AUTHORS   Nilssen,O., Berg,T., Riise,H.M., Ramachandran,U., Evjen,G.,
            Hansen,G.M., Malm,D., Tranebjaerg,L. and Tollersrud,O.K.
  TITLE     alpha-Mannosidosis: functional cloning of the lysosomal
            alpha-mannosidase cDNA and identification of a mutation in two
            affected siblings
  JOURNAL   Hum. Mol. Genet. 6 (5), 717-726 (1997)
  MEDLINE   97301768
   PUBMED   9158146
REFERENCE   5  (residues 1 to 1010)
  AUTHORS   Riise,H.M., Berg,T., Nilssen,O., Romeo,G., Tollersrud,O.K. and
            Ceccherini,I.
  TITLE     Genomic structure of the human lysosomal alpha-mannosidase gene
            (MANB)
  JOURNAL   Genomics 42 (2), 200-207 (1997)
  MEDLINE   97336044
   PUBMED   9192839
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U60899.1.
FEATURES             Location/Qualifiers
     source          1..1010
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19cen-q13.1"
     Protein         1..1010
                     /product="mannosidase, alpha, class 2B, member 1"
                     /note="mannosidase, alpha B, lysosomal"
     Region          51..637
                     /region_name="pfam01074, Glyco_hydro_38, Glycosyl
                     hydrolases family 38. Glycosyl hydrolases are key enzymes
                     of carbohydrate metabolism"
     CDS             1..1010
                     /gene="MAN2B1"
                     /coded_by="NM_000528.1:310..3342"
                     /db_xref="LocusID:4125"
                     /db_xref="MIM:248500"
ORIGIN      
        1 mgyarasgvc argcldsagp wtmsralrpp lpplcfflll laaagaragg yetcptvqpn
       61 mlnvhllpht hddvgwlktv dqyfygiknd iqhagvqyil dsvisallad ptrrfiyvei
      121 affsrwwhqq tnatqevvrd lvrqgrlefa nggwvmndea athygaivdq mtlglrfled
      181 tfgndgrprv awhidpfghs reqaslfaqm gfdgfffgrl dyqdkwvrmq klemeqvwra
      241 stslkpptad lftgvlpngy npprnlcwdv lcvdqplved prspeynake lvdyflnvat
      301 aqgryyrtnh tvmtmgsdfq yenanmwfkn ldklirlvna qqakgssvhv lystpacylw
      361 elnkanltws vkhddffpya dgphqfwtgy fssrpalkry erlsynflqv cnqlealvgl
      421 aanvgpygsg dsaplneama vlqhhdavsg tsrqhvandy arqlaagwgp cevllsnala
      481 rlrgfkdhft fcqqlnisic plsqtaarfq vivynplgrk vnwmvrlpvs egvfvvkdpn
      541 grtvpsdvvi fpssdsqahp pellfsaslp algfstysva qvprwkpqar apqpiprrsw
      601 spaltieneh iratfdpdtg llmeimnmnq qlllpvrqtf fwynasigdn esdqasgayi
      661 frpnqqkplp vsrwaqihlv ktplvqevhq nfsawcsqvv rlypgqrhle lewsvgpipv
      721 gdtwgkevis rfdtpletkg rfytdsngre ilerrrdyrp twklnqtepv agnyypvntr
      781 iyitdgnmql tvltdrsqgg sslrdgslel mvhrrllkdd grgvseplme ngsgawvrgr
      841 hlvlldtaqa aaaghrllae qevlapqvvl apgggaaynl gapprtqfsg lrrdlppsvh
      901 lltlaswgpe mvllrlehqf avgedsgrnl sapvtlnlrd lfstftitrl qettlvanql
      961 reaasrlkwt tntgptphqt pyqldpanit lepmeirtfl asvqwkevdg 
//



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1: NP_002829. protein tyrosine ...[gi:18641347] Links  


LOCUS       PTPRC                   1304 aa            linear   PRI 08-FEB-2002
DEFINITION  protein tyrosine phosphatase, receptor type, C, isoform 1
            precursor; protein tyrosine phosphatase, receptor type, c
            polypeptide; leukocyte-common antigen; T200 glycoprotein; human
            homolog of severe combined immunodeficiency due to PTPRC
            deficiency; SCID due to PTPRC deficiency; CD45 antigen [Homo
            sapiens].
ACCESSION   NP_002829
VERSION     NP_002829.2  GI:18641347
DBSOURCE    REFSEQ: accession NM_002838.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1304)
  AUTHORS   Ralph,S.J., Thomas,M.L., Morton,C.C. and Trowbridge,I.S.
  TITLE     Structural variants of human T200 glycoprotein (leukocyte-common
            antigen)
  JOURNAL   EMBO J. 6 (5), 1251-1257 (1987)
  MEDLINE   87275816
   PUBMED   2956090
REFERENCE   2  (residues 1 to 1304)
  AUTHORS   Streuli,M., Hall,L.R., Saga,Y., Schlossman,S.F. and Saito,H.
  TITLE     Differential usage of three exons generates at least five different
            mRNAs encoding human leukocyte common antigens
  JOURNAL   J. Exp. Med. 166 (5), 1548-1566 (1987)
  MEDLINE   88061067
   PUBMED   2824653
REFERENCE   3  (residues 1 to 1304)
  AUTHORS   Charbonneau,H., Tonks,N.K., Walsh,K.A. and Fischer,E.H.
  TITLE     The leukocyte common antigen (CD45): a putative receptor-linked
            protein tyrosine phosphatase
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 85 (19), 7182-7186 (1988)
  MEDLINE   89017162
   PUBMED   2845400
REFERENCE   4  (residues 1 to 1304)
  AUTHORS   Pingel,J.T. and Thomas,M.L.
  TITLE     Evidence that the leukocyte-common antigen is required for
            antigen-induced T lymphocyte proliferation
  JOURNAL   Cell 58 (6), 1055-1065 (1989)
  MEDLINE   89376557
   PUBMED   2550143
REFERENCE   5  (residues 1 to 1304)
  AUTHORS   Schraven,B., Samstag,Y., Altevogt,P. and Meuer,S.C.
  TITLE     Association of CD2 and CD45 on human T lymphocytes
  JOURNAL   Nature 345 (6270), 71-74 (1990)
  MEDLINE   90231464
   PUBMED   1970422
REFERENCE   6  (residues 1 to 1304)
  AUTHORS   Kaplan,R., Morse,B., Huebner,K., Croce,C., Howk,R., Ravera,M.,
            Ricca,G., Jaye,M. and Schlessinger,J.
  TITLE     Cloning of three human tyrosine phosphatases reveals a multigene
            family of receptor-linked protein-tyrosine-phosphatases expressed
            in brain
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (18), 7000-7004 (1990)
  MEDLINE   90384936
   PUBMED   2169617
REFERENCE   7  (residues 1 to 1304)
  AUTHORS   Petricoin,E.F. III, Ito,S., Williams,B.L., Audet,S., Stancato,L.F.,
            Gamero,A., Clouse,K., Grimley,P., Weiss,A., Beeler,J.,
            Finbloom,D.S., Shores,E.W., Abraham,R. and Larner,A.C.
  TITLE     Antiproliferative action of interferon-alpha requires components of
            T-cell-receptor signalling
  JOURNAL   Nature 390 (6660), 629-632 (1997)
  MEDLINE   98065953
   PUBMED   9403695
REFERENCE   8  (residues 1 to 1304)
  AUTHORS   Goff,L.K., van Soest,S., Timon,M., Tchilian,E. and Beverley,P.C.
  TITLE     Protein tyrosine phosphatase receptor type C polypeptide (PTPRC) on
            human chromosome band 1q31-->q32 localizes with marker D1S413(1) on
            a 610-kb yeast artificial chromosome
  JOURNAL   Cytogenet. Cell Genet. 87 (3-4), 223-224 (1999)
  MEDLINE   20169194
   PUBMED   10702677
REFERENCE   9  (residues 1 to 1304)
  AUTHORS   Irie-Sasaki,J., Sasaki,T., Matsumoto,W., Opavsky,A., Cheng,M.,
            Welstead,G., Griffiths,E., Krawczyk,C., Richardson,C.D., Aitken,K.,
            Iscove,N., Koretzky,G., Johnson,P., Liu,P., Rothstein,D.M. and
            Penninger,J.M.
  TITLE     CD45 is a JAK phosphatase and negatively regulates cytokine
            receptor signalling
  JOURNAL   Nature 409 (6818), 349-354 (2001)
  MEDLINE   21069057
   PUBMED   11201744
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Y00638.1 and Y00062.1.
            On Feb 8, 2002 this sequence version replaced gi:4506307.
            Summary: The protein encoded by this gene is a member of the
            protein tyrosine phosphatase (PTP) family. PTPs are known to be
            signaling molecules that regulate a variety of cellular processes
            including cell growth, differentiation, mitotic cycle, and
            oncogenic transformation. This PTP contains an extracellular
            domain, a single transmembrane segment and two tandem
            intracytoplasmic catalytic domains, and thus belongs to receptor
            type PTP. This gene is specifically expressed in hematopoietic
            cells. This PTP has been shown to be an essential regulator of T-
            and B-cell antigen receptor signaling. It functions through either
            direct interaction with components of the antigen receptor
            complexes, or by activating various Src family kinases required for
            the antigen receptor signaling. This PTP also suppresses JAK
            kinases, and thus functions as a regulator of cytokine receptor
            signaling. Four alternatively spliced transcripts variants of this
            gene, which encode distinct isoforms, have been reported.
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
FEATURES             Location/Qualifiers
     source          1..1304
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q31-q32"
     Protein         1..1304
                     /product="protein tyrosine phosphatase, receptor type, C,
                     isoform 1 precursor"
                     /EC_number="3.1.3.48"
                     /note="isoform 1 is encoded by transcript variant 1;
                     protein tyrosine phosphatase, receptor type, c
                     polypeptide; leukocyte-common antigen; T200 glycoprotein;
                     human homolog of severe combined immunodeficiency due to
                     PTPRC deficiency; SCID due to PTPRC deficiency; CD45
                     antigen"
     sig_peptide     1..23
     mat_peptide     24..1304
                     /product="protein tyrosine phosphatase, receptor type, C"
     Region          390..460
                     /region_name="Fibronectin type 3 domain"
                     /note="FN3"
                     /db_xref="CDD:smart00060"
     Region          390..460
                     /region_name="Fibronectin type III domain"
                     /note="fn3"
                     /db_xref="CDD:pfam00041"
     Region          483..563
                     /region_name="Fibronectin type III domain"
                     /note="fn3"
                     /db_xref="CDD:pfam00041"
     Region          483..558
                     /region_name="Fibronectin type 3 domain"
                     /note="FN3"
                     /db_xref="CDD:smart00060"
     Region          651..910
                     /region_name="Protein tyrosine phosphatase, catalytic
                     domain"
                     /note="PTPc"
                     /db_xref="CDD:smart00194"
     Region          675..909
                     /region_name="Protein-tyrosine phosphatase"
                     /note="Y_phosphatase"
                     /db_xref="CDD:pfam00102"
     Region          808..909
                     /region_name="Protein tyrosine phosphatase, catalytic
                     domain motif"
                     /note="PTPc_motif"
                     /db_xref="CDD:smart00404"
     Region          942..1224
                     /region_name="Protein tyrosine phosphatase, catalytic
                     domain"
                     /note="PTPc"
                     /db_xref="CDD:smart00194"
     Region          966..1224
                     /region_name="Protein-tyrosine phosphatase"
                     /note="Y_phosphatase"
                     /db_xref="CDD:pfam00102"
     Region          1114..1225
                     /region_name="Protein tyrosine phosphatase, catalytic
                     domain motif"
                     /note="PTPc_motif"
                     /db_xref="CDD:smart00404"
     CDS             1..1304
                     /gene="PTPRC"
                     /coded_by="NM_002838.2:93..4007"
                     /db_xref="MIM:151460"
                     /db_xref="LocusID:5788"
ORIGIN      
        1 mylwlkllaf gfafldtevf vtgqsptpsp tglttakmps vplssdplpt httafspast
       61 ferendfset ttslspdnts tqvspdsldn asafnttgvs svqtphlpth adsqtpsagt
      121 dtqtfsgsaa naklnptpgs naisdvpger stastfptdp vspltttlsl ahhssaalpa
      181 rtsnttitan tsdaylnase tttlspsgsa vistttiatt pskptcdeky anitvdylyn
      241 ketklftakl nvnenvecgn ntctnnevhn ltecknasvs ishnsctapd ktlildvppg
      301 vekfqlhdct qvekadttic lkwknietft cdtqnityrf qcgnmifdnk eiklenlepe
      361 heykcdseil ynnhkftnas kiiktdfgsp gepqiifcrs eaahqgvitw nppqrsfhnf
      421 tlcyiketek dclnldknli kydlqnlkpy tkyvlslhay iiakvqrngs aamchfttks
      481 appsqvwnmt vsmtsdnsmh vkcrpprdrn gpheryhlev eagntlvrne shkncdfrvk
      541 dlqystdytf kayfhngdyp gepfilhhst synskaliaf lafliivtsi allvvlykiy
      601 dlhkkrscnl deqqelverd dekqlmnvep ihadillety krkiadegrl flaefqsipr
      661 vfskfpikea rkpfnqnknr yvdilpydyn rvelseingd agsnyinasy idgfkeprky
      721 iaaqgprdet vddfwrmiwe qkatvivmvt rceegnrnkc aeywpsmeeg trafgdvvvk
      781 inqhkrcpdy iiqklnivnk kekatgrevt hiqftswpdh gvpedphlll klrrrvnafs
      841 nffsgpivvh csagvgrtgt yigidamleg leaenkvdvy gyvvklrrqr clmvqveaqy
      901 ilihqalvey nqfgetevnl selhpylhnm kkrdppseps pleaefqrlp syrswrtqhi
      961 gnqeenkskn rnsnvipydy nrvplkhele mskesehdsd essdddsdse epskyinasf
     1021 imsywkpevm iaaqgplket igdfwqmifq rkvkvivmlt elkhgdqeic aqywgegkqt
     1081 ygdievdlkd tdksstytlr vfelrhskrk dsrtvyqyqy tnwsveqlpa epkelismiq
     1141 vvkqklpqkn ssegnkhhks tpllihcrdg sqqtgifcal lnllesaete evvdifqvvk
     1201 alrkarpgmv stfeqyqfly dviastypaq ngqvkknnhq edkiefdnev dkvkqdancv
     1261 nplgapeklp eakeqaegse ptsgtegpeh svngpaspal nqgs
//



Revised: July 5, 2002.
 
 


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1: NP_001157. baculoviral IAP r...[gi:4502141] Links  


LOCUS       BIRC2                    618 aa            linear   PRI 31-OCT-2000
DEFINITION  baculoviral IAP repeat-containing protein 2; cIAP1; hiap-2;
            apoptosis inhibitor 1; NFR2-TRAF signalling complex protein [Homo
            sapiens].
ACCESSION   NP_001157
VERSION     NP_001157.1  GI:4502141
DBSOURCE    REFSEQ: accession NM_001166.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 618)
  AUTHORS   Rothe,M., Pan,M.G., Henzel,W.J., Ayres,T.M. and Goeddel,D.V.
  TITLE     The TNFR2-TRAF signaling complex contains two novel proteins
            related to baculoviral inhibitor of apoptosis proteins
  JOURNAL   Cell 83 (7), 1243-1252 (1995)
  MEDLINE   96128127
   PUBMED   8548810
REFERENCE   2  (residues 1 to 618)
  AUTHORS   Liston P, Roy N, Tamai K, Lefebvre C, Baird S, Cherton-Horvat G,
            Farahani R, McLean M, Ikeda JE, MacKenzie A and Korneluk RG.
  TITLE     Suppression of apoptosis in mammalian cells by NAIP and a related
            family of IAP genes
  JOURNAL   Nature 379 (6563), 349-353 (1996)
  MEDLINE   96149249
   PUBMED   8552191
REFERENCE   3  (residues 1 to 618)
  AUTHORS   Uren,A.G., Pakusch,M., Hawkins,C.J., Puls,K.L. and Vaux,D.L.
  TITLE     Cloning and expression of apoptosis inhibitory protein homologs
            that function to inhibit apoptosis and/or bind tumor necrosis
            factor receptor-associated factors
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 93 (10), 4974-4978 (1996)
  MEDLINE   96209843
   PUBMED   8643514
REFERENCE   4  (residues 1 to 618)
  AUTHORS   Rajcan-Separovic,E., Liston,P., Lefebvre,C. and Korneluk,R.G.
  TITLE     Assignment of human inhibitor of apoptosis protein (IAP) genes
            xiap, hiap-1, and hiap-2 to chromosomes Xq25 and 11q22-q23 by
            fluorescence in situ hybridization
  JOURNAL   Genomics 37 (3), 404-406 (1996)
  MEDLINE   97092895
   PUBMED   8938457
REFERENCE   5  (residues 1 to 618)
  AUTHORS   Young,S.S., Liston,P., Xuan,J.Y., McRoberts,C., Lefebvre,C.A. and
            Korneluk,R.G.
  TITLE     Genomic organization and physical map of the human inhibitors of
            apoptosis: HIAP1 and HIAP2
  JOURNAL   Mamm. Genome 10 (1), 44-48 (1999)
  MEDLINE   99111393
   PUBMED   9892732
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L49431.1 and U37547.1.
            Summary: The protein encoded by this gene is a member of a family
            of proteins that inhibits apoptosis by binding to tumor necrosis
            factor receptor-associated factors TRAF1 and TRAF2, probably by
            interfering with activation of ICE-like proteases. BIRC2 inhibits
            apoptosis induced by serum deprivation and menadione, a potent
            inducer of free radicals. The amino acid sequence predicts three
            baculovirus IAP repeat domains and a ring finger domain.
FEATURES             Location/Qualifiers
     source          1..618
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22"
     Protein         1..618
                     /product="baculoviral IAP repeat-containing protein 2"
                     /note="cIAP1; hiap-2; apoptosis inhibitor 1; NFR2-TRAF
                     signalling complex protein"
     Region          44..115
                     /region_name="Baculoviral inhibition of apoptosis protein
                     repeat"
                     /note="BIR"
                     /db_xref="CDD:BIR"
     Region          49..114
                     /region_name="Inhibitor of Apoptosis domain"
                     /note="BIR"
                     /db_xref="CDD:pfam00653"
     Region          49..113
                     /region_name="Zn binding domain involved in protein
                     protein interactions in caspase inhibition and spindle
                     assembly"
                     /note="BIR"
                     /db_xref="CDD:LOAD:bir"
     Region          182..252
                     /region_name="Baculoviral inhibition of apoptosis protein
                     repeat"
                     /note="BIR"
                     /db_xref="CDD:BIR"
     Region          187..250
                     /region_name="Inhibitor of Apoptosis domain"
                     /note="BIR"
                     /db_xref="CDD:pfam00653"
     Region          187..250
                     /region_name="Zn binding domain involved in protein
                     protein interactions in caspase inhibition and spindle
                     assembly"
                     /note="BIR"
                     /db_xref="CDD:LOAD:bir"
     Region          267..336
                     /region_name="Baculoviral inhibition of apoptosis protein
                     repeat"
                     /note="BIR"
                     /db_xref="CDD:BIR"
     Region          272..336
                     /region_name="Inhibitor of Apoptosis domain"
                     /note="BIR"
                     /db_xref="CDD:pfam00653"
     Region          272..336
                     /region_name="Zn binding domain involved in protein
                     protein interactions in caspase inhibition and spindle
                     assembly"
                     /note="BIR"
                     /db_xref="CDD:LOAD:bir"
     Region          455..543
                     /region_name="Caspase recruitment domain"
                     /note="CARD"
                     /db_xref="CDD:pfam00619"
     Region          455..541
                     /region_name="Caspase recruitment domain"
                     /note="CARD"
                     /db_xref="CDD:CARD"
     CDS             1..618
                     /gene="BIRC2"
                     /coded_by="NM_001166.2:1160..3016"
                     /db_xref="LocusID:329"
                     /db_xref="MIM:601712"
ORIGIN      
        1 mhktasqrlf pgpsyqniks imedstilsd wtnsnkqkmk ydfscelyrm stystfpagv
       61 pvserslara gfyytgvndk vkcfccglml dnwklgdspi qkhkqlypsc sfiqnlvsas
      121 lgstskntsp mrnsfahsls ptlehsslfs gsysslspnp lnsravedis ssrtnpysya
      181 msteearflt yhmwpltfls pselaragfy yigpgdrvac facggklsnw epkddamseh
      241 rrhfpncpfl ensletlrfs isnlsmqtha armrtfmywp ssvpvqpeql asagfyyvgr
      301 nddvkcfccd gglrcwesgd dpwvehakwf prceflirmk gqefvdeiqg ryphlleqll
      361 stsdttgeen adppiihfgp gesssedavm mntpvvksal emgfnrdlvk qtvqskiltt
      421 genyktvndi vsallnaede kreeekekqa eemasddlsl irknrmalfq qltcvlpild
      481 nllkanvink qehdiikqkt qiplqareli dtilvkgnaa anifknclke idstlyknlf
      541 vdknmkyipt edvsglslee qlrrlqeert ckvcmdkevs vvfipcghlv vcqecapslr
      601 kcpicrgiik gtvrtfls
//



Revised: July 5, 2002.
 
 


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1: NP_000492. elastin [Homo sap...[gi:5881413] Links  


LOCUS       ELN                      757 aa            linear   PRI 27-AUG-2002
DEFINITION  elastin [Homo sapiens].
ACCESSION   NP_000492
VERSION     NP_000492.1  GI:5881413
DBSOURCE    REFSEQ: accession NM_000501.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Indik,Z., Yoon,K., Morrow,S.D., Cicila,G., Rosenbloom,J.,
            Rosenbloom,J. and Ornstein-Goldstein,N.
  TITLE     Structure of the 3' region of the human elastin gene: great
            abundance of Alu repetitive sequences and few coding sequences
  JOURNAL   Connect. Tissue Res. 16 (3), 197-211 (1987)
  MEDLINE   87274906
   PUBMED   3038460
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Indik,Z., Yeh,H., Ornstein-Goldstein,N., Sheppard,P., Anderson,N.,
            Rosenbloom,J.C., Peltonen,L. and Rosenbloom,J.
  TITLE     Alternative splicing of human elastin mRNA indicated by sequence
            analysis of cloned genomic and complementary DNA
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 84 (16), 5680-5684 (1987)
  MEDLINE   87289668
   PUBMED   3039501
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Fazio,M.J., Olsen,D.R., Kuivaniemi,H., Chu,M.L., Davidson,J.M.,
            Rosenbloom,J. and Uitto,J.
  TITLE     Isolation and characterization of human elastin cDNAs, and
            age-associated variation in elastin gene expression in cultured
            skin fibroblasts
  JOURNAL   Lab. Invest. 58 (3), 270-277 (1988)
  MEDLINE   88156138
   PUBMED   2831431
REFERENCE   4  (residues 1 to 757)
  AUTHORS   Fazio,M.J., Olsen,D.R., Kauh,E.A., Baldwin,C.T., Indik,Z.,
            Ornstein-Goldstein,N., Yeh,H., Rosenbloom,J. and Uitto,J.
  TITLE     Cloning of full-length elastin cDNAs from a human skin fibroblast
            recombinant cDNA library: further elucidation of alternative
            splicing utilizing exon-specific oligonucleotides
  JOURNAL   J. Invest. Dermatol. 91 (5), 458-464 (1988)
  MEDLINE   89009960
   PUBMED   3171221
REFERENCE   5  (residues 1 to 757)
  AUTHORS   Fazio,M.J., Mattei,M.G., Passage,E., Chu,M.L., Black,D.,
            Solomon,E., Davidson,J.M. and Uitto,J.
  TITLE     Human elastin gene: new evidence for localization to the long arm
            of chromosome 7
  JOURNAL   Am. J. Hum. Genet. 48 (4), 696-703 (1991)
  MEDLINE   91196727
   PUBMED   2014796
REFERENCE   6  (residues 1 to 757)
  AUTHORS   Curran,M.E., Atkinson,D.L., Ewart,A.K., Morris,C.A., Leppert,M.F.
            and Keating,M.T.
  TITLE     The elastin gene is disrupted by a translocation associated with
            supravalvular aortic stenosis
  JOURNAL   Cell 73 (1), 159-168 (1993)
  MEDLINE   93214988
   PUBMED   8096434
REFERENCE   7  (residues 1 to 757)
  AUTHORS   Ewart,A.K., Morris,C.A., Atkinson,D., Jin,W., Sternes,K.,
            Spallone,P., Stock,A.D., Leppert,M. and Keating,M.T.
  TITLE     Hemizygosity at the elastin locus in a developmental disorder,
            Williams syndrome
  JOURNAL   Nat. Genet. 5 (1), 11-16 (1993)
  MEDLINE   94035109
   PUBMED   7693128
REFERENCE   8  (residues 1 to 757)
  AUTHORS   Li,D.Y., Brooke,B., Davis,E.C., Mecham,R.P., Sorensen,L.K.,
            Boak,B.B., Eichwald,E. and Keating,M.T.
  TITLE     Elastin is an essential determinant of arterial morphogenesis
  JOURNAL   Nature 393 (6682), 276-280 (1998)
  MEDLINE   98268782
   PUBMED   9607766
REFERENCE   9  (residues 1 to 757)
  AUTHORS   Tassabehji,M., Metcalfe,K., Hurst,J., Ashcroft,G.S., Kielty,C.,
            Wilmot,C., Donnai,D., Read,A.P. and Jones,C.J.
  TITLE     An elastin gene mutation producing abnormal tropoelastin and
            abnormal elastic fibres in a patient with autosomal dominant cutis
            laxa
  JOURNAL   Hum. Mol. Genet. 7 (6), 1021-1028 (1998)
  MEDLINE   98248427
   PUBMED   9580666
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M17282.1.
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q11.23"
     Protein         1..757
                     /product="elastin"
     CDS             1..757
                     /gene="ELN"
                     /coded_by="NM_000501.1:1..2274"
                     /note="elastin C precursor"
                     /db_xref="LocusID:2006"
                     /db_xref="MIM:130160"
ORIGIN      
        1 magltaaapr pgvlllllsi lhpsrpggvp gaipggvpgg vfypgaglga lgggalgpgg
       61 kplkpvpggl agaglgaglg afpavtfpga lvpggvadaa aaykaakaga glggvpgvgg
      121 lgvsagavvp qpgagvkpgk vpgvglpgvy pggvlpgarf pgvgvlpgvp tgagvkpkap
      181 gvggafagip gvgpfggpqp gvplgypika pklpggyglp yttgklpygy gpggvagaag
      241 kagyptgtgv gpqaaaaaaa kaaakfgaga agvlpgvgga gvpgvpgaip giggiagvgt
      301 paaaaaaaaa akaakygaaa glvpggpgfg pgvvgvpgag vpgvgvpgag ipvvpgagip
      361 gaavpgvvsp eaaakaaaka akygarpgvg vggiptygvg aggfpgfgvg vggipgvagv
      421 psvggvpgvg gvpgvgispe aqaaaaakaa kygvgtpaaa aakaaakaaq fglvpgvgva
      481 pgvgvapgvg vapgvglapg vgvapgvgva pgvgvapgig pggvaaaaks aakvaakaql
      541 raaaglgagi pglgvgvgvp glgvgagvpg lgvgagvpgf gagadegvrr slspelregd
      601 psssqhlpst pssprvpgal aaakaakyga avpgvlgglg alggvgipgg vvgagpaaaa
      661 aaakaaakaa qfglvgaagl gglgvgglgv pgvgglggip paaaakaaky gaaglggvlg
      721 gagqfplggv aarpgfglsp ifpggaclgk acgrkrk
//



Revised: July 5, 2002.
 
 


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1: NP_001765. CD37 antigen; leu...[gi:4502663] Links  


LOCUS       CD37                     281 aa            linear   PRI 28-MAY-2002
DEFINITION  CD37 antigen; leukocyte surface antigen CD37; cell differentiation
            antigen 37 [Homo sapiens].
ACCESSION   NP_001765
VERSION     NP_001765.1  GI:4502663
DBSOURCE    REFSEQ: accession NM_001774.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 281)
  AUTHORS   Schwartz-Albiez,R., Dorken,B., Hofmann,W. and Moldenhauer,G.
  TITLE     The B cell-associated CD37 antigen (gp40-52). Structure and
            subcellular expression of an extensively glycosylated glycoprotein
  JOURNAL   J. Immunol. 140 (3), 905-914 (1988)
  MEDLINE   88116711
   PUBMED   3257508
REFERENCE   2  (residues 1 to 281)
  AUTHORS   Classon,B.J., Williams,A.F., Willis,A.C., Seed,B. and
            Stamenkovic,I.
  TITLE     The primary structure of the human leukocyte antigen CD37, a
            species homologue of the rat MRC OX-44 antigen
  JOURNAL   J. Exp. Med. 169 (4), 1497-1502 (1989)
  MEDLINE   89176904
   PUBMED   2466944
  REMARK    revised by [3]
REFERENCE   3  (residues 1 to 281)
  AUTHORS   Classon,B.J., Williams,A.F., Willis,A.C., Seed,B. and
            Stamenkovic,I.
  TITLE     The primary structure of the human leukocyte antigen CD37, a
            species homologue of the rat MRC OX-44 antigen
  JOURNAL   J. Exp. Med. 172 (3), 1007 (1990)
  MEDLINE   90354767
   PUBMED   2388030
REFERENCE   4  (residues 1 to 281)
  AUTHORS   Horejsi,V. and Vlcek,C.
  TITLE     Novel structurally distinct family of leucocyte surface
            glycoproteins including CD9, CD37, CD53 and CD63
  JOURNAL   FEBS Lett. 288 (1-2), 1-4 (1991)
  MEDLINE   91348240
   PUBMED   1879540
REFERENCE   5  (residues 1 to 281)
  AUTHORS   Virtaneva,K.I., Angelisova,P., Baumruker,T., Horejsi,V.,
            Nevanlinna,H. and Schroder,J.
  TITLE     The genes for CD37, CD53, and R2, all members of a novel gene
            family, are located on different chromosomes
  JOURNAL   Immunogenetics 37 (6), 461-465 (1993)
  MEDLINE   93170894
   PUBMED   8436422
REFERENCE   6  (residues 1 to 281)
  AUTHORS   Wright,M.D., Rochelle,J.M., Tomlinson,M.G., Seldin,M.F. and
            Williams,A.F.
  TITLE     Gene structure, chromosomal localization, and protein sequence of
            mouse CD53 (Cd53): evidence that the transmembrane 4 superfamily
            arose by gene duplication
  JOURNAL   Int. Immunol. 5 (2), 209-216 (1993)
  MEDLINE   93200067
   PUBMED   8452817
REFERENCE   7  (residues 1 to 281)
  AUTHORS   Angelisova,P., Hilgert,I. and Horejsi,V.
  TITLE     Association of four antigens of the tetraspans family (CD37, CD53,
            TAPA-1, and R2/C33) with MHC class II glycoproteins
  JOURNAL   Immunogenetics 39 (4), 249-256 (1994)
  MEDLINE   94164694
   PUBMED   8119731
REFERENCE   8  (residues 1 to 281)
  AUTHORS   Serru,V., Le Naour,F., Billard,M., Azorsa,D.O., Lanza,F.,
            Boucheix,C. and Rubinstein,E.
  TITLE     Selective tetraspan-integrin complexes (CD81/alpha4beta1,
            CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting
            tetraspan interactions
  JOURNAL   Biochem. J. 340 (Pt 1), 103-111 (1999)
  MEDLINE   99247901
   PUBMED   10229664
REFERENCE   9  (residues 1 to 281)
  AUTHORS   Berditchevski,F.
  TITLE     Complexes of tetraspanins with integrins: more than meets the eye
  JOURNAL   J. Cell. Sci. 114 (Pt 23), 4143-4151 (2001)
  MEDLINE   21601835
   PUBMED   11739647
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X14046.1.
            Summary: The protein encoded by this gene is a member of the
            transmembrane 4 superfamily, also known as the tetraspanin family.
            Most of these members are cell-surface proteins that are
            characterized by the presence of four hydrophobic domains. The
            proteins mediate signal transduction events that play a role in the
            regulation of cell development, activation, growth and motility.
            This encoded protein is a cell surface glycoprotein that is known
            to complex with integrins and other transmembrane 4 superfamily
            proteins. It may play a role in T-cell-B-cell interactions.
FEATURES             Location/Qualifiers
     source          1..281
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13-q13.4"
     Protein         1..281
                     /product="CD37 antigen"
                     /note="leukocyte surface antigen CD37; cell
                     differentiation antigen 37"
     Region          12..270
                     /region_name="Tetraspanin family"
                     /note="transmembrane4"
                     /db_xref="CDD:pfam00335"
     CDS             1..281
                     /gene="CD37"
                     /coded_by="NM_001774.1:64..909"
                     /db_xref="LocusID:951"
                     /db_xref="MIM:151523"
ORIGIN      
        1 msaqesclsl ikyflfvfnl fffvlgslif cfgiwilidk tsfvsfvgla fvplqiwskv
       61 laisgiftmg iallgcvgal kelrcllgly fgmllllfat qitlgilist qraqlerslr
      121 dvvektiqky gtnpeetaae eswdyvqfql rccgwhypqd wfqvlilrgn gseahrvpcs
      181 cynlsatnds tildkvilpq lsrlghlars rhsadicavp aeshiyregc aqglqkwlhn
      241 nlisivgicl gvgllelgfm tlsiflcrnl dhvynrlary r
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_003346. uncoupling protei...[gi:13259541] Links  


LOCUS       UCP2                     309 aa            linear   PRI 09-MAR-2001
DEFINITION  uncoupling protein 2 [Homo sapiens].
ACCESSION   NP_003346
VERSION     NP_003346.2  GI:13259541
DBSOURCE    REFSEQ: accession NM_003355.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Fleury,C., Neverova,M., Collins,S., Raimbault,S., Champigny,O.,
            Levi-Meyrueis,C., Bouillaud,F., Seldin,M.F., Surwit,R.S.,
            Ricquier,D. and Warden,C.H.
  TITLE     Uncoupling protein-2: a novel gene linked to obesity and
            hyperinsulinemia
  JOURNAL   Nat. Genet. 15 (3), 269-272 (1997)
  MEDLINE   97207646
   PUBMED   9054939
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Gimeno,R.E., Dembski,M., Weng,X., Deng,N., Shyjan,A.W.,
            Gimeno,C.J., Iris,F., Ellis,S.J., Woolf,E.A. and Tartaglia,L.A.
  TITLE     Cloning and characterization of an uncoupling protein homolog: a
            potential molecular mediator of human thermogenesis
  JOURNAL   Diabetes 46 (5), 900-906 (1997)
  MEDLINE   97278985
   PUBMED   9133562
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Boss,O., Samec,S., Paoloni-Giacobino,A., Rossier,C., Dulloo,A.,
            Seydoux,J., Muzzin,P. and Giacobino,J.P.
  TITLE     Uncoupling protein-3: a new member of the mitochondrial carrier
            family with tissue-specific expression
  JOURNAL   FEBS Lett. 408 (1), 39-42 (1997)
  MEDLINE   97324095
   PUBMED   9180264
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Vidal-Puig,A., Solanes,G., Grujic,D., Flier,J.S. and Lowell,B.B.
  TITLE     UCP3: an uncoupling protein homologue expressed preferentially and
            abundantly in skeletal muscle and brown adipose tissue
  JOURNAL   Biochem. Biophys. Res. Commun. 235 (1), 79-82 (1997)
  MEDLINE   97339440
   PUBMED   9196039
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Argyropoulos,G., Brown,A.M., Peterson,R., Likes,C.E., Watson,D.K.
            and Garvey,W.T.
  TITLE     Structure and organization of the human uncoupling protein 2 gene
            and identification of a common biallelic variant in Caucasian and
            African-American subjects
  JOURNAL   Diabetes 47 (4), 685-687 (1998)
  MEDLINE   98227655
   PUBMED   9568704
REFERENCE   6  (residues 1 to 309)
  AUTHORS   Pecqueur,C., Cassard-Doulcier,A.M., Raimbault,S., Miroux,B.,
            Fleury,C., Gelly,C., Bouillaud,F. and Ricquier,D.
  TITLE     Functional organization of the human uncoupling protein-2 gene, and
            juxtaposition to the uncoupling protein-3 gene
  JOURNAL   Biochem. Biophys. Res. Commun. 255 (1), 40-46 (1999)
  MEDLINE   99185293
   PUBMED   10082652
  REMARK    In Fig.2, accession numbers for human and mouse genomic sequences
            are incorrectly published. GenBank association of accession numbers
            with species is correct.
REFERENCE   7  (residues 1 to 309)
  AUTHORS   Ricquier,D. and Bouillaud,F.
  TITLE     The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and
            AtUCP
  JOURNAL   Biochem. J. 345 Pt 2, 161-179 (2000)
  MEDLINE   20088647
   PUBMED   10620491
REFERENCE   8  (residues 1 to 309)
  AUTHORS   Jezek,P. and Urbankova,E.
  TITLE     Specific sequence of motifs of mitochondrial uncoupling proteins
  JOURNAL   IUBMB Life 49 (1), 63-70 (2000)
  MEDLINE   20233297
   PUBMED   10772343
  REMARK    Describes transmembrane, matrix and cytosolic domains, and unique
            signatures of the mitochondrial anion carrier and the mitochondrial
            uncoupling protein families.
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF096289.1.
            On Mar 9, 2001 this sequence version replaced gi:4507805.
            Summary: Mitochondrial uncoupling proteins (UCP) are members of the
            larger family of mitochondrial anion carrier proteins (MACP). UCPs
            separate oxidative phosphorylation from ATP synthesis with energy
            dissipated as heat, also referred to as the mitochondrial proton
            leak. UCPs facilitate the transfer of anions from the inner to the
            outer mitochondrial membrane and the return transfer of protons
            from the outer to the inner mitochondrial membrane. They also
            reduce the mitochondrial membrane potential in mammalian cells.
            Tissue specificity occurs for the different UCPs and the exact
            methods of how UCPs transfer H+/OH- are not known. UCPs contain the
            three homologous protein domains of MACPs. This gene is expressed
            in many tissues, with the greatest expression in skeletal muscle.
            It is thought to play a role in nonshivering thermogenesis, obesity
            and diabetes. Chromosomal order is 5'-UCP3-UCP2-3'.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q13"
     Protein         1..309
                     /product="uncoupling protein 2"
     Region          10..109
                     /region_name="Mitochondrial carrier proteins"
                     /note="mito_carr"
                     /db_xref="CDD:pfam00153"
     Region          17..34
                     /region_name="transmembrane domain"
     Region          78..100
                     /region_name="transmembrane domain"
     Region          112..208
                     /region_name="Mitochondrial carrier proteins"
                     /note="mito_carr"
                     /db_xref="CDD:pfam00153"
     Region          120..137
                     /region_name="transmembrane domain"
     Region          174..197
                     /region_name="transmembrane domain"
     Region          211..299
                     /region_name="Mitochondrial carrier proteins"
                     /note="mito_carr"
                     /db_xref="CDD:pfam00153"
     Region          216..235
                     /region_name="transmembrane domain"
     Region          264..273
                     /region_name="purine nucleotide binding domain"
     Region          269..291
                     /region_name="transmembrane domain"
     CDS             1..309
                     /gene="UCP2"
                     /coded_by="NM_003355.2:381..1310"
                     /db_xref="LocusID:7351"
                     /db_xref="MIM:601693"
ORIGIN      
        1 mvgfkatdvp ptatvkflga gtaaciadli tfpldtakvr lqiqgesqgp vratasaqyr
       61 gvmgtiltmv rtegprslyn glvaglqrqm sfasvrigly dsvkqfytkg sehasigsrl
      121 lagsttgala vavaqptdvv kvrfqaqara gggrryqstv nayktiaree gfrglwkgts
      181 pnvarnaivn caelvtydli kdallkanlm tddlpchfts afgagfcttv iaspvdvvkt
      241 rymnsalgqy ssaghcaltm lqkegprafy kgfmpsflrl gswnvvmfvt yeqlkralma
      301 actsreapf
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_000197. interleukin 2 rec...[gi:4557882] Links  


LOCUS       IL2RG                    369 aa            linear   PRI 27-AUG-2002
DEFINITION  interleukin 2 receptor, gamma chain, precursor; Interleukin-2
            receptor, gamma; common cytokine receptor gamma chain; CD132 [Homo
            sapiens].
ACCESSION   NP_000197
VERSION     NP_000197.1  GI:4557882
DBSOURCE    REFSEQ: accession NM_000206.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 369)
  AUTHORS   Takeshita,T., Asao,H., Ohtani,K., Ishii,N., Kumaki,S., Tanaka,N.,
            Munakata,H., Nakamura,M. and Sugamura,K.
  TITLE     Cloning of the gamma chain of the human IL-2 receptor
  JOURNAL   Science 257 (5068), 379-382 (1992)
  MEDLINE   92335883
   PUBMED   1631559
REFERENCE   2  (residues 1 to 369)
  AUTHORS   Noguchi,M., Yi,H., Rosenblatt,H.M., Filipovich,A.H., Adelstein,S.,
            Modi,W.S., McBride,O.W. and Leonard,W.J.
  TITLE     Interleukin-2 receptor gamma chain mutation results in X-linked
            severe combined immunodeficiency in humans
  JOURNAL   Cell 73 (1), 147-157 (1993)
  MEDLINE   93214986
   PUBMED   8462096
REFERENCE   3  (residues 1 to 369)
  AUTHORS   Noguchi M, Adelstein S, Cao X and Leonard WJ.
  TITLE     Characterization of the human interleukin-2 receptor gamma chain
            gene
  JOURNAL   J. Biol. Chem. 268 (18), 13601-13608 (1993)
  MEDLINE   93293887
   PUBMED   8514792
REFERENCE   4  (residues 1 to 369)
  AUTHORS   Puck,J.M., Deschenes,S.M., Porter,J.C., Dutra,A.S., Brown,C.J.,
            Willard,H.F. and Henthorn,P.S.
  TITLE     The interleukin-2 receptor gamma chain maps to Xq13.1 and is
            mutated in X-linked severe combined immunodeficiency, SCIDX1
  JOURNAL   Hum. Mol. Genet. 2 (8), 1099-1104 (1993)
  MEDLINE   94004847
   PUBMED   8401490
REFERENCE   5  (residues 1 to 369)
  AUTHORS   Kondo,M., Takeshita,T., Ishii,N., Nakamura,M., Watanabe,S., Arai,K.
            and Sugamura,K.
  TITLE     Sharing of the interleukin-2 (IL-2) receptor gamma chain between
            receptors for IL-2 and IL-4
  JOURNAL   Science 262 (5141), 1874-1877 (1993)
  MEDLINE   94090315
   PUBMED   8266076
REFERENCE   6  (residues 1 to 369)
  AUTHORS   Noguchi,M., Nakamura,Y., Russell,S.M., Ziegler,S.F., Tsang,M.,
            Cao,X. and Leonard,W.J.
  TITLE     Interleukin-2 receptor gamma chain: a functional component of the
            interleukin-7 receptor
  JOURNAL   Science 262 (5141), 1877-1880 (1993)
  MEDLINE   94090316
   PUBMED   8266077
REFERENCE   7  (residues 1 to 369)
  AUTHORS   Russell,S.M., Keegan,A.D., Harada,N., Nakamura,Y., Noguchi,M.,
            Leland,P., Friedmann,M.C., Miyajima,A., Puri,R.K., Paul,W.E. et al.
  TITLE     Interleukin-2 receptor gamma chain: a functional component of the
            interleukin-4 receptor
  JOURNAL   Science 262 (5141), 1880-1883 (1993)
  MEDLINE   94090317
   PUBMED   8266078
REFERENCE   8  (residues 1 to 369)
  AUTHORS   Bani,L., Pasquier,V., Kryworuchko,M., Salamero,J. and Theze,J.
  TITLE     Unstimulated human CD4 lymphocytes express a cytoplasmic immature
            form of the common cytokine receptor gamma-chain
  JOURNAL   J. Immunol. 167 (1), 344-349 (2001)
  MEDLINE   21311891
   PUBMED   11418669
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D11086.1.
            Summary:  The interleukin 2 (IL2) receptor gamma chain (IL2RG), an
            important signalling component of many interleukin receptors
            (IL2,IL4,IL7,IL9, and IL15), is thus referred to as the common
            gamma chain.  Mutations in this X-chromosome-linked gene cause
            X-linked severe combined immunodeficiency (XSCID).
FEATURES             Location/Qualifiers
     source          1..369
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.1"
                     /cell_line="MOLT4"
                     /cell_type="T cell"
                     /tissue_type="Lymphocyte"
     Protein         1..369
                     /product="interleukin 2 receptor, gamma chain, precursor"
                     /note="Interleukin-2 receptor, gamma; common cytokine
                     receptor gamma chain; CD132"
     sig_peptide     1..22
     mat_peptide     23..369
                     /product="interleukin 2 receptor gamma chain"
     CDS             1..369
                     /gene="IL2RG"
                     /coded_by="NM_000206.1:15..1124"
                     /db_xref="LocusID:3561"
                     /db_xref="MIM:308380"
ORIGIN      
        1 mlkpslpfts llflqlpllg vglnttiltp ngnedttadf flttmptdsl svstlplpev
       61 qcfvfnveym nctwnsssep qptnltlhyw yknsdndkvq kcshylfsee itsgcqlqkk
      121 eihlyqtfvv qlqdpreprr qatqmlklqn lvipwapenl tlhklsesql elnwnnrfln
      181 hclehlvqyr tdwdhswteq svdyrhkfsl psvdgqkryt frvrsrfnpl cgsaqhwsew
      241 shpihwgsnt skenpflfal eavvisvgsm gliisllcvy fwlertmpri ptlknledlv
      301 teyhgnfsaw sgvskglaes lqpdyserlc lvseippkgg algegpgasp cnqhspywap
      361 pcytlkpet
//



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1: NP_001817. CDC28 protein kin...[gi:4502857] Links  


LOCUS       CKS1B                     79 aa            linear   PRI 22-OCT-2002
DEFINITION  CDC28 protein kinase 1B; CDC2-associated protein CKS1; cell
            division control protein CKS1; NB4 apoptosis/differentiation
            related protein; PNAS-143; CDC28 protein kinase 1 [Homo sapiens].
ACCESSION   NP_001817
VERSION     NP_001817.1  GI:4502857
DBSOURCE    REFSEQ: accession NM_001826.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 79)
  AUTHORS   Richardson,H.E., Stueland,C.S., Thomas,J., Russell,P. and Reed,S.I.
  TITLE     Human cDNAs encoding homologs of the small p34Cdc28/Cdc2-associated
            protein of Saccharomyces cerevisiae and Schizosaccharomyces pombe
  JOURNAL   Genes Dev. 4 (8), 1332-1344 (1990)
  MEDLINE   91032985
   PUBMED   2227411
REFERENCE   2  (residues 1 to 79)
  AUTHORS   Bourne,Y., Watson,M.H., Hickey,M.J., Holmes,W., Rocque,W.,
            Reed,S.I. and Tainer,J.A.
  TITLE     Crystal structure and mutational analysis of the human CDK2 kinase
            complex with cell cycle-regulatory protein CksHs1
  JOURNAL   Cell 84 (6), 863-874 (1996)
  MEDLINE   96182647
   PUBMED   8601310
REFERENCE   3  (residues 1 to 79)
  AUTHORS   Demetrick,D.J., Zhang,H. and Beach,D.H.
  TITLE     Chromosomal mapping of the human genes CKS1 to 8q21 and CKS2 to
            9q22
  JOURNAL   Cytogenet. Cell Genet. 73 (3), 250-254 (1996)
  MEDLINE   96302345
   PUBMED   8697818
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X54941.1.
            Summary: CKS1B protein binds to the catalytic subunit of the cyclin
            dependent kinases and is essential for their biological function.
            The CKS1B mRNA is found to be expressed in different patterns
            through the cell cycle in HeLa cells, which reflects a specialized
            role for the encoded protein.
FEATURES             Location/Qualifiers
     source          1..79
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21.2"
     Protein         1..79
                     /product="CDC28 protein kinase 1B"
                     /note="CDC2-associated protein CKS1; cell division control
                     protein CKS1; NB4 apoptosis/differentiation related
                     protein; PNAS-143; CDC28 protein kinase 1"
     Region          2..66
                     /region_name="Cyclin-dependent kinase regulatory subunit"
                     /note="CKS"
                     /db_xref="CDD:pfam01111"
     CDS             1..79
                     /gene="CKS1B"
                     /coded_by="NM_001826.1:10..249"
                     /db_xref="LocusID:1163"
                     /db_xref="MIM:116900"
ORIGIN      
        1 mshkqiyysd kyddeefeyr hvmlpkdiak lvpkthlmse sewrnlgvqq sqgwvhymih
       61 epephillfr rplpkkpkk
//



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1: NP_037409. Rac GTPase activa...[gi:21361397] Links  


LOCUS       RACGAP1                  632 aa            linear   PRI 10-JUN-2002
DEFINITION  Rac GTPase activating protein 1; GTPase activating protein [Homo
            sapiens].
ACCESSION   NP_037409
VERSION     NP_037409.2  GI:21361397
DBSOURCE    REFSEQ: accession NM_013277.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 632)
  AUTHORS   Kawashima,T., Hirose,K., Satoh,T., Kaneko,A., Ikeda,Y., Kaziro,Y.,
            Nosaka,T. and Kitamura,T.
  TITLE     MgcRacGAP is involved in the control of growth and differentiation
            of hematopoietic cells
  JOURNAL   Blood 96 (6), 2116-2124 (2000)
  MEDLINE   20435340
   PUBMED   10979956
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AL136794.1.
            On Jun 10, 2002 this sequence version replaced gi:7019433.
FEATURES             Location/Qualifiers
     source          1..632
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p11.1"
                     /clone="DKFZp434C011"
                     /tissue_type="testis"
                     /clone_lib="434 (synonym: htes3). Vector pSport1; host
                     DH10B; sites NotI + SalI"
                     /dev_stage="adult"
     Protein         1..632
                     /product="Rac GTPase activating protein 1"
                     /note="GTPase activating protein"
     Region          42..107
                     /region_name="Tropomyosin"
                     /note="Tropomyosin"
                     /db_xref="CDD:pfam00261"
     Region          287..335
                     /region_name="Phorbol esters/diacylglycerol binding domain
                     (C1 domain)"
                     /note="DAG_PE-bind"
                     /db_xref="CDD:pfam00130"
     Region          287..335
                     /region_name="Protein kinase C conserved region 1 (C1)
                     domains (Cysteine-rich domains)"
                     /note="C1"
                     /db_xref="CDD:smart00109"
     Region          360..532
                     /region_name="GTPase-activator protein for Rho-like
                     GTPases"
                     /note="RhoGAP"
                     /db_xref="CDD:smart00324"
     Region          363..504
                     /region_name="RhoGAP domain"
                     /note="RhoGAP"
                     /db_xref="CDD:pfam00620"
     CDS             1..632
                     /gene="RACGAP1"
                     /coded_by="NM_013277.2:225..2123"
                     /note="similarity to GTPase-activating proteins"
                     /db_xref="LocusID:29127"
                     /db_xref="MIM:604980"
ORIGIN      
        1 mdtmmlnvrn lfeqlvrrve ilsegnevqf iqlakdfedf rkkwqrtdhe lgkykdllmk
       61 aetersaldv klkharnqvd veikrrqrae adceklerqi qliremlmcd tsgsiqlsee
      121 qksalaflnr gqpsssnagn krlstidesg silsdisfdk tdesldwdss lvktfklkkr
      181 ekrrstsrqf vdgppgpvkk trsigsavdq gnesivaktt vtvpndggpi eavstietvp
      241 ywtrsrrktg tlqpwnsdst lnsrqleprt etdsvgtpqs nggmrlhdfv sktvikpesc
      301 vpcgkrikfg klslkcrdcr vvshpecrdr cplpciptli gtpvkigegm ladfvsqtsp
      361 mipsivvhcv neieqrglte tglyrisgcd rtvkelkekf lrvktvplls kvddihaics
      421 llkdflrnlk eplltfrlnr afmeaaeitd ednsiaamyq avgelpqanr dtlaflmihl
      481 qrvaqsphtk mdvanlakvf gptivahavp npdpvtmlqd ikrqpkvver llslpleyws
      541 qfmmveqeni dplhviensn afstpqtpdi kvsllgpvtt pehqllktps ssslsqrvrs
      601 tltkntprfg sksksatnlg rqgnffaspm lk
//



Revised: July 5, 2002.
 
 


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1: NP_005845. receptor (calcito...[gi:5032021] Links  


LOCUS       RAMP2                    175 aa            linear   PRI 02-DEC-2000
DEFINITION  receptor (calcitonin) activity modifying protein 2 precursor;
            calcitonin receptor-like receptor activity modifying protein 2;
            receptor-activity-modifying protein 2 [Homo sapiens].
ACCESSION   NP_005845
VERSION     NP_005845.1  GI:5032021
DBSOURCE    REFSEQ: accession NM_005854.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 175)
  AUTHORS   McLatchie,L.M., Fraser,N.J., Main,M.J., Wise,A., Brown,J.,
            Thompson,N., Solari,R., Lee,M.G. and Foord,S.M.
  TITLE     RAMPs regulate the transport and ligand specificity of the
            calcitonin-receptor-like receptor
  JOURNAL   Nature 393 (6683), 333-339 (1998)
  MEDLINE   98282119
   PUBMED   9620797
REFERENCE   2  (residues 1 to 175)
  AUTHORS   Foord,S.M. and Marshall,F.H.
  TITLE     RAMPs: accessory proteins for seven transmembrane domain receptors
  JOURNAL   Trends Pharmacol. Sci. 20 (5), 184-187 (1999)
  MEDLINE   99284784
   PUBMED   10354609
REFERENCE   3  (residues 1 to 175)
  AUTHORS   Derst C, Engel H, Grzeschik K and Daut J.
  TITLE     Genomic structure and chromosome mapping of human and mouse RAMP
            genes
  JOURNAL   Cytogenet. Cell Genet. 90 (1-2), 115-118 (2000)
  MEDLINE   20515595
   PUBMED   11060459
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AJ001015.1.
            Summary: The protein encoded by this gene is a member of the RAMP
            family of single-transmembrane-domain proteins, called receptor
            (calcitonin) activity modifying proteins (RAMPs). RAMPs are type I
            transmembrane proteins with an extracellular N terminus and a
            cytoplasmic C terminus. RAMPs are required to transport
            calcitonin-receptor-like receptor (CRLR) to the plasma membrane.
            CRLR, a receptor with seven transmembrane domains, can function as
            either a calcitonin-gene-related peptide (CGRP) receptor or an
            adrenomedullin receptor, depending on which members of the RAMP
            family are expressed. In the presence of this (RAMP2) protein, CRLR
            functions as an adrenomedullin receptor. The RAMP2 protein is
            involved in core glycosylation and transportation of adrenomedullin
            receptor to the cell surface.
FEATURES             Location/Qualifiers
     source          1..175
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /map="17"
     Protein         1..175
                     /product="receptor (calcitonin) activity modifying protein
                     2 precursor"
                     /note="calcitonin receptor-like receptor activity
                     modifying protein 2; receptor-activity-modifying protein
                     2"
     sig_peptide     1..35
     mat_peptide     36..175
                     /product="receptor (calcitonin) activity modifying protein
                     2"
     CDS             1..175
                     /gene="RAMP2"
                     /coded_by="NM_005854.1:69..596"
                     /db_xref="LocusID:10266"
                     /db_xref="MIM:605154"
ORIGIN      
        1 maslrverag gprlprtrvg rpaavrllll lgavlnphea laqplpttgt pgseggtvkn
       61 yetavqfcwn hykdqmdpie kdwcdwamis rpystlrdcl ehfaelfdlg fpnplaerii
      121 fethqihfan cslvqptfsd ppedvllami iapiclipfl itlvvwrskd seaqa
//



Revised: July 5, 2002.
 
 


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1: NP_003990. oncostatin M rece...[gi:4557040] Links  


LOCUS       OSMR                     979 aa            linear   PRI 16-MAY-2002
DEFINITION  oncostatin M receptor [Homo sapiens].
ACCESSION   NP_003990
VERSION     NP_003990.1  GI:4557040
DBSOURCE    REFSEQ: accession NM_003999.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 979)
  AUTHORS   Mosley,B., De Imus,C., Friend,D., Boiani,N., Thoma,B., Park,L.S.
            and Cosman,D.
  TITLE     Dual oncostatin M (OSM) receptors. Cloning and characterization of
            an alternative signaling subunit conferring OSM-specific receptor
            activation
  JOURNAL   J. Biol. Chem. 271 (51), 32635-32643 (1996)
  MEDLINE   97115791
   PUBMED   8999038
REFERENCE   2  (residues 1 to 979)
  AUTHORS   Auguste,P., Guillet,C., Fourcin,M., Olivier,C., Veziers,J.,
            Pouplard-Barthelaix,A. and Gascan,H.
  TITLE     Signaling of type II oncostatin M receptor
  JOURNAL   J. Biol. Chem. 272 (25), 15760-15764 (1997)
  MEDLINE   97332660
   PUBMED   9188471
REFERENCE   3  (residues 1 to 979)
  AUTHORS   Cichy,J., Rose-John,S. and Pure,E.
  TITLE     Regulation of the type II oncostatin M receptor expression in
            lung-derived epithelial cells
  JOURNAL   FEBS Lett. 429 (3), 412-416 (1998)
  MEDLINE   98324837
   PUBMED   9662460
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U60805.1.
            Summary: Oncostatin M is a member of the IL6 family of cytokines.
            Functional receptors for IL6 family cytokines are multisubunit
            complexes involving members of the hematopoietin receptor
            superfamily. Many IL6 cytokines utilize gp130 as a common receptor
            subunit. OSM binds to the gp130 receptor subunit and, in
            association with the leukemia inhibitory factor receptor, induces a
            proliferative response in permissive cells. OSMR is an alternative
            subunit (for an OSM receptor complex (a heterodimer of gp130 and
            OSMR) that is activated by OSM but not by LIF.
FEATURES             Location/Qualifiers
     source          1..979
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5p13.1"
     Protein         1..979
                     /product="oncostatin M receptor"
     Region          539..607
                     /region_name="Fibronectin type III domain"
                     /note="fn3"
                     /db_xref="CDD:pfam00041"
     Region          539..602
                     /region_name="Fibronectin type 3 domain"
                     /note="FN3"
                     /db_xref="CDD:smart00060"
     variation       553
                     /allele="D"
                     /allele="N"
                     /db_xref="dbSNP:2278329"
     CDS             1..979
                     /gene="OSMR"
                     /coded_by="NM_003999.1:368..3307"
                     /db_xref="LocusID:9180"
                     /db_xref="MIM:601743"
ORIGIN      
        1 malfavfqtt ffltllslrt yqsevlaerl pltpvslkvs tnstrqslhl qwtvhnlpyh
       61 qelkmvfqiq isrietsnvi wvgnysttvk wnqvlhwswe selplecath fvrikslvdd
      121 akfpepnfws nwssweevsv qdstgqdilf vfpkdklvee gtnvticyvs rniqnnvscy
      181 legkqihgeq ldphvtafnl nsvpfirnkg tniyceasqg nvsegmkgiv lfvskvleep
      241 kdfscetedf ktlhctwdpg tdtalgwskq psqsytlfes fsgekklcth knwcnwqitq
      301 dsqetynftl iaenylrkrs vnilfnlthr vylmnpfsvn fenvnatnai mtwkvhsirn
      361 nftylcqiel hgegkmmqyn vsikvngeyf lselepatey marvrcadas hfwkwsewsg
      421 qnfttleaap seapdvwriv slepgnhtvt lfwkplsklh angkilfynv vvenldkpss
      481 selhsipapa nstklildrc syqicviann svgaspasvi visadpenke veeeriagte
      541 ggfslswkpq pgdvigyvvd wcdhtqdvlg dfqwknvgpn ttstvistda frpgvrydfr
      601 iyglstkria cllekktgys qelapsdnph vlvdtltshs ftlswkdyst esqpgfiqgy
      661 hvylkskarq chprfekavl sdgsecckyk idnpeekali vdnlkpesfy effitpftsa
      721 gegpsatftk vttpdehssm lihillpmvf cvllimvmcy lksqwiketc ypdipdpyks
      781 silslikfke nphliimnvs dcipdaievv skpegtkiqf lgtrksltet eltkpnylyl
      841 lpteknhsgp gpcicfenlt ynqaasdsgs cghvpvspka psmlglmtsp envlkalekn
      901 ymnslgeipa getslnyvsq laspmfgdkd slptnpveap hcseykmqma vslrlalppp
      961 tensslssit lldpgehyc
//



Revised: July 5, 2002.
 
 


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1: NP_004070. cathepsin S prepr...[gi:23110962] Links  


LOCUS       CTSS                     331 aa            linear   PRI 18-SEP-2002
DEFINITION  cathepsin S preproprotein [Homo sapiens].
ACCESSION   NP_004070
VERSION     NP_004070.3  GI:23110962
DBSOURCE    REFSEQ: accession NM_004079.3
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 331)
  AUTHORS   Shi,G.P., Munger,J.S., Meara,J.P., Rich,D.H. and Chapman,H.A.
  TITLE     Molecular cloning and expression of human alveolar macrophage
            cathepsin S, an elastinolytic cysteine protease
  JOURNAL   J. Biol. Chem. 267 (11), 7258-7262 (1992)
  MEDLINE   92218373
   PUBMED   1373132
REFERENCE   2  (residues 1 to 331)
  AUTHORS   Wiederanders,B., Bromme,D., Kirschke,H., von Figura,K., Schmidt,B.
            and Peters,C.
  TITLE     Phylogenetic conservation of cysteine proteinases. Cloning and
            expression of a cDNA coding for human cathepsin S
  JOURNAL   J. Biol. Chem. 267 (19), 13708-13713 (1992)
  MEDLINE   92317106
   PUBMED   1377692
REFERENCE   3  (residues 1 to 331)
  AUTHORS   Shi,G.P., Webb,A.C., Foster,K.E., Knoll,J.H., Lemere,C.A.,
            Munger,J.S. and Chapman,H.A.
  TITLE     Human cathepsin S: chromosomal localization, gene structure, and
            tissue distribution
  JOURNAL   J. Biol. Chem. 269 (15), 11530-11536 (1994)
  MEDLINE   94209337
   PUBMED   8157683
REFERENCE   4  (residues 1 to 331)
  AUTHORS   Fengler,A. and Brandt,W.
  TITLE     Three-dimensional structures of the cysteine proteases cathepsins K
            and S deduced by knowledge-based modelling and active site
            characteristics
  JOURNAL   Protein Eng. 11 (11), 1007-1013 (1998)
  MEDLINE   99092748
   PUBMED   9876921
REFERENCE   5  (residues 1 to 331)
  AUTHORS   Cao,H. and Hegele,R.A.
  TITLE     Human cathepsin S gene (CTSS) promoter -25G/A polymorphism
  JOURNAL   J. Hum. Genet. 45 (2), 94-95 (2000)
  MEDLINE   20186449
   PUBMED   10721671
REFERENCE   6  (residues 1 to 331)
  AUTHORS   Hsieh,C.S., deRoos,P., Honey,K., Beers,C. and Rudensky,A.Y.
  TITLE     A role for cathepsin L and cathepsin S in peptide generation for
            MHC class II presentation
  JOURNAL   J. Immunol. 168 (6), 2618-2625 (2002)
  MEDLINE   21881729
   PUBMED   11884425
REFERENCE   7  (residues 1 to 331)
  AUTHORS   Gibson,D., Flannery,T., Mulligan,K., Mirakhur,M. and McCormick,D.
  TITLE     The role of the cysteine proteinase cathepsin S in astrocytoma
            invasion
  JOURNAL   Neuropathol Appl Neurobiol 28 (2), 156 (2002)
   PUBMED   11972823
REFERENCE   8  (residues 1 to 331)
  AUTHORS   Schwarz,G., Boehncke,W.H., Braun,M., Schroter,C.J., Burster,T.,
            Flad,T., Dressel,D., Weber,E., Schmid,H. and Kalbacher,H.
  TITLE     Cathepsin S activity is detectable in human keratinocytes and is
            selectively upregulated upon stimulation with interferon-gamma
  JOURNAL   J. Invest. Dermatol. 119 (1), 44-49 (2002)
  MEDLINE   22155367
   PUBMED   12164923
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC002642.1, AL356292.21,
            BQ006623.1 and M90696.1.
            On Sep 18, 2002 this sequence version replaced gi:20070178.
            Summary: The protein encoded by this gene, a member of the
            peptidase C1 family, is a lysosomal cysteine proteinase that may
            participate in the degradation of antigenic proteins to peptides
            for presentation on MHC class II molecules. The encoded protein can
            function as an elastase over a broad pH range in alveolar
            macrophages. Transcript variants utilizing alternative
            polyadenylation signals exist for this gene.
FEATURES             Location/Qualifiers
     source          1..331
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21"
                     /clone="MGC:3886 IMAGE:3610589"
                     /clone_lib="NIH_MGC_39"
     Protein         1..331
                     /product="cathepsin S preproprotein"
                     /EC_number="3.4.22.27"
     sig_peptide     1..16
     Proprotein      17..331
     mat_peptide     115..331
                     /product="cathepsin S"
     Region          115..329
                     /region_name="pfam00112, Peptidase_C1, Papain family
                     cysteine protease"
     Region          115..329
                     /region_name="smart00645, Pept_C1, Papain family cysteine
                     protease"
     CDS             1..331
                     /gene="CTSS"
                     /coded_by="NM_004079.3:134..1129"
                     /db_xref="LocusID:1520"
                     /db_xref="MIM:116845"
ORIGIN      
        1 mkrlvcvllv cssavaqlhk dptldhhwhl wkktygkqyk ekneeavrrl iweknlkfvm
       61 lhnlehsmgm hsydlgmnhl gdmtseevms lmsslrvpsq wqrnityksn pnrilpdsvd
      121 wrekgcvtev kyqgscgacw afsavgalea qlklktgklv slsaqnlvdc stekygnkgc
      181 nggfmttafq yiidnkgids dasypykamd qkcqydskyr aatcskytel pygredvlke
      241 avankgpvsv gvdarhpsff lyrsgvyyep sctqnvnhgv lvvgygdlng keywlvknsw
      301 ghnfgeegyi rmarnkgnhc giasfpsype i
//



Revised: July 5, 2002.
 
 


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1: NP_003807. a disintegrin and...[gi:4501915] Links  


LOCUS       ADAM9                    819 aa            linear   PRI 26-JUN-2002
DEFINITION  a disintegrin and metalloproteinase domain 9 preproprotein; meltrin
            gamma [Homo sapiens].
ACCESSION   NP_003807
VERSION     NP_003807.1  GI:4501915
DBSOURCE    REFSEQ: accession NM_003816.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 819)
  AUTHORS   Nomura,N., Miyajima,N., Sazuka,T., Tanaka,A., Kawarabayasi,Y.,
            Sato,S., Nagase,T., Seki,N., Ishikawa,K. and Tabata,S.
  TITLE     Prediction of the coding sequences of unidentified human genes. I.
            The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
            analysis of randomly sampled cDNA clones from human immature
            myeloid cell line KG-1
  JOURNAL   DNA Res. 1 (1), 27-35 (1994)
  MEDLINE   96051387
   PUBMED   7584026
REFERENCE   2  (residues 1 to 819)
  AUTHORS   Nomura,N., Miyajima,N., Sazuka,T., Tanaka,A., Kawarabayasi,Y.,
            Sato,S., Nagase,T., Seki,N., Ishikawa,K. and Tabata,S.
  TITLE     Prediction of the coding sequences of unidentified human genes. I.
            The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
            analysis of randomly sampled cDNA clones from human immature
            myeloid cell line KG-1 (supplement)
  JOURNAL   DNA Res. 1 (1), 47-56 (1994)
  MEDLINE   96051389
   PUBMED   7584028
REFERENCE   3  (residues 1 to 819)
  AUTHORS   Weskamp,G., Kratzschmar,J., Reid,M.S. and Blobel,C.P.
  TITLE     MDC9, a widely expressed cellular disintegrin containing
            cytoplasmic SH3 ligand domains
  JOURNAL   J. Cell Biol. 132 (4), 717-726 (1996)
  MEDLINE   96178079
   PUBMED   8647900
REFERENCE   4  (residues 1 to 819)
  AUTHORS   Izumi,Y., Hirata,M., Hasuwa,H., Iwamoto,R., Umata,T., Miyado,K.,
            Tamai,Y., Kurisaki,T., Sehara-Fujisawa,A., Ohno,S. and Mekada,E.
  TITLE     A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and
            PKCdelta are involved in TPA-induced ectodomain shedding of
            membrane-anchored heparin-binding EGF-like growth factor
  JOURNAL   EMBO J. 17 (24), 7260-7272 (1998)
  MEDLINE   99077794
   PUBMED   9857183
REFERENCE   5  (residues 1 to 819)
  AUTHORS   Roghani,M., Becherer,J.D., Moss,M.L., Atherton,R.E.,
            Erdjument-Bromage,H., Arribas,J., Blackburn,R.K., Weskamp,G.,
            Tempst,P. and Blobel,C.P.
  TITLE     Metalloprotease-disintegrin MDC9: intracellular maturation and
            catalytic activity
  JOURNAL   J. Biol. Chem. 274 (6), 3531-3540 (1999)
  MEDLINE   99121091
   PUBMED   9920899
REFERENCE   6  (residues 1 to 819)
  AUTHORS   Howard,L., Nelson,K.K., Maciewicz,R.A. and Blobel,C.P.
  TITLE     Interaction of the metalloprotease disintegrins MDC9 and MDC15 with
            two SH3 domain-containing proteins, endophilin I and SH3PX1
  JOURNAL   J. Biol. Chem. 274 (44), 31693-31699 (1999)
  MEDLINE   20002705
   PUBMED   10531379
REFERENCE   7  (residues 1 to 819)
  AUTHORS   Nelson,K.K., Schlondorff,J. and Blobel,C.P.
  TITLE     Evidence for an interaction of the metalloprotease-disintegrin
            tumour necrosis factor alpha convertase (TACE) with mitotic arrest
            deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9
            with a novel MAD2-related protein, MAD2beta
  JOURNAL   Biochem. J. 343 Pt 3, 673-680 (1999)
  MEDLINE   99458684
   PUBMED   10527948
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U41766.1.
            Summary: This gene encodes disintegrin and metalloprotease (ADAM)
            domain 9, which is a member of the ADAM protein family. Members of
            this family are membrane-anchored proteins structurally related to
            snake venom disintegrins, and have been implicated in a variety of
            biologic processes involving  cell-cell and cell-matrix
            interactions, including fertilization, muscle development, and
            neurogenesis. The member encoded by this gene interacts with SH3
            domain-containing proteins, binds mitotic arrest deficient 2 beta
            protein, and is also involved in TPA-induced ectodomain shedding of
            membrane-anchored heparin-binding EGF-like growth factor.
FEATURES             Location/Qualifiers
     source          1..819
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.21"
     Protein         1..819
                     /product="a disintegrin and metalloproteinase domain 9
                     preproprotein"
                     /note="meltrin gamma"
     sig_peptide     1..29
     Proprotein      30..819
     mat_peptide     80..819
                     /product="a disintegrin and metalloproteinase domain 9"
     Region          80..176
                     /region_name="pfam01562, Pep_M12B_propep, Reprolysin
                     family propeptide. This region is the propeptide for
                     members of peptidase family M12B. The propeptide contains
                     a sequence motif similar to the 'cysteine switch' of the
                     matrixins. This motif is found at the C terminus of the
                     alignment but is not well aligned"
     Region          206..412
                     /region_name="metalloproteinase domain"
     Region          212..406
                     /region_name="pfam01421, Reprolysin (M12B) family zinc
                     metalloprotease. The members of this family are enzymes
                     that cleave peptides. These proteases require zinc for
                     catalysis. Members of this family are also known as
                     adamalysins. Most members of this family are snake venom
                     endopeptidases, but there are also some mammalian proteins
                     and fertilin. Fertilin and closely related proteins appear
                     to not have some active site residues and may not be
                     active enzymes"
     Region          322..362
                     /region_name="smart00235, ZnMc, Zinc-dependent
                     metalloprotease; Neutral zinc metallopeptidases. This
                     alignment represents a subset of known subfamilies.
                     Highest similarity occurs in the HExxH zinc-binding site/
                     active site"
     Region          423..498
                     /region_name="smart00050, DISIN, Homologues of snake
                     disintegrins ; Snake disintegrins inhibit the binding of
                     ligands to integrin receptors. They contain a 'RGD'
                     sequence, identical to the recognition site of many
                     adhesion proteins. Molecules containing both disintegrin
                     and metalloprotease domains are known as ADAMs"
     Region          425..498
                     /region_name="pfam00200, disintegrin, Disintegrin"
     Region          500..637
                     /region_name="smart00608, ACR, ADAM Cysteine-Rich Domain"
     Region          504..643
                     /region_name="cysteine-rich domain"
     Region          644..673
                     /region_name="EGF-like domain"
     Region          699..718
                     /region_name="transmembrane domain"
     Region          719..819
                     /region_name="cytoplasmic domain"
     CDS             1..819
                     /gene="ADAM9"
                     /coded_by="NM_003816.1:79..2538"
                     /db_xref="LocusID:8754"
                     /db_xref="MIM:602713"
ORIGIN      
        1 mgsgarfpsg tlrvrwllll glvgpvlgaa rpgfqqtshl ssyeiitpwr ltrerreapr
       61 pyskqvsyvi qaegkehiih lernkdllpe dfvvytynke gtlitdhpni qnhchyrgyv
      121 egvhnssial sdcfglrgll hlenasygie plqnsshfeh iiyrmddvyk eplkcgvsnk
      181 dieketakde eeeppsmtql lrrrravlpq tryvelfivv dkerydmmgr nqtavreemi
      241 llanyldsmy imlnirivlv gleiwtngnl inivggagdv lgnfvqwrek flitrrrhds
      301 aqlvlkkgfg gtagmafvgt vcsrshaggi nvfgqitvet fasivahelg hnlgmnhddg
      361 rdcscgaksc imnsgasgsr nfsscsaedf ekltlnkggn cllnipkpde aysapscgnk
      421 lvdageecdc gtpkeceldp ccegstcklk sfaecaygdc ckdcrflpgg tlcrgktsec
      481 dvpeycngss qfcqpdvfiq ngypcqnnka ycyngmcqyy daqcqvifgs kakaapkdcf
      541 ievnskgdrf gncgfsgney kkcatgnalc gklqcenvqe ipvfgivpai iqtpsrgtkc
      601 wgvdfqlgsd vpdpgmvneg tkcgagkicr nfqcvdasvl nydcdvqkkc hghgvcnsnk
      661 nchcengwap pncetkgygg svdsgptyne mntalrdgll vffflivpli vcaififikr
      721 dqlwrsyfrk krsqtyesdg knqanpsrqp gsvprhvspv tpprevpiya nrfavptyaa
      781 kqpqqfpsrp pppqpkvssq gnliparpap applysslt
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_002955. S100 calcium-bind...[gi:21614544] Links  


LOCUS       S100A8                    93 aa            linear   PRI 27-AUG-2002
DEFINITION  S100 calcium-binding protein A8; cystic fibrosis antigen;
            calgranulin A [Homo sapiens].
ACCESSION   NP_002955
VERSION     NP_002955.2  GI:21614544
DBSOURCE    REFSEQ: accession NM_002964.3
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Dorin,J.R., Novak,M., Hill,R.E., Brock,D.J., Secher,D.S. and van
            Heyningen,V.
  TITLE     A clue to the basic defect in cystic fibrosis from cloning the CF
            antigen gene
  JOURNAL   Nature 326 (6113), 614-617 (1987)
  MEDLINE   87173041
   PUBMED   3561500
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Odink,K., Cerletti,N., Bruggen,J., Clerc,R.G., Tarcsay,L.,
            Zwadlo,G., Gerhards,G., Schlegel,R. and Sorg,C.
  TITLE     Two calcium-binding proteins in infiltrate macrophages of
            rheumatoid arthritis
  JOURNAL   Nature 330 (6143), 80-82 (1987)
  MEDLINE   88039099
   PUBMED   3313057
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Lagasse,E. and Clerc,R.G.
  TITLE     Cloning and expression of two human genes encoding calcium-binding
            proteins that are regulated during myeloid differentiation
  JOURNAL   Mol. Cell. Biol. 8 (6), 2402-2410 (1988)
  MEDLINE   88302148
   PUBMED   3405210
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Dorin,J.R., Emslie,E. and van Heyningen,V.
  TITLE     Related calcium-binding proteins map to the same subregion of
            chromosome 1q and to an extended region of synteny on mouse
            chromosome 3
  JOURNAL   Genomics 8 (3), 420-426 (1990)
  MEDLINE   91139109
   PUBMED   2149559
REFERENCE   5  (residues 1 to 93)
  AUTHORS   Engelkamp,D., Schafer,B.W., Mattei,M.G., Erne,P. and Heizmann,C.W.
  TITLE     Six S100 genes are clustered on human chromosome 1q21:
            identification of two genes coding for the two previously
            unreported calcium-binding proteins S100D and S100E
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 90 (14), 6547-6551 (1993)
  MEDLINE   93342029
   PUBMED   8341667
REFERENCE   6  (residues 1 to 93)
  AUTHORS   Schafer,B.W., Wicki,R., Engelkamp,D., Mattei,M.G. and Heizmann,C.W.
  TITLE     Isolation of a YAC clone covering a cluster of nine S100 genes on
            human chromosome 1q21: rationale for a new nomenclature of the S100
            calcium-binding protein family
  JOURNAL   Genomics 25 (3), 638-643 (1995)
  MEDLINE   95278932
   PUBMED   7759097
REFERENCE   7  (residues 1 to 93)
  AUTHORS   Schafer,B.W. and Heizmann,C.W.
  TITLE     The S100 family of EF-hand calcium-binding proteins: functions and
            pathology
  JOURNAL   Trends Biochem. Sci. 21 (4), 134-140 (1996)
  MEDLINE   96273192
   PUBMED   8701470
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Y00278.1 and A12027.1.
            On Jun 26, 2002 this sequence version replaced gi:4506771.
            Summary: The protein encoded by this gene is a member of the S100
            family of proteins containing 2 EF-hand calcium-binding motifs.
            S100 proteins are localized in the cytoplasm and/or nucleus of a
            wide range of cells, and involved in the regulation of a number of
            cellular processes such as cell cycle progression and
            differentiation. S100 genes include at least 13 members which are
            located as a cluster on chromosome 1q21. This protein may function
            in the inhibition of casein kinase and as a cytokine. Altered
            expression of this protein is associated with the disease cystic
            fibrosis.
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21"
     Protein         1..93
                     /product="S100 calcium-binding protein A8"
                     /note="cystic fibrosis antigen; calgranulin A"
     Region          5..48
                     /region_name="pfam01023, S_100, S-100/ICaBP type calcium
                     binding domain. The S-100 domain is a subfamily of the
                     EF-hand calcium binding proteins"
     Region          20..33
                     /region_name="Calcium binding region"
     Region          59..71
                     /region_name="Calcium binding region"
     CDS             1..93
                     /gene="S100A8"
                     /coded_by="NM_002964.3:56..337"
                     /note="calgranulin A"
                     /db_xref="LocusID:6279"
                     /db_xref="MIM:123885"
ORIGIN      
        1 mltelekaln siidvyhkys likgnfhavy rddlkkllet ecpqyirkkg advwfkeldi
       61 ntdgavnfqe flilvikmgv aahkkshees hke
//



Revised: July 5, 2002.
 
 


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1: NP_001403. eukaryotic transl...[gi:4503499] Links  


LOCUS       EIF1A                    144 aa            linear   PRI 04-AUG-2002
DEFINITION  eukaryotic translation initiation factor 4C [Homo sapiens].
ACCESSION   NP_001403
VERSION     NP_001403.1  GI:4503499
DBSOURCE    REFSEQ: accession NM_001412.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 144)
  AUTHORS   Dever,T.E., Wei,C.L., Benkowski,L.A., Browning,K., Merrick,W.C. and
            Hershey,J.W.
  TITLE     Determination of the amino acid sequence of rabbit, human, and
            wheat germ protein synthesis factor eIF-4C by cloning and chemical
            sequencing
  JOURNAL   J. Biol. Chem. 269 (5), 3212-3218 (1994)
  MEDLINE   94148809
   PUBMED   8106356
REFERENCE   2  (residues 1 to 144)
  AUTHORS   Lahn,B.T. and Page,D.C.
  TITLE     Functional coherence of the human Y chromosome
  JOURNAL   Science 278 (5338), 675-680 (1997)
  MEDLINE   98022381
   PUBMED   9381176
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L18960.1.
FEATURES             Location/Qualifiers
     source          1..144
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="X"
                     /note="subject has leukemia"
     Protein         1..144
                     /product="eukaryotic translation initiation factor 4C"
     Region          26..113
                     /region_name="pfam01176, eIF-1a, Eukaryotic initiation
                     factor 1A"
     Region          28..110
                     /region_name="smart00652, eIF1a, eukaryotic translation
                     initiation factor 1A"
     CDS             1..144
                     /gene="EIF1A"
                     /coded_by="NM_001412.1:208..642"
                     /db_xref="LocusID:1964"
                     /db_xref="MIM:300186"
ORIGIN      
        1 mpknkgkggk nrrrgknene sekrelvfke dgqeyaqvik mlgngrleam cfdgvkrlch
       61 irgklrkkvw intsdiilvg lrdyqdnkad vilkynadea rslkaygelp ehakinetdt
      121 fgpgdddeiq fddigddded iddi
//



Revised: July 5, 2002.
 
 


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1: NP_003002. SET translocation...[gi:4506891] Links  


LOCUS       SET                      277 aa            linear   PRI 31-OCT-2000
DEFINITION  SET translocation (myeloid leukemia-associated); SET gene; SET,
            translocation [Homo sapiens].
ACCESSION   NP_003002
VERSION     NP_003002.1  GI:4506891
DBSOURCE    REFSEQ: accession NM_003011.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   von Lindern,M., van Baal,S., Wiegant,J., Raap,A., Hagemeijer,A. and
            Grosveld,G.
  TITLE     Can, a putative oncogene associated with myeloid leukemogenesis,
            may be activated by fusion of its 3' half to different genes:
            characterization of the set gene
  JOURNAL   Mol. Cell. Biol. 12 (8), 3346-3355 (1992)
  MEDLINE   92334332
   PUBMED   1630450
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Vaesen M, Barnikol-Watanabe S, Gotz H, Awni LA, Cole T, Zimmermann
            B, Kratzin HD and Hilschmann N.
  TITLE     Purification and characterization of two putative HLA class II
            associated proteins: PHAPI and PHAPII
  JOURNAL   Biol. Chem. Hoppe-Seyler 375 (2), 113-126 (1994)
  MEDLINE   94250340
   PUBMED   8192856
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Nagata,K., Kawase,H., Handa,H., Yano,K., Yamasaki,M., Ishimi,Y.,
            Okuda,A., Kikuchi,A. and Matsumoto,K.
  TITLE     Replication factor encoded by a putative oncogene, set, associated
            with myeloid leukemogenesis
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 92 (10), 4279-4283 (1995)
  MEDLINE   95273346
   PUBMED   7753797
REFERENCE   4  (residues 1 to 277)
  AUTHORS   Li,M., Makkinje,A. and Damuni,Z.
  TITLE     The myeloid leukemia-associated protein SET is a potent inhibitor
            of protein phosphatase 2A
  JOURNAL   J. Biol. Chem. 271 (19), 11059-11062 (1996)
  MEDLINE   96212163
   PUBMED   8626647
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M93651.1.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Homo sapiens"
                     /isolate="Acute undifferentiated leukemia patient"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34"
                     /sex="male"
                     /tissue_type="bone marrow; testis"
                     /tissue_lib="lambda EMBL3, lambda gt11"
     Protein         1..277
                     /product="SET translocation (myeloid leukemia-associated)"
                     /note="SET gene; SET, translocation"
     Region          22..225
                     /region_name="Nucleosome assembly protein (NAP)"
                     /note="NAP_family"
                     /db_xref="CDD:pfam00956"
     Region          29..76
                     /region_name="Nucleosome assembly protein (NAP)"
                     /note="NAP_family"
                     /db_xref="CDD:pfam00956"
     CDS             1..277
                     /gene="SET"
                     /coded_by="NM_003011.1:4..837"
                     /db_xref="LocusID:6418"
                     /db_xref="MIM:600960"
ORIGIN      
        1 msaqaakvsk kelnsnhdga detsekeqqe aiehidevqn eidrlneqas eeilkveqky
       61 nklrqpffqk rseliakipn fwvttfvnhp qvsallgeed eealhyltrv evtefediks
      121 gyridfyfde npyfenkvls kefhlnesgd pssksteikw ksgkdltkrs sqtqnkasrk
      181 rqheepesff twftdhsdag adelgevikd diwpnplqyy lvpdmddeeg egeeddddde
      241 eeegledide egdedegeed edddegeege edegedd
//



Revised: July 5, 2002.
 
 


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1: NP_005493. ATP-binding casse...[gi:21536376] Links  


LOCUS       ABCA1                   2261 aa            linear   PRI 27-AUG-2002
DEFINITION  ATP-binding cassette, sub-family A member 1; ATP-binding cassette
            1; high density lipoprotein deficiency, Tangier type, 1;
            cholesterol efflux regulatory protein [Homo sapiens].
ACCESSION   NP_005493
VERSION     NP_005493.2  GI:21536376
DBSOURCE    REFSEQ: accession NM_005502.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2261)
  AUTHORS   Luciani,M.F., Denizot,F., Savary,S., Mattei,M.G. and Chimini,G.
  TITLE     Cloning of two novel ABC transporters mapping on human chromosome 9
  JOURNAL   Genomics 21 (1), 150-159 (1994)
  MEDLINE   94375008
   PUBMED   8088782
REFERENCE   2  (residues 1 to 2261)
  AUTHORS   Becq,F., Hamon,Y., Bajetto,A., Gola,M., Verrier,B. and Chimini,G.
  TITLE     ABC1, an ATP binding cassette transporter required for phagocytosis
            of apoptotic cells, generates a regulated anion flux after
            expression in Xenopus laevis oocytes
  JOURNAL   J. Biol. Chem. 272 (5), 2695-2699 (1997)
  MEDLINE   97160572
   PUBMED   9006906
REFERENCE   3  (residues 1 to 2261)
  AUTHORS   Rust,S., Walter,M., Funke,H., von Eckardstein,A., Cullen,P.,
            Kroes,H.Y., Hordijk,R., Geisel,J., Kastelein,J., Molhuizen,H.O.,
            Schreiner,M., Mischke,A., Hahmann,H.W. and Assmann,G.
  TITLE     Assignment of Tangier disease to chromosome 9q31 by a graphical
            linkage exclusion strategy
  JOURNAL   Nat. Genet. 20 (1), 96-98 (1998)
  MEDLINE   98400267
   PUBMED   9731541
REFERENCE   4  (residues 1 to 2261)
  AUTHORS   Langmann,T., Klucken,J., Reil,M., Liebisch,G., Luciani,M.F.,
            Chimini,G., Kaminski,W.E. and Schmitz,G.
  TITLE     Molecular cloning of the human ATP-binding cassette transporter 1
            (hABC1): evidence for sterol-dependent regulation in macrophages
  JOURNAL   Biochem. Biophys. Res. Commun. 257 (1), 29-33 (1999)
  MEDLINE   99194549
   PUBMED   10092505
REFERENCE   5  (residues 1 to 2261)
  AUTHORS   Brooks-Wilson,A., Marcil,M., Clee,S.M., Zhang,L.H., Roomp,K., van
            Dam,M., Yu,L., Brewer,C., Collins,J.A., Molhuizen,H.O., Loubser,O.,
            Ouelette,B.F., Fichter,K., Ashbourne-Excoffon,K.J., Sensen,C.W.,
            Scherer,S., Mott,S., Denis,M., Martindale,D., Frohlich,J.,
            Morgan,K., Koop,B., Pimstone,S., Kastelein,J.J., Hayden,M.R. et al.
  TITLE     Mutations in ABC1 in Tangier disease and familial high-density
            lipoprotein deficiency
  JOURNAL   Nat. Genet. 22 (4), 336-345 (1999)
  MEDLINE   99364411
   PUBMED   10431236
REFERENCE   6  (residues 1 to 2261)
  AUTHORS   Bodzioch,M., Orso,E., Klucken,J., Langmann,T., Bottcher,A.,
            Diederich,W., Drobnik,W., Barlage,S., Buchler,C.,
            Porsch-Ozcurumez,M., Kaminski,W.E., Hahmann,H.W., Oette,K.,
            Rothe,G., Aslanidis,C., Lackner,K.J. and Schmitz,G.
  TITLE     The gene encoding ATP-binding cassette transporter 1 is mutated in
            Tangier disease
  JOURNAL   Nat. Genet. 22 (4), 347-351 (1999)
  MEDLINE   99364412
   PUBMED   10431237
REFERENCE   7  (residues 1 to 2261)
  AUTHORS   Rust,S., Rosier,M., Funke,H., Real,J., Amoura,Z., Piette,J.C.,
            Deleuze,J.F., Brewer,H.B., Duverger,N., Denefle,P. and Assmann,G.
  TITLE     Tangier disease is caused by mutations in the gene encoding
            ATP-binding cassette transporter 1
  JOURNAL   Nat. Genet. 22 (4), 352-355 (1999)
  MEDLINE   99364413
   PUBMED   10431238
REFERENCE   8  (residues 1 to 2261)
  AUTHORS   Lawn,R.M., Wade,D.P., Garvin,M.R., Wang,X., Schwartz,K.,
            Porter,J.G., Seilhamer,J.J., Vaughan,A.M. and Oram,J.F.
  TITLE     The Tangier disease gene product ABC1 controls the cellular
            apolipoprotein-mediated lipid removal pathway
  JOURNAL   J. Clin. Invest. 104 (8), R25-R31 (1999)
  MEDLINE   99454823
   PUBMED   10525055
REFERENCE   9  (residues 1 to 2261)
  AUTHORS   Remaley,A.T., Rust,S., Rosier,M., Knapper,C., Naudin,L.,
            Broccardo,C., Peterson,K.M., Koch,C., Arnould,I., Prades,C.,
            Duverger,N., Funke,H., Assman,G., Dinger,M., Dean,M., Chimini,G.,
            Santamarina-Fojo,S., Fredrickson,D.S., Denefle,P. and Brewer,H.B.
            Jr.
  TITLE     Human ATP-binding cassette transporter 1 (ABC1): genomic
            organization and identification of the genetic defect in the
            original Tangier disease kindred
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 96 (22), 12685-12690 (1999)
  MEDLINE   20006295
   PUBMED   10535983
REFERENCE   10 (residues 1 to 2261)
  AUTHORS   Pullinger,C.R., Hakamata,H., Duchateau,P.N., Eng,C.,
            Aouizerat,B.E., Cho,M.H., Fielding,C.J. and Kane,J.P.
  TITLE     Analysis of hABC1 gene 5' end: additional peptide sequence,
            promoter region, and four polymorphisms
  JOURNAL   Biochem. Biophys. Res. Commun. 271 (2), 451-455 (2000)
  MEDLINE   20261282
   PUBMED   10799318
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF165281.1 and AF275948.1.
            On Jun 21, 2002 this sequence version replaced gi:5915658.
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters.  ABC proteins transport various molecules across
            extra- and intracellular membranes.  ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White).  This protein is a member of the ABC1 subfamily.  Members
            of the ABC1 subfamily comprise the only major ABC subfamily found
            exclusively in multicellular eukaryotes.  With cholesterol as its
            substrate, this protein functions as a cholesteral efflux pump in
            the cellular lipid removal pathway.  Mutations in this gene have
            been associated with Tangier's disease and familial high-density
            lipoprotein deficiency.
FEATURES             Location/Qualifiers
     source          1..2261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q31.1"
     Protein         1..2261
                     /product="ATP-binding cassette, sub-family A member 1"
                     /note="ATP-binding cassette 1; high density lipoprotein
                     deficiency, Tangier type, 1; cholesterol efflux regulatory
                     protein"
     variation       219
                     /allele="R"
                     /allele="K"
                     /db_xref="dbSNP:2230806"
     variation       771
                     /allele="M"
                     /allele="V"
                     /db_xref="dbSNP:2066718"
     variation       825
                     /allele="I"
                     /allele="V"
                     /db_xref="dbSNP:2066715"
     variation       831
                     /allele="D"
                     /allele="N"
                     /db_xref="dbSNP:2472458"
     Region          926..1107
                     /region_name="pfam00005, ABC_tran, ABC transporter. ABC
                     transporters for a large family of proteins responsible
                     for translocation of a variety of compounds across
                     biological membranes. ABC transporters are the largest
                     family of proteins in many completely sequenced bacteria.
                     ABC transporters are composed of two copies of this domain
                     and two copies of a transmembrane domain pfam00664. These
                     four domains may belong to a single polypeptide or belong
                     in different polypeptide chains"
     variation       1005
                     /allele="K"
                     /allele="E"
                     /db_xref="dbSNP:2482437"
     variation       1555
                     /allele="I"
                     /allele="T"
                     /db_xref="dbSNP:1997618"
     variation       1587
                     /allele="R"
                     /allele="K"
                     /db_xref="dbSNP:2230808"
     variation       1648
                     /allele="P"
                     /allele="L"
                     /db_xref="dbSNP:1883024"
     Region          1939..2120
                     /region_name="pfam00005, ABC_tran, ABC transporter. ABC
                     transporters for a large family of proteins responsible
                     for translocation of a variety of compounds across
                     biological membranes. ABC transporters are the largest
                     family of proteins in many completely sequenced bacteria.
                     ABC transporters are composed of two copies of this domain
                     and two copies of a transmembrane domain pfam00664. These
                     four domains may belong to a single polypeptide or belong
                     in different polypeptide chains"
     CDS             1..2261
                     /gene="ABCA1"
                     /coded_by="NM_005502.2:314..7099"
                     /db_xref="LocusID:19"
                     /db_xref="MIM:600046"
ORIGIN      
        1 macwpqlrll lwknltfrrr qtcqllleva wplfiflili svrlsyppye qhechfpnka
       61 mpsagtlpwv qgiicnannp cfryptpgea pgvvgnfnks ivarlfsdar rlllysqkdt
      121 smkdmrkvlr tlqqikksss nlklqdflvd netfsgflyh nlslpkstvd kmlradvilh
      181 kvflqgyqlh ltslcngsks eemiqlgdqe vselcglpre klaaaervlr snmdilkpil
      241 rtlnstspfp skelaeatkt llhslgtlaq elfsmrswsd mrqevmfltn vnssssstqi
      301 yqavsrivcg hpeggglkik slnwyednny kalfggngte edaetfydns ttpycndlmk
      361 nlessplsri iwkalkpllv gkilytpdtp atrqvmaevn ktfqelavfh dlegmweels
      421 pkiwtfmens qemdlvrmll dsrdndhfwe qqldgldwta qdivaflakh pedvqssngs
      481 vytwreafne tnqairtisr fmecvnlnkl epiatevwli nksmellder kfwagivftg
      541 itpgsielph hvkykirmdi dnvertnkik dgywdpgpra dpfedmryvw ggfaylqdvv
      601 eqaiirvltg tekktgvymq qmpypcyvdd iflrvmsrsm plfmtlawiy svaviikgiv
      661 yekearlket mrimgldnsi lwfswfissl ipllvsagll vvilklgnll pysdpsvvfv
      721 flsvfavvti lqcflistlf sranlaaacg giiyftlylp yvlcvawqdy vgftlkifas
      781 llspvafgfg ceyfalfeeq gigvqwdnlf espveedgfn lttsvsmmlf dtflygvmtw
      841 yieavfpgqy giprpwyfpc tksywfgees dekshpgsnq kriseicmee epthlklgvs
      901 iqnlvkvyrd gmkvavdgla lnfyegqits flghngagkt ttmsiltglf pptsgtayil
      961 gkdirsemst irqnlgvcpq hnvlfdmltv eehiwfyarl kglsekhvka emeqmaldvg
     1021 lpssklkskt sqlsggmqrk lsvalafvgg skvvildept agvdpysrrg iwelllkyrq
     1081 grtiilsthh mdeadvlgdr iaiishgklc cvgsslflkn qlgtgyyltl vkkdvessls
     1141 scrnssstvs ylkkedsvsq sssdaglgsd hesdtltidv saisnlirkh vsearlvedi
     1201 gheltyvlpy eaakegafve lfheiddrls dlgissygis ettleeiflk vaeesgvdae
     1261 tsdgtlparr nrrafgdkqs clrpftedda adpndsdidp esretdllsg mdgkgsyqvk
     1321 gwkltqqqfv allwkrllia rrsrkgffaq ivlpavfvci alvfslivpp fgkypslelq
     1381 pwmyneqytf vsndapedtg tlellnaltk dpgfgtrcme gnpipdtpcq ageeewttap
     1441 vpqtimdlfq ngnwtmqnps pacqcssdki kkmlpvcppg agglpppqrk qntadilqdl
     1501 tgrnisdylv ktyvqiiaks lknkiwvnef ryggfslgvs ntqalppsqe vndaikqmkk
     1561 hlklakdssa drflnslgrf mtgldtknnv kvwfnnkgwh aissflnvin nailranlqk
     1621 genpshygit afnhplnltk qqlsevalmt tsvdvlvsic vifamsfvpa sfvvfliqer
     1681 vskakhlqfi sgvkpviywl snfvwdmcny vvpatlviii ficfqqksyv sstnlpvlal
     1741 llllygwsit plmypasfvf kipstayvvl tsvnlfigin gsvatfvlel ftdnklnnin
     1801 dilksvflif phfclgrgli dmvknqamad alerfgenrf vsplswdlvg rnlfamaveg
     1861 vvfflitvli qyrffirprp vnaklsplnd ededvrrerq rildgggqnd ileikeltki
     1921 yrrkrkpavd ricvgippge cfgllgvnga gksstfkmlt gdttvtrgda flnknsilsn
     1981 ihevhqnmgy cpqfdaitel ltgrehveff allrgvpeke vgkvgewair klglvkygek
     2041 yagnysggnk rklstamali ggppvvflde pttgmdpkar rflwncalsv vkegrsvvlt
     2101 shsmeeceal ctrmaimvng rfrclgsvqh lknrfgdgyt ivvriagsnp dlkpvqdffg
     2161 lafpgsvlke khrnmlqyql psslsslari fsilsqskkr lhiedysvsq ttldqvfvnf
     2221 akdqsdddhl kdlslhknqt vvdvavltsf lqdekvkesy v
//



Revised: July 5, 2002.
 
 


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Oct 21 2002 11:56:56 

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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_003015. intersectin 1 (SH...[gi:4504797] Links  


LOCUS       ITSN1                   1721 aa            linear   PRI 31-OCT-2000
DEFINITION  intersectin 1 (SH3 domain protein); intersectin (SH3 domain protein
            1A); SH3 domain protein-1A; human intersectin-SH3 domain-containing
            protein SH3P17 [Homo sapiens].
ACCESSION   NP_003015
VERSION     NP_003015.1  GI:4504797
DBSOURCE    REFSEQ: accession NM_003024.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1721)
  AUTHORS   Chen,H. and Antonarakis,S.E.
  TITLE     The SH3D1A gene maps to human chromosome 21q22.1-->q22.2
  JOURNAL   Cytogenet. Cell Genet. 78 (3-4), 213-215 (1997)
  MEDLINE   98127038
   PUBMED   9465890
REFERENCE   2  (residues 1 to 1721)
  AUTHORS   Guipponi,M., Scott,H.S., Chen,H., Schebesta,A., Rossier,C. and
            Antonarakis,S.E.
  TITLE     Two isoforms of a human intersectin (ITSN) protein are produced by
            brain-specific alternative splicing in a stop codon
  JOURNAL   Genomics 53 (3), 369-376 (1998)
  MEDLINE   99017974
   PUBMED   9799604
REFERENCE   3  (residues 1 to 1721)
  AUTHORS   Yamabhai,M., Hoffman,N.G., Hardison,N.L., McPherson,P.S.,
            Castagnoli,L., Cesareni,G. and Kay,B.K.
  TITLE     Intersectin, a novel adaptor protein with two Eps15 homology and
            five Src homology 3 domains
  JOURNAL   J. Biol. Chem. 273 (47), 31401-31407 (1998)
  MEDLINE   99030416
   PUBMED   9813051
REFERENCE   4  (residues 1 to 1721)
  AUTHORS   Guipponi,M., Scott,H.S., Hattori,M., Ishii,K., Sakaki,Y. and
            Antonarakis,S.E.
  TITLE     Genomic structure, sequence, and refined mapping of the human
            intersectin gene (ITSN), which encompasses 250 kb on chromosome
            21q22.1-->q22.2
  JOURNAL   Cytogenet. Cell Genet. 83 (3-4), 218-220 (1998)
  MEDLINE   99172091
   PUBMED   10072581
REFERENCE   5  (residues 1 to 1721)
  AUTHORS   Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS,
            Toyoda A, Ishii K, Totoki Y, Choi DK, Soeda E, Ohki M, Takagi T,
            Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J,
            Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M
            and Schudy A.
  TITLE     The DNA sequence of human chromosome 21. The chromosome 21 mapping
            and sequencing consortium
  JOURNAL   Nature 405 (6784), 311-319 (2000)
  MEDLINE   20289799
   PUBMED   10830953
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF064244.1.
FEATURES             Location/Qualifiers
     source          1..1721
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.1-q22.2"
                     /tissue_type="brain"
                     /dev_stage="fetus"
     Protein         1..1721
                     /product="intersectin 1 (SH3 domain protein)"
                     /note="intersectin (SH3 domain protein 1A); SH3 domain
                     protein-1A; human intersectin-SH3 domain-containing
                     protein SH3P17"
     Region          15..100
                     /region_name="Eps15 homology domain"
                     /note="EH"
                     /db_xref="CDD:EH"
     Region          214..292
                     /region_name="Eps15 homology domain"
                     /note="EH"
                     /db_xref="CDD:EH"
     Region          471..674
                     /region_name="Myosin tail"
                     /note="Myosin_tail"
                     /db_xref="CDD:pfam01576"
     Region          551..677
                     /region_name="Ezrin/radixin/moesin family"
                     /note="ERM"
                     /db_xref="CDD:pfam00769"
     Region          744..804
                     /region_name="SH3 domain"
                     /note="SH3"
                     /db_xref="CDD:pfam00018"
     Region          744..804
                     /region_name="Src homology 3 domains"
                     /note="SH3"
                     /db_xref="CDD:SH3"
     Region          917..969
                     /region_name="SH3 domain"
                     /note="SH3"
                     /db_xref="CDD:pfam00018"
     Region          917..969
                     /region_name="Src homology 3 domains"
                     /note="SH3"
                     /db_xref="CDD:SH3"
     Region          1004..1056
                     /region_name="Src homology 3 domains"
                     /note="SH3"
                     /db_xref="CDD:SH3"
     Region          1005..1056
                     /region_name="SH3 domain"
                     /note="SH3"
                     /db_xref="CDD:pfam00018"
     Region          1076..1134
                     /region_name="Src homology 3 domains"
                     /note="SH3"
                     /db_xref="CDD:SH3"
     Region          1077..1133
                     /region_name="SH3 domain"
                     /note="SH3"
                     /db_xref="CDD:pfam00018"
     Region          1158..1210
                     /region_name="Src homology 3 domains"
                     /note="SH3"
                     /db_xref="CDD:SH3"
     Region          1159..1209
                     /region_name="SH3 domain"
                     /note="SH3"
                     /db_xref="CDD:pfam00018"
     Region          1242..1422
                     /region_name="Guanine nucleotide exchange factor for
                     Rho/Rac/Cdc42-like GTPases"
                     /note="RhoGEF"
                     /db_xref="CDD:RhoGEF"
     Region          1242..1422
                     /region_name="RhoGEF domain"
                     /note="RhoGEF"
                     /db_xref="CDD:pfam00621"
     Region          1597..1681
                     /region_name="Protein kinase C conserved region 2 (CalB)"
                     /note="C2"
                     /db_xref="CDD:C2"
     Region          1598..1677
                     /region_name="C2 domain"
                     /note="C2"
                     /db_xref="CDD:pfam00168"
     CDS             1..1721
                     /gene="ITSN1"
                     /coded_by="NM_003024.1:107..5272"
                     /db_xref="LocusID:6453"
                     /db_xref="MIM:602442"
ORIGIN      
        1 maqfptpfgg sldiwaitve erakhdqqfh slkpisgfit gdqarnfffq sglpqpvlaq
       61 iwaladmnnd grmdqvefsi amkliklklq gyqlpsalpp vmkqqpvais sappfgmggi
      121 asmppltava pvpmgsipvv gmsptlvssv ptaavpplan gappviqplp afahpaatlp
      181 ksssfsrsgp gsqlntklqk aqsfdvasvp pvaewavpqs srlkyrqlfn shdktmsghl
      241 tgpqartilm qsslpqaqla siwnlsdidq dgkltaeefi lamhlidvam sgqplppvlp
      301 peyippsfrr vrsgsgisvi sstsvdqrlp eepvledeqq qlekklpvtf edkkrenfer
      361 gnlelekrrq alleqqrkeq erlaqlerae qerkererqe qerkrqlele kqlekqrele
      421 rqreeerrke ierreaakre lerqrqlewe rnrrqellnq rnkeqedivv lkakkktlef
      481 elealndkkh qlegklqdir crlttqrqei estnksrelr iaeithlqqq lqesqqmlgr
      541 lipekqilnd qlkqvqqnsl hrdslvtlkr aleakelarq hlrdqldeve ketrsklqei
      601 difnnqlkel reihnkqqlq kqksmeaerl kqkeqerkii elekqkeeaq rraqerdkqw
      661 lehvqqedeh qrprklheee klkreesvkk kdgeekgkqe aqdklgrlfh qhqepakpav
      721 qapwstaekg pltisaqenv kvvyyralyp fesrshdeit iqpgdivmvk gewvdesqtg
      781 epgwlggelk gktgwfpany aekipenevp apvkpvtdst sapapklalr etpaplavts
      841 sepsttpnnw adfsstwpts tnekpetdnw dawaaqpslt vpsagqlrqr saftpatatg
      901 sspspvlgqg ekveglqaqa lypwrakkdn hlnfnkndvi tvleqqdmww fgevqgqkgw
      961 fpksyvklis gpirkstsmd sgssespasl krvaspaakp vvsgeefiam ytyesseqgd
     1021 ltfqqgdvil vtkkdgdwwt gtvgdkagvf psnyvrlkds egsgtagktg slgkkpeiaq
     1081 viasytatgp eqltlapgql ilirkknpgg wwegelqarg kkrqigwfpa nyvkllnpgt
     1141 skitpteppk stalaavcqv igmydytaqn ddelafnkgq iinvlnkedp dwwkgevngq
     1201 vglfpsnyvk lttdmdpsqq wcsdlhlldm ltpterkrqg yihelivtee nyvndlqlvt
     1261 eifqkplmes elltekevam ifvnwkelim cnikllkalr vrkkmsgekm pvkmigdils
     1321 aqlphmqpyi rfcsrqlnga aliqqktdea pdfkefvkrl emdprckgmp lssfilkpmq
     1381 rvtrypliik nilentpenh pdhshlkhal ekaeelcsqv negvrekens drlewiqahv
     1441 qceglseqlv fnsvtnclgp rkflhsgkly kaknnkelyg flfndflllt qitkplgssg
     1501 tdkvfspksn lqykmyktpi flnevlvklp tdpsgdepif hishidrvyt lraesinert
     1561 awvqkikaas elyietekkk rekaylvrsq ratgigrlmv nvvegielkp crshgksnpy
     1621 cevtmgsqch itktiqdtln pkwnsncqff irdleqevlc itvferdqfs pddflgrtei
     1681 rvadikkdqg skgpvtkcll lhevptgeiv vrldlqlfde p
//



Revised: July 5, 2002.
 
 


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1: NP_002493. nuclear factor of...[gi:19923223] Links  


LOCUS       NFKB2                    933 aa            linear   PRI 04-APR-2002
DEFINITION  nuclear factor of kappa light polypeptide gene enhancer in B-cells
            2 (p49/p100); Nuclear factor of kappa light chain gene enhancer in
            B-cells 2 [Homo sapiens].
ACCESSION   NP_002493
VERSION     NP_002493.2  GI:19923223
DBSOURCE    REFSEQ: accession NM_002502.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X61498.1.
            On Apr 4, 2002 this sequence version replaced gi:4505383.
FEATURES             Location/Qualifiers
     source          1..933
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q24"
     Protein         1..933
                     /product="nuclear factor of kappa light polypeptide gene
                     enhancer in B-cells 2 (p49/p100)"
                     /note="Nuclear factor of kappa light chain gene enhancer
                     in B-cells 2"
     Region          37..220
                     /region_name="Rel homology domain (RHD)"
                     /note="RHD"
                     /db_xref="CDD:pfam00554"
     Region          227..326
                     /region_name="ig-like, plexins, transcription factors"
                     /note="IPT"
                     /db_xref="CDD:smart00429"
     Region          229..326
                     /region_name="IPT/TIG domain"
                     /note="TIG"
                     /db_xref="CDD:pfam01833"
     Region          527..557
                     /region_name="Ank repeat"
                     /note="ank"
                     /db_xref="CDD:pfam00023"
     Region          598..628
                     /region_name="Ank repeat"
                     /note="ank"
                     /db_xref="CDD:pfam00023"
     Region          667..695
                     /region_name="Ank repeat"
                     /note="ank"
                     /db_xref="CDD:pfam00023"
     Region          667..695
                     /region_name="ankyrin repeats"
                     /note="ANK"
                     /db_xref="CDD:smart00248"
     CDS             1..933
                     /gene="NFKB2"
                     /coded_by="NM_002502.2:164..2965"
                     /db_xref="LocusID:4791"
                     /db_xref="MIM:164012"
ORIGIN      
        1 mescynpgld giieyddfkl nssivepkep apetadgpyl viveqpkqrg frfrygcegp
       61 shgglpgass ekgrktyptv kicnyegpak ievdlvthsd pprahahslv gkqcselgic
      121 avsvgpkdmt aqfnnlgvlh vtkknmmgtm iqklqrqrlr srpqglteae qreleqeake
      181 lkkvmdlsiv rlrfsaflra sdgsfslplk pvtsqpihds kspgasnlki srmdktagsv
      241 rggdevyllc dkvqkddiev rfyeddengw qafgdfsptd vhkqyaivfr tppyhkmkie
      301 rpvtvflqlk rkrggdvsds kqftyyplve dkeevqrkrr kalptfsqpf gggshmgggs
      361 ggaaggygga ggggslgffp sslayspyqs gagpmrcypg ggggaqmaat vpsrdsgeea
      421 aepsapsrtp qcepqapeml qrareynarl fglahaapsp trllrhrgrr allagqrhll
      481 taqdengdtp lhlaiihgqt svieqivyvi hhaqdlgvvn ltnhlhqtpl hlavitgqts
      541 vvsfllrvga dpalldrhgd samhlalrag agapellral lqsgapavpq llhmpdfegl
      601 ypvhlavrar specldllvd sgaeveater qggrtalhla temeelglvt hlvtklranv
      661 nartfagntp lhlaaglgyp tltrlllkag adihaeneep lcplpsppts dsdsdsegpe
      721 kdtrssfrgh tpldltcstl vktlllnaaq ntmeppltpp spagpglslg dtalqnleql
      781 ldgpeaqgsw aelaerlglr slvdtyrqtt spsgsllrsy elaggdlagl lealsdmgle
      841 egvrllrgpe trdklpstev kedsaygsqs veqeaeklgp ppeppgglsh ghpqpqvtdl
      901 lpapsplpgp pvqrphlfqi lfntphppls wdk
//



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1: NP_005555. lipocalin 2 (onco...[gi:5031853] Links  


LOCUS       LCN2                     198 aa            linear   PRI 01-NOV-2000
DEFINITION  lipocalin 2 (oncogene 24p3) [Homo sapiens].
ACCESSION   NP_005555
VERSION     NP_005555.1  GI:5031853
DBSOURCE    REFSEQ: accession NM_005564.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 198)
  AUTHORS   Kjeldsen,L., Johnsen,A.H., Sengelov,H. and Borregaard,N.
  TITLE     Isolation and primary structure of NGAL, a novel protein associated
            with human neutrophil gelatinase
  JOURNAL   J. Biol. Chem. 268 (14), 10425-10432 (1993)
  MEDLINE   93252928
   PUBMED   7683678
REFERENCE   2  (residues 1 to 198)
  AUTHORS   Bundgaard,J.R., Sengelov,H., Borregaard,N. and Kjeldsen,L.
  TITLE     Molecular cloning and expression of a cDNA encoding NGAL: a
            lipocalin expressed in human neutrophils
  JOURNAL   Biochem. Biophys. Res. Commun. 202 (3), 1468-1475 (1994)
  MEDLINE   94338365
   PUBMED   8060329
REFERENCE   3  (residues 1 to 198)
  AUTHORS   Cowland,J.B. and Borregaard,N.
  TITLE     Molecular characterization and pattern of tissue expression of the
            gene for neutrophil gelatinase-associated lipocalin from humans
  JOURNAL   Genomics 45 (1), 17-23 (1997)
  MEDLINE   97480711
   PUBMED   9339356
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X99133.1.
FEATURES             Location/Qualifiers
     source          1..198
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34"
                     /cell_type="leukocyte"
     Protein         1..198
                     /product="lipocalin 2 (oncogene 24p3)"
     Region          46..189
                     /region_name="Lipocalin / cytosolic fatty-acid binding
                     protein family"
                     /note="lipocalin"
                     /db_xref="CDD:pfam00061"
     CDS             1..198
                     /gene="LCN2"
                     /coded_by="NM_005564.1:1..597"
                     /db_xref="LocusID:3934"
                     /db_xref="MIM:600181"
ORIGIN      
        1 mplgllwlgl allgalhaqa qdstsdlipa pplskvplqq nfqdnqfqgk wyvvglagna
       61 ilredkdpqk myatiyelke dksynvtsvl frkkkcdywi rtfvpgcqpg eftlgniksy
      121 pgltsylvrv vstnynqham vffkkvsqnr eyfkitlygr tkeltselke nfirfskylg
      181 lpenhivfpv pidqcidg
//



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1: NP_002347. myristoylated ala...[gi:11125772] Links  


LOCUS       MARCKS                   332 aa            linear   PRI 27-AUG-2002
DEFINITION  myristoylated alanine-rich protein kinase C substrate; 80K-L;
            phosphomyristin; myristoylated alanine-rich protein kinase C
            substrate (MARCKS, 80K-L) [Homo sapiens].
ACCESSION   NP_002347
VERSION     NP_002347.4  GI:11125772
DBSOURCE    REFSEQ: accession NM_002356.4
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Harlan,D.M., Graff,J.M., Stumpo,D.J., Eddy,R.L. Jr., Shows,T.B.,
            Boyle,J.M. and Blackshear,P.J.
  TITLE     The human myristoylated alanine-rich C kinase substrate (MARCKS)
            gene (MACS). Analysis of its gene product, promoter, and
            chromosomal localization
  JOURNAL   J. Biol. Chem. 266 (22), 14399-14405 (1991)
  MEDLINE   91317795
   PUBMED   1860846
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Hartwig,J.H., Thelen,M., Rosen,A., Janmey,P.A., Nairn,A.C. and
            Aderem,A.
  TITLE     MARCKS is an actin filament crosslinking protein regulated by
            protein kinase C and calcium-calmodulin
  JOURNAL   Nature 356 (6370), 618-622 (1992)
  MEDLINE   92220195
   PUBMED   1560845
REFERENCE   3  (sites)
  AUTHORS   Sakai,K., Hirai,M., Kudoh,J., Minoshima,S. and Shimizu,N.
  TITLE     Molecular cloning and chromosomal mapping of a cDNA encoding human
            80K-L protein: major substrate for protein kinase C
  JOURNAL   Genomics 14 (1), 175-178 (1992)
  MEDLINE   93052291
   PUBMED   1427823
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Blackshear,P.J.
  TITLE     The MARCKS family of cellular protein kinase C substrates
  JOURNAL   J. Biol. Chem. 268 (3), 1501-1504 (1993)
  MEDLINE   93131879
   PUBMED   8420923
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Taniguchi,H. and Manenti,S.
  TITLE     Interaction of myristoylated alanine-rich protein kinase C
            substrate (MARCKS) with membrane phospholipids
  JOURNAL   J. Biol. Chem. 268 (14), 9960-9963 (1993)
  MEDLINE   93252971
   PUBMED   8486722
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Rao,P.H., Murty,V.V., Gaidano,G., Hauptschein,R., Dalla-Favera,R.
            and Chaganti,R.S.
  TITLE     Subregional mapping of 8 single copy loci to chromosome 6 by
            fluorescence in situ hybridization
  JOURNAL   Cytogenet. Cell Genet. 66 (4), 272-273 (1994)
  MEDLINE   94215320
   PUBMED   8162705
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Aderem,A.
  TITLE     The MARCKS family of protein kinase-C substrates
  JOURNAL   Biochem. Soc. Trans. 23 (3), 587-591 (1995)
  MEDLINE   96077232
   PUBMED   8566422
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D10522.1.
            On Nov 8, 2000 this sequence version replaced gi:11064247.
            Summary: The protein encoded by this gene is a substrate for
            protein kinase C. It is localized to the plasma membrane and is an
            actin filament crosslinking protein. Phosphorylation by protein
            kinase C or binding to calcium-calmodulin inhibits its association
            with actin and with the plasma membrane, leading to its presence in
            the cytoplasm. The protein is thought to be involved in cell
            motility, phagocytosis, membrane trafficking and mitogenesis.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.2"
     Protein         1..332
                     /product="myristoylated alanine-rich protein kinase C
                     substrate"
                     /note="80K-L; phosphomyristin; myristoylated alanine-rich
                     protein kinase C substrate (MARCKS, 80K-L)"
     misc_feature    1..7
                     /note="myristoylation domain"
     misc_feature    152..176
                     /note="phosphorylation site domain"
     CDS             1..332
                     /gene="MARCKS"
                     /coded_by="NM_002356.4:370..1368"
                     /db_xref="LocusID:4082"
                     /db_xref="MIM:177061"
ORIGIN      
        1 mgaqfsktaa kgeaaaerpg eaavasspsk angqenghvk vngdaspaaa esgakeelqa
       61 ngsapaadke epaaagsgaa spssaekgep aaaaapeaga spvekeapae geaaepgsat
      121 aaegeaasaa sstsspkaed gatpspsnet pkkkkkrfsf kksfklsgfs fkknkkeage
      181 ggeaeapaae ggkdeaagga aaaaaeagaa sgeqaaapge eaaageegaa ggdpqeakpq
      241 eaavapekpp asdetkaaee pskveekkae eagasaaace apsaagpgap peqeaapaee
      301 paaaaassac aapsqeaqpe cspeappaea ae
//



Revised: July 5, 2002.
 
 


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1: NP_036515. osteoclast stimul...[gi:21361409] Links  


LOCUS       OSTF1                    217 aa            linear   PRI 10-JUN-2002
DEFINITION  osteoclast stimulating factor 1 [Homo sapiens].
ACCESSION   NP_036515
VERSION     NP_036515.2  GI:21361409
DBSOURCE    REFSEQ: accession NM_012383.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Strausberg,R.
  TITLE     Homo sapiens osteoclast stimulating factor 1 (OSTF1), mRNA
  JOURNAL   Unpublished (2001)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC007459.1.
            On Jun 10, 2002 this sequence version replaced gi:6912564.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.1-24.2"
                     /clone="MGC:12230 IMAGE:4052054"
                     /tissue_type="Kidney, hypernephroma"
                     /clone_lib="NIH_MGC_58"
                     /lab_host="DH10B"
                     /note="Vector: pDNR-LIB"
     Protein         1..217
                     /product="osteoclast stimulating factor 1"
     Region          20..71
                     /region_name="SH3 domain"
                     /note="SH3"
                     /db_xref="CDD:pfam00018"
     Region          20..71
                     /region_name="Src homology 3 domains"
                     /note="SH3"
                     /db_xref="CDD:smart00326"
     Region          109..141
                     /region_name="Ank repeat"
                     /note="ank"
                     /db_xref="CDD:pfam00023"
     Region          143..173
                     /region_name="Ank repeat"
                     /note="ank"
                     /db_xref="CDD:pfam00023"
     Region          143..167
                     /region_name="ankyrin repeats"
                     /note="ANK"
                     /db_xref="CDD:smart00248"
     CDS             1..217
                     /gene="OSTF1"
                     /coded_by="NM_012383.2:109..762"
                     /db_xref="LocusID:26578"
ORIGIN      
        1 mskpppkpvk pgeggqvkvf ralytfeprt pdelyfeegd iiyitdmsdt nwwkgtskgr
       61 tglipsnyva eqaesidnpl heaakrgnls wlrecldnrv gvngldkags talywachgg
      121 hkdivemlft qpnielnqqn klgdtalhaa awkgyadivq lflakgartd lrniekklaf
      181 dmatnaacas llkkkqgtda vrtlsnaedy lddedsd
//



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1: NP_001701. complement factor...[gi:4502397] Links  


LOCUS       BF                       764 aa            linear   PRI 25-JUN-2001
DEFINITION  complement factor B preproprotein; B-factor, properdin; C3
            proactivator; C3 proaccelerator; glycine-rich beta-glycoprotein;
            C3/C5 convertase [Homo sapiens].
ACCESSION   NP_001701
VERSION     NP_001701.1  GI:4502397
DBSOURCE    REFSEQ: accession NM_001710.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Woods,D.E., Markham,A.F., Ricker,A.T., Goldberger,G. and
            Colten,H.R.
  TITLE     Isolation of cDNA clones for the human complement protein factor B,
            a class III major histocompatibility complex gene product
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 79 (18), 5661-5665 (1982)
  MEDLINE   83039428
   PUBMED   6957884
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Campbell,R.D. and Porter,R.R.
  TITLE     Molecular cloning and characterization of the gene coding for human
            complement protein factor B
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 80 (14), 4464-4468 (1983)
  MEDLINE   83273641
   PUBMED   6308626
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Morley,B.J. and Campbell,R.D.
  TITLE     Internal homologies of the Ba fragment from human complement
            component Factor B, a class III MHC antigen
  JOURNAL   EMBO J. 3 (1), 153-157 (1984)
  MEDLINE   84158524
   PUBMED   6323161
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Mole,J.E., Anderson,J.K., Davison,E.A. and Woods,D.E.
  TITLE     Complete primary structure for the zymogen of human complement
            factor B
  JOURNAL   J. Biol. Chem. 259 (6), 3407-3412 (1984)
  MEDLINE   84161997
   PUBMED   6546754
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Campbell RD, Bentley DR and Morley BJ.
  TITLE     The factor B and C2 genes
  JOURNAL   Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306 (1129), 367-378
            (1984)
  MEDLINE   85038857
   PUBMED   6149579
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Campbell,R.D.
  TITLE     The molecular genetics and polymorphism of C2 and factor B
  JOURNAL   Br. Med. Bull. 43 (1), 37-49 (1987)
  MEDLINE   88051634
   PUBMED   3315100
REFERENCE   7  (residues 1 to 764)
  AUTHORS   Wu,L.C., Morley,B.J. and Campbell,R.D.
  TITLE     Cell-specific expression of the human complement protein factor B
            gene: evidence for the role of two distinct 5'-flanking elements
  JOURNAL   Cell 48 (2), 331-342 (1987)
  MEDLINE   87102880
   PUBMED   3643061
REFERENCE   8  (residues 1 to 764)
  AUTHORS   Davrinche,C., Abbal,M. and Clerc,A.
  TITLE     Molecular characterization of human complement factor B subtypes
  JOURNAL   Immunogenetics 32 (5), 309-312 (1990)
  MEDLINE   91065702
   PUBMED   2249879
REFERENCE   9  (residues 1 to 764)
  AUTHORS   Schwaeble,W., Luttig,B., Sokolowski,T., Estaller,C., Weiss,E.H.,
            Meyer zum Buschenfelde,K.H., Whaley,K. and Dippold,W.
  TITLE     Human complement factor B: functional properties of a recombinant
            zymogen of the alternative activation pathway convertase
  JOURNAL   Immunobiology 188 (3), 221-232 (1993)
  MEDLINE   94041399
   PUBMED   8225386
REFERENCE   10 (residues 1 to 764)
  AUTHORS   Horiuchi,T., Kim,S., Matsumoto,M., Watanabe,I., Fujita,S. and
            Volanakis,J.E.
  TITLE     Human complement factor B: cDNA cloning, nucleotide sequencing,
            phenotypic conversion by site-directed mutagenesis and expression
  JOURNAL   Mol. Immunol. 30 (17), 1587-1592 (1993)
  MEDLINE   94067177
   PUBMED   8247029
REFERENCE   11 (residues 1 to 764)
  AUTHORS   Mejia,J.E., Jahn,I., de la Salle,H. and Hauptmann,G.
  TITLE     Human factor B. Complete cDNA sequence of the BF*S allele
  JOURNAL   Hum. Immunol. 39 (1), 49-53 (1994)
  MEDLINE   94237735
   PUBMED   8181962
REFERENCE   12 (residues 1 to 764)
  AUTHORS   Yu CY.
  TITLE     Molecular genetics of the human MHC complement gene cluster
  JOURNAL   Exp. Clin. Immunogenet. 15 (4), 213-230 (1998)
  MEDLINE   99171993
   PUBMED   10072631
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L15702.1 and BC004143.1.
            Summary: This gene encodes complement factor B, a component of the
            alternative pathway of complement activation. Factor B circulates
            in the blood as a single chain polypeptide. Upon activation of the
            alternative pathway, it is cleaved by complement factor D yielding
            the noncatalytic chain Ba and the catalytic subunit Bb. The active
            subunit Bb is a serine protease which associates with C3b to form
            the alternative pathway C3 convertase. Bb is involved in the
            proliferation of preactivated B lymphocytes, while Ba inhibits
            their proliferation. This gene localizes to the major
            histocompatibility complex (MHC) class III region on chromosome 6.
            This cluster includes several genes involved in regulation of the
            immune reaction. The polyadenylation site of this gene is 421 bp
            from the 5' end of the gene for complement component 2.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.3"
     Protein         1..764
                     /product="complement factor B preproprotein"
                     /EC_number="3.4.21.47"
                     /note="B-factor, properdin; C3 proactivator; C3
                     proaccelerator; glycine-rich beta-glycoprotein; C3/C5
                     convertase"
     sig_peptide     1..25
     Proprotein      26..764
     mat_peptide     26..259
                     /product="Ba"
     variation       32
                     /allele="Q"
                     /allele="R"
                     /db_xref="dbSNP:641153"
     Region          55..83
                     /region_name="Domain abundant in complement control
                     proteins"
                     /note="CCP"
                     /db_xref="CDD:smart00032"
     Region          103..158
                     /region_name="Domain abundant in complement control
                     proteins"
                     /note="CCP"
                     /db_xref="CDD:smart00032"
     Region          103..158
                     /region_name="Sushi domain (SCR repeat)"
                     /note="sushi"
                     /db_xref="CDD:pfam00084"
     Region          165..218
                     /region_name="Domain abundant in complement control
                     proteins"
                     /note="CCP"
                     /db_xref="CDD:smart00032"
     Region          168..218
                     /region_name="Sushi domain (SCR repeat)"
                     /note="sushi"
                     /db_xref="CDD:pfam00084"
     mat_peptide     260..764
                     /product="Bb"
     Region          269..470
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          270..468
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     variation       365
                     /allele="I"
                     /allele="M"
                     /db_xref="dbSNP:1803306"
     Region          488..751
                     /region_name="Trypsin-like serine protease"
                     /note="Tryp_SPc"
                     /db_xref="CDD:smart00020"
     Region          491..752
                     /region_name="Trypsin"
                     /note="trypsin"
                     /db_xref="CDD:pfam00089"
     CDS             1..764
                     /gene="BF"
                     /coded_by="NM_001710.2:130..2424"
                     /db_xref="LocusID:629"
                     /db_xref="MIM:138470"
ORIGIN      
        1 mgsnlspqlc lmpfilglls ggvtttpwsl aqpqgscsle gveikggsfr llqegqaley
       61 vcpsgfypyp vqtrtcrstg swstlktqdq ktvrkaecra ihcprphdfe ngeywprspy
      121 ynvsdeisfh cydgytlrgs anrtcqvngr wsgqtaicdn gagycsnpgi pigtrkvgsq
      181 yrledsvtyh csrgltlrgs qrrtcqeggs wsgtepscqd sfmydtpqev aeaflsslte
      241 tiegvdaedg hgpgeqqkrk ivldpsgsmn iylvldgsds igasnftgak kclvnliekv
      301 asygvkpryg lvtyatypki wvkvseadss nadwvtkqln einyedhklk sgtntkkalq
      361 avysmmswpd dvppegwnrt rhviilmtdg lhnmggdpit videirdlly igkdrknpre
      421 dyldvyvfgv gplvnqvnin alaskkdneq hvfkvkdmen ledvfyqmid esqslslcgm
      481 vwehrkgtdy hkqpwqakis virpskghes cmgavvseyf vltaahcftv ddkehsikvs
      541 vggekrdlei evvlfhpnyn ingkkeagip efydydvali klknklkygq tirpiclpct
      601 egttralrlp ptttcqqqke ellpaqdika lfvseeekkl trkevyikng dkkgscerda
      661 qyapgydkvk disevvtprf lctggvspya dpntcrgdsg gplivhkrsr fiqvgviswg
      721 vvdvcknqkr qkqvpahard fhinlfqvlp wlkeklqded lgfl
//



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1: NP_005401. selenoprotein P p...[gi:11038621] Links  


LOCUS       SEPP1                    381 aa            linear   PRI 16-NOV-2000
DEFINITION  selenoprotein P precursor [Homo sapiens].
ACCESSION   NP_005401
VERSION     NP_005401.2  GI:11038621
DBSOURCE    REFSEQ: accession NM_005410.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Hill KE, Lloyd RS and Burk RF.
  TITLE     Conserved nucleotide sequences in the open reading frame and 3'
            untranslated region of selenoprotein P mRNA
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 90 (2), 537-541 (1993)
  MEDLINE   93133823
   PUBMED   8421687
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Hill KE, Dasouki M, Phillips JA 3rd and Burk RF.
  TITLE     Human selenoprotein P gene maps to 5q31
  JOURNAL   Genomics 36 (3), 550-551 (1996)
  MEDLINE   97038702
   PUBMED   8884283
REFERENCE   3  (residues 1 to 381)
  AUTHORS   Mostert,V., Lombeck,I. and Abel,J.
  TITLE     A novel method for the purification of selenoprotein P from human
            plasma
  JOURNAL   Arch. Biochem. Biophys. 357 (2), 326-330 (1998)
  MEDLINE   98413836
   PUBMED   9735174
REFERENCE   4  (residues 1 to 381)
  AUTHORS   Mostert,V.
  TITLE     Selenoprotein P: properties, functions, and regulation
  JOURNAL   Arch. Biochem. Biophys. 376 (2), 433-438 (2000)
  MEDLINE   20239644
   PUBMED   10775431
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z11793.1.
            On Oct 30, 2000 this sequence version replaced gi:4885591.
            Summary: Selenoprotein P is an extracellular glycoprotein and is
            the only selenoprotein known to contain multiple selenocysteine
            residues. Two isoforms of this protein are Sep51 and Sep61. Sep51
            lacks part of the C-terminal sequence. Selenoprotein P binds
            heparin and associates with endothelial cells. They are implicated
            as an oxidant defense in the extracellular space and in the
            transport of selenium.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31"
     Protein         1..381
                     /product="selenoprotein P precursor"
     sig_peptide     1..19
     mat_peptide     20..381
                     /product="selenoprotein P"
     CDS             1..381
                     /gene="SEPP1"
                     /coded_by="NM_005410.1:37..1182"
                     /note="tga codes for  selenocysteine; encodes 61 kDa
                     protein"
                     /db_xref="LocusID:6414"
                     /db_xref="MIM:601484"
ORIGIN      
        1 mwrslglala lcllpsggte sqdqsslckq ppawsirdqd pmlnsngsvt vvallqasuy
       61 lciieaskle dlrvklkkeg ysnisyivvn hqgissrlky thlknkvseh ipvyqqeenq
      121 tdvwtllngs kddfliydrc grlvyhlglp fsfltfpyve eaikiaycek kcgncslttl
      181 kdedfckrvs latvdktvet psphyhhehh hnhghqhlgs selsenqqpg apnapthpap
      241 pglhhhhkhk gqhrqghpen rdmpasedlq dlqkklcrkr cinqllcklp tdselaprsu
      301 cchcrhlife ktgsaituqc kenlpslcsu qglraeenit escqurlppa auqisqqlip
      361 teasasuruk nqakkueups n
//



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1: NP_003864. neuropilin 1 [Hom...[gi:4505457] Links  


LOCUS       NRP1                     923 aa            linear   PRI 01-NOV-2000
DEFINITION  neuropilin 1 [Homo sapiens].
ACCESSION   NP_003864
VERSION     NP_003864.1  GI:4505457
DBSOURCE    REFSEQ: accession NM_003873.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 923)
  AUTHORS   He,Z. and Tessier-Lavigne,M.
  TITLE     Neuropilin is a receptor for the axonal chemorepellent Semaphorin
            III
  JOURNAL   Cell 90 (4), 739-751 (1997)
  MEDLINE   97433084
   PUBMED   9288753
REFERENCE   2  (residues 1 to 923)
  AUTHORS   Chen,H., Chedotal,A., He,Z., Goodman,C.S. and Tessier-Lavigne,M.
  TITLE     Neuropilin-2, a novel member of the neuropilin family, is a high
            affinity receptor for the semaphorins Sema E and Sema IV but not
            Sema III
  JOURNAL   Neuron 19 (3), 547-559 (1997)
  MEDLINE   97470888
   PUBMED   9331348
REFERENCE   3  (residues 1 to 923)
  AUTHORS   Soker,S., Takashima,S., Miao,H.Q., Neufeld,G. and Klagsbrun,M.
  TITLE     Neuropilin-1 is expressed by endothelial and tumor cells as an
            isoform-specific receptor for vascular endothelial growth factor
  JOURNAL   Cell 92 (6), 735-745 (1998)
  MEDLINE   98188099
   PUBMED   9529250
REFERENCE   4  (residues 1 to 923)
  AUTHORS   Rossignol,M., Beggs,A.H., Pierce,E.A. and Klagsbrun,M.
  TITLE     Human neuropilin-1 and neuropilin-2 map to 10p12 and 2q34,
            respectively
  JOURNAL   Genomics 57 (3), 459-460 (1999)
  MEDLINE   99263513
   PUBMED   10329017
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF018956.1.
FEATURES             Location/Qualifiers
     source          1..923
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12"
     Protein         1..923
                     /product="neuropilin 1"
     Region          27..141
                     /region_name="Domain first found in C1r, C1s, uEGF, and
                     bone morphogenetic protein."
                     /note="CUB"
                     /db_xref="CDD:CUB"
     Region          27..138
                     /region_name="CUB domain"
                     /note="CUB"
                     /db_xref="CDD:pfam00431"
     Region          147..263
                     /region_name="Domain first found in C1r, C1s, uEGF, and
                     bone morphogenetic protein."
                     /note="CUB"
                     /db_xref="CDD:CUB"
     Region          147..262
                     /region_name="CUB domain"
                     /note="CUB"
                     /db_xref="CDD:pfam00431"
     Region          278..421
                     /region_name="F5/8 type C domain"
                     /note="F5_F8_type_C"
                     /db_xref="CDD:pfam00754"
     Region          434..580
                     /region_name="F5/8 type C domain"
                     /note="F5_F8_type_C"
                     /db_xref="CDD:pfam00754"
     Region          645..811
                     /region_name="Domain in meprin, A5, receptor protein
                     tyrosine phosphatase mu (and others)"
                     /note="MAM"
                     /db_xref="CDD:MAM"
     Region          650..811
                     /region_name="MAM domain"
                     /note="MAM"
                     /db_xref="CDD:pfam00629"
     CDS             1..923
                     /gene="NRP1"
                     /coded_by="NM_003873.1:1..2772"
                     /db_xref="LocusID:8829"
                     /db_xref="MIM:602069"
ORIGIN      
        1 merglpllca vlalvlapag afrndecgdt ikiespgylt spgyphsyhp sekcewliqa
       61 pdpyqrimin fnphfdledr dckydyvevf dgenenghfr gkfcgkiapp pvvssgpflf
      121 ikfvsdyeth gagfsiryei fkrgpecsqn yttpsgviks pgfpekypns lectyivfap
      181 kmseiilefe sfdlepdsnp pggmfcrydr leiwdgfpdv gphigrycgq ktpgrirsss
      241 gilsmvfytd saiakegfsa nysvlqssvs edfkcmealg mesgeihsdq itassqystn
      301 wsaersrlny pengwtpged syrewiqvdl gllrfvtavg tqgaisketk kkyyvktyki
      361 dvssngedwi tikegnkpvl fqgntnptdv vvavfpkpli trfvrikpat wetgismrfe
      421 vygckitdyp csgmlgmvsg lisdsqitss nqgdrnwmpe nirlvtsrsg walppaphsy
      481 inewlqidlg eekivrgiii qggkhrenkv fmrkfkigys nngsdwkmim ddskrkaksf
      541 egnnnydtpe lrtfpalstr firiyperat hgglglrmel lgceveapta gpttpngnlv
      601 decdddqanc hsgtgddfql tggttvlate kptvidstiq sefptygfnc efgwgshktf
      661 chwehdnhvq lkwsvltskt gpiqdhtgdg nfiysqaden qkgkvarlvs pvvysqnsah
      721 cmtfwyhmsg shvgtlrvkl ryqkpeeydq lvwmaighqg dhwkegrvll hkslklyqvi
      781 fegeigkgnl ggiavddisi nnhisqedca kpadldkknp eikidetgst pgyegegegd
      841 knisrkpgnv lktlepilit iiamsalgvl lgavcgvvly cacwhngmse rnlsalenyn
      901 felvdgvklk kdklntqsty sea
//



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1: NP_066953. peptidylprolyl is...[gi:10863927] Links  


LOCUS       PPIA                     165 aa            linear   PRI 02-NOV-2000
DEFINITION  peptidylprolyl isomerase A (cyclophilin A) [Homo sapiens].
ACCESSION   NP_066953
VERSION     NP_066953.1  GI:10863927
DBSOURCE    REFSEQ: accession NM_021130.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 165)
  AUTHORS   Haendler,B., Hofer-Warbinek,R. and Hofer,E.
  TITLE     Complementary DNA for human T-cell cyclophilin
  JOURNAL   EMBO J. 6 (4), 947-950 (1987)
  MEDLINE   87246530
   PUBMED   3297675
REFERENCE   2  (residues 1 to 165)
  AUTHORS   Haendler,B. and Hofer,E.
  TITLE     Characterization of the human cyclophilin gene and of related
            processed pseudogenes
  JOURNAL   Eur. J. Biochem. 190 (3), 477-482 (1990)
  MEDLINE   90322991
   PUBMED   2197089
REFERENCE   3  (residues 1 to 165)
  AUTHORS   Holzman,T.F., Egan,D.A., Edalji,R., Simmer,R.L., Helfrich,R.,
            Taylor,A. and Burres,N.S.
  TITLE     Preliminary characterization of a cloned neutral isoelectric form
            of the human peptidyl prolyl isomerase cyclophilin
  JOURNAL   J. Biol. Chem. 266 (4), 2474-2479 (1991)
  MEDLINE   91115871
   PUBMED   1989998
REFERENCE   4  (residues 1 to 165)
  AUTHORS   Willenbrink,W., Halaschek,J., Schuffenhauer,S., Kunz,J. and
            Steinkasserer,A.
  TITLE     Cyclophilin A, the major intracellular receptor for the
            immunosuppressant cyclosporin A, maps to chromosome 7p11.2-p13:
            four pseudogenes map to chromosomes 3, 10, 14, and 18
  JOURNAL   Genomics 28 (1), 101-104 (1995)
  MEDLINE   96070439
   PUBMED   7590732
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X52851.1.
FEATURES             Location/Qualifiers
     source          1..165
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p13-p11.2"
                     /clone="CPH-70"
                     /cell_type="leucocyte"
                     /clone_lib="Lambda EMBL3"
     Protein         1..165
                     /product="peptidylprolyl isomerase A (cyclophilin A)"
                     /EC_number="5.2.1.8"
     Region          5..164
                     /region_name="Cyclophilin type peptidyl-prolyl cis-trans
                     isomerase"
                     /note="pro_isomerase"
                     /db_xref="CDD:pfam00160"
     CDS             1..165
                     /gene="PPIA"
                     /coded_by="NM_021130.1:45..542"
                     /db_xref="LocusID:5478"
                     /db_xref="MIM:123840"
ORIGIN      
        1 mvnptvffdi avdgeplgrv sfelfadkvp ktaenfrals tgekgfgykg scfhriipgf
       61 mcqggdftrh ngtggksiyg ekfedenfil khtgpgilsm anagpntngs qffictakte
      121 wldgkhvvfg kvkegmnive amerfgsrng ktskkitiad cgqle
//



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1: NP_005019. phosphatidylinosi...[gi:6857820] Links  


LOCUS       PIP5K2A                  406 aa            linear   PRI 27-AUG-2002
DEFINITION  phosphatidylinositol-4-phosphate 5-kinase type II alpha;
            1-phosphatidylinositol-4-phosphate kinase; diphosphoinositide
            kinase; PtdIns(4)P-5-kinase B isoform;
            1-phosphatidylinositol-4-phosphate-5-kinase isoform C; type II
            phosphatidylinositol-4-phosphate 5-kinase 53 K isoform [Homo
            sapiens].
ACCESSION   NP_005019
VERSION     NP_005019.2  GI:6857820
DBSOURCE    REFSEQ: accession NM_005028.3
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 406)
  AUTHORS   Boronenkov,I.V. and Anderson,R.A.
  TITLE     The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a
            novel family of lipid kinases
  JOURNAL   J. Biol. Chem. 270 (7), 2881-2884 (1995)
  MEDLINE   95155363
   PUBMED   7852364
REFERENCE   2  (residues 1 to 406)
  AUTHORS   Divecha,N., Truong,O., Hsuan,J.J., Hinchliffe,K.A. and Irvine,R.F.
  TITLE     The cloning and sequence of the C isoform of PtdIns4P 5-kinase
  JOURNAL   Biochem. J. 309 (Pt 3), 715-719 (1995)
  MEDLINE   95366942
   PUBMED   7639683
REFERENCE   3  (residues 1 to 406)
  AUTHORS   Loijens,J.C., Boronenkov,I.V., Parker,G.J. and Anderson,R.A.
  TITLE     The phosphatidylinositol 4-phosphate 5-kinase family
  JOURNAL   Adv. Enzyme Regul. 36, 115-140 (1996)
  MEDLINE   97023384
   PUBMED   8869744
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC018034.1.
            On Feb 3, 2000 this sequence version replaced gi:4826910.
            Summary: Phosphatidylinositol-4,5-bisphosphate, the precursor to
            second messengers of the phosphoinositide signal transduction
            pathways, is thought to be involved in the regulation of secretion,
            cell proliferation, differentiation, and motility. The protein
            encoded by this gene is one of a family of enzymes capable of
            catalyzing the phosphorylation of phosphatidylinositol-4-phosphate
            on the fifth hydroxyl of the myo-inositol ring to form
            phosphatidylinositol-4,5-bisphosphate. The amino acid sequence of
            this enzyme does not show homology to other kinases, but the
            recombinant protein does exhibit kinase activity. This gene is a
            member of the phosphatidylinositol-4-phosphate 5-kinase family.
FEATURES             Location/Qualifiers
     source          1..406
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p11.23"
                     /clone="MGC:26205 IMAGE:4817357"
                     /clone_lib="NIH_MGC_95"
     Protein         1..406
                     /product="phosphatidylinositol-4-phosphate 5-kinase type
                     II alpha"
                     /note="1-phosphatidylinositol-4-phosphate kinase;
                     diphosphoinositide kinase; PtdIns(4)P-5-kinase B isoform;
                     1-phosphatidylinositol-4-phosphate-5-kinase isoform C;
                     type II phosphatidylinositol-4-phosphate 5-kinase 53 K
                     isoform"
     Region          62..406
                     /region_name="smart00330, PIPKc, Phosphatidylinositol
                     phosphate kinases"
     Region          114..405
                     /region_name="pfam01504, PIP5K,
                     Phosphatidylinositol-4-phosphate 5-Kinase. This family
                     contains a region from the common kinase core found in the
                     type I phosphatidylinositol-4-phosphate 5-kinase (PIP5K)
                     family. The family consists of various type I, II and III
                     PIP5K enzymes. PIP5K catalyses the formation of
                     phosphoinositol-4,5-bisphosphate via the phosphorylation
                     of phosphatidylinositol-4-phosphate a precursor in the
                     phosphinositide signaling pathway"
     CDS             1..406
                     /gene="PIP5K2A"
                     /coded_by="NM_005028.3:230..1450"
                     /db_xref="LocusID:5305"
                     /db_xref="MIM:603140"
ORIGIN      
        1 matpgnlgss vlasktktkk khfvaqkvkl frasdpllsv lmwgvnhsin elshvqipvm
       61 lmpddfkays kikvdnhlfn kenmpshfkf keycpmvfrn lrerfgiddq dfqnsltrsa
      121 plpndsqars garfhtsydk ryiiktitse dvaemhnilk kyhqyivech gitllpqflg
      181 myrlnvdgve iyvivtrnvf shrlsvyrky dlkgstvare asdkekakel ptlkdndfin
      241 egqkiyiddn nkkvfleklk kdveflaqlk lmdysllvgi hdveraeqee veceendgee
      301 egesdgthpv gtppdspgnt lnsspplapg efdpnidvyg ikchensprk evyfmaiidi
      361 lthydakkka ahaaktvkhg agaeistvnp eqyskrfldf ighilt
//



Revised: July 5, 2002.
 
 


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1: NP_006126. F-actin capping p...[gi:5453597] Links  


LOCUS       CAPZA1                   286 aa            linear   PRI 16-MAY-2002
DEFINITION  F-actin capping protein alpha-1 subunit; Cap Z [Homo sapiens].
ACCESSION   NP_006126
VERSION     NP_006126.1  GI:5453597
DBSOURCE    REFSEQ: accession NM_006135.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 286)
  AUTHORS   Barron-Casella,E.A., Torres,M.A., Scherer,S.W., Heng,H.H.,
            Tsui,L.C. and Casella,J.F.
  TITLE     Sequence analysis and chromosomal localization of human Cap Z.
            Conserved residues within the actin-binding domain may link Cap Z
            to gelsolin/severin and profilin protein families
  JOURNAL   J. Biol. Chem. 270 (37), 21472-21479 (1995)
  MEDLINE   95394897
   PUBMED   7665558
REFERENCE   2  (residues 1 to 286)
  AUTHORS   Hart,M.C., Korshunova,Y.O. and Cooper,J.A.
  TITLE     Vertebrates have conserved capping protein alpha isoforms with
            specific expression patterns
  JOURNAL   Cell Motil. Cytoskeleton 38 (2), 120-132 (1997)
  MEDLINE   97470757
   PUBMED   9331217
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U56637.1.
            Summary: CAPZA1 is a member of the F-actin capping protein alpha
            subunit family. This gene encodes the alpha subunit of the
            barbed-end actin binding protein.  The protein regulates growth of
            the actin filament by capping the barbed end of growing actin
            filaments.
FEATURES             Location/Qualifiers
     source          1..286
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p12"
     Protein         1..286
                     /product="F-actin capping protein alpha-1 subunit"
                     /note="Cap Z"
     Region          12..282
                     /region_name="F-actin capping protein alpha subunit"
                     /note="F-actin_cap_A"
                     /db_xref="CDD:pfam01267"
     CDS             1..286
                     /gene="CAPZA1"
                     /coded_by="NM_006135.1:1..861"
                     /db_xref="LocusID:829"
                     /db_xref="MIM:601580"
ORIGIN      
        1 madfddrvsd eekvriaakf ithappgefn evfndvrlll nndnllrega ahafaqynmd
       61 qftpvkiegy edqvlitehg dlgnsrfldp rnkisfkfdh lrkeasdpqp eeadgglksw
      121 rescdsalra yvkdhysngf ctvyaktidg qqtiiacies hqfqpknfwn grwrsewkft
      181 itpptaqvvg vlkiqvhyye dgnvqlvshk dvqdsltvsn eaqtakefik iienaeneyq
      241 taisenyqtm sdttfkalrr qlpvtrtkid wnkilsykig kemqna
//



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1: NP_002843. pentaxin-related ...[gi:4506333] Links  


LOCUS       PTX3                     381 aa            linear   PRI 31-OCT-2000
DEFINITION  pentaxin-related gene, rapidly induced by IL-1 beta; Pentraxin-3
            [Homo sapiens].
ACCESSION   NP_002843
VERSION     NP_002843.1  GI:4506333
DBSOURCE    REFSEQ: accession NM_002852.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 381)
  AUTHORS   Lee TH, Wisniewski HG and Vilcek J.
  TITLE     A novel secretory tumor necrosis factor-inducible protein (TSG-6)
            is a member of the family of hyaluronate binding proteins, closely
            related to the adhesion receptor CD44
  JOURNAL   J. Cell Biol. 116 (2), 545-557 (1992)
  MEDLINE   92112993
   PUBMED   1730767
REFERENCE   2  (residues 1 to 381)
  AUTHORS   Breviario,F., d'Aniello,E.M., Golay,J., Peri,G., Bottazzi,B.,
            Bairoch,A., Saccone,S., Marzella,R., Predazzi,V., Rocchi,M. et al.
  TITLE     Interleukin-1-inducible genes in endothelial cells. Cloning of a
            new gene related to C-reactive protein and serum amyloid P
            component
  JOURNAL   J. Biol. Chem. 267 (31), 22190-22197 (1992)
  MEDLINE   93054498
   PUBMED   1429570
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X63613.1.
FEATURES             Location/Qualifiers
     source          1..381
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q25"
                     /clone="PTX3/E"
                     /cell_line="HUVEC"
                     /clone_lib="ZAP-FB1"
     Protein         1..381
                     /product="pentaxin-related gene, rapidly induced by IL-1
                     beta"
                     /note="Pentraxin-3"
     Region          175..381
                     /region_name="Pentraxin / C-reactive protein / pentaxin
                     family"
                     /note="PTX"
                     /db_xref="CDD:PTX"
     Region          182..377
                     /region_name="Pentaxin family"
                     /note="pentaxin"
                     /db_xref="CDD:pfam00354"
     CDS             1..381
                     /gene="PTX3"
                     /coded_by="NM_002852.1:68..1213"
                     /db_xref="LocusID:5806"
                     /db_xref="MIM:602492"
ORIGIN      
        1 mhllailfca lwsavlaens ddydlmyvnl dneidnglhp tedptpcdcg qehsewdklf
       61 imlensqmre rmllqatddv lrgelqrlre elgrlaesla rpcapgapae arltsaldel
      121 lqatrdagrr larmegaeaq rpeeagrala avleelrqtr adlhavqgwa arswlpagce
      181 tailfpmrsk kifgsvhpvr pmrlesfsac iwvkatdvln ktilfsygtk rnpyeiqlyl
      241 syqsivfvvg geenklvaea mvslgrwthl cgtwnseegl tslwvngela attvematgh
      301 ivpeggilqi gqekngccvg ggfdetlafs grltgfniwd svlsneeire tggaeschir
      361 gnivgwgvte iqphggaqyv s
//



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1: NP_004325. bone marrow strom...[gi:4757874] Links  


LOCUS       BST1                     318 aa            linear   PRI 27-AUG-2002
DEFINITION  bone marrow stromal cell antigen 1 precursor [Homo sapiens].
ACCESSION   NP_004325
VERSION     NP_004325.1  GI:4757874
DBSOURCE    REFSEQ: accession NM_004334.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 318)
  AUTHORS   Kaisho,T., Ishikawa,J., Oritani,K., Inazawa,J., Tomizawa,H.,
            Muraoka,O., Ochi,T. and Hirano,T.
  TITLE     BST-1, a surface molecule of bone marrow stromal cell lines that
            facilitates pre-B-cell growth
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 91 (12), 5325-5329 (1994)
  MEDLINE   94261578
   PUBMED   8202488
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D21878.1.
            Summary: Bone marrow stromal cell antigen-1 is a stromal cell
            line-derived glycosylphosphatidylinositol-anchored molecule that
            facilitates pre-B-cell growth. The deduced amino acid sequence
            exhibits 33% similarity with CD38. BST1 expression is enhanced in
            bone marrow stromal cell lines derived from patients with
            rheumatoid arthritis. The polyclonal B-cell abnormalities in
            rheumatoid arthritis may be, at least in part, attributed to BST1
            overexpression in the stromal cell population.
FEATURES             Location/Qualifiers
     source          1..318
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p15"
     Protein         1..318
                     /product="bone marrow stromal cell antigen 1 precursor"
                     /function="facilitates pre-B-cell growth"
     sig_peptide     1..28
     mat_peptide     29..318
                     /product="bone marrow stromal cell antigen 1"
     Region          40..280
                     /region_name="pfam02267, Rib_hydrolayse, ADP-ribosyl
                     cyclase. ADP-ribosyl cyclase EC:3.2.2.5 (also know as
                     cyclic ADP-ribose hydrolase or CD38) synthesizes
                     cyclic-ADP ribose, a second messenger for glucose-induced
                     insulin secretion"
     CDS             1..318
                     /gene="BST1"
                     /coded_by="NM_004334.1:128..1084"
                     /db_xref="LocusID:683"
                     /db_xref="MIM:600387"
ORIGIN      
        1 maaqgcaasr llqlllqlll lllllaagga rarwraegts ahlrdiflgr caeyrallsp
       61 eqrnknctai weafkvaldk dpcsvlpsdy dlfinlsrhs iprdkslfwe nshllvnsfa
      121 dntrrfmpls dvlygrvadf lswcrqknds gldyqscpts edcennpvds fwkrasiqys
      181 kdssgvihvm lngseptgay pikgffadye ipnlqkekit rieiwvmhei ggpnvescge
      241 gsmkvlekrl kdmgfqysci ndyrpvkllq cvdhsthpdc alksaaaatq rkapslyteq
      301 ragliiplfl vlasrtql
//



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1: NP_002603. pyruvate dehydrog...[gi:4505693] Links  


LOCUS       PDK4                     411 aa            linear   PRI 31-OCT-2000
DEFINITION  pyruvate dehydrogenase kinase, isoenzyme 4 [Homo sapiens].
ACCESSION   NP_002603
VERSION     NP_002603.1  GI:4505693
DBSOURCE    REFSEQ: accession NM_002612.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Gudi R, Bowker-Kinley MM, Kedishvili NY, Zhao Y and Popov KM.
  TITLE     Diversity of the pyruvate dehydrogenase kinase gene family in
            humans
  JOURNAL   J. Biol. Chem. 270 (48), 28989-28994 (1995)
  MEDLINE   96081973
   PUBMED   7499431
  REMARK    Erratum:[[published erratum appears in J Biol Chem 1996 Jan
            12;271(2):1250]]
REFERENCE   2  (residues 1 to 411)
  AUTHORS   Rowles,J., Scherer,S.W., Xi,T., Majer,M., Nickle,D.C.,
            Rommens,J.M., Popov,K.M., Harris,R.A., Riebow,N.L., Xia,J.,
            Tsui,L., Bogardus,C. and Prochazka,M.
  TITLE     Cloning and characterization of PDK4 on 7q21.3 encoding a fourth
            pyruvate dehydrogenase kinase isoenzyme in human
  JOURNAL   J. Biol. Chem. 271 (37), 22376-22382 (1996)
  MEDLINE   96394293
   PUBMED   8798399
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U54617.1.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.3-q22.1"
                     /tissue_type="frontal cortex"
     Protein         1..411
                     /product="pyruvate dehydrogenase kinase, isoenzyme 4"
     Region          235..362
                     /region_name="Histidine kinase"
                     /note="signal"
                     /db_xref="CDD:pfam00512"
     Region          245..356
                     /region_name="Histidine kinase-like ATPases"
                     /note="HATPase_c"
                     /db_xref="CDD:HATPase_c"
     CDS             1..411
                     /gene="PDK4"
                     /coded_by="NM_002612.1:223..1458"
                     /db_xref="LocusID:5166"
                     /db_xref="MIM:602527"
ORIGIN      
        1 mkaarfvlrs agslngaglv prevehfsry spsplsmkql ldfgsenace rtsfaflrqe
       61 lpvrlanilk eidilptqlv ntssvqlvks wyiqslmdlv efhekspddq kalsdfvdtl
      121 ikvrnrhhnv vptmaqgiie ykdactvdpv tnqnlqyfld rfymnristr mlmnqhilif
      181 sdsqtgnpsh igsidpncdv vavvqdafec srmlcdqyyl sspelkltqv ngkfpdqpih
      241 ivyvpshlhh mlfelfknam ratvehqenq psltpieviv vlgkedltik isdrgggvpl
      301 riidrlfsyt ystaptpvmd nsrnaplagf gyglpisrly akyfqgdlnl yslsgygtda
      361 iiylkalsse sieklpvfnk safkhyqmss eaddwcipsr epknlakeva m
//



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1: NP_006191. proprotein conver...[gi:20336246] Links  


LOCUS       PCSK5                    913 aa            linear   PRI 27-AUG-2002
DEFINITION  proprotein convertase subtilisin/kexin type 5 preproprotein;
            protease PC6; prohormone convertase 5; subtilisin/kexin-like
            protease PC5; proprotein convertase PC5 [Homo sapiens].
ACCESSION   NP_006191
VERSION     NP_006191.2  GI:20336246
DBSOURCE    REFSEQ: accession NM_006200.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 913)
  AUTHORS   Mbikay,M., Seidah,N.G., Chretien,M. and Simpson,E.M.
  TITLE     Chromosomal assignment of the genes for proprotein convertases PC4,
            PC5, and PACE 4 in mouse and human
  JOURNAL   Genomics 26 (1), 123-129 (1995)
  MEDLINE   95301277
   PUBMED   7782070
REFERENCE   2  (residues 1 to 913)
  AUTHORS   Miranda,L., Wolf,J., Pichuantes,S., Duke,R. and Franzusoff,A.
  TITLE     Isolation of the human PC6 gene encoding the putative host protease
            for HIV-1 gp160 processing in CD4+ T lymphocytes
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 93 (15), 7695-7700 (1996)
  MEDLINE   96353880
   PUBMED   8755538
REFERENCE   3  (residues 1 to 913)
  AUTHORS   Mercure,C., Jutras,I., Day,R., Seidah,N.G. and Reudelhuber,T.L.
  TITLE     Prohormone convertase PC5 is a candidate processing enzyme for
            prorenin in the human adrenal cortex
  JOURNAL   Hypertension 28 (5), 840-846 (1996)
  MEDLINE   97057493
   PUBMED   8901832
REFERENCE   4  (residues 1 to 913)
  AUTHORS   van de Loo,J.W., Creemers,J.W., Kas,K., Roebroek,A.J. and Van de
            Ven,W.J.
  TITLE     Assignment of the human proprotein convertase gene PCSK5 to
            chromosome 9q21.3
  JOURNAL   Cytogenet. Cell Genet. 75 (4), 227-229 (1996)
  MEDLINE   97220055
   PUBMED   9067430
REFERENCE   5  (residues 1 to 913)
  AUTHORS   Lissitzky,J.C., Luis,J., Munzer,J.S., Benjannet,S., Parat,F.,
            Chretien,M., Marvaldi,J. and Seidah,N.G.
  TITLE     Endoproteolytic processing of integrin pro-alpha subunits involves
            the redundant function of furin and proprotein convertase (PC) 5A,
            but not paired basic amino acid converting enzyme (PACE) 4, PC5B or
            PC7
  JOURNAL   Biochem. J. 346 Pt 1, 133-138 (2000)
  MEDLINE   20125591
   PUBMED   10657249
REFERENCE   6  (residues 1 to 913)
  AUTHORS   Bassi,D.E., Mahloogi,H. and Klein-Szanto,A.J.
  TITLE     The proprotein convertases furin and PACE4 play a significant role
            in tumor progression
  JOURNAL   Mol. Carcinog. 28 (2), 63-69 (2000)
  MEDLINE   20362110
   PUBMED   10900462
REFERENCE   7  (residues 1 to 913)
  AUTHORS   Yana,I. and Weiss,S.J.
  TITLE     Regulation of membrane type-1 matrix metalloproteinase activation
            by proprotein convertases
  JOURNAL   Mol. Biol. Cell 11 (7), 2387-2401 (2000)
  MEDLINE   20346965
   PUBMED   10888676
REFERENCE   8  (residues 1 to 913)
  AUTHORS   Pearton,D.J., Nirunsuksiri,W., Rehemtulla,A., Lewis,S.P.,
            Presland,R.B. and Dale,B.A.
  TITLE     Proprotein convertase expression and localization in epidermis:
            evidence for multiple roles and substrates
  JOURNAL   Exp. Dermatol. 10 (3), 193-203 (2001)
  MEDLINE   21275449
   PUBMED   11380615
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012064.1.
            On Apr 28, 2002 this sequence version replaced gi:11321619.
            Summary: The protein encoded by this gene belongs to the
            subtilisin-like proprotein convertase family. The members of this
            family are proprotein convertases that process latent precursor
            proteins into their biologically active products. This encoded
            protein mediates posttranslational endoproteolytic processing for
            several integrin alpha subunits. It is thought to process prorenin,
            pro-membrane type-1 matrix metalloproteinase and HIV-1 glycoprotein
            gp160. Two alternatively spliced transcripts are described for this
            gene but only one has its full length nature known.
FEATURES             Location/Qualifiers
     source          1..913
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q21.3"
                     /clone="MGC:19910 IMAGE:4562734"
                     /clone_lib="NIH_MGC_14"
     Protein         1..913
                     /product="proprotein convertase subtilisin/kexin type 5
                     preproprotein"
                     /EC_number="3.4.21.-"
                     /note="protease PC6; prohormone convertase 5;
                     subtilisin/kexin-like protease PC5; proprotein convertase
                     PC5"
     sig_peptide     1..32
     Proprotein      33..913
     mat_peptide     115..913
                     /product="proprotein convertase subtilisin/kexin type 5"
     Region          125..448
                     /region_name="pfam00082, Peptidase_S8, Subtilase family.
                     Subtilases are a family of serine proteases. They appear
                     to have independently and convergently evolved an
                     Asp/Ser/His catalytic triad, like that found in the
                     trypsin serine proteases (see pfam00089). Structure is an
                     alpha/beta fold containing a 7-stranded parallel beta
                     sheet, order 2314567"
     Region          462..600
                     /region_name="pfam01483, P, Proprotein convertase
                     P-domain. A unique feature of the eukaryotic
                     subtilisin-like proprotein convertases is the presence of
                     an additional highly conserved sequence of approximately
                     150 residues (P domain) located immediately downstream of
                     the catalytic domain"
     Region          634..842
                     /region_name="pfam00757, Furin-like, Furin-like cysteine
                     rich region"
     Region          635..680
                     /region_name="smart00261, FU, Furin-like repeats"
     Region          636..860
                     /region_name="pfam03302, VSP, Giardia variant-specific
                     surface protein"
     Region          681..786
                     /region_name="pfam03302, VSP, Giardia variant-specific
                     surface protein"
     Region          683..729
                     /region_name="smart00261, FU, Furin-like repeats"
     Region          704..865
                     /region_name="pfam03302, VSP, Giardia variant-specific
                     surface protein"
     Region          734..776
                     /region_name="smart00261, FU, Furin-like repeats"
     Region          833..867
                     /region_name="smart00261, FU, Furin-like repeats"
     CDS             1..913
                     /gene="PCSK5"
                     /coded_by="NM_006200.2:478..3219"
                     /db_xref="LocusID:5125"
                     /db_xref="MIM:600488"
ORIGIN      
        1 mgwgsrcccp grldllcvla llggcllpvc rtrvytnhwa vkiaggfpea nriaskygfi
       61 nigqigalkd yyhfyhsrti krsvissrgt hsfismepkv ewiqqqvvkk rtkrdydfsr
      121 aqstyfndpk wpsmwymhcs dnthpcqsdm niegawkrgy tgknivvtil ddgierthpd
      181 lmqnydalas cdvngndldp mprydasnen khgtrcagev aaaannshct vgiafnakig
      241 gvrmldgdvt dmveaksvsf npqhvhiysa swgpdddgkt vdgpapltrq afengvrmgr
      301 rglgsvfvwa sgnggrskdh cscdgytnsi ytisisstae sgkkpwylee csstlattys
      361 sgesydkkii ttdlrqrctd nhtgtsasap maagiialal eanpfltwrd vqhvivrtsr
      421 aghlnandwk tnaagfkvsh lygfglmdae amvmeaekwt tvprqhvcve stdrqiktir
      481 pnsavrsiyk asgcsdnpnr hvnylehvvv ritithprrg dlaiyltsps gtrsqllanr
      541 lfdhsmegfk nwefmtihcw geraagdwvl evydtpsqlr nfktpgklke wslvlygtsv
      601 qpysptnefp kverfrysrv edptddygte dyagpcdpec sevgcdgpgp dhcndclhyy
      661 yklknntric vsscppghyh adkkrcrkca pncescfgsh gdqcmsckyg yflneetnsc
      721 vthcpdgsyq dtkknlcrkc sencktctef hnctecrdgl slqgsrcsvs cedgryfngq
      781 dcqpchrfca tcagagadgc inctegyfme dgrcvqscsi syyfdhssen gyksckkcdi
      841 scltcngpgf knctscpsgy lldlgmcqmg aickdatees waeggfcmlv kknnlcqrkv
      901 lqqlccktct fqg
//



Revised: July 5, 2002.
 
 


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1: NP_006264. small inducible c...[gi:13435402] Links  


LOCUS       CCL7                      99 aa            linear   PRI 30-AUG-2002
DEFINITION  small inducible cytokine A7 precursor; monocyte chemoattractant
            protein 3 [Homo sapiens].
ACCESSION   NP_006264
VERSION     NP_006264.2  GI:13435402
DBSOURCE    REFSEQ: accession NM_006273.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 99)
  AUTHORS   Van Damme,J., Proost,P., Lenaerts,J.P. and Opdenakker,G.
  TITLE     Structural and functional identification of two human,
            tumor-derived monocyte chemotactic proteins (MCP-2 and MCP-3)
            belonging to the chemokine family
  JOURNAL   J. Exp. Med. 176 (1), 59-65 (1992)
  MEDLINE   92308855
   PUBMED   1613466
REFERENCE   2  (residues 1 to 99)
  AUTHORS   Minty,A., Chalon,P., Guillemot,J.C., Kaghad,M., Liauzun,P.,
            Magazin,M., Miloux,B., Minty,C., Ramond,P., Vita,N., Lupker,J.,
            Shire,D., Ferrara,P. and Caput,D.
  TITLE     Molecular cloning of the MCP-3 chemokine gene and regulation of its
            expression
  JOURNAL   Eur. Cytokine Netw. 4 (2), 99-110 (1993)
  MEDLINE   93305913
   PUBMED   8318676
REFERENCE   3  (residues 1 to 99)
  AUTHORS   Opdenakker,G., Froyen,G., Fiten,P., Proost,P. and Van Damme,J.
  TITLE     Human monocyte chemotactic protein-3 (MCP-3): molecular cloning of
            the cDNA and comparison with other chemokines
  JOURNAL   Biochem. Biophys. Res. Commun. 191 (2), 535-542 (1993)
  MEDLINE   93213290
   PUBMED   8461011
REFERENCE   4  (residues 1 to 99)
  AUTHORS   Opdenakker,G., Fiten,P., Nys,G., Froyen,G., Van Roy,N.,
            Speleman,F., Laureys,G. and Van Damme,J.
  TITLE     The human MCP-3 gene (SCYA7): cloning, sequence analysis, and
            assignment to the C-C chemokine gene cluster on chromosome
            17q11.2-q12
  JOURNAL   Genomics 21 (2), 403-408 (1994)
  MEDLINE   94375065
   PUBMED   7916328
REFERENCE   5  (residues 1 to 99)
  AUTHORS   Kim,K.S., Rajarathnam,K., Clark-Lewis,I. and Sykes,B.D.
  TITLE     Structural characterization of a monomeric chemokine: monocyte
            chemoattractant protein-3
  JOURNAL   FEBS Lett. 395 (2-3), 277-282 (1996)
  MEDLINE   97053697
   PUBMED   8898111
REFERENCE   6  (residues 1 to 99)
  AUTHORS   Meunier,S., Bernassau,J.M., Guillemot,J.C., Ferrara,P. and
            Darbon,H.
  TITLE     Determination of the three-dimensional structure of CC chemokine
            monocyte chemoattractant protein 3 by 1H two-dimensional NMR
            spectroscopy
  JOURNAL   Biochemistry (N.Y.) 36 (15), 4412-4422 (1997)
  MEDLINE   97263733
   PUBMED   9109648
REFERENCE   7  (residues 1 to 99)
  AUTHORS   Wang,J.M., Ueda,H., Howard,O.M., Grimm,M.C., Chertov,O., Gong,X.,
            Gong,W., Resau,J.H., Broder,C.C., Evans,G., Arthur,L.O.,
            Ruscetti,F.W. and Oppenheim,J.J.
  TITLE     HIV-1 envelope gp120 inhibits the monocyte response to chemokines
            through CD4 signal-dependent chemokine receptor down-regulation
  JOURNAL   J. Immunol. 161 (8), 4309-4317 (1998)
  MEDLINE   98451487
   PUBMED   9780207
REFERENCE   8  (residues 1 to 99)
  AUTHORS   Rabin,R.L., Park,M.K., Liao,F., Swofford,R., Stephany,D. and
            Farber,J.M.
  TITLE     Chemokine receptor responses on T cells are achieved through
            regulation of both receptor expression and signaling
  JOURNAL   J. Immunol. 162 (7), 3840-3850 (1999)
  MEDLINE   99218399
   PUBMED   10201901
REFERENCE   9  (residues 1 to 99)
  AUTHORS   Mirzadegan,T., Diehl,F., Ebi,B., Bhakta,S., Polsky,I., McCarley,D.,
            Mulkins,M., Weatherhead,G.S., Lapierre,J.M., Dankwardt,J.,
            Morgans,D. Jr., Wilhelm,R. and Jarnagin,K.
  TITLE     Identification of the binding site for a novel class of CCR2b
            chemokine receptor antagonists: binding to a common chemokine
            receptor motif within the helical bundle
  JOURNAL   J. Biol. Chem. 275 (33), 25562-25571 (2000)
  MEDLINE   20400491
   PUBMED   10770925
REFERENCE   10 (residues 1 to 99)
  AUTHORS   McQuibban,G.A., Gong,J.H., Tam,E.M., McCulloch,C.A., Clark-Lewis,I.
            and Overall,C.M.
  TITLE     Inflammation dampened by gelatinase A cleavage of monocyte
            chemoattractant protein-3
  JOURNAL   Science 289 (5482), 1202-1206 (2000)
  MEDLINE   20407467
   PUBMED   10947989
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X71087.1.
            On Mar 23, 2001 this sequence version replaced gi:10835244.
            Summary: This gene encodes monocyte chemotactic protein 3, a
            secreted chemokine which attracts macrophages during inflammation
            and metastasis. It is a member of the C-C subfamily of chemokines
            which are characterized by having two adjacent cysteine residues.
            The protein is an in vivo substrate of matrix metalloproteinase 2,
            an enzyme which degrades components of the extracellular matrix.
            This gene is part of a cluster of C-C chemokine family members on
            chromosome 17q.
FEATURES             Location/Qualifiers
     source          1..99
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2-q12"
     Protein         1..99
                     /product="small inducible cytokine A7 precursor"
                     /note="monocyte chemoattractant protein 3"
     sig_peptide     1..23
     mat_peptide     24..99
                     /product="small inducible cytokine A7"
     Region          24..90
                     /region_name="pfam00048, IL8, Small cytokines
                     (intecrine/chemokine), interleukin-8 like. Includes a
                     number of secreted growth factors and interferons involved
                     in mitogenic, chemotactic, and inflammatory activity.
                     Structure contains two highly conserved disulfide bonds"
     Region          31..90
                     /region_name="smart00199, SCY, Intercrine alpha family
                     (small cytokine C-X-C) (chemokine CXC); Family of
                     cytokines involved in cell-specific chemotaxis, mediation
                     of cell growth, and the inflammatory response"
     misc_feature    34..35
                     /note="adjacent cysteines characteristic of C-C
                     chemokines"
     CDS             1..99
                     /gene="CCL7"
                     /coded_by="NM_006273.2:71..370"
                     /db_xref="LocusID:6354"
                     /db_xref="MIM:158106"
ORIGIN      
        1 mkasaallcl lltaaafspq glaqpvgint sttccyrfin kkipkqrles yrrttsshcp
       61 reavifktkl dkeicadptq kwvqdfmkhl dkktqtpkl
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_002975. small inducible c...[gi:4506845] Links  


LOCUS       SCYA4                     92 aa            linear   PRI 26-JAN-2002
DEFINITION  small inducible cytokine A4; lymphocyte-activation gene 1; small
            inducible cytokine A4 (homologous to mouse Mip-1b) [Homo sapiens].
ACCESSION   NP_002975
VERSION     NP_002975.1  GI:4506845
DBSOURCE    REFSEQ: accession NM_002984.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 92)
  AUTHORS   Lipes,M.A., Napolitano,M., Jeang,K.T., Chang,N.T. and Leonard,W.J.
  TITLE     Identification, cloning, and characterization of an immune
            activation gene
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 85 (24), 9704-9708 (1988)
  MEDLINE   89071764
   PUBMED   2462251
REFERENCE   2  (residues 1 to 92)
  AUTHORS   Brown,K.D., Zurawski,S.M., Mosmann,T.R. and Zurawski,G.
  TITLE     A family of small inducible proteins secreted by leukocytes are
            members of a new superfamily that includes leukocyte and
            fibroblast-derived inflammatory agents, growth factors, and
            indicators of various activation processes
  JOURNAL   J. Immunol. 142 (2), 679-687 (1989)
  MEDLINE   89093958
   PUBMED   2521353
REFERENCE   3  (residues 1 to 92)
  AUTHORS   Zipfel,P.F., Balke,J., Irving,S.G., Kelly,K. and Siebenlist,U.
  TITLE     Mitogenic activation of human T cells induces two closely related
            genes which share structural similarities with a new family of
            secreted factors
  JOURNAL   J. Immunol. 142 (5), 1582-1590 (1989)
  MEDLINE   89140347
   PUBMED   2521882
REFERENCE   4  (residues 1 to 92)
  AUTHORS   Chang,H.C. and Reinherz,E.L.
  TITLE     Isolation and characterization of a cDNA encoding a putative
            cytokine which is induced by stimulation via the CD2 structure on
            human T lymphocytes
  JOURNAL   Eur. J. Immunol. 19 (6), 1045-1051 (1989)
  MEDLINE   89325421
   PUBMED   2568930
REFERENCE   5  (residues 1 to 92)
  AUTHORS   Irving,S.G., Zipfel,P.F., Balke,J., McBride,O.W., Morton,C.C.,
            Burd,P.R., Siebenlist,U. and Kelly,K.
  TITLE     Two inflammatory mediator cytokine genes are closely linked and
            variably amplified on chromosome 17q
  JOURNAL   Nucleic Acids Res. 18 (11), 3261-3270 (1990)
  MEDLINE   90287702
   PUBMED   1972563
REFERENCE   6  (residues 1 to 92)
  AUTHORS   Baixeras,E., Roman-Roman,S., Jitsukawa,S., Genevee,C., Mechiche,S.,
            Viegas-Pequignot,E., Hercend,T. and Triebel,F.
  TITLE     Cloning and expression of a lymphocyte activation gene (LAG-1)
  JOURNAL   Mol. Immunol. 27 (11), 1091-1102 (1990)
  MEDLINE   91061800
   PUBMED   2247088
REFERENCE   7  (residues 1 to 92)
  AUTHORS   Rubbert,A., Combadiere,C., Ostrowski,M., Arthos,J., Dybul,M.,
            Machado,E., Cohn,M.A., Hoxie,J.A., Murphy,P.M., Fauci,A.S. and
            Weissman,D.
  TITLE     Dendritic cells express multiple chemokine receptors used as
            coreceptors for HIV entry
  JOURNAL   J. Immunol. 160 (8), 3933-3941 (1998)
  MEDLINE   98217183
   PUBMED   9558100
REFERENCE   8  (residues 1 to 92)
  AUTHORS   Zaitseva,M.B., Lee,S., Rabin,R.L., Tiffany,H.L., Farber,J.M.,
            Peden,K.W., Murphy,P.M. and Golding,H.
  TITLE     CXCR4 and CCR5 on human thymocytes: biological function and role in
            HIV-1 infection
  JOURNAL   J. Immunol. 161 (6), 3103-3113 (1998)
  MEDLINE   98414309
   PUBMED   9743377
REFERENCE   9  (residues 1 to 92)
  AUTHORS   Nieto,M., Navarro,F., Perez-Villar,J.J., del Pozo,M.A.,
            Gonzalez-Amaro,R., Mellado,M., Frade,J.M., Martinez-A,C.,
            Lopez-Botet,M. and Sanchez-Madrid,F.
  TITLE     Roles of chemokines and receptor polarization in NK-target cell
            interactions
  JOURNAL   J. Immunol. 161 (7), 3330-3339 (1998)
  MEDLINE   98430649
   PUBMED   9759849
REFERENCE   10 (residues 1 to 92)
  AUTHORS   Rahimpour,R., Mitchell,G., Khandaker,M.H., Kong,C., Singh,B.,
            Xu,L., Ochi,A., Feldman,R.D., Pickering,J.G., Gill,B.M. and
            Kelvin,D.J.
  TITLE     Bacterial superantigens induce down-modulation of CC chemokine
            responsiveness in human monocytes via an alternative chemokine
            ligand-independent mechanism
  JOURNAL   J. Immunol. 162 (4), 2299-2307 (1999)
  MEDLINE   99138930
   PUBMED   9973507
REFERENCE   11 (residues 1 to 92)
  AUTHORS   Kokkotou,E.G., Sankale,J.L., Mani,I., Gueye-Ndiaye,A., Schwartz,D.,
            Essex,M.E., Mboup,S. and Kanki,P.J.
  TITLE     In vitro correlates of HIV-2-mediated HIV-1 protection
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 97 (12), 6797-6802 (2000)
  MEDLINE   20300981
   PUBMED   10841574
REFERENCE   12 (residues 1 to 92)
  AUTHORS   Ariel,A., Lider,O., Brill,A., Cahalon,L., Savion,N., Varon,D. and
            Hershkoviz,R.
  TITLE     Induction of interactions between CD44 and hyaluronic acid by a
            short exposure of human T cells to diverse pro-inflammatory
            mediators
  JOURNAL   Immunology 100 (3), 345-351 (2000)
  MEDLINE   20387643
   PUBMED   10929056
REFERENCE   13 (residues 1 to 92)
  AUTHORS   Modi,W.S., Bergeron,J. and Sanford,M.
  TITLE     The human MIP-1beta chemokine is encoded by two paralogous genes,
            ACT-2 and LAG-1
  JOURNAL   Immunogenetics 53 (7), 543-549 (2001)
  MEDLINE   21541404
   PUBMED   11685466
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from J04130.1.
FEATURES             Location/Qualifiers
     source          1..92
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q12"
     Protein         1..92
                     /product="small inducible cytokine A4"
                     /note="lymphocyte-activation gene 1; small inducible
                     cytokine A4 (homologous to mouse Mip-1b)"
     sig_peptide     1..23
                     /note="act-2 protein signal peptide"
     variation       12
                     /allele="M"
                     /allele="V"
                     /db_xref="dbSNP:1049752"
     mat_peptide     24..92
                     /product="act-2 protein"
     Region          24..89
                     /region_name="Small cytokines (intecrine/chemokine),
                     interleukin-8 like"
                     /note="IL8"
                     /db_xref="CDD:pfam00048"
     Region          31..89
                     /region_name="Intercrine alpha family (small cytokine
                     C-X-C) (chemokine CXC)."
                     /note="SCY"
                     /db_xref="CDD:smart00199"
     variation       80
                     /allele="S"
                     /allele="T"
                     /db_xref="dbSNP:1719152"
     CDS             1..92
                     /gene="SCYA4"
                     /coded_by="NM_002984.1:109..387"
                     /db_xref="LocusID:6351"
                     /db_xref="MIM:182284"
ORIGIN      
        1 mklcvtvlsl lmlvaafcsp alsapmgsdp ptaccfsyta rklprnfvvd yyetsslcsq
       61 pavvfqtkrs kqvcadpses wvqeyvydle ln
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_005556. lymphocyte cytoso...[gi:5031855] Links  


LOCUS       LCP2                     533 aa            linear   PRI 07-SEP-2002
DEFINITION  lymphocyte cytosolic protein 2; SH2 domain-containing leukocyte
            protein of 76kD; 76 kDa tyrosine phosphoprotein; lymphocyte
            cytosolic protein 2 (SH2 domain containing leukocyte protein of
            76kD) [Homo sapiens].
ACCESSION   NP_005556
VERSION     NP_005556.1  GI:5031855
DBSOURCE    REFSEQ: accession NM_005565.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Jackman,J.K., Motto,D.G., Sun,Q., Tanemoto,M., Turck,C.W.,
            Peltz,G.A., Koretzky,G.A. and Findell,P.R.
  TITLE     Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein
            associated with Grb2 in T cells
  JOURNAL   J. Biol. Chem. 270 (13), 7029-7032 (1995)
  MEDLINE   95221345
   PUBMED   7706237
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Motto,D.G., Ross,S.E., Wu,J., Hendricks-Taylor,L.R. and
            Koretzky,G.A.
  TITLE     Implication of the GRB2-associated phosphoprotein SLP-76 in T cell
            receptor-mediated interleukin 2 production
  JOURNAL   J. Exp. Med. 183 (4), 1937-1943 (1996)
  MEDLINE   96298954
   PUBMED   8666952
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Sunden,S.L., Carr,L.L., Clements,J.L., Motto,D.G. and Koretzky,G.A.
  TITLE     Polymorphism in and localization of the gene LCP2 (SLP-76) to
            chromosome 5q33.1-qter
  JOURNAL   Genomics 35 (1), 269-270 (1996)
  MEDLINE   96299772
   PUBMED   8661136
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U20158.1.
            Summary: SLP-76 was originally identified as a substrate of the
            ZAP-70 protein tyrosine kinase following T cell receptor (TCR)
            ligation in the leukemic T cell line Jurkat. The SLP-76 locus has
            been localized to human chromosome 5q33 and the gene structure has
            been partially characterized in mice. The human and murine cDNAs
            both encode 533 amino acid proteins that are 72% identical and
            comprised of three modular domains. The NH2-terminus contains an
            acidic region that includes a PEST domain and several tyrosine
            residues which are phosphorylated following TCR ligation. SLP-76
            also contains a central proline-rich domain and a COOH-terminal SH2
            domain. A number of additional proteins have been identified that
            associate with SLP-76 both constitutively and inducibly following
            receptor ligation, supporting the notion that SLP-76 functions as
            an adaptor or scaffold protein. Studies using SLP-76 deficient T
            cell lines or mice have provided strong evidence that SLP-76 plays
            a positive role in promoting T cell development and activation as
            well as mast cell and platelet function [PROW].
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q33.1-qter"
     Protein         1..533
                     /product="lymphocyte cytosolic protein 2"
                     /note="SH2 domain-containing leukocyte protein of 76kD; 76
                     kDa tyrosine phosphoprotein; lymphocyte cytosolic protein
                     2 (SH2 domain containing leukocyte protein of 76kD)"
     Region          12..74
                     /region_name="smart00454, SAM, Sterile alpha motif;
                     Widespread domain in signalling and nuclear proteins. In
                     EPH-related tyrosine kinases, appears to mediate cell-cell
                     initiated signal transduction via the binding of
                     SH2-containing proteins to a conserved tyrosine that is
                     phosphorylated. In many cases mediates homodimerisation"
     Region          420..510
                     /region_name="smart00252, SH2, Src homology 2 domains; Src
                     homology 2 domains bind phosphotyrosine-containing
                     polypeptides via 2 surface pockets. Specificity is
                     provided via interaction with residues that are distinct
                     from the phosphotyrosine. Only a single occurrence of a
                     SH2 domain has been found in S. cerevisiae"
     Region          422..514
                     /region_name="encodes src homology 2 domain"
     Region          422..505
                     /region_name="pfam00017, SH2, SH2 domain"
     CDS             1..533
                     /gene="LCP2"
                     /coded_by="NM_005565.2:208..1809"
                     /db_xref="LocusID:3937"
                     /db_xref="MIM:601603"
ORIGIN      
        1 malrnvpfrs evlgwdpdsl adyfkklnyk dcekavkkyh idgarflnlt endiqkfpkl
       61 rvpilsklsq einkneerrs iftrkpqvpr fpeeteshee dnggwssfee ddyespnddq
      121 dgeddgdyes pneeeeapve ddadyeppps ndeealqnsi lpakpfpnsn smyidrppsg
      181 ktpqqppvpp qrpmaalppp pagrnhsplp ppqtnheeps rsrnhktakl papsidrstk
      241 ppldrslapf drepftlgkk ppfsdkpsip agrslgehlp kiqkpplppt terhersspl
      301 pgkkppvpkh gwgpdrrend eddvhqrplp qpallpmssn tfpsrstkps pmnplpsshm
      361 pgafsesnss fpqsaslppy fsqgpsnrpp iraegrnfpl plpnkprpps paeeenslne
      421 ewyvsyitrp eaeaalrkin qdgtflvrds skktttnpyv lmvlykdkvy niqiryqkes
      481 qvyllgtglr gkedflsvsd iidyfrkmpl llidgknrgs ryqctlthaa gyp
//



Revised: July 5, 2002.
 
 


Disclaimer | Write to the Help Desk
NCBI | NLM | NIH 

 

Oct 21 2002 11:56:56 

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   Search PubMed Protein Nucleotide PopSet Taxonomy Genome OMIM Structure Domains GEO Books Books2 MapViewDr TestDb UniSTS CDD SNP Journals UniGene  for        
 
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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_000570. chemokine (C-C mo...[gi:4502639] Links  


LOCUS       CCR5                     352 aa            linear   PRI 02-MAY-2001
DEFINITION  chemokine (C-C motif) receptor 5; chemokine (C-C) receptor 5; HIV-1
            fusion co-receptor; chemr13 [Homo sapiens].
ACCESSION   NP_000570
VERSION     NP_000570.1  GI:4502639
DBSOURCE    REFSEQ: accession NM_000579.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Samson,M., Labbe,O., Mollereau,C., Vassart,G. and Parmentier,M.
  TITLE     Molecular cloning and functional expression of a new human
            CC-chemokine receptor gene
  JOURNAL   Biochemistry 35 (11), 3362-3367 (1996)
  MEDLINE   96241590
   PUBMED   8639485
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Deng,H., Liu,R., Ellmeier,W., Choe,S., Unutmaz,D., Burkhart,M., Di
            Marzio,P., Marmon,S., Sutton,R.E., Hill,C.M., Davis,C.B.,
            Peiper,S.C., Schall,T.J., Littman,D.R. and Landau,N.R.
  TITLE     Identification of a major co-receptor for primary isolates of HIV-1
  JOURNAL   Nature 381 (6584), 661-666 (1996)
  MEDLINE   96260017
   PUBMED   8649511
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Choe,H., Farzan,M., Sun,Y., Sullivan,N., Rollins,B., Ponath,P.D.,
            Wu,L., Mackay,C.R., LaRosa,G., Newman,W., Gerard,N., Gerard,C. and
            Sodroski,J.
  TITLE     The beta-chemokine receptors CCR3 and CCR5 facilitate infection by
            primary HIV-1 isolates
  JOURNAL   Cell 85 (7), 1135-1148 (1996)
  MEDLINE   96270515
   PUBMED   8674119
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Raport,C.J., Gosling,J., Schweickart,V.L., Gray,P.W. and Charo,I.F.
  TITLE     Molecular cloning and functional characterization of a novel human
            CC chemokine receptor (CCR5) for RANTES, MIP-1beta, and MIP-1alpha
  JOURNAL   J. Biol. Chem. 271 (29), 17161-17166 (1996)
  MEDLINE   96291862
   PUBMED   8663314
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Combadiere,C., Ahuja,S.K., Tiffany,H.L. and Murphy,P.M.
  TITLE     Cloning and functional expression of CC CKR5, a human monocyte CC
            chemokine receptor selective for MIP-1(alpha), MIP-1(beta), and
            RANTES
  JOURNAL   J. Leukoc. Biol. 60 (1), 147-152 (1996)
  MEDLINE   96295970
   PUBMED   8699119
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Daugherty,B.L. and Springer,M.S.
  TITLE     The beta-chemokine receptor genes CCR1 (CMKBR1), CCR2 (CMKBR2), and
            CCR3 (CMKBR3) cluster within 285 kb on human chromosome 3p21
  JOURNAL   Genomics 41 (2), 294-295 (1997)
  MEDLINE   97288534
   PUBMED   9143512
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Kuhmann,S.E., Platt,E.J., Kozak,S.L. and Kabat,D.
  TITLE     Polymorphisms in the CCR5 genes of African green monkeys and mice
            implicate specific amino acids in infections by simian and human
            immunodeficiency viruses
  JOURNAL   J. Virol. 71 (11), 8642-8656 (1997)
  MEDLINE   98001387
   PUBMED   9343222
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Mummidi,S., Ahuja,S.S., McDaniel,B.L. and Ahuja,S.K.
  TITLE     The human CC chemokine receptor 5 (CCR5) gene. Multiple transcripts
            with 5'-end heterogeneity, dual promoter usage, and evidence for
            polymorphisms within the regulatory regions and noncoding exons
  JOURNAL   J. Biol. Chem. 272 (49), 30662-30671 (1997)
  MEDLINE   98049523
   PUBMED   9388201
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Maho,A., Bensimon,A., Vassart,G. and Parmentier,M.
  TITLE     Mapping of the CCXCR1, CX3CR1, CCBP2 and CCR9 genes to the CCR
            cluster within the 3p21.3 region of the human genome
  JOURNAL   Cytogenet. Cell Genet. 87 (3-4), 265-268 (1999)
  MEDLINE   20169206
   PUBMED   10702689
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF031237.1.
            Summary: This gene encodes a member of the beta chemokine receptor
            family, which is predicted to be a seven transmembrane protein
            similar to G protein-coupled receptors. This protein is expressed
            by T cells and macrophages, and is known to be an important
            co-receptor for macrophage-tropic virus, including HIV, to enter
            host cells. Defective alleles of this gene have been associated
            with the HIV infection resistance. The ligands of this receptor
            include monocyte chemoattractant protein 2 (MCP-2), macrophage
            inflammatory protein 1 alpha (MIP-1 alpha), macrophage inflammatory
            protein 1 beta (MIP-1 beta) and regulated on activation normal T
            expressed and secreted protein (RANTES). Expression of this gene
            was also detected in a promyeloblastic cell line, suggesting that
            this protein may play a role in granulocyte lineage proliferation
            and differentiation. This gene is located at the chemokine receptor
            gene cluster region.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21"
     Protein         1..352
                     /product="chemokine (C-C motif) receptor 5"
                     /note="chemokine (C-C) receptor 5; HIV-1 fusion
                     co-receptor; chemr13"
     Region          47..297
                     /region_name="7 transmembrane receptor (rhodopsin family)"
                     /note="7tm_1"
                     /db_xref="CDD:pfam00001"
     variation       55
                     /allele="Q"
                     /allele="L"
                     /db_xref="dbSNP:1799863"
     variation       223
                     /allele="Q"
                     /allele="R"
                     /db_xref="dbSNP:1800452"
     CDS             1..352
                     /gene="CCR5"
                     /coded_by="NM_000579.1:358..1416"
                     /db_xref="LocusID:1234"
                     /db_xref="MIM:601373"
ORIGIN      
        1 mdyqvsspiy dinyytsepc qkinvkqiaa rllpplyslv fifgfvgnml vililinckr
       61 lksmtdiyll nlaisdlffl ltvpfwahya aaqwdfgntm cqlltglyfi gffsgiffii
      121 lltidrylav vhavfalkar tvtfgvvtsv itwvvavfas lpgiiftrsq keglhytcss
      181 hfpysqyqfw knfqtlkivi lglvlpllvm vicysgilkt llrcrnekkr hravrlifti
      241 mivyflfwap ynivlllntf qeffglnncs ssnrldqamq vtetlgmthc cinpiiyafv
      301 gekfrnyllv ffqkhiakrf ckccsifqqe aperassvyt rstgeqeisv gl
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_005169. B-cell CLL/lympho...[gi:4885087] Links  


LOCUS       BCL3                     446 aa            linear   PRI 31-JUL-2002
DEFINITION  B-cell CLL/lymphoma 3; B-cell lymphoma 3-encoded protein; B-cell
            leukemia/lymphoma 3; chronic lymphatic leukemia protein [Homo
            sapiens].
ACCESSION   NP_005169
VERSION     NP_005169.1  GI:4885087
DBSOURCE    REFSEQ: accession NM_005178.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 446)
  AUTHORS   Ohno,H., Takimoto,G. and McKeithan,T.W.
  TITLE     The candidate proto-oncogene bcl-3 is related to genes implicated
            in cell lineage determination and cell cycle control
  JOURNAL   Cell 60 (6), 991-997 (1990)
  MEDLINE   90199880
   PUBMED   2180580
REFERENCE   2  (residues 1 to 446)
  AUTHORS   Wulczyn,F.G., Naumann,M. and Scheidereit,C.
  TITLE     Candidate proto-oncogene bcl-3 encodes a subunit-specific inhibitor
            of transcription factor NF-kappa B
  JOURNAL   Nature 358 (6387), 597-599 (1992)
  MEDLINE   92365824
   PUBMED   1501714
REFERENCE   3  (residues 1 to 446)
  AUTHORS   Franzoso,G., Bours,V., Park,S., Tomita-Yamaguchi,M., Kelly,K. and
            Siebenlist,U.
  TITLE     The candidate oncoprotein Bcl-3 is an antagonist of p50/NF-kappa
            B-mediated inhibition
  JOURNAL   Nature 359 (6393), 339-342 (1992)
  MEDLINE   93024882
   PUBMED   1406939
REFERENCE   4  (residues 1 to 446)
  AUTHORS   Naumann,M., Wulczyn,F.G. and Scheidereit,C.
  TITLE     The NF-kappa B precursor p105 and the proto-oncogene product Bcl-3
            are I kappa B molecules and control nuclear translocation of
            NF-kappa B
  JOURNAL   EMBO J. 12 (1), 213-222 (1993)
  MEDLINE   93154323
   PUBMED   8428580
REFERENCE   5  (residues 1 to 446)
  AUTHORS   Bours,V., Franzoso,G., Azarenko,V., Park,S., Kanno,T., Brown,K. and
            Siebenlist,U.
  TITLE     The oncoprotein Bcl-3 directly transactivates through kappa B
            motifs via association with DNA-binding p50B homodimers
  JOURNAL   Cell 72 (5), 729-739 (1993)
  MEDLINE   93201596
   PUBMED   8453667
REFERENCE   6  (residues 1 to 446)
  AUTHORS   Fujita,T., Nolan,G.P., Liou,H.C., Scott,M.L. and Baltimore,D.
  TITLE     The candidate proto-oncogene bcl-3 encodes a transcriptional
            coactivator that activates through NF-kappa B p50 homodimers
  JOURNAL   Genes Dev. 7 (7B), 1354-1363 (1993)
  MEDLINE   93321864
   PUBMED   8330739
REFERENCE   7  (residues 1 to 446)
  AUTHORS   McKeithan,T.W., Ohno,H., Dickstein,J. and Hume,E.
  TITLE     Genomic structure of the candidate proto-oncogene BCL3
  JOURNAL   Genomics 24 (1), 120-126 (1994)
  MEDLINE   95203866
   PUBMED   7896265
REFERENCE   8  (residues 1 to 446)
  AUTHORS   Watanabe,N., Iwamura,T., Shinoda,T. and Fujita,T.
  TITLE     Regulation of NFKB1 proteins by the candidate oncoprotein BCL-3:
            generation of NF-kappaB homodimers from the cytoplasmic pool of
            p50-p105 and nuclear translocation
  JOURNAL   EMBO J. 16 (12), 3609-3620 (1997)
  MEDLINE   97361841
   PUBMED   9218802
REFERENCE   9  (residues 1 to 446)
  AUTHORS   Bundy,D.L. and McKeithan,T.W.
  TITLE     Diverse effects of BCL3 phosphorylation on its modulation of
            NF-kappaB p52 homodimer binding to DNA
  JOURNAL   J. Biol. Chem. 272 (52), 33132-33139 (1997)
  MEDLINE   98070516
   PUBMED   9407099
REFERENCE   10 (residues 1 to 446)
  AUTHORS   Brasier,A.R., Lu,M., Hai,T., Lu,Y. and Boldogh,I.
  TITLE     NF-kappa B-inducible BCL-3 expression is an autoregulatory loop
            controlling nuclear p50/NF-kappa B1 residence
  JOURNAL   J. Biol. Chem. 276 (34), 32080-32093 (2001)
  MEDLINE   21402875
   PUBMED   11387332
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M31732.1.
            Summary: This gene is a proto-oncogene candidate. It is identified
            by its translocation into the immunoglobulin alpha-locus in some
            cases of B-cell leukemia. The protein encoded by this gene contains
            seven ankyrin repeats, which are most closely related to those
            found in I kappa B proteins. This protein functions as a
            transcriptional co-activator that activates through its association
            with NF-kappa B homodimers. The expression of this gene can be
            induced by NF-kappa B, which forms a part of the autoregulatory
            loop that controls the nuclear residence of p50 NF-kappa B.
FEATURES             Location/Qualifiers
     source          1..446
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.1-q13.2"
     Protein         1..446
                     /product="B-cell CLL/lymphoma 3"
                     /note="B-cell lymphoma 3-encoded protein; B-cell
                     leukemia/lymphoma 3; chronic lymphatic leukemia protein"
     Region          165..195
                     /region_name="pfam00023, ank, Ankyrin repeat. Ankyrin
                     repeats generally consist of a beta, alpha, alpha, beta
                     order of secondary structures. The repeats associate to
                     form a higher order structure"
     Region          233..264
                     /region_name="pfam00023, ank, Ankyrin repeat. Ankyrin
                     repeats generally consist of a beta, alpha, alpha, beta
                     order of secondary structures. The repeats associate to
                     form a higher order structure"
     Region          233..262
                     /region_name="smart00248, ANK, ankyrin repeats; Ankyrin
                     repeats are about 33 amino acids long and occur in at
                     least four consecutive copies. They are involved in
                     protein-protein interactions. The core of the repeat seems
                     to be an helix-loop-helix structure"
     Region          268..297
                     /region_name="pfam00023, ank, Ankyrin repeat. Ankyrin
                     repeats generally consist of a beta, alpha, alpha, beta
                     order of secondary structures. The repeats associate to
                     form a higher order structure"
     Region          268..296
                     /region_name="smart00248, ANK, ankyrin repeats; Ankyrin
                     repeats are about 33 amino acids long and occur in at
                     least four consecutive copies. They are involved in
                     protein-protein interactions. The core of the repeat seems
                     to be an helix-loop-helix structure"
     CDS             1..446
                     /gene="BCL3"
                     /coded_by="NM_005178.2:42..1382"
                     /db_xref="LocusID:602"
                     /db_xref="MIM:109560"
ORIGIN      
        1 mdegpvdlrt rpkaaglpga alplrkrplr apspepaapr gaaglvvpld plrggcdlpa
       61 vpgpphglar pealyypgal lplyptramg spfplvnlpt plypmmcpme hplsadiama
      121 tradedgdtp lhiavvqgnl pavhrlvnlf qqggreldiy nnlrqtplhl avittlpsvv
      181 rllvtagasp maldrhgqta ahlacehrsp tclralldsa apgtldlear nydgltalhv
      241 avntecqetv qlllergadi davdiksgrs plihavenns lsmvqlllqh ganvnaqmys
      301 gssalhsasg rgllplvrtl vrsgadsslk nchndtplmv arsrrvidil rgkatrpast
      361 sqpdpspdrs antspesssr lssngllsas pssspsqspp rdppgfpmap pnfflpspsp
      421 paflpfagvl rgpgrpvpps papggs
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_000086. cartilage oligome...[gi:4557483] Links  


LOCUS       COMP                     757 aa            linear   PRI 31-OCT-2000
DEFINITION  cartilage oligomeric matrix protein presursor; pseudoachondroplasia
            (epiphyseal dysplasia 1, multiple); cartilage oligomeric matrix
            protein(pseudoachondroplasia, epiphyseal dysplasia 1, multiple);
            epiphyseal dysplasia, multiple 1 [Homo sapiens].
ACCESSION   NP_000086
VERSION     NP_000086.1  GI:4557483
DBSOURCE    REFSEQ: accession NM_000095.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Briggs,M.D., Rasmussen,I.M., Weber,J.L., Yuen,J., Reinker,K.,
            Garber,A.P., Rimoin,D.L. and Cohn,D.H.
  TITLE     Genetic linkage of mild pseudoachondroplasia (PSACH) to markers in
            the pericentromeric region of chromosome 19
  JOURNAL   Genomics 18 (3), 656-660 (1993)
  MEDLINE   94140366
   PUBMED   8307576
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Oehlmann,R., Summerville,G.P., Yeh,G., Weaver,E.J., Jimenez,S.A.
            and Knowlton,R.G.
  TITLE     Genetic linkage mapping of multiple epiphyseal dysplasia to the
            pericentromeric region of chromosome 19
  JOURNAL   Am. J. Hum. Genet. 54 (1), 3-10 (1994)
  MEDLINE   94106516
   PUBMED   8279467
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Newton,G., Weremowicz,S., Morton,C.C., Copeland,N.G., Gilbert,D.J.,
            Jenkins,N.A. and Lawler,J.
  TITLE     Characterization of human and mouse cartilage oligomeric matrix
            protein
  JOURNAL   Genomics 24 (3), 435-439 (1994)
  MEDLINE   95229140
   PUBMED   7713493
REFERENCE   4  (residues 1 to 757)
  AUTHORS   Briggs MD, Hoffman SM, King LM, Olsen AS, Mohrenweiser H, Leroy JG,
            Mortier GR, Rimoin DL, Lachman RS, Gaines ES et al.
  TITLE     Pseudoachondroplasia and multiple epiphyseal dysplasia due to
            mutations in the cartilage oligomeric matrix protein gene
  JOURNAL   Nat. Genet. 10 (3), 330-336 (1995)
  MEDLINE   95400302
   PUBMED   7670472
REFERENCE   5  (residues 1 to 757)
  AUTHORS   Ballo,R., Briggs,M.D., Cohn,D.H., Knowlton,R.G., Beighton,P.H. and
            Ramesar,R.S.
  TITLE     Multiple epiphyseal dysplasia, ribbing type: a novel point mutation
            in the COMP gene in a South African family
  JOURNAL   Am. J. Med. Genet. 68 (4), 396-400 (1997)
  MEDLINE   97173141
   PUBMED   9021009
REFERENCE   6  (residues 1 to 757)
  AUTHORS   Briggs,M.D., Mortier,G.R., Cole,W.G., King,L.M., Golik,S.S.,
            Bonaventure,J., Nuytinck,L., De Paepe,A., Leroy,J.G., Biesecker,L.,
            Lipson,M., Wilcox,W.R., Lachman,R.S., Rimoin,D.L., Knowlton,R.G.
            and Cohn,D.H.
  TITLE     Diverse mutations in the gene for cartilage oligomeric matrix
            protein in the pseudoachondroplasia-multiple epiphyseal dysplasia
            disease spectrum
  JOURNAL   Am. J. Hum. Genet. 62 (2), 311-319 (1998)
  MEDLINE   98130533
   PUBMED   9463320
REFERENCE   7  (residues 1 to 757)
  AUTHORS   Rosenberg,K., Olsson,H., Morgelin,M. and Heinegard,D.
  TITLE     Cartilage oligomeric matrix protein shows high affinity
            zinc-dependent interaction with triple helical collagen
  JOURNAL   J. Biol. Chem. 273 (32), 20397-20403 (1998)
  MEDLINE   98352080
   PUBMED   9685393
REFERENCE   8  (residues 1 to 757)
  AUTHORS   Hecht,J.T., Deere,M., Putnam,E., Cole,W., Vertel,B., Chen,H. and
            Lawler,J.
  TITLE     Characterization of cartilage oligomeric matrix protein (COMP) in
            human normal and pseudoachondroplasia musculoskeletal tissues
  JOURNAL   Matrix Biol. 17 (4), 269-278 (1998)
  MEDLINE   98420391
   PUBMED   9749943
REFERENCE   9  (residues 1 to 757)
  AUTHORS   Delot,E., King,L.M., Briggs,M.D., Wilcox,W.R. and Cohn,D.H.
  TITLE     Trinucleotide expansion mutations in the cartilage oligomeric
            matrix protein (COMP) gene
  JOURNAL   Hum. Mol. Genet. 8 (1), 123-128 (1999)
  MEDLINE   99105925
   PUBMED   9887340
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L32137.1.
            Summary: Cartilage oligomeric matrix protein (COMP) is a
            noncollagenous extracellular matrix (ECM) protein. It consists of
            five identical glycoprotein subunits, each with EGF-like and
            calcium-binding (thrombospondin-like) domains. Oligomerization
            results from formation of a five-stranded coiled coil and
            disulfides.  COMP contains an RGD sequence although its functional
            significance is uncertain.  Binding to other ECM proteins such as
            collagen appears to depend on divalent cations.  Mutations can
            cause the osteochondrodysplasias pseudochondroplasia (PSACH) and
            multiple epiphyseal dysplasia (MED).
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.1"
     Protein         1..757
                     /product="cartilage oligomeric matrix protein presursor"
                     /note="pseudoachondroplasia (epiphyseal dysplasia 1,
                     multiple); cartilage oligomeric matrix
                     protein(pseudoachondroplasia, epiphyseal dysplasia 1,
                     multiple); epiphyseal dysplasia, multiple 1"
     sig_peptide     1..20
                     /gene="COMP"
     mat_peptide     21..757
                     /product="cartilage oligomeric matrix protein mature
                     peptide"
     CDS             1..757
                     /gene="COMP"
                     /coded_by="NM_000095.1:26..2299"
                     /db_xref="LocusID:1311"
                     /db_xref="MIM:600310"
ORIGIN      
        1 mvpdtacvll ltlaalgasg qgqsplgsdl gpqmlrelqe tnaalqdvrd wlrqqvreit
       61 flkntvmecd acgmqqsvrt glpsvrpllh capgfcfpgv aciqtesggr cgpcpagftg
      121 ngshctdvne cnahpcfprv rcintspgfr ceacppgysg pthqgvglaf akankqvctd
      181 inecetgqhn cvpnsvcint rgsfqcgpcq pgfvgdqasg cqrgaqrfcp dgspsecheh
      241 adcvlerdgs rscvcrvgwa gngilcgrdt dldgfpdekl rcpepqcrkd ncvtvpnsgq
      301 edvdrdgigd acdpdadgdg vpnekdncpl vrnpdqrntd edkwgdacdn crsqknddqk
      361 dtdqdgrgda cdddidgdri rnqadncprv pnsdqkdsdg dgigdacdnc pqksnpdqad
      421 vdhdfvgdac dsdqdqdgdg hqdsrdncpt vpnsaqedsd hdgqgdacdd dddndgvpds
      481 rdncrlvpnp gqedadrdgv gdvcqddfda dkvvdkidvc penaevtltd frafqtvvld
      541 pegdaqidpn wvvlnqgrei vqtmnsdpgl avgytafngv dfegtfhvnt vtdddyagfi
      601 fgyqdsssfy vvmwkqmeqt ywqanpfrav aepgiqlkav ksstgpgeql rnalwhtgdt
      661 esqvrllwkd prnvgwkdkk syrwflqhrp qvgyirvrfy egpelvadsn vvldttmrgg
      721 rlgvfcfsqe niiwanlryr cndtipedye thqlrqa
//



Revised: July 5, 2002.
 
 


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NCBI | NLM | NIH 

 

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1: NP_000469. tissue non-specif...[gi:13787193] Links  


LOCUS       ALPL                     524 aa            linear   PRI 24-APR-2001
DEFINITION  tissue non-specific alkaline phosphatase precursor;
            glycerophosphatase; alkaline phosphomonoesterase [Homo sapiens].
ACCESSION   NP_000469
VERSION     NP_000469.2  GI:13787193
DBSOURCE    REFSEQ: accession NM_000478.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 524)
  AUTHORS   Weiss,M.J., Henthorn,P.S., Lafferty,M.A., Slaughter,C., Raducha,M.
            and Harris,H.
  TITLE     Isolation and characterization of a cDNA encoding a human
            liver/bone/kidney-type alkaline phosphatase
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 83 (19), 7182-7186 (1986)
  MEDLINE   87016911
   PUBMED   3532105
REFERENCE   2  (residues 1 to 524)
  AUTHORS   Weiss,M.J., Ray,K., Henthorn,P.S., Lamb,B., Kadesch,T. and
            Harris,H.
  TITLE     Structure of the human liver/bone/kidney alkaline phosphatase gene
  JOURNAL   J. Biol. Chem. 263 (24), 12002-12010 (1988)
  MEDLINE   88298884
   PUBMED   3165380
REFERENCE   3  (residues 1 to 524)
  AUTHORS   Kishi,F., Matsuura,S. and Kajii,T.
  TITLE     Nucleotide sequence of the human liver-type alkaline phosphatase
            cDNA
  JOURNAL   Nucleic Acids Res. 17 (5), 2129 (1989)
  MEDLINE   89183624
   PUBMED   2928120
REFERENCE   4  (residues 1 to 524)
  AUTHORS   Orimo,H., Goseki-Sone,M., Sato,S. and Shimada,T.
  TITLE     Detection of deletion 1154-1156 hypophosphatasia mutation using
            TNSALP exon amplification
  JOURNAL   Genomics 42 (2), 364-366 (1997)
  MEDLINE   97336068
   PUBMED   9192863
REFERENCE   5  (residues 1 to 524)
  AUTHORS   Mornet,E.
  TITLE     Hypophosphatasia: the mutations in the tissue-nonspecific alkaline
            phosphatase gene
  JOURNAL   Hum. Mutat. 15 (4), 309-315 (2000)
  MEDLINE   20202136
   PUBMED   10737975
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB011406.1 and M24428.1.
            On Apr 25, 2001 this sequence version replaced gi:4502063.
            Summary: There are at least four distinct but related alkaline
            phosphatases: intestinal, placental, placental-like, and
            liver/bone/kidney (tissue non-specific). The first three are
            located together on chromosome 2 while the tissue non-specific form
            is located on chromosome 1. The product of this gene is a membrane
            bound glycosylated enzyme that is not expressed in any particular
            tissue and is, therefore, referred to as the tissue non-specific
            form of the enzyme. The exact physiological function of the
            alkaline phosphatases is not known. A proposed function of this
            form of the enzyme is matrix mineralization, however, mice that
            lack a functional form of this enzyme show normal skeletal
            development. This enzyme has been linked directly to a disorder
            known as hypophosphatasia, a disorder that is characterized by
            hypercalcemia and includes skeletal  defects. The character of this
            disorder can vary, however, depending on the specific mutation
            since this determines age of onset and severity of symptoms.
FEATURES             Location/Qualifiers
     source          1..524
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.1-p34"
     Protein         1..524
                     /product="tissue non-specific alkaline phosphatase
                     precursor"
                     /EC_number="3.1.3.1"
                     /note="glycerophosphatase; alkaline phosphomonoesterase"
     sig_peptide     1..17
     Region          14..490
                     /region_name="Alkaline phosphatase"
                     /note="alk_phosphatase"
                     /db_xref="CDD:pfam00245"
     mat_peptide     18..524
                     /product="tissue non-specific alkaline phosphatase"
     Region          52..491
                     /region_name="Alkaline phosphatase homologues"
                     /note="alkPPc"
                     /db_xref="CDD:alkPPc"
     Site            110
                     /site_type="active"
     CDS             1..524
                     /gene="ALPL"
                     /coded_by="NM_000478.2:247..1821"
                     /db_xref="LocusID:249"
                     /db_xref="MIM:171760"
ORIGIN      
        1 mispflvlai gtcltnslvp ekekdpkywr dqaqetlkya lelqklntnv aknvimflgd
       61 gmgvstvtaa rilkgqlhhn pgeetrlemd kfpfvalskt yntnaqvpds agtataylcg
      121 vkanegtvgv saatersrcn ttqgnevtsi lrwakdagks vgivtttrvn hatpsaayah
      181 sadrdwysdn emppealsqg ckdiayqlmh nirdidvimg ggrkymypkn ktdveyesde
      241 kargtrldgl dlvdtwksfk prykhshfiw nrtelltldp hnvdyllglf epgdmqyeln
      301 rnnvtdpsls emvvvaiqil rknpkgffll veggridhgh hegkakqalh eavemdraig
      361 qagsltssed tltvvtadhs hvftfggytp rgnsifglap mlsdtdkkpf tailygngpg
      421 ykvvggeren vsmvdyahnn yqaqspvplr hethggedva vfskgpmahl lhgvheqnyv
      481 phvmayaaci ganlghcapa ssagslaagp lllalalypl svlf
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_002017. fibronectin 1 iso...[gi:16933542] Links  


LOCUS       FN1                     2355 aa            linear   PRI 27-AUG-2002
DEFINITION  fibronectin 1 isoform 1 preproprotein; cold-insoluble globulin
            [Homo sapiens].
ACCESSION   NP_002017
VERSION     NP_002017.1  GI:16933542
DBSOURCE    REFSEQ: accession NM_002026.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2355)
  AUTHORS   Kornblihtt,A.R., Vibe-Pedersen,K. and Baralle,F.E.
  TITLE     Isolation and characterization of cDNA clones for human and bovine
            fibronectins
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 80 (11), 3218-3222 (1983)
  MEDLINE   83221567
   PUBMED   6304699
REFERENCE   2  (residues 1 to 2355)
  AUTHORS   Kornblihtt,A.R., Vibe-Pedersen,K. and Baralle,F.E.
  TITLE     Human fibronectin: molecular cloning evidence for two mRNA species
            differing by an internal segment coding for a structural domain
  JOURNAL   EMBO J. 3 (1), 221-226 (1984)
  MEDLINE   84158533
   PUBMED   6200322
REFERENCE   3  (residues 1 to 2355)
  AUTHORS   Kornblihtt,A.R., Vibe-Pedersen,K. and Baralle,F.E.
  TITLE     Human fibronectin: cell specific alternative mRNA splicing
            generates polypeptide chains differing in the number of internal
            repeats
  JOURNAL   Nucleic Acids Res. 12 (14), 5853-5868 (1984)
  MEDLINE   84272258
   PUBMED   6462919
REFERENCE   4  (residues 1 to 2355)
  AUTHORS   Bernard,M.P., Kolbe,M., Weil,D. and Chu,M.L.
  TITLE     Human cellular fibronectin: comparison of the carboxyl-terminal
            portion with rat identifies primary structural domains separated by
            hypervariable regions
  JOURNAL   Biochemistry 24 (11), 2698-2704 (1985)
  MEDLINE   85280409
   PUBMED   2992573
REFERENCE   5  (residues 1 to 2355)
  AUTHORS   Umezawa,K., Kornblihtt,A.R. and Baralle,F.E.
  TITLE     Isolation and characterization of cDNA clones for human liver
            fibronectin
  JOURNAL   FEBS Lett. 186 (1), 31-34 (1985)
  MEDLINE   85231203
   PUBMED   2989004
REFERENCE   6  (residues 1 to 2355)
  AUTHORS   Kornblihtt,A.R., Umezawa,K., Vibe-Pedersen,K. and Baralle,F.E.
  TITLE     Primary structure of human fibronectin: differential splicing may
            generate at least 10 polypeptides from a single gene
  JOURNAL   EMBO J. 4 (7), 1755-1759 (1985)
  MEDLINE   85284965
   PUBMED   2992939
REFERENCE   7  (residues 1 to 2355)
  AUTHORS   Sekiguchi,K., Klos,A.M., Kurachi,K., Yoshitake,S. and Hakomori,S.
  TITLE     Human liver fibronectin complementary DNAs: identification of two
            different messenger RNAs possibly encoding the alpha and beta
            subunits of plasma fibronectin
  JOURNAL   Biochemistry 25 (17), 4936-4941 (1986)
  MEDLINE   87026578
   PUBMED   3021206
REFERENCE   8  (residues 1 to 2355)
  AUTHORS   Gutman,A., Yamada,K.M. and Kornblihtt,A.
  TITLE     Human fibronectin is synthesized as a pre-propolypeptide
  JOURNAL   FEBS Lett. 207 (1), 145-148 (1986)
  MEDLINE   87030890
   PUBMED   3770189
REFERENCE   9  (residues 1 to 2355)
  AUTHORS   Dean,D.C., Bowlus,C.L. and Bourgeois,S.
  TITLE     Cloning and analysis of the promotor region of the human
            fibronectin gene
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 84 (7), 1876-1880 (1987)
  MEDLINE   87175578
   PUBMED   3031656
REFERENCE   10 (residues 1 to 2355)
  AUTHORS   Gutman,A. and Kornblihtt,A.R.
  TITLE     Identification of a third region of cell-specific alternative
            splicing in human fibronectin mRNA
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 84 (20), 7179-7182 (1987)
  MEDLINE   88041070
   PUBMED   3478690
REFERENCE   11 (residues 1 to 2355)
  AUTHORS   Wu,B.L., Milunsky,A., Wyandt,H., Hoth,C., Baldwin,C. and Skare,J.
  TITLE     In situ hybridization applied to Waardenburg syndrome
  JOURNAL   Cytogenet. Cell Genet. 63 (1), 29-32 (1993)
  MEDLINE   93193471
   PUBMED   8449034
REFERENCE   12 (residues 1 to 2355)
  AUTHORS   french-Constant,C.
  TITLE     Alternative splicing of fibronectin--many different proteins but
            few different functions
  JOURNAL   Exp. Cell Res. 221 (2), 261-271 (1995)
  MEDLINE   96086744
   PUBMED   7493623
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X02761.1 and M15801.1.
            Summary: This gene encodes fibronectin, a glycoprotein present in a
            soluble dimeric form in plasma, and in a dimeric or multimeric form
            at the cell surface and in extracellular matrix. Fibronectin is
            involved in cell adhesion and migration processes including
            embryogenesis, wound healing, blood coagulation, host defense, and
            metastasis. The gene has three regions subject to alternative
            splicing, with the potential to produce 20 different transcript
            variants. However, the full length sequence of only two variants is
            known.
            Transcript Variant: This variant (1) lacks an exon containing the
            EDII (extra domain II) region. It encodes a 2355 aa isoform of the
            protein.
FEATURES             Location/Qualifiers
     source          1..2355
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q34"
     Protein         1..2355
                     /product="fibronectin 1 isoform 1 preproprotein"
                     /note="cold-insoluble globulin"
     sig_peptide     1..26
     Proprotein      27..2355
     mat_peptide     32..2355
                     /product="fibronectin 1, isoform 1"
     Region          52..92
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          52..87
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     Region          97..140
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          97..135
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     Region          141..184
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          141..179
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     Region          186..230
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          186..225
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     Region          231..275
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          231..270
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     Region          308..347
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          311..341
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     Region          353..401
                     /region_name="smart00059, FN2, Fibronectin type 2 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Also occurs in coagulation factor
                     XII, 2 type IV collagenases, PDC-109, and
                     cation-independent mannose-6-phosphate and secretory
                     phospholipase A2 receptors. In fibronectin, PDC-109, and
                     the collagenases, this domain contributes to
                     collagen-binding function"
     Region          360..401
                     /region_name="pfam00040, fn2, Fibronectin type II domain"
     Region          413..461
                     /region_name="smart00059, FN2, Fibronectin type 2 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Also occurs in coagulation factor
                     XII, 2 type IV collagenases, PDC-109, and
                     cation-independent mannose-6-phosphate and secretory
                     phospholipase A2 receptors. In fibronectin, PDC-109, and
                     the collagenases, this domain contributes to
                     collagen-binding function"
     Region          420..461
                     /region_name="pfam00040, fn2, Fibronectin type II domain"
     Region          470..508
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          471..508
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     Region          523..560
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          523..555
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     Region          561..604
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          561..599
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     Region          616..688
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          619..688
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          745..798
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          826..891
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          826..889
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          908..986
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          910..988
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          998..1075
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          1000..1076
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          1175..1256
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          1177..1258
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          1268..1334
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          1270..1334
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          1359..1437
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          1361..1438
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          1449..1527
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          1451..1530
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          1543..1621
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          1545..1623
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          1633..1711
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          1635..1713
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          1723..1794
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          1725..1803
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          1815..1892
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          1817..1894
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          1904..1982
                     /region_name="smart00060, FN3, Fibronectin type 3 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. The tenth fibronectin type III
                     repeat contains a RGD cell recognition sequence in a
                     flexible loop between 2 strands. Type III modules are
                     present in both extracellular and intracellular proteins"
     Region          1906..1984
                     /region_name="pfam00041, fn3, Fibronectin type III domain"
     Region          2175..2219
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          2175..2214
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     Region          2220..2261
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          2220..2257
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     Region          2264..2304
                     /region_name="smart00058, FN1, Fibronectin type 1 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Found also in coagulation factor
                     XII, HGF activator and tissue-type plasminogen activator.
                     In t-PA and fibronectin, this domain type contributes to
                     fibrin-binding"
     Region          2264..2299
                     /region_name="pfam00039, fn1, Fibronectin type I domain"
     CDS             1..2355
                     /gene="FN1"
                     /coded_by="NM_002026.1:268..7335"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="LocusID:2335"
                     /db_xref="MIM:135600"
ORIGIN      
        1 mlrgpgpgll llavqclgta vpstgasksk rqaqqmvqpq spvavsqskp gcydngkhyq
       61 inqqwertyl gnalvctcyg gsrgfncesk peaeetcfdk ytgntyrvgd tyerpkdsmi
      121 wdctcigagr grisctianr cheggqsyki gdtwrrphet ggymlecvcl gngkgewtck
      181 piaekcfdha agtsyvvget wekpyqgwmm vdctclgegs gritctsrnr cndqdtrtsy
      241 rigdtwskkd nrgnllqcic tgngrgewkc erhtsvqtts sgsgpftdvr aavyqpqphp
      301 qpppyghcvt dsgvvysvgm qwlktqgnkq mlctclgngv scqetavtqt yggnsngepc
      361 vlpftyngrt fyscttegrq dghlwcstts nyeqdqkysf ctdhtvlvqt rggnsngalc
      421 hfpflynnhn ytdctsegrr dnmkwcgttq nydadqkfgf cpmaaheeic ttnegvmyri
      481 gdqwdkqhdm ghmmrctcvg ngrgewtcia ysqlrdqciv dditynvndt fhkrheeghm
      541 lnctcfgqgr grwkcdpvdq cqdsetgtfy qigdswekyv hgvryqcycy grgigewhcq
      601 plqtypsssg pvevfitetp sqpnshpiqw napqpshisk yilrwrpkns vgrwkeatip
      661 ghlnsytikg lkpgvvyegq lisiqqyghq evtrfdfttt ststpvtsnt vtgettpfsp
      721 lvatsesvte itassfvvsw vsasdtvsgf rveyelseeg depqyldlps tatsvnipdl
      781 lpgrkyivnv yqisedgeqs lilstsqtta pdappdptvd qvddtsivvr wsrpqapitg
      841 yrivyspsve gsstelnlpe tansvtlsdl qpgvqyniti yaveenqest pvviqqettg
      901 tprsdtvpsp rdlqfvevtd vkvtimwtpp esavtgyrvd vipvnlpgeh gqrlpisrnt
      961 faevtglspg vtyyfkvfav shgreskplt aqqttkldap tnlqfvnetd stvlvrwtpp
     1021 raqitgyrlt vgltrrgqpr qynvgpsvsk yplrnlqpas eytvslvaik gnqespkatg
     1081 vfttlqpgss ippyntevte ttivitwtpa prigfklgvr psqggeapre vtsdsgsivv
     1141 sgltpgveyv ytiqvlrdgq erdapivnkv vtplspptnl hleanpdtgv ltvswerstt
     1201 pditgyritt tptngqqgns leevvhadqs sctfdnlspg leynvsvytv kddkesvpis
     1261 dtiipavppp tdlrftnigp dtmrvtwapp psidltnflv ryspvkneed vaelsispsd
     1321 navvltnllp gteyvvsvss vyeqhestpl rgrqktglds ptgidfsdit ansftvhwia
     1381 pratitgyri rhhpehfsgr predrvphsr nsitltnltp gteyvvsiva lngreespll
     1441 igqqstvsdv prdlevvaat ptslliswda pavtvryyri tygetggnsp vqeftvpgsk
     1501 statisglkp gvdytitvya vtgrgdspas skpisinyrt eidkpsqmqv tdvqdnsisv
     1561 kwlpssspvt gyrvtttpkn gpgptktkta gpdqtemtie glqptveyvv svyaqnpsge
     1621 sqplvqtavt nidrpkglaf tdvdvdsiki awespqgqvs ryrvtysspe dgihelfpap
     1681 dgeedtaelq glrpgseytv svvalhddme sqpligtqst aipaptdlkf tqvtptslsa
     1741 qwtppnvqlt gyrvrvtpke ktgpmkeinl apdsssvvvs glmvatkyev svyalkdtlt
     1801 srpaqgvvtt lenvspprra rvtdatetti tiswrtktet itgfqvdavp angqtpiqrt
     1861 ikpdvrsyti tglqpgtdyk iylytlndna rsspvvidas taidapsnlr flattpnsll
     1921 vswqpprari tgyiikyekp gspprevvpr prpgvteati tglepgteyt iyvialknnq
     1981 ksepligrkk tdelpqlvtl phpnlhgpei ldvpstvqkt pfvthpgydt gngiqlpgts
     2041 gqqpsvgqqm ifeehgfrrt tppttatpir hrprpyppnv gqealsqtti swapfqdtse
     2101 yiischpvgt deeplqfrvp gtstsatltg ltrgatynii vealkdqqrh kvreevvtvg
     2161 nsvneglnqp tddscfdpyt vshyavgdew ermsesgfkl lcqclgfgsg hfrcdssrwc
     2221 hdngvnykig ekwdrqgeng qmmsctclgn gkgefkcdph eatcyddgkt yhvgeqwqke
     2281 ylgaicsctc fggqrgwrcd ncrrpggeps pegttgqsyn qysqryhqrt ntnvncpiec
     2341 fmpldvqadr edsre
//



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1: NP_001801. centromere protei...[gi:21735415] Links  


LOCUS       CENPB                    599 aa            linear   PRI 07-SEP-2002
DEFINITION  centromere protein B; centromere protein B (80kD); centromere
            autoantigen B [Homo sapiens].
ACCESSION   NP_001801
VERSION     NP_001801.1  GI:21735415
DBSOURCE    REFSEQ: accession NM_001810.3
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 599)
  AUTHORS   Earnshaw,W.C., Sullivan,K.F., Machlin,P.S., Cooke,C.A.,
            Kaiser,D.A., Pollard,T.D., Rothfield,N.F. and Cleveland,D.W.
  TITLE     Molecular cloning of cDNA for CENP-B, the major human centromere
            autoantigen
  JOURNAL   J. Cell Biol. 104 (4), 817-829 (1987)
  MEDLINE   87166180
   PUBMED   2435739
REFERENCE   2  (residues 1 to 599)
  AUTHORS   Sullivan,K.F. and Glass,C.A.
  TITLE     CENP-B is a highly conserved mammalian centromere protein with
            homology to the helix-loop-helix family of proteins
  JOURNAL   Chromosoma 100 (6), 360-370 (1991)
  MEDLINE   91372020
   PUBMED   1893793
REFERENCE   3  (residues 1 to 599)
  AUTHORS   Yoda,K., Kitagawa,K., Masumoto,H., Muro,Y. and Okazaki,T.
  TITLE     A human centromere protein, CENP-B, has a DNA binding domain
            containing four potential alpha helices at the NH2 terminus, which
            is separable from dimerizing activity
  JOURNAL   J. Cell Biol. 119 (6), 1413-1427 (1992)
  MEDLINE   93107144
   PUBMED   1469042
REFERENCE   4  (residues 1 to 599)
  AUTHORS   Sugimoto,K., Yata,H. and Himeno,M.
  TITLE     Mapping of the human CENP-B gene to chromosome 20 and the CENP-C
            gene to chromosome 12 by a rapid cycle DNA amplification procedure
  JOURNAL   Genomics 17 (1), 240-242 (1993)
  MEDLINE   94010896
   PUBMED   8406460
REFERENCE   5  (residues 1 to 599)
  AUTHORS   Seki,N., Saito,T., Kitagawa,K., Masumoto,H., Okazaki,T. and
            Hori,T.A.
  TITLE     Mapping of the human centromere protein B gene (CENPB) to
            chromosome 20p13 by fluorescence in situ hybridization
  JOURNAL   Genomics 24 (1), 187-188 (1994)
  MEDLINE   95203879
   PUBMED   7896278
REFERENCE   6  (residues 1 to 599)
  AUTHORS   Kitagawa,K., Masumoto,H., Ikeda,M. and Okazaki,T.
  TITLE     Analysis of protein-DNA and protein-protein interactions of
            centromere protein B (CENP-B) and properties of the DNA-CENP-B
            complex in the cell cycle
  JOURNAL   Mol. Cell. Biol. 15 (3), 1602-1612 (1995)
  MEDLINE   95166245
   PUBMED   7862152
REFERENCE   7  (residues 1 to 599)
  AUTHORS   Ando,S., Yang,H., Nozaki,N., Okazaki,T. and Yoda,K.
  TITLE     CENP-A, -B, and -C chromatin complex that contains the I-type
            alpha-satellite array constitutes the prekinetochore in HeLa cells
  JOURNAL   Mol. Cell. Biol. 22 (7), 2229-2241 (2002)
  MEDLINE   21881955
   PUBMED   11884609
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL109804.41.
            Summary: This gene product is a highly conserved protein associated
            with the centromere. It is a DNA-binding protein containing a
            helix-loop-helix DNA binding motif at the N-terminus, and a
            dimerization domain at the C-terminus. The DNA binding domain
            recognizes and binds a 17-bp sequence (CENP-B box) in the
            centromeric satellite DNA. This protein is proposed to play an
            important role in the assembly of specific centromere structures in
            interphase nuclei and on mitotic chromosomes. It is also considered
            a major centromere autoantigen recognized by sera from patients
            with anti-centromere antibodies.
FEATURES             Location/Qualifiers
     source          1..599
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20p13"
                     /cell_type="peripheral lymphocytes"
                     /clone_lib="lambda EMBL 3 genomic"
     Protein         1..599
                     /product="centromere protein B"
                     /note="centromere protein B (80kD); centromere autoantigen
                     B"
     Region          3..134
                     /region_name="pfam03221, Transposase_Tc5, Tc5 transposase"
     Region          74..135
                     /region_name="smart00674, CENPB, Putative DNA-binding
                     domain in centromere protein B, mouse jerky and
                     transposases"
     Region          204..391
                     /region_name="pfam03184, CENP-B, CENP-B protein.
                     Centromere Protein B (CENP-B) is a DNA-binding protein
                     localized to the centromere. Within the N-terminal 125
                     residues, there is a DNA-binding domain, which binds to a
                     corresponding 17bp CENP-B box sequence. In the C-terminal
                     59 residues, CENP-B has a dimerization domain. CENP-B
                     dimers either bind two separate DNA molecules or
                     alternatively, they may bind two CENP-B boxes on one DNA
                     molecule, with the intervening stretch of DNA forming a
                     loop structure. The CENP-B DNA-binding domain consists of
                     two repeating units, RP1 and RP2. RP1 has been shown to
                     consist of four helices in a helix- turn-helix structure"
     CDS             1..599
                     /gene="CENPB"
                     /coded_by="NM_001810.3:1..1800"
                     /db_xref="LocusID:1059"
                     /db_xref="MIM:117140"
ORIGIN      
        1 mgpkrrqltf reksriiqev eenpdlrkge iarrfnipps tlstilknkr ailaserkyg
       61 vastcrktnk lspydklegl liawfqqira aglpvkgiil kekalriaee lgmddftasn
      121 gwldrfrrrh gvvscsgvar ararnaaprt paapaspaav psegsggstt gwrareeqpp
      181 svaegyasqd vfsatetslw ydflpdqaag lcggdgrprq atqrlsvllc anadgseklp
      241 plvagksakp ragqaglpcd ytanskggvt tqalakylka ldtrmaaesr rvlllagrla
      301 aqsldtsglr hvqlaffppg tvhplergvv qqvkghyrqa mllkamaale gqdpsglqlg
      361 ltealhfvaa awqavepsdi aacfreagfg ggpnatitts lksegeeeee eeeeeeeeeg
      421 egeeeeeege eeeeeggege elgeeeevee egdvdsdeee eedeessseg leaedwaqgv
      481 veaggsfgay gaqeeaqcpt lhfleggeds dsdseeedde eeddededdd ddeedgdevp
      541 vpsfgeamay famvkrylts fpiddrvqsh ilhlehdlvh vtrknharqa gvrglghqs
//



Revised: July 5, 2002.
 
 


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1: NP_002014. fibromodulin prec...[gi:4503763] Links  


LOCUS       FMOD                     376 aa            linear   PRI 31-OCT-2000
DEFINITION  fibromodulin precursor [Homo sapiens].
ACCESSION   NP_002014
VERSION     NP_002014.1  GI:4503763
DBSOURCE    REFSEQ: accession NM_002023.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Antonsson,P., Heinegard,D. and Oldberg,A.
  TITLE     Structure and deduced amino acid sequence of the human fibromodulin
            gene
  JOURNAL   Biochim. Biophys. Acta 1174 (2), 204-206 (1993)
  MEDLINE   93363641
   PUBMED   8357838
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Roughley,P.J. and Lee,E.R.
  TITLE     Cartilage proteoglycans: structure and potential functions
  JOURNAL   Microsc. Res. Tech. 28 (5), 385-397 (1994)
  MEDLINE   95003201
   PUBMED   7919526
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Hildebrand,A., Romaris,M., Rasmussen,L.M., Heinegard,D.,
            Twardzik,D.R., Border,W.A. and Ruoslahti,E.
  TITLE     Interaction of the small interstitial proteoglycans biglycan,
            decorin and fibromodulin with transforming growth factor beta
  JOURNAL   Biochem. J. 302 (Pt 2), 527-534 (1994)
  MEDLINE   94379985
   PUBMED   8093006
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Sztrolovics,R., Chen,X.N., Grover,J., Roughley,P.J. and
            Korenberg,J.R.
  TITLE     Localization of the human fibromodulin gene (FMOD) to chromosome
            1q32 and completion of the cDNA sequence
  JOURNAL   Genomics 23 (3), 715-717 (1994)
  MEDLINE   95154849
   PUBMED   7851907
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X75546.1 and U05291.1.
            Summary: Fibromodulin is a member of a family of small interstitial
            proteoglycans, containing a central region composed of leucine-rich
            repeats with 4 keratan sulfate chains flanked by disulfide-bonded
            terminal domains. It may participate in the assembly of the
            extracellular matrix as it interacts with type I and type II
            collagen fibrils and inhibits fibrillogenesis in vitro. It may also
            regulate TGF-beta activities by sequestering TGF-beta into the
            extracellular matrix.
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q32"
     Protein         1..376
                     /product="fibromodulin precursor"
     sig_peptide     1..18
     mat_peptide     19..376
                     /product="fibromodulin"
     Region          76..109
                     /region_name="Leucine rich repeat N-terminal domain"
                     /note="LRRNT"
                     /db_xref="CDD:LRRNT"
     Region          76..105
                     /region_name="Leucine rich repeat N-terminal domain"
                     /note="LRRNT"
                     /db_xref="CDD:pfam01462"
     CDS             1..376
                     /gene="FMOD"
                     /coded_by="NM_002023.2:21..1151"
                     /db_xref="LocusID:2331"
                     /db_xref="MIM:600245"
ORIGIN      
        1 mqwaslllla glfslsqaqy eddphwwfhy lrsqqstyyd pydpypyety epypygvdeg
       61 paytygspsp pdprdcpqec dcppnfltam ycdnrnlkyl pfvpsrmkyv yfqnnqitsi
      121 qegvfdnatg llwialhgnq itsdkvgrkv fsklrhlerl yldhnnltrm pgplprslre
      181 lhldhnqisr vpnnalegle nltalylqhd eiqevgssmr glrslilldl synhlrkvpd
      241 glpsaleqly mehnnvytvp dsyfrgapkl lyvrlshnsl tnnglasntf nssslleldl
      301 synqlqkipp vntnlenlyl qgnrinefsi ssfctvvdvv nfsklqvvrl dgneikrsam
      361 padaplclrl asliei
//



Revised: July 5, 2002.
 
 


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1: NP_036249. chromobox homolog...[gi:6912292] Links  


LOCUS       CBX5                     191 aa            linear   PRI 27-AUG-2002
DEFINITION  chromobox homolog 5 (HP1 alpha homolog, Drosophila); chromobox
            homolog 5 (Drosophila HP1 alpha) [Homo sapiens].
ACCESSION   NP_036249
VERSION     NP_036249.1  GI:6912292
DBSOURCE    REFSEQ: accession NM_012117.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Ye,Q. and Worman,H.J.
  TITLE     Interaction between an integral protein of the nuclear envelope
            inner membrane and human chromodomain proteins homologous to
            Drosophila HP1
  JOURNAL   J. Biol. Chem. 271 (25), 14653-14656 (1996)
  MEDLINE   96278941
   PUBMED   8663349
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from S62077.1.
            Summary: Heterochromatin protein-1 (HP1) is a methyl-lysine binding
            protein localized at heterochromatin sites, where it mediates gene
            silencing.[supplied by OMIM].
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
     Protein         1..191
                     /product="chromobox homolog 5 (HP1 alpha homolog,
                     Drosophila)"
                     /note="chromobox homolog 5 (Drosophila HP1 alpha)"
     Region          20..71
                     /region_name="smart00298, CHROMO, Chromatin organization
                     modifier domain"
     Region          20..57
                     /region_name="pfam00385, chromo, 'chromo' (CHRromatin
                     Organization MOdifier) domain"
     Region          115..176
                     /region_name="smart00300, ChSh, Chromo Shadow Domain"
     Region          119..175
                     /region_name="pfam01393, Chromo_shadow, Chromo shadow
                     domain. This domain is distantly related to pfam00385.
                     This domain is always found in association with a chromo
                     domain"
     CDS             1..191
                     /gene="CBX5"
                     /coded_by="NM_012117.1:135..710"
                     /db_xref="LocusID:23468"
                     /db_xref="MIM:604478"
ORIGIN      
        1 mgkktkrtad ssssedeeey vvekvldrrv vkgqveyllk wkgfseehnt wepeknldcp
       61 elisefmkky kkmkegennk preksesnkr ksnfsnsadd ikskkkreqs ndiargferg
      121 lepekiigat dscgdlmflm kwkdtdeadl vlakeanvkc pqiviafyee rltwhayped
      181 aenkeketak s
//



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1: NP_000376. aquaporin 1; aqua...[gi:4502177] Links  


LOCUS       AQP1                     269 aa            linear   PRI 07-SEP-2002
DEFINITION  aquaporin 1; aquaporin 1 (channel-forming integral protein, 28kDa);
            Aquaporin-1 (channel-forming integral protein, 28kDa); Colton blood
            group [Homo sapiens].
ACCESSION   NP_000376
VERSION     NP_000376.1  GI:4502177
DBSOURCE    REFSEQ: accession NM_000385.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Denker,B.M., Smith,B.L., Kuhajda,F.P. and Agre,P.
  TITLE     Identification, purification, and partial characterization of a
            novel Mr 28,000 integral membrane protein from erythrocytes and
            renal tubules
  JOURNAL   J. Biol. Chem. 263 (30), 15634-15642 (1988)
  MEDLINE   89008472
   PUBMED   3049610
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Preston,G.M. and Agre,P.
  TITLE     Isolation of the cDNA for erythrocyte integral membrane protein of
            28 kilodaltons: member of an ancient channel family
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 88 (24), 11110-11114 (1991)
  MEDLINE   92107900
   PUBMED   1722319
REFERENCE   3  (residues 1 to 269)
  AUTHORS   Moon,C., Preston,G.M., Griffin,C.A., Jabs,E.W. and Agre,P.
  TITLE     The human aquaporin-CHIP gene. Structure, organization, and
            chromosomal localization
  JOURNAL   J. Biol. Chem. 268 (21), 15772-15778 (1993)
  MEDLINE   93340184
   PUBMED   8340403
REFERENCE   4  (residues 1 to 269)
  AUTHORS   Li,X., Yu,H. and Koide,S.S.
  TITLE     The water channel gene in human uterus
  JOURNAL   Biochem. Mol. Biol. Int. 32 (2), 371-377 (1994)
  MEDLINE   94290349
   PUBMED   7517253
REFERENCE   5  (residues 1 to 269)
  AUTHORS   Knepper,M.A.
  TITLE     The aquaporin family of molecular water channels
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 91 (14), 6255-6258 (1994)
  MEDLINE   94294360
   PUBMED   7517546
REFERENCE   6  (residues 1 to 269)
  AUTHORS   Preston,G.M., Smith,B.L., Zeidel,M.L., Moulds,J.J. and Agre,P.
  TITLE     Mutations in aquaporin-1 in phenotypically normal humans without
            functional CHIP water channels
  JOURNAL   Science 265 (5178), 1585-1587 (1994)
  MEDLINE   94360246
   PUBMED   7521540
REFERENCE   7  (residues 1 to 269)
  AUTHORS   Smith,B.L., Preston,G.M., Spring,F.A., Anstee,D.J. and Agre,P.
  TITLE     Human red cell aquaporin CHIP. I. Molecular characterization of ABH
            and Colton blood group antigens
  JOURNAL   J. Clin. Invest. 94 (3), 1043-1049 (1994)
  MEDLINE   94365170
   PUBMED   7521882
REFERENCE   8  (residues 1 to 269)
  AUTHORS   Keen,T.J., Inglehearn,C.F., Patel,R.J., Green,E.D., Peluso,D.C. and
            Bhattacharya,S.S.
  TITLE     Localization of the aquaporin 1 (AQP1) gene within a YAC contig
            containing the polymorphic markers D7S632 and D7S526
  JOURNAL   Genomics 25 (2), 599-600 (1995)
  MEDLINE   95309937
   PUBMED   7540589
REFERENCE   9  (residues 1 to 269)
  AUTHORS   Ruiz,A. and Bok,D.
  TITLE     Characterization of the 3' UTR sequence encoded by the AQP-1 gene
            in human retinal pigment epithelium
  JOURNAL   Biochim. Biophys. Acta 1282 (2), 174-178 (1996)
  MEDLINE   96326579
   PUBMED   8703970
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U41517.1 and M77829.1.
            Summary: Aquaporin 1 (AQP1) ia a molecular water channel protein.
            Aquaporins are a family of small integral membrane proteins related
            to the major intrinsic protein (MIP or AQP0).  Aquaporin 1 a
            homotetramer with 6 bilayer spanning domains and and
            N-glycosylation sites.  The protein physically resembles channel
            proteins and is abundant in erythrocytes and renal tubes.  AQP1 is
            a possible candidate for disorders involving imbalance in ocular
            fluid movement.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p14"
     Protein         1..269
                     /product="aquaporin 1"
                     /note="aquaporin 1 (channel-forming integral protein,
                     28kDa); Aquaporin-1 (channel-forming integral protein,
                     28kDa); Colton blood group"
     Region          4..227
                     /region_name="pfam00230, MIP, Major intrinsic protein. MIP
                     (Major Intrinsic Protein) family proteins exhibit
                     essentially two distinct types of channel properties: (1)
                     specific water transport by the aquaporins, and (2) small
                     neutral solutes transport, such as glycerol by the
                     glycerol facilitators"
     CDS             1..269
                     /gene="AQP1"
                     /coded_by="NM_000385.2:39..848"
                     /note="channel-forming integral membrane protein"
                     /db_xref="LocusID:358"
                     /db_xref="MIM:107776"
                     /db_xref="MIM:110450"
ORIGIN      
        1 masefkkklf wravvaefla ttlfvfisig salgfkypvg nnqtavqdnv kvslafglsi
       61 atlaqsvghi sgahlnpavt lglllscqis ifralmyiia qcvgaivata ilsgitsslt
      121 gnslgrndla dgvnsgqglg ieiigtlqlv lcvlattdrr rrdlggsapl aiglsvalgh
      181 llaidytgcg inparsfgsa vithnfsnhw ifwvgpfigg alavliydfi laprssdltd
      241 rvkvwtsgqv eeydldaddi nsrvemkpk
//



Revised: July 5, 2002.
 
 


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1: NP_006696. growth arrest and...[gi:5729836] Links  


LOCUS       GADD45G                  159 aa            linear   PRI 01-NOV-2000
DEFINITION  growth arrest and DNA-damage-inducible, gamma; GADD45-gamma;
            gadd-related protein, 17 kD [Homo sapiens].
ACCESSION   NP_006696
VERSION     NP_006696.1  GI:5729836
DBSOURCE    REFSEQ: accession NM_006705.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 159)
  AUTHORS   Beadling,C., Johnson,K.W. and Smith,K.A.
  TITLE     Isolation of interleukin 2-induced immediate-early genes
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 90 (7), 2719-2723 (1993)
  MEDLINE   93219355
   PUBMED   7681987
REFERENCE   2  (residues 1 to 159)
  AUTHORS   Takekawa,M. and Saito,H.
  TITLE     A family of stress-inducible GADD45-like proteins mediate
            activation of the stress-responsive MTK1/MEKK4 MAPKKK
  JOURNAL   Cell 95 (4), 521-530 (1998)
  MEDLINE   99043506
   PUBMED   9827804
REFERENCE   3  (residues 1 to 159)
  AUTHORS   Nakayama,K., Hara,T., Hibi,M., Hirano,T. and Miyajima,A.
  TITLE     A novel oncostatin M-inducible gene OIG37 forms a gene family with
            MyD118 and GADD45 and negatively regulates cell growth
  JOURNAL   J. Biol. Chem. 274 (35), 24766-24772 (1999)
  MEDLINE   99386956
   PUBMED   10455148
REFERENCE   4  (residues 1 to 159)
  AUTHORS   Suzuki,M., Watanabe,T.K., Fujiwara,T., Nakamura,Yp.6., Takahashi,E.
            and Tanigami,A.
  TITLE     Molecular cloning, expression, and mapping of a novel human cDNA,
            GRP17, highly homologous to human gadd45 and murine MyD118
  JOURNAL   J. Hum. Genet. 44 (5), 300-303 (1999)
  MEDLINE   99426078
   PUBMED   10496071
REFERENCE   5  (residues 1 to 159)
  AUTHORS   Gong R, Yu L, Zhang H, Tu Q, Zhao Y, Yang J, Xu Y and Zhao S.
  TITLE     Assignment of human GADD45G to chromosome 9q22.1-->q22.3 by
            radiation hybrid mapping
  JOURNAL   Cytogenet. Cell Genet. 88 (1-2), 95-96 (2000)
  MEDLINE   20237539
   PUBMED   10773677
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF079806.1 and AF265659.1.
            Summary: This gene is a member of a group of genes whose transcript
            levels are increased following stressful growth arrest conditions
            and treatment with DNA-damaging agents. The protein encoded by this
            gene responds to environmental stresses by mediating activation of
            the p38/JNK pathway via MTK1/MEKK4 kinase. The GADD45G is highly
            expressed in placenta.
FEATURES             Location/Qualifiers
     source          1..159
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q22.1-q22.2"
     Protein         1..159
                     /product="growth arrest and DNA-damage-inducible, gamma"
                     /note="GADD45-gamma; gadd-related protein, 17 kD"
     variation       112
                     /allele="S"
                     /allele="G"
                     /db_xref="dbSNP:3138505"
     CDS             1..159
                     /gene="GADD45G"
                     /coded_by="NM_006705.2:110..589"
                     /note="MyD118/Gadd45 related protein"
                     /db_xref="LocusID:10912"
                     /db_xref="MIM:604949"
ORIGIN      
        1 mtleevrgqd tvpestarmq gagkalhell lsaqrqgclt agvyesakvl nvdpdnvtfc
       61 vlaageedeg dialqihftl iqafccendi divrvgdvqr laaivgagee agapgdlhci
      121 lisnpnedaw kdpaleklsl fceesrsvnd wvpsitlpe
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_001839. collagen, type VI...[gi:15011913] Links  


LOCUS       COL6A1                  1028 aa            linear   PRI 25-JUL-2001
DEFINITION  collagen, type VI, alpha 1 precursor; collagen VI, alpha-1
            polypeptide; collagen alpha 1(VI) chain; short-chain collagen;
            collagen, intimal [Homo sapiens].
ACCESSION   NP_001839
VERSION     NP_001839.1  GI:15011913
DBSOURCE    REFSEQ: accession NM_001848.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1028)
  AUTHORS   Weil,D., Mattei,M.G., Passage,E., N'Guyen,V.C., Pribula-Conway,D.,
            Mann,K., Deutzmann,R., Timpl,R. and Chu,M.L.
  TITLE     Cloning and chromosomal localization of human genes encoding the
            three chains of type VI collagen
  JOURNAL   Am. J. Hum. Genet. 42 (3), 435-445 (1988)
  MEDLINE   88161046
   PUBMED   3348212
REFERENCE   2  (residues 1 to 1028)
  AUTHORS   Chu,M.L., Conway,D., Pan,T.C., Baldwin,C., Mann,K., Deutzmann,R.
            and Timpl,R.
  TITLE     Amino acid sequence of the triple-helical domain of human collagen
            type VI
  JOURNAL   J. Biol. Chem. 263 (35), 18601-18606 (1988)
  MEDLINE   89066644
   PUBMED   3198591
REFERENCE   3  (residues 1 to 1028)
  AUTHORS   Chu,M.L., Pan,T.C., Conway,D., Kuo,H.J., Glanville,R.W., Timpl,R.,
            Mann,K. and Deutzmann,R.
  TITLE     Sequence analysis of alpha 1(VI) and alpha 2(VI) chains of human
            type VI collagen reveals internal triplication of globular domains
            similar to the A domains of von Willebrand factor and two alpha
            2(VI) chain variants that differ in the carboxy terminus
  JOURNAL   EMBO J. 8 (7), 1939-1946 (1989)
  MEDLINE   90005396
   PUBMED   2551668
REFERENCE   4  (residues 1 to 1028)
  AUTHORS   Saitta,B. and Chu,M.L.
  TITLE     Characterization of the human alpha 1(VI) collagen promoter and its
            comparison with human alpha 2(VI) promoters
  JOURNAL   Eur. J. Biochem. 234 (2), 542-549 (1995)
  MEDLINE   96128186
   PUBMED   8536701
REFERENCE   5  (residues 1 to 1028)
  AUTHORS   Trikka,D., Davis,T., Lapenta,V., Brahe,C. and Kessling,A.M.
  TITLE     Human COL6A1: genomic characterization of the globular domains,
            structural and evolutionary comparison with COL6A2
  JOURNAL   Mamm. Genome 8 (5), 342-345 (1997)
  MEDLINE   97262101
   PUBMED   9107679
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X15880.1, M20776.1, X92430.1
            and X15879.1.
            Summary: The collagens are a superfamily of proteins that play a
            role in maintaining the integrity of various tissues. Collagens are
            extracellular matrix proteins and have a triple-helical domain as
            their common structural element. Collagen VI is a major structural
            component of microfibrils. The basic structural unit of collagen VI
            is a heterotrimer of the alpha1(VI), alpha2(VI), and alpha3(VI)
            chains. The alpha2(VI) and alpha3(VI) chains are encoded by the
            COL6A2 and COL6A3 genes, respectively. The protein encoded by this
            gene is the alpha 1 subunit of type VI collagen (alpha1(VI) chain).
            Mutations in the genes that code for the collagen VI subunits
            result in the autosomal dominant disorder, Bethlem myopathy.
FEATURES             Location/Qualifiers
     source          1..1028
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..1028
                     /product="collagen, type VI, alpha 1 precursor"
                     /note="collagen VI, alpha-1 polypeptide; collagen alpha
                     1(VI) chain; short-chain collagen; collagen, intimal"
     Region          1..256
                     /region_name="amino-terminal globular domain"
     sig_peptide     1..19
     mat_peptide     20..1028
                     /product="collagen, type VI, alpha 1"
     Region          35..218
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          37..218
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          255..296
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          255..296
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          255..296
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          255..289
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          257..592
                     /region_name="triple-helical domain"
     Region          257..296
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          319..376
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          320..378
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          323..382
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          326..385
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          329..388
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          332..387
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          593..1028
                     /region_name="C-terminal globular domain"
     Region          613..776
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          615..797
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          827..1003
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          829..1013
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     CDS             1..1028
                     /gene="COL6A1"
                     /coded_by="NM_001848.1:98..3184"
                     /db_xref="LocusID:1291"
                     /db_xref="MIM:120220"
ORIGIN      
        1 mraarallpl llqacwtaaq depetprava fqdcpvdlff vldtsesval rlkpygalvd
       61 kvksftkrfi dnlrdryyrc drnlvwnaga lhysdeveii qgltrmpggr dalkssvdav
      121 kyfgkgtytd caikkgleql lvggshlken kylivvtdgh plegykepcg gledavneak
      181 hlgvkvfsva itpdhleprl siiatdhtyr rnftaadwgq srdaeeaisq tidtivdmik
      241 nnveqvccsf ecqpargppg lrgdpgfege rgkpglpgek geagdpgrpg dlgpvgyqgm
      301 kgekgsrgek gsrgpkgykg ekgkrgidgv dgvkgemgyp glpgckgspg fdgiqgppgp
      361 kgdpgafglk gekgepgadg eagrpgargp sgdegpagep gppgekgeag degnpgpdga
      421 pgerggpger gprgtpgprg prgdpgeagp qgdqgregpv gvpgdpgeag pigpkgyrgd
      481 egppgsegar gapgpagppg dpglmgerge dgpagngteg fpgfpgypgn rgapgingtk
      541 gypglkgdeg eagdpgddnn diaprgvkga kgyrgpegpq gppghqgppg pdeceildii
      601 mkmcscceck cgpidllfvl dssesiglqn feiakdfvvk vidrlsrdel vkfepgqsya
      661 gvvqyshsqm qehvslrsps irnvqelkea ikslqwmagg tftgealqyt rdqllppspn
      721 nrialvitdg rsdtqrdttp lnvlcspgiq vvsvgikdvf dfipgsdqln viscqglaps
      781 qgrpglslvk enyaelleda flknvtaqic idkkcpdytc pitfsspadi tilldgsasv
      841 gshnfdttkr fakrlaerfl tagrtdpahd vrvavvqysg tgqqrperas lqflqnytal
      901 asavdamdfi ndatdvndal gyvtrfyrea ssgaakkrll lfsdgnsqga tpaaiekavq
      961 eaqragieif vvvvgrqvne phirvlvtgk taeydvayge shlfrvpsyq allrgvfhqt
     1021 vsrkvalg
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_542410. alpha 2 type XI c...[gi:18201915] Links  


LOCUS       COL11A2                 1629 aa            linear   PRI 18-JAN-2002
DEFINITION  alpha 2 type XI collagen, isoform 3 preproprotein [Homo sapiens].
ACCESSION   NP_542410
VERSION     NP_542410.1  GI:18201915
DBSOURCE    REFSEQ: accession NM_080679.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1629)
  AUTHORS   Kimura,T., Cheah,K.S., Chan,S.D., Lui,V.C., Mattei,M.G., van der
            Rest,M., Ono,K., Solomon,E., Ninomiya,Y. and Olsen,B.R.
  TITLE     The human alpha 2(XI) collagen (COL11A2) chain. Molecular cloning
            of cDNA and genomic DNA reveals characteristics of a fibrillar
            collagen with differences in genomic organization
  JOURNAL   J. Biol. Chem. 264 (23), 13910-13916 (1989)
  MEDLINE   89340485
   PUBMED   2760050
REFERENCE   2  (residues 1 to 1629)
  AUTHORS   Zhidkova,N.I., Brewton,R.G. and Mayne,R.
  TITLE     Molecular cloning of PARP (proline/arginine-rich protein) from
            human cartilage and subsequent demonstration that PARP is a
            fragment of the NH2-terminal domain of the collagen alpha 2(XI)
            chain
  JOURNAL   FEBS Lett. 326 (1-3), 25-28 (1993)
  MEDLINE   93314796
   PUBMED   8325374
REFERENCE   3  (residues 1 to 1629)
  AUTHORS   Tsumaki,N. and Kimura,T.
  TITLE     Differential expression of an acidic domain in the amino-terminal
            propeptide of mouse pro-alpha 2(XI) collagen by complex alternative
            splicing
  JOURNAL   J. Biol. Chem. 270 (5), 2372-2378 (1995)
  MEDLINE   95138212
   PUBMED   7836472
REFERENCE   4  (residues 1 to 1629)
  AUTHORS   Vikkula,M., Mariman,E.C., Lui,V.C., Zhidkova,N.I., Tiller,G.E.,
            Goldring,M.B., van Beersum,S.E., de Waal Malefijt,M.C., van den
            Hoogen,F.H., Ropers,H.H. et al.
  TITLE     Autosomal dominant and recessive osteochondrodysplasias associated
            with the COL11A2 locus
  JOURNAL   Cell 80 (3), 431-437 (1995)
  MEDLINE   95163096
   PUBMED   7859284
REFERENCE   5  (residues 1 to 1629)
  AUTHORS   Zhidkova,N.I., Justice,S.K. and Mayne,R.
  TITLE     Alternative mRNA processing occurs in the variable region of the
            pro-alpha 1(XI) and pro-alpha 2(XI) collagen chains
  JOURNAL   J. Biol. Chem. 270 (16), 9486-9493 (1995)
  MEDLINE   95238468
   PUBMED   7721876
REFERENCE   6  (residues 1 to 1629)
  AUTHORS   Vuristo,M.M., Pihlajamaa,T., Vandenberg,P., Prockop,D.J. and
            Ala-Kokko,L.
  TITLE     The human COL11A2 gene structure indicates that the gene has not
            evolved with the genes for the major fibrillar collagens
  JOURNAL   J. Biol. Chem. 270 (39), 22873-22881 (1995)
  MEDLINE   96032717
   PUBMED   7559422
REFERENCE   7  (residues 1 to 1629)
  AUTHORS   Lui,V.C., Ng,L.J., Sat,E.W. and Cheah,K.S.
  TITLE     The human alpha 2(XI) collagen gene (COL11A2): completion of coding
            information, identification of the promoter sequence, and precise
            localization within the major histocompatibility complex reveal
            overlap with the KE5 gene
  JOURNAL   Genomics 32 (3), 401-412 (1996)
  MEDLINE   96435918
   PUBMED   8838804
REFERENCE   8  (residues 1 to 1629)
  AUTHORS   Lui,V.C., Ng,L.J., Sat,E.W., Nicholls,J. and Cheah,K.S.
  TITLE     Extensive alternative splicing within the amino-propeptide coding
            domain of alpha2(XI) procollagen mRNAs. Expression of transcripts
            encoding truncated pro-alpha chains
  JOURNAL   J. Biol. Chem. 271 (28), 16945-16951 (1996)
  MEDLINE   96279277
   PUBMED   8663204
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U32169.1, U41065.1 and
            U41068.1.
            Summary: This gene encodes one of the two alpha chains of type XI
            collagen, a minor fibrillar collagen. It is located on chromosome 6
            very close to but separate from the gene for retinoid X receptor
            beta. Type XI collagen is a heterotrimer but the third alpha chain
            is a post-translationally modified alpha 1 type II chain.
            Proteolytic processing of this type XI chain produces PARP, a
            proline/arginine-rich protein that is an amino terminal domain.
            Mutations in this gene are associated with type III Stickler
            syndrome, otospondylomegaepiphyseal dysplasia (OSMED syndrome),
            Weissenbacher-Zweymuller syndrome, and autosomal dominant
            nonsyndromic sensorineural 13 deafness. Three transcript variants
            encoding different isoforms have been identified for this gene.
            Transcript Variant: This variant (3) does not contain exons 6, 7
            and 8. This results in an isoform (3) that is 107 aa shorter than
            isoform 1.
FEATURES             Location/Qualifiers
     source          1..1629
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.3"
     Protein         1..1629
                     /product="alpha 2 type XI collagen, isoform 3
                     preproprotein"
                     /note="isoform 3 is encoded by transcript variant 3"
     sig_peptide     1..22
     mat_peptide     23..1393
                     /product="alpha 2 type XI collagen, isoform 3"
     Proprotein      24..1629
     Region          31..213
                     /region_name="Thrombospondin N-terminal -like domain"
                     /note="TSPN"
                     /db_xref="CDD:pfam02210"
     Region          31..213
                     /region_name="Thrombospondin N-terminal -like domains."
                     /note="TSPN"
                     /db_xref="CDD:smart00210"
     Region          59..700
                     /region_name="PARP"
     Region          83..208
                     /region_name="Laminin G domain"
                     /note="LamG"
                     /db_xref="CDD:smart00282"
     Region          1433..1628
                     /region_name="Fibrillar collagens C-terminal domain"
                     /note="COLFI"
                     /db_xref="CDD:smart00038"
     Region          1450..1627
                     /region_name="Fibrillar collagen C-terminal domain"
                     /note="COLFI"
                     /db_xref="CDD:pfam01410"
     CDS             1..1629
                     /gene="COL11A2"
                     /coded_by="NM_080679.1:225..5114"
                     /db_xref="LocusID:1302"
                     /db_xref="MIM:120290"
ORIGIN      
        1 mercsrchrl llllplvlgl saapgwagap pvdvlralrf pslpdgvrra kgicpadvay
       61 rvarpaqlsa ptrqlfpggf pkdfslltvv rtrpglqapl ltlysaqgvr qlglelgrpv
      121 rflyedqtgr pqppsqpvfr glsladgkwh rvavavkgqs vtlivdckkr vtrplprsar
      181 pvldthgvii fgarildeev fegdvqelai vpgvqaayes ceqkeleceg gqrerpqnqq
      241 phraqrspqq qpsrlhrpqn qepqsqaahg prglkgekge pavlepgmlv egppgpegpa
      301 gligppgiqg npgpvgdpge rgppgraglp gsdgapgppg tslmlpfrfg sgggdkgpvv
      361 aaqeaqaqai lqqarlalrg ppgpmgytgr pgplgqpgsp glkgesgdlg pqgprgpqgl
      421 tgslgkagrr gragadgarg mpgdpgvkgd rgfdglpglp gekghrgdtg aqglpgppge
      481 dgergddgei gprglpgesg prgllgpkgp pgipgppgvr gmdgpqgpkg slgpqgepgp
      541 pgqqgtpgtq glpgpqgaig phgekgpqgk pglpgmpgsd gppghpgkeg ppgtkgnqgp
      601 sgpqgplgyp gprgvkgvdg irglkghkge kgedgfpgfk gdigvkgdrg evgvpgsrge
      661 dgpegpkgrt gptgdpgppg lmgekgklgv pglpgypgrq gpkgslgfpg fpgasgekga
      721 rglsgksgpr gergptgprg qrgprgatgk sgakgtsggd gphgppgerg lpgpqgpngf
      781 pgpkgppgpp gkdglpghpg qrgevgfqgk tgppgppgvv gpqgaagetg pmgerghpgp
      841 pgppgeqglp gtagkegtkg dpgppgapgk dgpaglrgfp gerglpgtag gpglkgnegp
      901 sgppgpagsp gergaagsgg pigrqgrpgp qgppgaagek gvpgekgpig ptgrdgvqgp
      961 vglpgpagpp gvagedgdkg evgdpgqkgt kgnkgehgpp gppgpigpvg qpgaagadge
     1021 pgargpqghf gakgdegtrg fngppgpigl qglpgpsgek getgdvgpmg ppgppgprgp
     1081 agpngadgpq gppggvgnlg ppgekgepge sgspgiqgep gvkgprgerg ekgesgqpge
     1141 pgppgakgpq gddgpkgnpg pvgfpgdpgp pgeggprgqd gakgdrgedg epgqpgspgp
     1201 tgengppgpl gkrgpagspg segrqggkga kgdpgaigap gktgpvgpag pagkpgpdgl
     1261 rglpgsvgqq grpgatgqag ppgpvgppgl pglrgdagak gekghpglig ligppgeqge
     1321 kgdrglpgpq gspgqkgemg ipgasgpigp ggppglpgpa gpkgakgatg pggpkgekgv
     1381 qgppghpgpp geviqplpiq mpkktrrsvd gsrlmqedea iptggapgsp ggleeifgsl
     1441 dslreeieqm rrptgtqdsp artcqdlklc hpelpdgeyw vdpnqgcard afrvfcnfta
     1501 ggetcvtprd dvtqfsyvds egspvgvvql tflrllsvsa hqdvsypcsg aardgplrlr
     1561 ganedelspe tspyvkefrd gcqtqqgrtv levrtpvleq lpvldasfsd lgapprrggv
     1621 llgpvcfmg
//



Revised: July 5, 2002.
 
 


Disclaimer | Write to the Help Desk
NCBI | NLM | NIH 

 

Oct 21 2002 11:56:56 

BLinkBLinkRelated SequencesRelated SequencesDomain RelativesDomain RelativesDomainsDomainsMap ViewerMap ViewerNucleotideNucleotideOMIMOMIMPubMedPubMedSNPSNPTaxonomyTaxonomyLinkOutLinkOutHelpHelp  


&&&&&&&


    
 
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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_009043. thrombospondin 3 ...[gi:6005902] Links  


LOCUS       THBS3                    956 aa            linear   PRI 27-AUG-2002
DEFINITION  thrombospondin 3 [Homo sapiens].
ACCESSION   NP_009043
VERSION     NP_009043.1  GI:6005902
DBSOURCE    REFSEQ: accession NM_007112.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 956)
  AUTHORS   Vos,H.L., Devarayalu,S., de Vries,Y. and Bornstein,P.
  TITLE     Thrombospondin 3 (Thbs3), a new member of the thrombospondin gene
            family
  JOURNAL   J. Biol. Chem. 267 (17), 12192-12196 (1992)
  MEDLINE   92291102
   PUBMED   1601886
REFERENCE   2  (residues 1 to 956)
  AUTHORS   Bornstein,P., Devarayalu,S., Edelhoff,S. and Disteche,C.M.
  TITLE     Isolation and characterization of the mouse thrombospondin 3
            (Thbs3) gene
  JOURNAL   Genomics 15 (3), 607-613 (1993)
  MEDLINE   93224149
   PUBMED   8468055
REFERENCE   3  (residues 1 to 956)
  AUTHORS   Qabar,A.N., Lin,Z., Wolf,F.W., O'Shea,K.S., Lawler,J. and
            Dixit,V.M.
  TITLE     Thrombospondin 3 is a developmentally regulated heparin binding
            protein
  JOURNAL   J. Biol. Chem. 269 (2), 1262-1269 (1994)
  MEDLINE   94117438
   PUBMED   8288588
REFERENCE   4  (residues 1 to 956)
  AUTHORS   Adolph,K.W., Long,G.L., Winfield,S., Ginns,E.I. and Bornstein,P.
  TITLE     Structure and organization of the human thrombospondin 3 gene
            (THBS3)
  JOURNAL   Genomics 27 (2), 329-336 (1995)
  MEDLINE   96044440
   PUBMED   7558000
REFERENCE   5  (residues 1 to 956)
  AUTHORS   Qabar,A., Derick,L., Lawler,J. and Dixit,V.
  TITLE     Thrombospondin 3 is a pentameric molecule held together by
            interchain disulfide linkage involving two cysteine residues
  JOURNAL   J. Biol. Chem. 270 (21), 12725-12729 (1995)
  MEDLINE   95279412
   PUBMED   7759526
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from L38969.1.
FEATURES             Location/Qualifiers
     source          1..956
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q21"
                     /tissue_type="lung"
                     /dev_stage="fetal"
     Protein         1..956
                     /product="thrombospondin 3"
     Region          23..193
                     /region_name="pfam02210, TSPN, Thrombospondin N-terminal
                     -like domain"
     Region          23..193
                     /region_name="smart00210, TSPN, Thrombospondin N-terminal
                     -like domains; Heparin-binding and cell adhesion domain of
                     thrombospondin"
     Region          316..351
                     /region_name="smart00179, EGF_CA, Calcium-binding EGF-like
                     domain"
     CDS             1..956
                     /gene="THBS3"
                     /coded_by="NM_007112.1:1..2871"
                     /db_xref="LocusID:7059"
                     /db_xref="MIM:188062"
ORIGIN      
        1 metqelrgal allllcffts asqdlqvidl ltvgesrqmv avaekirtal ltagdiylls
       61 tfrlppkqgg vlfglysrqd ntrwleasvv gkinkvlvry qredgkvhav nlqqagladg
      121 rthtvllrlr gpsrpspalh lyvdcklgdq haglpalapi ppaevdglei rtgqkaylrm
      181 qgfvesmkii lggsmarvga lsecpfqgde sihsavtnal hsilgeqtka lvtqltlfnq
      241 ilvelrddir dqvkemslir ntimecqvcg fheqrshcsp npcfrgvdcm evyeypgyrc
      301 gpcppglqgn gthcsdinec ahadpcfpgs scintmpgfh ceacprgykg tqvsgvgidy
      361 araskqvcnd idecndgnng gcdpnsictn tvgsfkcgpc rlgflgnqsq gclpartchs
      421 pahspchiha hclferngav scqcnvgwag ngnvcgtdtd idgypdqalp cmdnnkhckq
      481 dnclltpnsg qedadndgvg dqcdddadgd giknvedncr lfpnkdqqns dtdsfgdacd
      541 ncpnvpnndq kdtdgngegd acdndvdgdg ipngldncpk vpnplqtdrd edgvgdacds
      601 cpemsnptqt dadsdlvgdv cdtnedsdgd ghqdtkdncp qlpnssqlds dndglgdecd
      661 gdddndgipd yvppgpdncr lvpnpnqkds dgngvgdvce ddfdndavvd pldvcpesae
      721 vtltdfrayq tvvldpegda qidpnwvvln qgmeivqtmn sdpglavgyt afngvdfegt
      781 fhvntvtddd yagflfsyqd sgrfyvvmwk qteqtywqat pfravaqpgl qlkavtsvsg
      841 pgehlrnalw htghtpdqvr llwtdprnvg wrdktsyrwq llhrpqvgyi rvklyegpql
      901 vadsgviidt smrggrlgvf cfsqeniiws nlqyrcndtv pedfepfrrq llqgrv
//



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1: NP_037385. dickkopf homolog ...[gi:7019363] Links  


LOCUS       DKK3                     350 aa            linear   PRI 04-OCT-2002
DEFINITION  dickkopf homolog 3; RIG-like 7-1; RIG-like 5-6 [Homo sapiens].
ACCESSION   NP_037385 NP_056966
VERSION     NP_037385.1  GI:7019363
DBSOURCE    REFSEQ: accession NM_013253.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 350)
  AUTHORS   Krupnik,V.E., Sharp,J.D., Jiang,C., Robison,K., Chickering,T.W.,
            Amaravadi,L., Brown,D.E., Guyot,D., Mays,G., Leiby,K., Chang,B.,
            Duong,T., Goodearl,A.D., Gearing,D.P., Sokol,S.Y. and McCarthy,S.A.
  TITLE     Functional and structural diversity of the human Dickkopf gene
            family
  JOURNAL   Gene 238 (2), 301-313 (1999)
  MEDLINE   20035735
   PUBMED   10570958
REFERENCE   2  (residues 1 to 350)
  AUTHORS   Tsuji,T., Miyazaki,M., Sakaguchi,M., Inoue,Y. and Namba,M.
  TITLE     A REIC gene shows down-regulation in human immortalized cells and
            human tumor-derived cell lines
  JOURNAL   Biochem. Biophys. Res. Commun. 268 (1), 20-24 (2000)
  MEDLINE   20119095
   PUBMED   10652205
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF177396.1.
FEATURES             Location/Qualifiers
     source          1..350
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.2"
     Protein         1..350
                     /product="dickkopf homolog 3"
                     /note="RIG-like 7-1; RIG-like 5-6"
     variation       236
                     /allele="M"
                     /allele="V"
                     /db_xref="dbSNP:2291598"
     variation       335
                     /allele="R"
                     /allele="G"
                     /db_xref="dbSNP:3206824"
     CDS             1..350
                     /gene="DKK3"
                     /coded_by="NM_013253.1:38..1090"
                     /note="secreted protein"
                     /db_xref="LocusID:27122"
                     /db_xref="MIM:605416"
ORIGIN      
        1 mqrlgatllc lllaaavpta papaptatsa pvkpgpalsy pqeeatlnem freveelmed
       61 tqhklrsave emeaeeaaak assevnlanl ppsyhnetnt dtkvgnntih vhreihkitn
      121 nqtgqmvfse tvitsvgdee grrsheciid edcgpsmycq fasfqytcqp crgqrmlctr
      181 dseccgdqlc vwghctkmat rgsngticdn qrdcqpglcc afqrgllfpv ctplpvegel
      241 chdpasrlld litwelepdg aldrcpcasg llcqphshsl vyvckptfvg srdqdgeill
      301 prevpdeyev gsfmeevrqe ledlerslte emalgepaaa aaallggeei 
//



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1: NP_005536. immunoglobulin su...[gi:5031809] Links  


LOCUS       ISLR                     428 aa            linear   PRI 01-NOV-2000
DEFINITION  immunoglobulin superfamily containing leucine-rich repeat [Homo
            sapiens].
ACCESSION   NP_005536
VERSION     NP_005536.1  GI:5031809
DBSOURCE    REFSEQ: accession NM_005545.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 428)
  AUTHORS   Nagasawa A, Kudoh J, Noda S, Mashima Y, Wright A, Oguchi Y and
            Shimizu N.
  TITLE     Human and mouse ISLR (immunoglobulin superfamily containing
            leucine-rich repeat) genes: genomic structure and tissue expression
  JOURNAL   Genomics 61 (1), 37-43 (1999)
  MEDLINE   99443870
   PUBMED   10512678
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB003184.1.
FEATURES             Location/Qualifiers
     source          1..428
                     /organism="Homo sapiens"
                     /isolate="Caucasian"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q23-q24"
                     /tissue_type="retina"
                     /clone_lib="human retina 5'-STRECH cDNA library
                     (CLONTECH)"
     Protein         1..428
                     /product="immunoglobulin superfamily containing
                     leucine-rich repeat"
     sig_peptide     1..18
     Region          180..229
                     /region_name="Leucine rich repeat C-terminal domain"
                     /note="LRRCT"
                     /db_xref="CDD:LRRCT"
     Region          180..217
                     /region_name="Leucine rich repeat C-terminal domain"
                     /note="LRRCT"
                     /db_xref="CDD:pfam01463"
     Region          249..334
                     /region_name="Immunoglobulin"
                     /note="IG"
                     /db_xref="CDD:IG"
     CDS             1..428
                     /gene="ISLR"
                     /coded_by="NM_005545.1:99..1385"
                     /db_xref="LocusID:3671"
                     /db_xref="MIM:602059"
ORIGIN      
        1 mqelhllwwa lllglaqacp epcdcgekyg fqiadcayrd lesvppgfpa nvttlslsan
       61 rlpglpegaf revpllqslw lahneirtva agalaslshl ksldlshnli sdfawsdlhn
      121 lsalqllkmd sneltfiprd afrslralrs lqlnhnrlht laegtftplt alshlqinen
      181 pfdctcgivw lktwalttav sipeqdniac tsphvlkgtp lsrlpplpcs apsvqlsyqp
      241 sqdgaelrpg fvlalhcdvd gqpapqlhwh iqipsgivei tspnvgtdgr alpgtpvass
      301 qprfqafang sllipdfgkl eegtysclat nelgsaessv dvalatpgeg gedtlgrrfh
      361 gkavegkgcy tvdnevqpsg pednvviiyl sragnpeaav aegvpgqlpp gllllgqsll
      421 lfffltsf
//



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1: NP_001949. eukaryotic transl...[gi:4503475] Links  


LOCUS       EEF1A2                   463 aa            linear   PRI 31-OCT-2000
DEFINITION  eukaryotic translation elongation factor 1 alpha 2 [Homo sapiens].
ACCESSION   NP_001949
VERSION     NP_001949.1  GI:4503475
DBSOURCE    REFSEQ: accession NM_001958.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 463)
  AUTHORS   Knudsen,S.M., Frydenberg,J., Clark,B.F. and Leffers,H.
  TITLE     Tissue-dependent variation in the expression of elongation factor-1
            alpha isoforms: isolation and characterisation of a cDNA encoding a
            novel variant of human elongation-factor 1 alpha
  JOURNAL   Eur. J. Biochem. 215 (3), 549-554 (1993)
  MEDLINE   93358875
   PUBMED   8354261
REFERENCE   2  (residues 1 to 463)
  AUTHORS   Lund A, Knudsen SM, Vissing H, Clark B and Tommerup N.
  TITLE     Assignment of human elongation factor 1alpha genes: EEF1A maps to
            chromosome 6q14 and EEF1A2 to 20q13.3
  JOURNAL   Genomics 36 (2), 359-361 (1996)
  MEDLINE   96411697
   PUBMED   8812466
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X70940.1.
FEATURES             Location/Qualifiers
     source          1..463
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13.3"
                     /clone_lib="lambda ZAPII; AMA"
     Protein         1..463
                     /product="eukaryotic translation elongation factor 1 alpha
                     2"
     Region          5..416
                     /region_name="Elongation factor Tu family"
                     /note="GTP_EFTU"
                     /db_xref="CDD:pfam00009"
     CDS             1..463
                     /gene="EEF1A2"
                     /coded_by="NM_001958.1:84..1475"
                     /db_xref="LocusID:1917"
                     /db_xref="MIM:602959"
ORIGIN      
        1 mgkekthini vvighvdsgk stttghliyk cggidkrtie kfekeaaemg kgsfkyawvl
       61 dklkaererg itidislwkf ettkyyitii dapghrdfik nmitgtsqad cavlivaagv
      121 gefeagiskn gqtrehalla ytlgvkqliv gvnkmdstep aysekrydei vkevsayikk
      181 igynpatvpf vpisgwhgdn mlepspnmpw fkgwkverke gnasgvslle aldtilpptr
      241 ptdkplrlpl qdvykiggig tvpvgrvetg ilrpgmvvtf apvnittevk svemhheals
      301 ealpgdnvgf nvknvsvkdi rrgnvcgdsk sdppqeaaqf tsqviilnhp gqisagyspv
      361 idchtahiac kfaelkekid rrsgkkledn pkslksgdaa ivemvpgkpm cvesfsqypp
      421 lgrfavrdmr qtvavgvikn vekksggagk vtksaqkaqk agk
//



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1: NP_006279. Thy-1 cell surfac...[gi:19923362] Links  


LOCUS       THY1                     161 aa            linear   PRI 04-APR-2002
DEFINITION  Thy-1 cell surface antigen; Thy-1 T-cell antigen [Homo sapiens].
ACCESSION   NP_006279
VERSION     NP_006279.2  GI:19923362
DBSOURCE    REFSEQ: accession NM_006288.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 161)
  AUTHORS   Poustka,A., Wellenreuther,R., Mewes,H.W., Weil,B. and Wiemann,S.
  TITLE     Homo sapiens Thy-1 cell surface antigen (THY1), mRNA
  JOURNAL   Unpublished (2000)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AL161958.1.
            On Apr 4, 2002 this sequence version replaced gi:5454118.
FEATURES             Location/Qualifiers
     source          1..161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.3-q23"
                     /clone="DKFZp761B15121"
                     /tissue_type="amygdala"
                     /clone_lib="761 (synonym: hamy2). Vector pSport1; host
                     DH10B; sites NotI + SalI"
                     /dev_stage="adult"
     Protein         1..161
                     /product="Thy-1 cell surface antigen"
                     /note="Thy-1 T-cell antigen"
     Region          33..105
                     /region_name="Immunoglobulin V-Type"
                     /note="IGv"
                     /db_xref="CDD:smart00406"
     CDS             1..161
                     /gene="THY1"
                     /coded_by="NM_006288.2:57..542"
                     /note="THY1 (Homo sapiens)"
                     /db_xref="LocusID:7070"
                     /db_xref="MIM:188230"
ORIGIN      
        1 mnlaisiall ltvlqvsrgq kvtsltaclv dqslrldcrh entssspiqy efsltretkk
       61 hvlfgtvgvp ehtyrsrtnf tskynmkvly lsaftskdeg tytcalhhsg hsppissqnv
      121 tvlrdklvkc egisllaqnt swllllllsl sllqatdfms l
//



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1: NP_001702. biglycan prepropr...[gi:4502403] Links  


LOCUS       BGN                      368 aa            linear   PRI 25-MAR-2002
DEFINITION  biglycan preproprotein; bone/cartilage proteoglycan-I; dermatan
            sulphate proteoglycan I [Homo sapiens].
ACCESSION   NP_001702
VERSION     NP_001702.1  GI:4502403
DBSOURCE    REFSEQ: accession NM_001711.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 368)
  AUTHORS   Fisher,L.W., Hawkins,G.R., Tuross,N. and Termine,J.D.
  TITLE     Purification and partial characterization of small proteoglycans I
            and II, bone sialoproteins I and II, and osteonectin from the
            mineral compartment of developing human bone
  JOURNAL   J. Biol. Chem. 262 (20), 9702-9708 (1987)
  MEDLINE   87250639
   PUBMED   3597437
REFERENCE   2  (residues 1 to 368)
  AUTHORS   Fisher,L.W., Termine,J.D. and Young,M.F.
  TITLE     Deduced protein sequence of bone small proteoglycan I (biglycan)
            shows homology with proteoglycan II (decorin) and several
            nonconnective tissue proteins in a variety of species
  JOURNAL   J. Biol. Chem. 264 (8), 4571-4576 (1989)
  MEDLINE   89174714
   PUBMED   2647739
REFERENCE   3  (residues 1 to 368)
  AUTHORS   Roughley,P.J. and White,R.J.
  TITLE     Dermatan sulphate proteoglycans of human articular cartilage. The
            properties of dermatan sulphate proteoglycans I and II
  JOURNAL   Biochem. J. 262 (3), 823-827 (1989)
  MEDLINE   90073579
   PUBMED   2590169
REFERENCE   4  (residues 1 to 368)
  AUTHORS   McBride,O.W., Fisher,L.W. and Young,M.F.
  TITLE     Localization of PGI (biglycan, BGN) and PGII (decorin, DCN, PG-40)
            genes on human chromosomes Xq13-qter and 12q, respectively
  JOURNAL   Genomics 6 (2), 219-225 (1990)
  MEDLINE   90169979
   PUBMED   1968422
REFERENCE   5  (residues 1 to 368)
  AUTHORS   Fleischmajer,R., Fisher,L.W., MacDonald,E.D., Jacobs,L. Jr.,
            Perlish,J.S. and Termine,J.D.
  TITLE     Decorin interacts with fibrillar collagen of embryonic and adult
            human skin
  JOURNAL   J. Struct. Biol. 106 (1), 82-90 (1991)
  MEDLINE   91283344
   PUBMED   2059554
REFERENCE   6  (residues 1 to 368)
  AUTHORS   Fisher,L.W., Heegaard,A.M., Vetter,U., Vogel,W., Just,W.,
            Termine,J.D. and Young,M.F.
  TITLE     Human biglycan gene. Putative promoter, intron-exon junctions, and
            chromosomal localization
  JOURNAL   J. Biol. Chem. 266 (22), 14371-14377 (1991)
  MEDLINE   91317791
   PUBMED   1860845
REFERENCE   7  (residues 1 to 368)
  AUTHORS   Traupe,H., van den Ouweland,A.M., van Oost,B.A., Vogel,W.,
            Vetter,U., Warren,S.T., Rocchi,M., Darlison,M.G. and Ropers,H.H.
  TITLE     Fine mapping of the human biglycan (BGN) gene within the Xq28
            region employing a hybrid cell panel
  JOURNAL   Genomics 13 (2), 481-483 (1992)
  MEDLINE   92307695
   PUBMED   1612609
REFERENCE   8  (residues 1 to 368)
  AUTHORS   Das,S., Metzenberg,A., Pai,G.S. and Gitschier,J.
  TITLE     Mutational analysis of the biglycan gene excludes it as a candidate
            for X-linked dominant chondrodysplasia punctata, dyskeratosis
            congenita, and incontinentia pigmenti
  JOURNAL   Am. J. Hum. Genet. 54 (5), 922-925 (1994)
  MEDLINE   94234162
   PUBMED   8178833
REFERENCE   9  (residues 1 to 368)
  AUTHORS   Geerkens,C., Vetter,U., Just,W., Fedarko,N.S., Fisher,L.W.,
            Young,M.F., Termine,J.D., Robey,P.G., Wohrle,D. and Vogel,W.
  TITLE     The X-chromosomal human biglycan gene BGN is subject to X
            inactivation but is transcribed like an X-Y homologous gene
  JOURNAL   Hum. Genet. 96 (1), 44-52 (1995)
  MEDLINE   95331765
   PUBMED   7607653
REFERENCE   10 (residues 1 to 368)
  AUTHORS   Xu,T., Bianco,P., Fisher,L.W., Longenecker,G., Smith,E.,
            Goldstein,S., Bonadio,J., Boskey,A., Heegaard,A.M., Sommer,B.,
            Satomura,K., Dominguez,P., Zhao,C., Kulkarni,A.B., Robey,P.G. and
            Young,M.F.
  TITLE     Targeted disruption of the biglycan gene leads to an
            osteoporosis-like phenotype in mice
  JOURNAL   Nat. Genet. 20 (1), 78-82 (1998)
  MEDLINE   98400263
   PUBMED   9731537
REFERENCE   11 (residues 1 to 368)
  AUTHORS   Inoue,A., Hayakawa,T., Otsuka,E., Kamiya,A., Suzuki,Y., Hirose,S.
            and Hagiwara,H.
  TITLE     Correlation between induction of expression of biglycan and
            mineralization by C-type natriuretic peptide in osteoblastic cells
  JOURNAL   J. Biochem. 125 (1), 103-108 (1999)
  MEDLINE   99098831
   PUBMED   9880804
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC002416.1 and M65151.1.
            Summary: The protein encoded by this gene is a small cellular or
            pericellular matrix proteoglycan that is closely related in
            structure to two other small proteoglycans, decorin and
            fibromodulin. The encoded protein and decorin are thought to be the
            result of a gene duplication. Decorin contains one attached
            glycosaminoglycan chain, while this protein probably contains two
            chains. For this reason, this protein is called biglycan. This
            protein is thought to function in connective tissue metabolism by
            binding to collagen fibrils and transfering growth factor-beta. It
            may promote neuronal survival. This gene is a candidate gene for
            the Happle syndrome.
FEATURES             Location/Qualifiers
     source          1..368
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq28"
                     /clone="MGC:2298 IMAGE:3162633"
                     /clone_lib="NIH_MGC_19"
     Protein         1..368
                     /product="biglycan preproprotein"
                     /note="bone/cartilage proteoglycan-I; dermatan sulphate
                     proteoglycan I"
     sig_peptide     1..16
     Proprotein      17..368
     mat_peptide     38..368
                     /product="biglycan"
     Region          62..94
                     /region_name="Leucine rich repeat N-terminal domain"
                     /note="LRRNT"
                     /db_xref="CDD:smart00013"
     Region          62..89
                     /region_name="Leucine rich repeat N-terminal domain"
                     /note="LRRNT"
                     /db_xref="CDD:pfam01462"
     CDS             1..368
                     /gene="BGN"
                     /coded_by="NM_001711.2:145..1251"
                     /db_xref="LocusID:633"
                     /db_xref="MIM:301870"
ORIGIN      
        1 mwplwrlvsl lalsqalpfe qrgfwdftld dgpfmmndee asgadtsgvl dpdsvtptys
       61 amcpfgchch lrvvqcsdlg lksvpkeisp dttlldlqnn diselrkddf kglqhlyalv
      121 lvnnkiskih ekafsplrkl qklyisknhl veippnlpss lvelrihdnr irkvpkgvfs
      181 glrnmnciem ggnplensgf epgafdglkl nylriseakl tgipkdlpet lnelhldhnk
      241 iqaieledll rysklyrlgl ghnqirmien gslsflptlr elhldnnkla rvpsglpdlk
      301 llqvvylhsn nitkvgvndf cpmgfgvkra yyngislfnn pvpywevqpa tfrcvtdrla
      361 iqfgnykk
//



Revised: July 5, 2002.
 
 


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1: NP_000081. alpha 1 type III ...[gi:4502951] Links  


LOCUS       COL3A1                  1466 aa            linear   PRI 27-AUG-2002
DEFINITION  alpha 1 type III collagen preproprotein; collagen, fetal [Homo
            sapiens].
ACCESSION   NP_000081
VERSION     NP_000081.1  GI:4502951
DBSOURCE    REFSEQ: accession NM_000090.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1466)
  AUTHORS   Loidl,H.R., Brinker,J.M., May,M., Pihlajaniemi,T., Morrow,S.,
            Rosenbloom,J. and Myers,J.C.
  TITLE     Molecular cloning and carboxyl-propeptide analysis of human type
            III procollagen
  JOURNAL   Nucleic Acids Res. 12 (24), 9383-9394 (1984)
  MEDLINE   85087944
   PUBMED   6096827
REFERENCE   2  (residues 1 to 1466)
  AUTHORS   Emanuel,B.S., Cannizzaro,L.A., Seyer,J.M. and Myers,J.C.
  TITLE     Human alpha 1(III) and alpha 2(V) procollagen genes are located on
            the long arm of chromosome 2
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 82 (10), 3385-3389 (1985)
  MEDLINE   85216505
   PUBMED   3858826
REFERENCE   3  (residues 1 to 1466)
  AUTHORS   Miskulin,M., Dalgleish,R., Kluve-Beckerman,B., Rennard,S.I.,
            Tolstoshev,P., Brantly,M. and Crystal,R.G.
  TITLE     Human type III collagen gene expression is coordinately modulated
            with the type I collagen genes during fibroblast growth
  JOURNAL   Biochemistry 25 (6), 1408-1413 (1986)
  MEDLINE   86187804
   PUBMED   3754462
REFERENCE   4  (residues 1 to 1466)
  AUTHORS   Mankoo,B.S. and Dalgleish,R.
  TITLE     Human pro alpha 1(III) collagen: cDNA sequence for the 3' end
  JOURNAL   Nucleic Acids Res. 16 (5), 2337 (1988)
  MEDLINE   88189827
   PUBMED   3357782
REFERENCE   5  (residues 1 to 1466)
  AUTHORS   Toman,P.D., Ricca,G.A. and de Crombrugghe,B.
  TITLE     Nucleotide sequence of a cDNA coding for the amino-terminal region
            of human prepro alpha 1(III) collagen
  JOURNAL   Nucleic Acids Res. 16 (14B), 7201 (1988)
  MEDLINE   88303360
   PUBMED   3405773
REFERENCE   6  (residues 1 to 1466)
  AUTHORS   Molyneux,K. and Dalgleish,R.
  TITLE     Human type III collagen 'variant' is a cDNA cloning artefact
  JOURNAL   Nucleic Acids Res. 16 (24), 11833 (1988)
  MEDLINE   89098346
   PUBMED   3211760
REFERENCE   7  (residues 1 to 1466)
  AUTHORS   Ala-Kokko,L., Kontusaari,S., Baldwin,C.T., Kuivaniemi,H. and
            Prockop,D.J.
  TITLE     Structure of cDNA clones coding for the entire prepro alpha 1 (III)
            chain of human type III procollagen. Differences in protein
            structure from type I procollagen and conservation of codon
            preferences
  JOURNAL   Biochem. J. 260 (2), 509-516 (1989)
  MEDLINE   89350838
   PUBMED   2764886
REFERENCE   8  (residues 1 to 1466)
  AUTHORS   Janeczko,R.A. and Ramirez,F.
  TITLE     Nucleotide and amino acid sequences of the entire human alpha 1
            (III) collagen
  JOURNAL   Nucleic Acids Res. 17 (16), 6742 (1989)
  MEDLINE   89386015
   PUBMED   2780304
REFERENCE   9  (residues 1 to 1466)
  AUTHORS   Cutting,G.R., McGinniss,M.J., Kasch,L.M., Tsipouras,P. and
            Antonarakis,S.E.
  TITLE     Physical mapping by PFGE localizes the COL3A1 and COL5A2 genes to a
            35-kb region on human chromosome 2
  JOURNAL   Genomics 8 (2), 407-410 (1990)
  MEDLINE   91065664
   PUBMED   1979060
REFERENCE   10 (residues 1 to 1466)
  AUTHORS   Cole,W.G., Chiodo,A.A., Lamande,S.R., Janeczko,R., Ramirez,F.,
            Dahl,H.H., Chan,D. and Bateman,J.F.
  TITLE     A base substitution at a splice site in the COL3A1 gene causes exon
            skipping and generates abnormal type III procollagen in a patient
            with Ehlers-Danlos syndrome type IV
  JOURNAL   J. Biol. Chem. 265 (28), 17070-17077 (1990)
  MEDLINE   91009133
   PUBMED   2145268
REFERENCE   11 (residues 1 to 1466)
  AUTHORS   Chiodo,A.A., Sillence,D.O., Cole,W.G. and Bateman,J.F.
  TITLE     Abnormal type III collagen produced by an exon-17-skipping mutation
            of the COL3A1 gene in Ehlers-Danlos syndrome type IV is not
            incorporated into the extracellular matrix
  JOURNAL   Biochem. J. 311 (Pt 3), 939-943 (1995)
  MEDLINE   96067614
   PUBMED   7487954
REFERENCE   12 (residues 1 to 1466)
  AUTHORS   Limongi,M.Z., Pelliccia,F. and Rocchi,A.
  TITLE     Assignment of the human nebulin gene (NEB) to chromosome band
            2q24.2 and the alpha 1 (III) collagen gene (COL3A1) to chromosome
            band 2q32.2 by in situ hybridization; the FRA2G common fragile site
            lies between the two genes in the 2q31 band
  JOURNAL   Cytogenet. Cell Genet. 77 (3-4), 259-260 (1997)
  MEDLINE   97430831
   PUBMED   9284930
REFERENCE   13 (residues 1 to 1466)
  AUTHORS   Schwarze,U., Schievink,W.I., Petty,E., Jaff,M.R.,
            Babovic-Vuksanovic,D., Cherry,K.J., Pepin,M. and Byers,P.H.
  TITLE     Haploinsufficiency for one COL3A1 allele of type III procollagen
            results in a phenotype similar to the vascular form of
            Ehlers-Danlos syndrome, Ehlers-Danlos syndrome type IV
  JOURNAL   Am. J. Hum. Genet. 69 (5), 989-1001 (2001)
  MEDLINE   21473749
   PUBMED   11577371
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X14420.1, AI755052.1 and
            M26939.1.
            Summary: This gene encodes a fibrillar collagen that is found in
            extensible connective tissues such as skin, lung, and the vascular
            system, frequently in association with type I collagen. Mutations
            in this gene are associated with Ehlers-Danlos syndrome type IV,
            and with aortic and arterial aneurysms. Although alternate
            transcripts have been detected for this gene, they are the result
            of mutations; these mutations alter splicing, often leading to the
            exclusion of multiple exons.
FEATURES             Location/Qualifiers
     source          1..1466
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31"
     Protein         1..1466
                     /product="alpha 1 type III collagen"
                     /note="Collagen III, alpha-1 polypeptide; collagen, fetal"
     Proprotein      1..1466
                     /note="collagen, fetal"
     sig_peptide     1..23
     Proprotein      24..1466
     Region          32..88
                     /region_name="pfam00093, vwc, von Willebrand factor type C
                     domain. The high cutoff was used to prevent overlap with
                     pfam00094"
     Region          32..88
                     /region_name="smart00214, VWC, von Willebrand factor (vWF)
                     type C domain"
     mat_peptide     149..1205
                     /product="alpha 1 type III collagen"
     Region          1231..1466
                     /region_name="smart00038, COLFI, Fibrillar collagens
                     C-terminal domain; Found at C-termini of fibrillar
                     collagens: Ephydatia muelleri procollagen EMF1alpha,
                     vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V
                     etc"
     Region          1248..1465
                     /region_name="pfam01410, COLFI, Fibrillar collagen
                     C-terminal domain. Found at C-termini of fibrillar
                     collagens: Ephydatia muelleri procollagen EMF1 alpha,
                     vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V
                     etc"
     CDS             1..1466
                     /gene="COL3A1"
                     /coded_by="NM_000090.2:118..4518"
                     /db_xref="LocusID:1281"
                     /db_xref="MIM:120180"
ORIGIN      
        1 mmsfvqkgsw lllallhpti ilaqqeaveg gcshlgqsya drdvwkpepc qicvcdsgsv
       61 lcddiicddq eldcpnpeip fgeccavcpq pptaptrppn gqgpqgpkgd pgppgipgrn
      121 gdpgipgqpg spgspgppgi cescptgpqn yspqydsydv ksgvavggla gypgpagppg
      181 ppgppgtsgh pgspgspgyq gppgepgqag psgppgppga igpsgpagkd gesgrpgrpg
      241 erglpgppgi kgpagipgfp gmkghrgfdg rngekgetga pglkgenglp gengapgpmg
      301 prgapgergr pglpgaagar gndgargsdg qpgppgppgt agfpgspgak gevgpagspg
      361 sngapgqrge pgpqghagaq gppgppging spggkgemgp agipgapglm gargppgpag
      421 angapglrgg agepgkngak gepgprgerg eagipgvpga kgedgkdgsp gepganglpg
      481 aagergapgf rgpagpngip gekgpagerg apgpagprga agepgrdgvp ggpgmrgmpg
      541 spggpgsdgk pgppgsqges grpgppgpsg prgqpgvmgf pgpkgndgap gkngerggpg
      601 gpgpqgppgk ngetgpqgpp gptgpggdkg dtgppgpqgl qglpgtggpp gengkpgepg
      661 pkgdagapga pggkgdagap gergppglag apglrggagp pgpeggkgaa gppgppgaag
      721 tpglqgmpge rgglgspgpk gdkgepggpg adgvpgkdgp rgptgpigpp gpagqpgdkg
      781 eggapglpgi agprgspger getgppgpag fpgapgqnge pggkgergap gekgeggppg
      841 vagppggsgp agppgpqgvk gergspggpg aagfpgargl pgppgsngnp gppgpsgspg
      901 kdgppgpagn tgapgspgvs gpkgdagqpg ekgspgaqgp pgapgplgia gitgarglag
      961 ppgmpgprgs pgpqgvkges gkpganglsg ergppgpqgl pglagtagep grdgnpgsdg
     1021 lpgrdgspgg kgdrgengsp gapgapghpg ppgpvgpagk sgdrgesgpa gpagapgpag
     1081 srgapgpqgp rgdkgetger gaagikghrg fpgnpgapgs pgpagqqgai gspgpagprg
     1141 pvgpsgppgk dgtsghpgpi gppgprgnrg ergsegspgh pgqpgppgpp gapgpccggv
     1201 gaaaiagigg ekaggfapyy gdepmdfkin tdeimtslks vngqieslis pdgsrknpar
     1261 ncrdlkfchp elksgeywvd pnqgckldai kvfcnmetge tcisanplnv prkhwwtdss
     1321 aekkhvwfge smdggfqfsy gnpelpedvl dvqlaflrll ssrasqnity hcknsiaymd
     1381 qasgnvkkal klmgsnegef kaegnskfty tvledgctkh tgewsktvfe yrtrkavrlp
     1441 ivdiapydig gpdqefgvdv gpvcfl
//



Revised: July 5, 2002.
 
 


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1: NP_001724. complement compon...[gi:4502493] Links  


LOCUS       C1R                      705 aa            linear   PRI 31-OCT-2000
DEFINITION  complement component 1, r subcomponent [Homo sapiens].
ACCESSION   NP_001724
VERSION     NP_001724.1  GI:4502493
DBSOURCE    REFSEQ: accession NM_001733.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 705)
  AUTHORS   Leytus SP, Kurachi K, Sakariassen KS and Davie EW.
  TITLE     Nucleotide sequence of the cDNA coding for human complement C1r
  JOURNAL   Biochemistry 25 (17), 4855-4863 (1986)
  MEDLINE   87026566
   PUBMED   3021205
REFERENCE   2  (residues 1 to 705)
  AUTHORS   Journet,A. and Tosi,M.
  TITLE     Cloning and sequencing of full-length cDNA encoding the precursor
            of human complement component C1r
  JOURNAL   Biochem. J. 240 (3), 783-787 (1986)
  MEDLINE   87156625
   PUBMED   3030286
REFERENCE   3  (residues 1 to 705)
  AUTHORS   Nguyen VC, Tosi M, Gross MS, Cohen-Haguenauer O, Jegou-Foubert C,
            de Tand MF, Meo T and Frezal J.
  TITLE     Assignment of the complement serine protease genes C1r and C1s to
            chromosome 12 region 12p13
  JOURNAL   Hum. Genet. 78 (4), 363-368 (1988)
  MEDLINE   88197151
   PUBMED   2834284
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X04701.1.
FEATURES             Location/Qualifiers
     source          1..705
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13"
     Protein         1..705
                     /product="complement component 1, r subcomponent"
                     /EC_number="3.4.21.41"
     sig_peptide     1..17
     mat_peptide     18..705
                     /product="complement component 1, r subcomponent"
     Region          27..141
                     /region_name="Domain first found in C1r, C1s, uEGF, and
                     bone morphogenetic protein."
                     /note="CUB"
                     /db_xref="CDD:CUB"
     Region          37..138
                     /region_name="CUB domain"
                     /note="CUB"
                     /db_xref="CDD:pfam00431"
     Region          142..181
                     /region_name="Calcium-binding EGF-like domain"
                     /note="EGF_CA"
                     /db_xref="CDD:EGF_CA"
     Region          156..190
                     /region_name="Epidermal growth factor-like domain"
                     /note="EGF"
                     /db_xref="CDD:EGF"
     Region          193..305
                     /region_name="Domain first found in C1r, C1s, uEGF, and
                     bone morphogenetic protein."
                     /note="CUB"
                     /db_xref="CDD:CUB"
     Region          193..302
                     /region_name="CUB domain"
                     /note="CUB"
                     /db_xref="CDD:pfam00431"
     Region          463..697
                     /region_name="Trypsin-like serine protease"
                     /note="Tryp_SPc"
                     /db_xref="CDD:Tryp_SPc"
     Region          464..697
                     /region_name="Trypsin"
                     /note="trypsin"
                     /db_xref="CDD:pfam00089"
     CDS             1..705
                     /gene="C1R"
                     /coded_by="NM_001733.1:52..2169"
                     /db_xref="LocusID:715"
                     /db_xref="MIM:216950"
ORIGIN      
        1 mwllyllvpa lfcraggsip ipqklfgevt splfpkpypn nfetttvitv ptgyrvklvf
       61 qqfdlepseg cfydyvkisa dkkslgrfcg qlgsplgnpp gkkefmsqgn kmlltfhtdf
      121 sneengtimf ykgflayyqa vdldecasrs klgeedpqpq cqhlchnyvg gyfcscrpgy
      181 elqedrhscq aecsselyte asgyissley prsyppdlrc nysirvergl tlhlkflepf
      241 diddhqqvhc pydqlqiyan gknigefcgk qrppdldtss navdllfftd esgdsrgwkl
      301 rytteiikcp qpktldefti iqnlqpqyqf rdyfiatckq gyqliegnqv lhsftavcqd
      361 dgtwhrampr ckikdcgqpr nlpngdfryt ttmgvntyka riqyychepy ykmqtragsr
      421 eseqgvytct aqgiwkneqk gekiprclpv cgkpvnpveq rqriiggqka kmgnfpwqvf
      481 tnihgrggga llgdrwilta ahtlypkehe aqsnasldvf lghtnveelm klgnhpirrv
      541 svhpdyrqde synfegdial lelensvtlg pnllpiclpd ndtfydlglm gyvsgfgvme
      601 ekiahdlrfv rlpvanpqac enwlrgknrm dvfsqnmfca ghpslkqdac qgdsggvfav
      661 rdpntdrwva tgivswgigc srgygfytkv lnyvdwikke meeed
//



Revised: July 5, 2002.
 
 


Disclaimer | Write to the Help Desk
NCBI | NLM | NIH 

 

Oct 21 2002 11:56:56 

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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_056988. translation initi...[gi:15451892] Links  


LOCUS       IF2                     1220 aa            linear   PRI 06-SEP-2001
DEFINITION  translation initiation factor IF2 [Homo sapiens].
ACCESSION   NP_056988
VERSION     NP_056988.2  GI:15451892
DBSOURCE    REFSEQ: accession NM_015904.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1220)
  AUTHORS   Lee,J.H., Choi,S.K., Roll-Mecak,A., Burley,S.K. and Dever,T.E.
  TITLE     Universal conservation in translation initiation revealed by human
            and archaeal homologs of bacterial translation initiation factor
            IF2
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 96 (8), 4342-4347 (1999)
  MEDLINE   99218282
   PUBMED   10200264
REFERENCE   2  (residues 1 to 1220)
  AUTHORS   Wilson,S.A., Sieiro-Vazquez,C., Edwards,N.J., Iourin,O.,
            Byles,E.D., Kotsopoulou,E., Adamson,C.S., Kingsman,S.M.,
            Kingsman,A.J. and Martin-Rendon,E.
  TITLE     Cloning and characterization of hIF2, a human homologue of
            bacterial translation initiation factor 2, and its interaction with
            HIV-1 matrix
  JOURNAL   Biochem. J. 342 (Pt 1), 97-103 (1999)
  MEDLINE   99362399
   PUBMED   10432305
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF078035.1 and AJ006776.1.
            On Sep 6, 2001 this sequence version replaced gi:7706232.
            Summary: This gene encodes a protein that functions as a
            translation initiation factor and is universally conserved. It
            encodes one of the two proteins identified as translation
            initiation factors, the other factor being a complex composed of
            three subunits. These translation factors act independently of each
            other, however, their function is the same: to position the
            initiator methionine tRNA on the start codon of the mRNA in
            association with the 40S ribosomal subunit and GTP so that
            translation initiates accurately.
FEATURES             Location/Qualifiers
     source          1..1220
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.1-q11.1"
     Protein         1..1220
                     /product="translation initiation factor IF2"
     Region          39..50
                     /region_name="poly-lysine"
     Region          94..99
                     /region_name="poly-lysine"
     Region          138..142
                     /region_name="poly-aspartic acid"
     Region          313..322
                     /region_name="poly-lysine"
     Region          353..356
                     /region_name="poly-glutamic acid"
     Region          361..364
                     /region_name="poly-glutamic acid"
     Region          491..496
                     /region_name="poly-glutamic acid"
     Region          529..567
                     /region_name="acidic region"
     Region          630..962
                     /region_name="Elongation factor Tu family"
                     /note="GTP_EFTU"
                     /db_xref="CDD:pfam00009"
     Region          1039..1162
                     /region_name="Initiation factor 2"
                     /note="IF2"
                     /db_xref="CDD:pfam02131"
     CDS             1..1220
                     /gene="IF2"
                     /coded_by="NM_015904.2:142..3804"
                     /db_xref="LocusID:9669"
                     /db_xref="MIM:606086"
ORIGIN      
        1 mgkkqknkse dstkddidld alaaeiegag aakeqepqks kgkkkkekkk qdfdeddilk
       61 eleelsleaq gikadretva vkptenneee ftskdkkkkg qkgkkqsfdd ndseeledkd
      121 skskktakpk vemysgsddd ddfnklpkka kgkaqksnkk wdgseededn skkikersri
      181 nssgesgdes deflqsrkgq kknqknkpgp niesgneddd asfkiktvaq kkaekkerer
      241 kkrdeekakl rklkekeele tgkkdqskqk esqrkfeeet vkskvtvdtg vipaseekae
      301 tptaaeddne gdkkkkdkkk kkgekeekek ekkkgpskat vkamqealak lkeeeerqkr
      361 eeeerikrle eleakrkeee rleqekrerk kqkekerker lkkegklltk sqreararae
      421 atlkllqaqg vevpskdslp kkrpiyedkk rkkipqqles kevsesmelc aavevmeqgv
      481 pekeetpppv epeeeedted aglddweama sdeetekveg ntvhievken peeeeeeeee
      541 eeedeeseee eeeegesegs egdeedekvs dekdsgktld kkpskemssd seydsdddrt
      601 keeraydkak rriekrrleh sknvnteklr apiicvlghv dtgktkildk lrhthvqdge
      661 aggitqqiwa tnvpleaine qtkmiknfdr envripgmli idtpghesfs nlrnrgsslc
      721 diailvvdim hglepqties inllkskkcp fivalnkidr lydwkkspds dvaatlkkqk
      781 kntkdefeer akaiivefaq qglnaalfye nkdprtfvsl vptsahtgdg mgsliyllve
      841 ltqtmlskrl ahceelraqv mevkalpgmg ttidviling rlkegdtiiv pgvegpivtq
      901 irglllpppm kelrvknqye khkeveaaqg vkilgkdlek tlaglpllva ykedeipvlk
      961 delihelkqt lnaikleekg vyvqastlgs lealleflkt sevpyagini gpvhkkdvmk
     1021 asvmlehdpq yavilafdvr ierdaqemad slgvrifsae iiyhlfdaft kyrqdykkqk
     1081 qeefkhiavf pckikilpqy ifnsrdpivm gvtveagqvk qgtpmcvpsk nfvdigivts
     1141 ieinhkqvdv akkgqevcvk iepipgespk mfgrhfeatd ilvskisrqs idalkdwfrd
     1201 emqksdwqli velkkvfeii 
//



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1: NP_000609. insulin-like grow...[gi:11024682] Links  


LOCUS       IGF1                     153 aa            linear   PRI 04-APR-2002
DEFINITION  insulin-like growth factor 1 (somatomedin C); insulin-like growth
            factor 1 (somatomedia C) [Homo sapiens].
ACCESSION   NP_000609
VERSION     NP_000609.1  GI:11024682
DBSOURCE    REFSEQ: accession NM_000618.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X57025.1.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q22-q23"
                     /tissue_type="liver"
                     /dev_stage="adult"
     Protein         1..153
                     /product="insulin-like growth factor 1 (somatomedin C)"
                     /note="insulin-like growth factor 1 (somatomedia C)"
     sig_peptide     1..48
     mat_peptide     49..118
                     /product="insulin-like growth factor 1 (somatomedin C)"
     Region          51..109
                     /region_name="Insulin / insulin-like growth factor /
                     relaxin family."
                     /note="IlGF"
                     /db_xref="CDD:smart00078"
     Region          51..109
                     /region_name="Insulin/IGF/Relaxin family"
                     /note="Insulin"
                     /db_xref="CDD:pfam00049"
     CDS             1..153
                     /gene="IGF1"
                     /coded_by="NM_000618.2:167..628"
                     /db_xref="LocusID:3479"
                     /db_xref="MIM:147440"
ORIGIN      
        1 mgkisslptq lfkccfcdfl kvkmhtmsss hlfylalcll tftssatagp etlcgaelvd
       61 alqfvcgdrg fyfnkptgyg sssrrapqtg ivdeccfrsc dlrrlemyca plkpaksars
      121 vraqrhtdmp ktqkevhlkn asrgsagnkn yrm
//



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1: NP_071756. popeye protein 3 ...[gi:21359947] Links  


LOCUS       POP3                     291 aa            linear   PRI 12-AUG-2002
DEFINITION  popeye protein 3 [Homo sapiens].
ACCESSION   NP_071756
VERSION     NP_071756.2  GI:21359947
DBSOURCE    REFSEQ: accession NM_022361.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 291)
  AUTHORS   Andree,B., Hillemann,T., Kessler-Icekson,G., Schmitt-John,T.,
            Jockusch,H., Arnold,H.H. and Brand,T.
  TITLE     Isolation and characterization of the novel popeye gene family
            expressed in skeletal muscle and heart
  JOURNAL   Dev. Biol. 223 (2), 371-382 (2000)
  MEDLINE   20341060
   PUBMED   10882522
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC022323.1.
            On Jun 9, 2002 this sequence version replaced gi:11641281.
            Summary: This gene encodes a member of the POP family of proteins
            containing three putative transmembrane domains. This gene is
            expressed in cardiac and skeletal muscle and may play an important
            role in these tissues during development.
FEATURES             Location/Qualifiers
     source          1..291
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q21"
                     /clone="MGC:22671 IMAGE:4293961"
                     /clone_lib="NIH_MGC_81"
     Protein         1..291
                     /product="popeye protein 3"
     CDS             1..291
                     /gene="POP3"
                     /coded_by="NM_022361.2:280..1155"
                     /db_xref="LocusID:64208"
                     /db_xref="MIM:605824"
ORIGIN      
        1 mernsslwkn lidehpvctt wkqeaegaiy hlasilfvvg fmggsgffgl lyvfsllglg
       61 flcsavwawv dvcaadifsw nfvlfvicfm qfvhiayqvr sitfarefqv lysslfqplg
      121 islpvfrtia lssevvtlek ehcyamqgkt sidklsllvs grirvtvdge flhyifplqf
      181 ldspewdslr pteegifqvt ltaetdcryv swrrkklyll faqhryisrl fsvligsdia
      241 dklyalndrv yigkryhydi rlpnfyqmst peirrspltq hfqnsrrycd k
//



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1: NP_001327. cathepsin Z prepr...[gi:22538442] Links  


LOCUS       CTSZ                     303 aa            linear   PRI 29-AUG-2002
DEFINITION  cathepsin Z preproprotein; cathepsin X precursor; preprocathepsin
            P; cathepsin Z precursor [Homo sapiens].
ACCESSION   NP_001327
VERSION     NP_001327.2  GI:22538442
DBSOURCE    REFSEQ: accession NM_001336.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 303)
  AUTHORS   Santamaria,I., Velasco,G., Pendas,A.M., Fueyo,A. and Lopez-Otin,C.
  TITLE     Cathepsin Z, a novel human cysteine proteinase with a short
            propeptide domain and a unique chromosomal location
  JOURNAL   J. Biol. Chem. 273 (27), 16816-16823 (1998)
  MEDLINE   98307916
   PUBMED   9642240
REFERENCE   2  (residues 1 to 303)
  AUTHORS   Nagler,D.K. and Menard,R.
  TITLE     Human cathepsin X: a novel cysteine protease of the papain family
            with a very short proregion and unique insertions
  JOURNAL   FEBS Lett. 434 (1-2), 135-139 (1998)
  MEDLINE   98408845
   PUBMED   9738465
REFERENCE   3  (residues 1 to 303)
  AUTHORS   Pungercar,J. and Ivanovski,G.
  TITLE     Identification and molecular cloning of cathepsin P, a novel human
            putative cysteine protease of the papain family
  JOURNAL   Pflugers Arch. 439 (3 Suppl), R116-R118 (2000)
  MEDLINE   20116863
   PUBMED   10653162
REFERENCE   4  (residues 1 to 303)
  AUTHORS   Pungercar,J., Viyjak,A., Ivanovski,G. and Krizaj,I.
  TITLE     Tissue expression and immunolocalization of a novel human cathepsin
            P
  JOURNAL   Pflugers Arch. 439 (3 Suppl), R119-R121 (2000)
  MEDLINE   20116864
   PUBMED   10653163
REFERENCE   5  (residues 1 to 303)
  AUTHORS   Guncar,G., Klemencic,I., Turk,B., Turk,V.,
            Karaoglanovic-Carmona,A., Juliano,L. and Turk,D.
  TITLE     Crystal structure of cathepsin X: a flip-flop of the ring of His23
            allows carboxy-monopeptidase and carboxy-dipeptidase activity of
            the protease
  JOURNAL   Structure Fold. Des. 8 (3), 305-313 (2000)
  MEDLINE   20211865
   PUBMED   10745011
REFERENCE   6  (residues 1 to 303)
  AUTHORS   Deussing,J., von Olshausen,I. and Peters,C.
  TITLE     Murine and human cathepsin Z: cDNA-cloning, characterization of the
            genes and chromosomal localization
  JOURNAL   Biochim. Biophys. Acta 1491 (1-3), 93-106 (2000)
  MEDLINE   20225452
   PUBMED   10760573
REFERENCE   7  (residues 1 to 303)
  AUTHORS   Bonthron,D.T., Hayward,B.E., Moran,V. and Strain,L.
  TITLE     Characterization of TH1 and CTSZ, two non-imprinted genes
            downstream of GNAS1 in chromosome 20q13
  JOURNAL   Hum. Genet. 107 (2), 165-175 (2000)
  MEDLINE   20483332
   PUBMED   11030415
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF136273.1.
            On Aug 29, 2002 this sequence version replaced gi:4503159.
            Summary: The protein encoded by this gene is a lysosomal cysteine
            proteinase and member of the peptidase C1 family. It exhibits both
            carboxy-monopeptidase and carboxy-dipeptidase activities. The
            encoded protein has also been known as cathepsin X and cathepsin P.
            This gene is expressed ubiquitously in cancer cell lines and
            primary tumors and, like other members of this family, may be
            involved in tumorigenesis. At least two transcript variants of this
            gene have been found, but the full-length nature of only one of
            them has been determined.
FEATURES             Location/Qualifiers
     source          1..303
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q13"
     Protein         1..303
                     /product="cathepsin Z preproprotein"
                     /note="cathepsin X precursor; preprocathepsin P; cathepsin
                     Z precursor"
     sig_peptide     1..23
     Protein         24..303
                     /product="cathepsin Z proprotein"
     mat_peptide     62..303
                     /product="cathepsin Z"
     Region          62..282
                     /region_name="smart00645, Pept_C1, Papain family cysteine
                     protease"
     Region          62..281
                     /region_name="pfam00112, Peptidase_C1, Papain family
                     cysteine protease"
     CDS             1..303
                     /gene="CTSZ"
                     /coded_by="NM_001336.2:126..1037"
                     /db_xref="LocusID:1522"
                     /db_xref="MIM:603169"
ORIGIN      
        1 marrgpgwrp llllvllaga aqgglyfrrg qtcyrplrgd glaplgrsty prpheylspa
       61 dlpkswdwrn vdgvnyasit rnqhipqycg scwahastsa madrinikrk gawpstllsv
      121 qnvidcgnag sceggndlsv wdyahqhgip detcnnyqak dqecdkfnqc gtcnefkech
      181 airnytlwrv gdygslsgre kmmaeiyang piscgimate rlanytggiy aeyqdttyin
      241 hvvsvagwgi sdgteywivr nswgepwger gwlrivtsty kdgkgarynl aieehctfgd
      301 piv
//



Revised: July 5, 2002.
 
 


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1: NP_001060. tubulin, beta pol...[gi:4507729] Links  


LOCUS       TUBB                     445 aa            linear   PRI 27-AUG-2002
DEFINITION  tubulin, beta polypeptide [Homo sapiens].
ACCESSION   NP_001060
VERSION     NP_001060.1  GI:4507729
DBSOURCE    REFSEQ: accession NM_001069.1
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 445)
  AUTHORS   Leffers,H., Wiemann,S. and Ansorge,W.
  TITLE     Cloning and vaccinia virus expression of a cDNA containing the
            complete coding seqeunce of human beta tubulin mRNA
  JOURNAL   Unpublished
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X79535.1.
FEATURES             Location/Qualifiers
     source          1..445
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.3"
                     /clone="nuk_278"
                     /cell_line="non fractionated non cultures normal
                     keratinocytes"
                     /cell_type="keratinocytes"
                     /tissue_type="skin"
                     /clone_lib="lambda ZapII"
     Protein         1..445
                     /product="tubulin, beta polypeptide"
     Region          45..244
                     /region_name="pfam00091, tubulin, Tubulin/FtsZ family,
                     GTPase domain. This family includes the tubulin alpha,
                     beta and gamma chains, as well as the bacterial FtsZ
                     family of proteins. Members of this family are involved in
                     polymer formation. FtsZ is the polymer-forming protein of
                     bacterial cell division. It is part of a ring in the
                     middle of the dividing cell that is required for
                     constriction of cell membrane and cell envelope to yield
                     two daughter cells. FtsZ and tubulin are GTPases. FtsZ can
                     polymerise into tubes, sheets, and rings in vitro and is
                     ubiquitous in eubacteria and archaea. Tubulin is the major
                     component of microtubules"
     Region          246..383
                     /region_name="pfam03953, tubulin_C, Tubulin/FtsZ family,
                     C-terminal domain. This family includes the tubulin alpha,
                     beta and gamma chains, as well as the bacterial FtsZ
                     family of proteins. Members of this family are involved in
                     polymer formation. FtsZ is the polymer-forming protein of
                     bacterial cell division. It is part of a ring in the
                     middle of the dividing cell that is required for
                     constriction of cell membrane and cell envelope to yield
                     two daughter cells. FtsZ and tubulin are GTPases. FtsZ can
                     polymerise into tubes, sheets, and rings in vitro and is
                     ubiquitous in eubacteria and archaea. Tubulin is the major
                     component of microtubules"
     variation       433
                     /allele="Q"
                     /allele="E"
                     /db_xref="dbSNP:1054419"
     CDS             1..445
                     /gene="TUBB"
                     /coded_by="NM_001069.1:64..1401"
                     /db_xref="LocusID:7280"
                     /db_xref="MIM:191130"
ORIGIN      
        1 mreivhiqag qcgnqigakf wevisdehgi dptgsyhgds dlqlerinvy yneaagnkyv
       61 prailvdlep gtmdsvrsgp fgqifrpdnf vfgqsgagnn wakghytega elvdsvldvv
      121 rkesescdcl qgfqlthslg ggtgsgmgtl liskireeyp drimntfsvm pspkvsdtvv
      181 epynatlsvh qlventdety sidnealydi cfrtlklttp tygdlnhlvs atmsgvttcl
      241 rfpgqlnadl rklavnmvpf prlhffmpgf apltsrgsqq yraltvpelt qqmfdsknmm
      301 aacdprhgry ltvaaifrgr msmkevdeqm lnvqnknssy fvewipnnvk tavcdipprg
      361 lkmsatfign staiqelfkr iseqftamfr rkaflhwytg egmdemefte aesnmndlvs
      421 eyqqyqdata deqgefeeee gedea
//



Revised: July 5, 2002.
 
 


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1: NP_001190. bone morphogeneti...[gi:4502421] Links  


LOCUS       BMP1                     730 aa            linear   PRI 03-FEB-2001
DEFINITION  bone morphogenetic protein 1, isoform 1, precursor; PCP [Homo
            sapiens].
ACCESSION   NP_001190
VERSION     NP_001190.1  GI:4502421
DBSOURCE    REFSEQ: accession NM_001199.1
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 730)
  AUTHORS   Wozney,J.M., Rosen,V., Celeste,A.J., Mitsock,L.M., Whitters,M.J.,
            Kriz,R.W., Hewick,R.M. and Wang,E.A.
  TITLE     Novel regulators of bone formation: molecular clones and activities
  JOURNAL   Science 242 (4885), 1528-1534 (1988)
  MEDLINE   89072730
   PUBMED   3201241
REFERENCE   2  (residues 1 to 730)
  AUTHORS   Tabas,J.A., Zasloff,M., Wasmuth,J.J., Emanuel,B.S., Altherr,M.R.,
            McPherson,J.D., Wozney,J.M. and Kaplan,F.S.
  TITLE     Bone morphogenetic protein: chromosomal localization of human genes
            for BMP1, BMP2A, and BMP3
  JOURNAL   Genomics 9 (2), 283-289 (1991)
  MEDLINE   91169531
   PUBMED   2004778
REFERENCE   3  (residues 1 to 730)
  AUTHORS   Takahara,K., Lyons,G.E. and Greenspan,D.S.
  TITLE     Bone morphogenetic protein-1 and a mammalian tolloid homologue
            (mTld) are encoded by alternatively spliced transcripts which are
            differentially expressed in some tissues
  JOURNAL   J. Biol. Chem. 269 (51), 32572-32578 (1994)
  MEDLINE   95096114
   PUBMED   7798260
REFERENCE   4  (residues 1 to 730)
  AUTHORS   Takahara,K., Lee,S., Wood,S. and Greenspan,D.S.
  TITLE     Structural organization and genetic localization of the human bone
            morphogenetic protein 1/mammalian tolloid gene
  JOURNAL   Genomics 29 (1), 9-15 (1995)
  MEDLINE   96079086
   PUBMED   8530106
REFERENCE   5  (residues 1 to 730)
  AUTHORS   Kessler,E., Takahara,K., Biniaminov,L., Brusel,M. and
            Greenspan,D.S.
  TITLE     Bone morphogenetic protein-1: the type I procollagen C-proteinase
  JOURNAL   Science 271 (5247), 360-362 (1996)
  MEDLINE   96144687
   PUBMED   8553073
REFERENCE   6  (residues 1 to 730)
  AUTHORS   Li,S.W., Sieron,A.L., Fertala,A., Hojima,Y., Arnold,W.V. and
            Prockop,D.J.
  TITLE     The C-proteinase that processes procollagens to fibrillar collagens
            is identical to the protein previously identified as bone
            morphogenic protein-1
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 93 (10), 5127-5130 (1996)
  MEDLINE   96209868
   PUBMED   8643539
REFERENCE   7  (residues 1 to 730)
  AUTHORS   Janitz,M., Heiser,V., Bottcher,U., Landt,O. and Lauster,R.
  TITLE     Three alternatively spliced variants of the gene coding for the
            human bone morphogenetic protein-1
  JOURNAL   J. Mol. Med. 76 (2), 141-146 (1998)
  MEDLINE   98160316
   PUBMED   9500680
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M22488.1.
            Summary: The BMP1 locus encodes a protein that is capable of
            inducing formation of cartilage in vivo.  Although other bone
            morphogenetic proteins are members of the TGF-beta superfamily,
            BMP1 encodes a protein that is not closely related to other known
            growth factors. BMP1 protein and procollagen C proteinase (PCP), a
            secreted metalloprotease requiring calcium and needed for cartilage
            and bone formation, are identical. PCP or BMP1 protein cleaves the
            C-terminal propeptides of procollagen I, II, and III and its
            activity is increased by the procollagen C-endopeptidase enhancer
            protein.  The BMP1 gene is expressed as alternatively spliced
            variants that share an N-terminal protease domain but differ in
            their C-terminal region.
            Transcript Variant: This is splice variant BMP1-1. BMP1-1 does not
            contain sequence from alternatively spliced exons 6, 11, 16, 19, 20
            and 22 through 26.
FEATURES             Location/Qualifiers
     source          1..730
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p21"
     Protein         1..730
                     /product="bone morphogenetic protein 1, isoform 1,
                     precursor"
                     /EC_number="3.4.24.-"
                     /note="PCP"
     sig_peptide     1..22
     Protein         23..730
                     /product="bone morphogenetic protein 1, isoform 1,
                     precursor"
                     /EC_number="3.4.24.-"
                     /note="PCP"
     mat_peptide     121..730
                     /product="bone morphogenetic protein 1"
     Region          121..321
                     /region_name="metalloprotease domain"
     Region          128..318
                     /region_name="Astacin (Peptidase family M12A)"
                     /note="Astacin"
                     /db_xref="CDD:pfam01400"
     Region          142..253
                     /region_name="Zinc-dependent metalloprotease"
                     /note="ZnMc"
                     /db_xref="CDD:ZnMc"
     Region          322..434
                     /region_name="CUB I domain"
     Region          322..434
                     /region_name="Domain first found in C1r, C1s, uEGF, and
                     bone morphogenetic protein."
                     /note="CUB"
                     /db_xref="CDD:CUB"
     Region          322..431
                     /region_name="CUB domain"
                     /note="CUB"
                     /db_xref="CDD:pfam00431"
     Region          435..547
                     /region_name="Domain first found in C1r, C1s, uEGF, and
                     bone morphogenetic protein."
                     /note="CUB"
                     /db_xref="CDD:CUB"
     Region          435..546
                     /region_name="CUB II domain"
     Region          435..544
                     /region_name="CUB domain"
                     /note="CUB"
                     /db_xref="CDD:pfam00431"
     Region          547..588
                     /region_name="EGF-like, calcium-binding domain"
     Region          547..579
                     /region_name="Calcium-binding EGF-like domain"
                     /note="EGF_CA"
                     /db_xref="CDD:EGF_CA"
     Region          550..588
                     /region_name="Epidermal growth factor-like domain"
                     /note="EGF"
                     /db_xref="CDD:EGF"
     Region          591..703
                     /region_name="CUB III domain"
     Region          591..703
                     /region_name="Domain first found in C1r, C1s, uEGF, and
                     bone morphogenetic protein."
                     /note="CUB"
                     /db_xref="CDD:CUB"
     Region          591..700
                     /region_name="CUB domain"
                     /note="CUB"
                     /db_xref="CDD:pfam00431"
     CDS             1..730
                     /gene="BMP1"
                     /coded_by="NM_001199.1:30..2222"
                     /note="splice variant BMP1-1"
                     /db_xref="LocusID:649"
                     /db_xref="MIM:112264"
ORIGIN      
        1 mpgvarlpll lgllllprpg rpldladyty dlaeeddsep lnykdpckaa aflgdialde
       61 edlrafqvqq avdlrrhtar kssikaavpg ntstpscqst ngqpqrgacg rwrgrsrsrr
      121 aatsrpervw pdgvipfvig gnftgsqrav frqamrhwek htcvtflert dedsyivfty
      181 rpcgccsyvg rrgggpqais igkncdkfgi vvhelghvvg fwhehtrpdr drhvsivren
      241 iqpgqeynfl kmepqevesl getydfdsim hyarntfsrg ifldtivpky evngvkppig
      301 qrtrlskgdi aqarklykcp acgetlqdst gnfsspeypn gysahmhcvw risvtpgeki
      361 ilnftsldly rsrlcwydyv evrdgfwrka plrgrfcgsk lpepivstds rlwvefrsss
      421 nwvgkgffav yeaicggdvk kdyghiqspn ypddyrpskv ciwriqvseg fhvgltfqsf
      481 eierhdscay dylevrdghs esstligryc gyekpddiks tssrlwlkfv sdgsinkagf
      541 avnffkevde csrpnrggce qrclntlgsy kcscdpgyel apdkrrceaa cggfltklng
      601 sitspgwpke yppnknciwq lvaptqyris lqfdffeteg ndvckydfve vrsgltadsk
      661 lhgkfcgsek pevitsqynn mrvefksdnt vskkgfkahf fsekrpalqp prgrphqlkf
      721 rvqkrnrtpq 
//



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1: NP_000934. peptidylprolyl is...[gi:4505991] Links  


LOCUS       PPIC                     212 aa            linear   PRI 14-MAY-2002
DEFINITION  peptidylprolyl isomerase C (cyclophilin C) [Homo sapiens].
ACCESSION   NP_000934
VERSION     NP_000934.1  GI:4505991
DBSOURCE    REFSEQ: accession NM_000943.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 212)
  AUTHORS   Strausberg,R.
  TITLE     Homo sapiens peptidylprolyl isomerase C (cyclophilin C) (PPIC),
            mRNA
  JOURNAL   Unpublished (2001)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC002678.1.
FEATURES             Location/Qualifiers
     source          1..212
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q23.2"
                     /clone="MGC:3673 IMAGE:3610178"
                     /tissue_type="Uterus, endometrium adenocarcinoma"
                     /clone_lib="NIH_MGC_44"
                     /lab_host="DH10B-R"
                     /note="Vector: pOTB7"
     Protein         1..212
                     /product="peptidylprolyl isomerase C (cyclophilin C)"
                     /EC_number="5.2.1.8"
     Region          39..199
                     /region_name="Cyclophilin type peptidyl-prolyl cis-trans
                     isomerase"
                     /note="pro_isomerase"
                     /db_xref="CDD:pfam00160"
     variation       190
                     /allele="S"
                     /allele="N"
                     /db_xref="dbSNP:451195"
     CDS             1..212
                     /gene="PPIC"
                     /coded_by="NM_000943.2:88..726"
                     /db_xref="LocusID:5480"
                     /db_xref="MIM:123842"
ORIGIN      
        1 mgpgprlllp lvlcvglgal vfssgaegfr krgpsvtakv ffdvrigdkd vgriviglfg
       61 kvvpktvenf valatgekgy gykgskfhrv ikdfmiqggd ittgdgtggv siygetfpde
      121 nfklkhygig wvsmanagpd tngsqffitl tkptwldgkh vvfgkvidgm tvvhsielqa
      181 tdghdrpltn csiinsgkid vktpfvveia dw
//



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1: NP_001075. procollagen-lysin...[gi:4505891] Links  


LOCUS       PLOD3                    738 aa            linear   PRI 18-AUG-2002
DEFINITION  procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3;
            procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3v; lysyl
            hydroxylase 3 [Homo sapiens].
ACCESSION   NP_001075
VERSION     NP_001075.1  GI:4505891
DBSOURCE    REFSEQ: accession NM_001084.2
KEYWORDS    .
SOURCE      human.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 738)
  AUTHORS   Valtavaara,M., Szpirer,C., Szpirer,J. and Myllyla,R.
  TITLE     Primary structure, tissue distribution, and chromosomal
            localization of a novel isoform of lysyl hydroxylase (lysyl
            hydroxylase 3)
  JOURNAL   J. Biol. Chem. 273 (21), 12881-12886 (1998)
  MEDLINE   98250732
   PUBMED   9582318
REFERENCE   2  (residues 1 to 738)
  AUTHORS   Passoja,K., Rautavuoma,K., Ala-Kokko,L., Kosonen,T. and
            Kivirikko,K.I.
  TITLE     Cloning and characterization of a third human lysyl hydroxylase
            isoform
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 95 (18), 10482-10486 (1998)
  MEDLINE   98393670
   PUBMED   9724729
REFERENCE   3  (residues 1 to 738)
  AUTHORS   Heikkinen,J., Risteli,M., Wang,C., Latvala,J., Rossi,M.,
            Valtavaara,M. and Myllyla,R.
  TITLE     Lysyl hydroxylase 3 is a multifunctional protein possessing
            collagen glucosyltransferase activity
  JOURNAL   J. Biol. Chem. 275 (46), 36158-36163 (2000)
  MEDLINE   20549631
   PUBMED   10934207
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC011674.1.
FEATURES             Location/Qualifiers
     source          1..738
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q22"
                     /clone="MGC:15175 IMAGE:4300048"
                     /tissue_type="Pancreas, epithelioid carcinoma"
                     /clone_lib="NIH_MGC_42"
                     /lab_host="DH10B-R"
                     /note="Vector: pOTB7"
     Protein         1..738
                     /product="procollagen-lysine, 2-oxoglutarate 5-dioxygenase
                     3"
                     /note="procollagen-lysine, 2-oxoglutarate 5-dioxygenase
                     3v; lysyl hydroxylase 3"
     variation       286
                     /allele="R"
                     /allele="W"
                     /db_xref="dbSNP:3178780"
     Region          564..736
                     /region_name="smart00702, P4Hc, Prolyl 4-hydroxylase alpha
                     subunit homologues; Mammalian enzymes catalyse
                     hydroxylation of collagen, for example. Prokaryotic
                     enzymes might catalyse hydroxylation of antibiotic
                     peptides. These are 2-oxoglutarate-dependent dioxygenases,
                     requiring 2-oxoglutarate and dioxygen as cosubstrates and
                     ferrous iron as a cofactor"
     Region          647..738
                     /region_name="pfam03171, 2OG-FeII_Oxy, 2OG-Fe(II)
                     oxygenase superfamily. This family contains members of the
                     2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase
                     superfamily. This family includes the C-terminal of prolyl
                     4-hydroxylase alpha subunit. The holoenzyme has the
                     activity EC:1.14.11.2 catalysing the reaction: Procollagen
                     L-proline + 2-oxoglutarate + O2 <=> procollagen trans-
                     4-hydroxy-L-proline + succinate + CO2. The full enzyme
                     consists of a alpha2 beta2 complex with the alpha subunit
                     contributing most of the parts of the active site. The
                     family also includes lysyl hydrolases, isopenicillin
                     synthases and AlkB"
     CDS             1..738
                     /gene="PLOD3"
                     /coded_by="NM_001084.2:323..2539"
                     /db_xref="LocusID:8985"
                     /db_xref="MIM:603066"
ORIGIN      
        1 mtssgpgprf llllplllpp aasasdrprg rdpvnpekll vitvataete gylrflrsae
       61 ffnytvrtlg lgeewrggdv artvgggqkv rwlkkemeky adredmiimf vdsydvilag
      121 sptellkkfv qsgsrllfsa esfcwpewgl aeqypevgtg krflnsggfi gfattihqiv
      181 rqwkykdddd dqlfytrlyl dpglreklsl nldhksrifq nlngaldevv lkfdrnrvri
      241 rnvaydtlpi vvhgngptkl qlnylgnyvp ngwtpeggcg fcnqdrrtlp ggqppprvfl
      301 avfveqptpf lprflqrlll ldyppdrvtl flhnnevfhe phiadswpql qdhfsavklv
      361 gpeealspge ardmamdlcr qdpecefyfs ldadavltnl qtlrilieen rkviapmlsr
      421 hgklwsnfwg alspdeyyar sedyvelvqr krvgvwnvpy isqayvirgd tlrmelpqrd
      481 vfsgsdtdpd mafcksfrdk giflhlsnqh efgrllatsr ydtehlhpdl wqifdnpvdw
      541 keqyihenys ralegegive qpcpdvywfp llseqmcdel vaemehygqw sggrhedsrl
      601 aggyenvptv dihmkqvgye dqwlqllrty vgpmteslfp gyhtkaravm nfvvryrpde
      661 qpslrphhds stftlnvaln hkgldyeggg crflrydcvi ssprkgwall hpgrlthyhe
      721 glpttwgtry imvsfvdp
//



Revised: July 5, 2002.
 
 


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1: NP_000084. alpha 1 type V co...[gi:16554579] Links  


LOCUS       COL5A1                  1838 aa            linear   PRI 31-OCT-2001
DEFINITION  alpha 1 type V collagen preproprotein [Homo sapiens].
ACCESSION   NP_000084
VERSION     NP_000084.2  GI:16554579
DBSOURCE    REFSEQ: accession NM_000093.2
KEYWORDS    .
SOURCE      Homo sapiens.
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1838)
  AUTHORS   Takahara,K., Sato,Y., Okazawa,K., Okamoto,N., Noda,A., Yaoi,Y. and
            Kato,I.
  TITLE     Complete primary structure of human collagen alpha 1 (V) chain
  JOURNAL   J. Biol. Chem. 266 (20), 13124-13129 (1991)
  MEDLINE   91302336
   PUBMED   2071595
REFERENCE   2  (residues 1 to 1838)
  AUTHORS   Greenspan,D.S., Cheng,W. and Hoffman,G.G.
  TITLE     The pro-alpha 1(V) collagen chain. Complete primary structure,
            distribution of expression, and comparison with the pro-alpha 1(XI)
            collagen chain
  JOURNAL   J. Biol. Chem. 266 (36), 24727-24733 (1991)
  MEDLINE   92105142
   PUBMED   1722213
REFERENCE   3  (residues 1 to 1838)
  AUTHORS   Greenspan,D.S., Byers,M.G., Eddy,R.L., Cheng,W., Jani-Sait,S. and
            Shows,T.B.
  TITLE     Human collagen gene COL5A1 maps to the q34.2----q34.3 region of
            chromosome 9, near the locus for nail-patella syndrome
  JOURNAL   Genomics 12 (4), 836-837 (1992)
  MEDLINE   92241890
   PUBMED   1572660
REFERENCE   4  (residues 1 to 1838)
  AUTHORS   Takahara,K., Hoffman,G.G. and Greenspan,D.S.
  TITLE     Complete structural organization of the human alpha 1 (V) collagen
            gene (COL5A1): divergence from the conserved organization of other
            characterized fibrillar collagen genes
  JOURNAL   Genomics 29 (3), 588-597 (1995)
  MEDLINE   96121369
   PUBMED   8575750
REFERENCE   5  (residues 1 to 1838)
  AUTHORS   De Paepe,A., Nuytinck,L., Hausser,I., Anton-Lamprecht,I. and
            Naeyaert,J.M.
  TITLE     Mutations in the COL5A1 gene are causal in the Ehlers-Danlos
            syndromes I and II
  JOURNAL   Am. J. Hum. Genet. 60 (3), 547-554 (1997)
  MEDLINE   97195540
   PUBMED   9042913
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D90279.1, L38808.1 and
            M76729.1.
            On Oct 31, 2001 this sequence version replaced gi:4502957.
            Summary: This gene encodes an alpha chain for one of the low
            abundance fibrillar collagens. Fibrillar collagen molecules are
            trimers that can be composed of one or more types of alpha chains.
            Type V collagen is found in tissues containing type I collagen and
            appears to regulate the assembly of heterotypic fibers composed of
            both type I and type V collagen. This gene product is closely
            related to type XI collagen and it is possible that the collagen
            chains of types V and XI constitute a single collagen type with
            tissue-specific chain combinations. Mutations in this gene are
            associated with Ehlers-Danlos syndrome, types I and II.
FEATURES             Location/Qualifiers
     source          1..1838
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.2-q34.3"
     Protein         1..1838
                     /product="alpha 1 type V collagen preproprotein"
     sig_peptide     1..37
     Proprotein      38..1838
     mat_peptide     38..1605
                     /product="alpha 1 type V collagen"
     Region          39..230
                     /region_name="Thrombospondin N-terminal -like domain"
                     /note="TSPN"
                     /db_xref="CDD:pfam02210"
     Region          39..230
                     /region_name="Thrombospondin N-terminal -like domains."
                     /note="TSPN"
                     /db_xref="CDD:smart00210"
     Region          99..226
                     /region_name="Laminin G domain"
                     /note="LamG"
                     /db_xref="CDD:smart00282"
     Region          1608..1837
                     /region_name="Fibrillar collagens C-terminal domain"
                     /note="COLFI"
                     /db_xref="CDD:smart00038"
     Region          1625..1836
                     /region_name="Fibrillar collagen C-terminal domain. Found
                     at C-termini of fibrillar collagens: Ephydatia muelleri
                     procollagen EMF1 alpha"
                     /note="COLFI"
                     /db_xref="CDD:pfam01410"
     CDS             1..1838
                     /gene="COL5A1"
                     /coded_by="NM_000093.2:383..5899"
                     /db_xref="LocusID:1289"
                     /db_xref="MIM:120215"
ORIGIN      
        1 mdvhtrwkar salrpgapll ppllllllwa pppsraaqpa dllkvldfhn lpdgitkttg
       61 fcatrrsskg pdvayrvtkd aqlsaptkql ypasafpedf silttvkakk gsqaflvsiy
      121 neqgiqqigl elgrspvfly edhtgkpgpe dyplfrginl sdgkwhrial svhkknvtli
      181 ldckkkttkf ldrsdhpmid ingiivfgtr ildeevfegd iqqllfvsdh raaydycehy
      241 spdcdtavpd tpqsqdpnpd eyytegdgeg etyyyeypyy edpedlgkep tpskkpveaa
      301 kettevpeel tptpteaapm petsegagke edvgigdydy vpsedyytps pyddltygeg
      361 eenpdqptdp gagaeiptst adtsnssnpa pppgegaddl egefteetir nldenyydpy
      421 ydptsspsei gpgmpanqdt iyegiggprg ekgqkgepai iepgmliegp pgpegpaglp
      481 gppgtmgptg qvgdpgergp pgrpglpgad glpgppgtml mlpfrfgggg dagskgpmvs
      541 aqesqaqail qqarlalrgp agpmgltgrp gpvgppgsgg lkgepgdvgp qgprgvqgpp
      601 gpagkpgrrg ragsdgargm pgqtgpkgdr gfdglaglpg ekghrgdpgp sgppgppgdd
      661 gergddgevg prglpgepgp rgllgpkgpp gppgppgvtg mdgqpgpkgn vgpqgepgpp
      721 gqqgnpgaqg lpgpqgaigp pgekgplgkp glpgmpgadg ppghpgkegp pgekggqgpp
      781 gpqgpigypg prgvkgadgi rglkgtkgek gedgfpgfkg dmgikgdrge igppgprged
      841 gpegpkgrgg pngdpgplgp pgekgklgvp glpgypgrqg pkgsigfpgf pgangekggr
      901 gtpgkpgprg qrgptgprge rgprgitgkp gpkgnsggdg pagppgergp ngpqgptgfp
      961 gpkgppgppg kdglpghpgq rgetgfqgkt gppgppgvvg pqgptgetgp mgerghpgpp
     1021 gppgeqglpg lagkegtkgd pgpaglpgkd gppglrgfpg drglpgpvga lglkgnegpp
     1081 gppgpagspg ergpagaagp igipgrpgpq gppgpagekg apgekgpqgp agrdglqgpv
     1141 glpgpagpvg ppgedgdkge igepgqkgsk gdkgeqgppg ptgpqgpigq pgpsgadgep
     1201 gprgqqglfg qkgdegprgf pgppgpvglq glpgppgekg etgdvgqmgp pgppgprgps
     1261 gapgadgpqg ppggignpga vgekgepgea gepgpsgrsg ppgpkgerge kgesgpsgaa
     1321 gppgpkgppg ddgpkgspgp vgfpgdpgpp gepgpagqdg ppgdkgddge pgqtgspgpt
     1381 gepgpsgppg krgppgpagp egrqgekgak geaglegppg ktgpigpqga pgkpgpdglr
     1441 gipgpvgeqg lpgspgpdgp pgpmgppglp glkgdsgpkg ekghpgligl igppgeqgek
     1501 gdrglpgpqg ssgpkgeqgi tgpsgpigpp gppglpgppg pkgakgssgp tgpkgeaghp
     1561 gppgppgppg eviqplpiqa srtrrnidas qllddgngen yvdyadgmee ifgslnslkl
     1621 eieqmkrplg tqqnpartck dlqlchpdfp dgeywvdpnq gcsrdsfkvy cnftaggstc
     1681 vfpdkksega ritswpkenp gswfsefkrg kllsyvdaeg npvgvvqmtf lrllsasahq
     1741 nvtyhcyqsv awqdaatgsy dkalrflgsn deemsydnnp yiralvdgca tkkgyqktvl
     1801 eidtpkveqv pivdimfndf geasqkfgfe vgpacfmg
//



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1: NP_001145. annexin V; endone...[gi:4502107] Links  


LOCUS       ANXA5                    320 aa            linear   PRI 31-OCT-2000
DEFINITION  annexin V; endonexin II; anchorin CII; lipocortin V; placental
            anticoagulant protein I [Homo sapiens].
ACCESSION   NP_001145
VERSION     NP_001145.1  GI:4502107
DBSOURCE    REFSEQ: aaccession NM_001154.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 320)
  AUTHORS   Funakoshi,T., Heimark,R.L., Hendrickson,L.E., McMullen,B.A. and
            Fujikawa,K.
  TITLE     Human placental anticoagulant protein: isolation and
            characterization
  JOURNAL   Biochemistry 26 (17), 5572-5578 (1987)
  MEDLINE   88050845
   PUBMED   2960376
REFERENCE   2  (residues 1 to 320)
  AUTHORS   Iwasaki A, Suda M, Nakao H, Nagoya T, Saino Y, Arai K, Mizoguchi T,
            Sato F, Yoshizaki H, Hirata M et al.
  TITLE     Structure and expression of cDNA for an inhibitor of blood
            coagulation isolated from human placenta: a new lipocortin-like
            protein
  JOURNAL   J. Biochem. 102 (5), 1261-1273 (1987)
  MEDLINE   88139278
   PUBMED   2963810
REFERENCE   3  (residues 1 to 320)
  AUTHORS   Funakoshi T, Hendrickson LE, McMullen BA and Fujikawa K.
  TITLE     Primary structure of human placental anticoagulant protein
  JOURNAL   Biochemistry 26 (25), 8087-8092 (1987)
  MEDLINE   88163463
   PUBMED   2964863
REFERENCE   4  (residues 1 to 320)
  AUTHORS   Kaplan R, Jaye M, Burgess WH, Schlaepfer DD and Haigler HT.
  TITLE     Cloning and expression of cDNA for human endonexin II, a Ca2+ and
            phospholipid binding protein
  JOURNAL   J. Biol. Chem. 263 (17), 8037-8043 (1988)
  MEDLINE   88228020
   PUBMED   2967291
REFERENCE   5  (residues 1 to 320)
  AUTHORS   Grundmann U, Abel KJ, Bohn H, Lobermann H, Lottspeich F and Kupper
            H.
  TITLE     Characterization of cDNA encoding human placental anticoagulant
            protein (PP4): homology with the lipocortin family
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 85 (11), 3708-3712 (1988)
  MEDLINE   88234495
   PUBMED   2967495
REFERENCE   6  (residues 1 to 320)
  AUTHORS   Maurer-Fogy I, Reutelingsperger CP, Pieters J, Bodo G, Stratowa C
            and Hauptmann R.
  TITLE     Cloning and expression of cDNA for human vascular anticoagulant, a
            Ca2+-dependent phospholipid-binding protein
  JOURNAL   Eur. J. Biochem. 174 (4), 585-592 (1988)
  MEDLINE   88271329
   PUBMED   2455636
REFERENCE   7  (residues 1 to 320)
  AUTHORS   Pepinsky RB, Tizard R, Mattaliano RJ, Sinclair LK, Miller GT,
            Browning JL, Chow EP, Burne C, Huang KS, Pratt D et al.
  TITLE     Five distinct calcium and phospholipid binding proteins share
            homology with lipocortin I
  JOURNAL   J. Biol. Chem. 263 (22), 10799-10811 (1988)
  MEDLINE   88273202
   PUBMED   2968983
REFERENCE   8  (residues 1 to 320)
  AUTHORS   Cookson,B.T., Engelhardt,S., Smith,C., Bamford,H.A., Prochazka,M.
            and Tait,J.F.
  TITLE     Organization of the human annexin V (ANX5) gene
  JOURNAL   Genomics 20 (3), 463-467 (1994)
  MEDLINE   94307733
   PUBMED   8034319
REFERENCE   9  (residues 1 to 320)
  AUTHORS   Demange,P., Voges,D., Benz,J., Liemann,S., Gottig,P., Berendes,R.,
            Burger,A. and Huber,R.
  TITLE     Annexin V: the key to understanding ion selectivity and voltage
            regulation?
  JOURNAL   Trends Biochem. Sci. 19 (7), 272-276 (1994)
  MEDLINE   94324081
   PUBMED   7519374
REFERENCE   10 (residues 1 to 320)
  AUTHORS   Fernandez,M.P., Morgan,R.O., Fernandez,M.R. and Carcedo,M.T.
  TITLE     The gene encoding human annexin V has a TATA-less promoter with a
            high G+C content
  JOURNAL   Gene 149 (2), 253-260 (1994)
  MEDLINE   95047484
   PUBMED   7958998
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U01691.1, J03745.1 and
            U01681.1.
            Summary:  Annexin V belongs to the annexin family of
            calcium-dependent phospholipid binding proteins some of which have
            been implicated in membrane-related events along exocytotic and
            endocytotic pathways. Annexin V is a phospholipase A2 and protein
            kinase C inhibitory protein with calcium channel activity and a
            potential role in cellular signal transduction, inflammation,
            growth and differentiation.  Annexin V has also been described as
            placental anticoagulant protein I, vascular anticoagulant-alpha,
            endonexin II, lipocortin V, placental protein 4 and anchorin CII.
            The gene spans 29 kb containing 13 exons, and encodes a single
            transcript of approximately 1.6 kb and a protein product with a
            molecular weight of about 35 kDa.
FEATURES             Location/Qualifiers
     source          1..320
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28-q32"
     Protein         1..320
                     /product="annexin V"
                     /note="endonexin II; anchorin CII; lipocortin V; placental
                     anticoagulant protein I"
     Region          20..84
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          32..84
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          91..156
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          104..156
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          174..240
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          188..240
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          248..315
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          263..315
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     CDS             1..320
                     /gene="ANXA5"
                     /coded_by="NM_001154.2:193..1155"
                     /note="anchorin CII, lipocortin V, endonexin II, placental
                     anticoagulant protein(PAP)-I, placental protein (PP)4,
                     vascular anticoagulant (VAC)-alpha"
                     /db_xref="LocusID:308"
                     /db_xref="MIM:131230"
ORIGIN      
        1 maqvlrgtvt dfpgfderad aetlrkamkg lgtdeesilt lltsrsnaqr qeisaafktl
       61 fgrdllddlk seltgkfekl ivalmkpsrl ydayelkhal kgagtnekvl teiiasrtpe
      121 elraikqvye eeygssledd vvgdtsgyyq rmlvvllqan rdpdagidea qveqdaqalf
      181 qagelkwgtd eekfitifgt rsvshlrkvf dkymtisgfq ieetidrets gnleqlllav
      241 vksirsipay laetlyyamk gagtddhtli rvmvsrseid lfnirkefrk nfatslysmi
      301 kgdtsgdykk allllcgedd
//



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1: NP_003496. frizzled 1; frizz...[gi:4503825] Links  


LOCUS       FZD1                     647 aa            linear   PRI 20-DEC-2001
DEFINITION  frizzled 1; frizzled (Drosophila) homolog 1; Frizzled, drosophila,
            homolog of, 1; Wnt receptor [Homo sapiens].
ACCESSION   NP_003496
VERSION     NP_003496.1  GI:4503825
DBSOURCE    REFSEQ: aaccession NM_003505.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (sites)
  AUTHORS   Sagara,N., Toda,G., Hirai,M., Terada,M. and Katoh,M.
  TITLE     Molecular cloning, differential expression, and chromosomal
            localization of human frizzled-1, frizzled-2, and frizzled-7
  JOURNAL   Biochem. Biophys. Res. Commun. 252 (1), 117-122 (1998)
  MEDLINE   99032814
   PUBMED   9813155
REFERENCE   2  (residues 1 to 647)
  AUTHORS   Gazit,A., Yaniv,A., Bafico,A., Pramila,T., Igarashi,M.,
            Kitajewski,J. and Aaronson,S.A.
  TITLE     Human frizzled 1 interacts with transforming Wnts to transduce a
            TCF dependent transcriptional response
  JOURNAL   Oncogene 18 (44), 5959-5966 (1999)
  MEDLINE   20027383
   PUBMED   10557084
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AB017363.1.
            Summary:  Members of the 'frizzled' gene family encode
            7-transmembrane domain proteins that are receptors for Wnt
            signaling proteins.  The FZD1 protein contains a signal peptide, a
            cysteine-rich domain in the N-terminal extracellular region, 7
            transmembrane domains, and a C-terminal PDZ domain-binding motif.
            The FZD1 transcript is expressed in various tissues.
FEATURES             Location/Qualifiers
     source          1..647
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21"
     Protein         1..647
                     /product="frizzled 1"
                     /note="frizzled (Drosophila) homolog 1; Frizzled,
                     drosophila, homolog of, 1; Wnt receptor"
     Region          106..228
                     /region_name="Fz domain. Also known as the CRD (cysteine
                     rich domain)"
                     /note="Fz"
                     /db_xref="CDD:pfam01392"
     Region          116..231
                     /region_name="Frizzled"
                     /note="FRI"
                     /db_xref="CDD:smart00063"
     Region          309..640
                     /region_name="Frizzled/Smoothened family membrane region.
                     This family contains the membrane spanning region of
                     frizzled and smoothened receptors. This membrane region is
                     predicted to contain seven transmembrane alpha helices.
                     Proteins related to drosophila frizzled are receptors for
                     the Wnt signaling molecules. The smoothened receptor
                     mediates hedgehog signaling"
                     /note="Frizzled"
                     /db_xref="CDD:pfam01534"
     CDS             1..647
                     /gene="FZD1"
                     /coded_by="NM_003505.1:414..2357"
                     /db_xref="LocusID:8321"
                     /db_xref="MIM:603408"
ORIGIN      
        1 maeeeapkks raagggaswe lcagalsarl aeegsgdagg rrrppvdprr larqlllllw
       61 lleaplllgv raqaagqgpg qgpgpgqqpp pppqqqqsgq qyngergisv pdhgycqpis
      121 iplctdiayn qtimpnllgh tnqedaglev hqfyplvkvq csaelkfflc smyapvctvl
      181 eqalppcrsl cerarqgcea lmnkfgfqwp dtlkcekfpv hgagelcvgq ntsdkgtptp
      241 sllpefwtsn pqhgggghrg gfpggagase rgkfscpral kvpsylnyhf lgekdcgapc
      301 eptkvyglmy fgpeelrfsr twigiwsvlc castlftvlt ylvdmrrfsy perpiiflsg
      361 cytavavayi agflledrvv cndkfaedga rtvaqgtkke gctilfmmly ffsmassiww
      421 vilsltwfla agmkwgheai eansqyfhla awavpaikti tilalgqvdg dvlsgvcfvg
      481 lnnvdalrgf vlaplfvylf igtsfllagf vslfrirtim khdgtktekl eklmvrigvf
      541 svlytvpati viacyfyeqa frdqwerswv aqscksyaip cphlqaggga pphppmspdf
      601 tvfmikylmt livgitsgfw iwsgktlnsw rkfytrltns kqgettv
//



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1: NP_006108. peroxisomal D3,D2...[gi:5174625] Links  


LOCUS       PECI                     359 aa            linear   PRI 27-AUG-2002
DEFINITION  peroxisomal D3,D2-enoyl-CoA isomerase [Homo sapiens].
ACCESSION   NP_006108
VERSION     NP_006108.1  GI:5174625
DBSOURCE    REFSEQ: aaccession NM_006117.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 359)
  AUTHORS   Geisbrecht,B.V., Zhang,D., Schulz,H. and Gould,S.J.
  TITLE     Characterization of PECI, a Novel Monofunctional D3,D2-Enoyl-CoA
            Isomerase of Mammalian Peroxisomes
  JOURNAL   J. Biol. Chem. (1999) In press
REFERENCE   2  (residues 1 to 359)
  AUTHORS   Suk,K., Kim,Y.H., Hwang,D.Y., Ihm,S.H., Yoo,H.J. and Lee,M.S.
  TITLE     Molecular cloning and expression of a novel human cDNA related to
            the diazepam binding inhibitor
  JOURNAL   Biochim. Biophys. Acta 1454 (1), 126-131 (1999)
  MEDLINE   99284489
   PUBMED   10354522
REFERENCE   3  (residues 1 to 359)
  AUTHORS   Geisbrecht,B.V., Zhang,D., Schulz,H. and Gould,S.J.
  TITLE     Characterization of PECI, a novel monofunctional Delta(3),
            Delta(2)-enoyl-CoA isomerase of mammalian peroxisomes
  JOURNAL   J. Biol. Chem. 274 (31), 21797-21803 (1999)
  MEDLINE   99348312
   PUBMED   10419495
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF153612.1.
FEATURES             Location/Qualifiers
     source          1..359
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.3"
     Protein         1..359
                     /product="peroxisomal D3,D2-enoyl-CoA isomerase"
                     /function="catalyzes the isomerization of peroxisomal
                     3-cis- and 2-trans-enoyl-CoAs"
     Region          4..79
                     /region_name="pfam00887, ACBP, Acyl CoA binding protein"
     Region          117..287
                     /region_name="pfam00378, ECH, Enoyl-CoA
                     hydratase/isomerase family. This family contains a diverse
                     set of enzymes including: Enoyl-CoA hydratase. Napthoate
                     synthase. Carnitate racemase. 3-hydoxybutyryl-CoA
                     dehydratase. Dodecanoyl-CoA delta-isomerase"
     CDS             1..359
                     /gene="PECI"
                     /coded_by="NM_006117.1:103..1182"
                     /db_xref="LocusID:10455"
ORIGIN      
        1 mrasqkdfen smnqvkllkk dpgnevklkl yalykqateg pcnmpkpgvf dlinkakwda
       61 wnalgslpke aarqnyvdlv sslspsless sqvepgtdrk stgfetlvvt sedgitkimf
      121 nrpkkknain temyheimra lkaaskddsi itvltgngdy yssgndltnf tdippggvee
      181 kaknnavllr efvgcfidfp kpliavvngp avgisvtllg lfdavyasdr atfhtpfshl
      241 gqspegcssy tfpkimspak atemlifgkk ltageacaqg lvtevfpdst fqkevwtrlk
      301 afaklppnal riskevirkr ereklhavna eecnvlqgrw lsdectnavv nflsrkskl
//



Revised: July 5, 2002.
 
 


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1: NP_036557. ras suppressor pr...[gi:6912638] Links  


LOCUS       RSU1                     277 aa            linear   PRI 27-AUG-2002
DEFINITION  ras suppressor protein 1 [Homo sapiens].
ACCESSION   NP_036557
VERSION     NP_036557.1  GI:6912638
DBSOURCE    REFSEQ: aaccession NM_012425.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 277)
  AUTHORS   Cutler,M.L., Bassin,R.H., Zanoni,L. and Talbot,N.
  TITLE     Isolation of rsp-1, a novel cDNA capable of suppressing v-Ras
            transformation
  JOURNAL   Mol. Cell. Biol. 12 (9), 3750-3756 (1992)
  MEDLINE   92375042
   PUBMED   1508180
REFERENCE   2  (residues 1 to 277)
  AUTHORS   Tsuda,T. and Cutler,M.L.
  TITLE     Human RSU1 is highly homologous to mouse Rsu-1 and localizes to
            human chromosome 10
  JOURNAL   Genomics 18 (2), 461-462 (1993)
  MEDLINE   94117031
   PUBMED   8288261
REFERENCE   3  (residues 1 to 277)
  AUTHORS   Tsuda,T. and Cutler,M.
  TITLE     Isolation of rsp-1, a novel cDNA capable of suppressing v-Ras
            transformant
  JOURNAL   Unpublished
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L12535.1.
            Summary:  Studies in mouse and human cell lines suggest this gene
            is involved in the Ras signal transduction pathway, growth
            inhibition, and nerve-growth factor induced differentiation. The
            gene was initially isolated in mouse based on it's ability to
            inhibit v-Ras transformation.
FEATURES             Location/Qualifiers
     source          1..277
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10p12.31"
     Protein         1..277
                     /product="ras suppressor protein 1"
     CDS             1..277
                     /gene="RSU1"
                     /coded_by="NM_012425.2:70..903"
                     /db_xref="LocusID:6251"
                     /db_xref="MIM:179555"
ORIGIN      
        1 mskslkklve esreknqpev dmsdrgisnm ldvnglftls hitqlvlshn kltmvppnia
       61 elknlevlnf fnnqieelpt qisslqklkh lnlgmnrlnt lprgfgslpa levldltynn
      121 lsenslpgnf fylttlraly lsdndfeilp pdigkltklq ilslrdndli slpkeigelt
      181 qlkelhiqgn rltvlppelg nldltgqkqv fkaennpwvt piadqfqlgv shvfeyirse
      241 tykylygrhm qanpeppkkn ndkskkisrk plaaknr
//



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1: NP_036400. similar to vaccin...[gi:7110641] Links  


LOCUS       PLD3                     437 aa            linear   PRI 09-OCT-2002
DEFINITION  similar to vaccinia virus HindIII K4L ORF [Homo sapiens].
ACCESSION   NP_036400
VERSION     NP_036400.1  GI:7110641
DBSOURCE    REFSEQ: aaccession NM_012268.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Cao,J.X., Koop,B.F. and Upton,C.
  TITLE     A human homolog of the vaccinia virus HindIII K4L gene is a member
            of the phospholipase D superfamily
  JOURNAL   Virus Res. 48 (1), 11-18 (1997)
  MEDLINE   97284916
   PUBMED   9140189
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Pedersen,K.M., Finsen,B., Celis,J.E. and Jensen,N.A.
  TITLE     Expression of a novel murine phospholipase D homolog coincides with
            late neuronal development in the forebrain
  JOURNAL   J. Biol. Chem. 273 (47), 31494-31504 (1998)
  MEDLINE   99030428
   PUBMED   9813063
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U60644.1.
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.2"
                     /clone="I.M.A.G.E Consortium Clone ID 159455"
                     /sex="female"
                     /tissue_type="breast"
                     /dev_stage="adult"
     Protein         1..437
                     /product="similar to vaccinia virus HindIII K4L ORF"
     Region          145..170
                     /region_name="Phospholipase D. Active site motif.
                     Phosphatidylcholine-hydrolyzing phospholipase D (PLD)
                     isoforms are activated by ADP-ribosylation factors (ARFs).
                     PLD produces phosphatidic acid from phosphatidylcholine,
                     which may be essential for the formation of certain types
                     of transport vesicles or may be constitutive vesicular
                     transport to signal transduction pathways. PC-hydrolyzing
                     PLD is a homologue of cardiolipin synthase,
                     phosphatidylserine synthase, bacterial PLDs, and viral
                     proteins. Each of these appears to possess a domain
                     duplication which is apparent by the presence of two
                     motifs containing well-conserved histidine, lysine, and/or
                     asparagine residues which may contribute to the active
                     site. aspartic acid. An E. coli endonuclease (nuc) and
                     similar proteins appear to be PLD homologues but possess
                     only one of these motifs. The profile contained here
                     represents only the putative active site regions, since an
                     accurate multiple alignment of the repeat units has not
                     been achieved"
                     /note="PLDc"
                     /db_xref="CDD:pfam00614"
     Region          145..170
                     /region_name="Phospholipase D. Active site motifs"
                     /note="PLDc"
                     /db_xref="CDD:smart00155"
     CDS             1..437
                     /gene="PLD3"
                     /coded_by="NM_012268.1:488..1801"
                     /note="similar to Vaccinia virus HindIII K4L ORF, and to
                     Vaccinia virus p37 (HindIII F13L ORF)"
                     /db_xref="LocusID:23646"
ORIGIN      
        1 mtqlflweyg dlhlfgpnqr papcydpcea vlvesipegl dfpnastgnp stsqawlgll
       61 agahssldia sfywtltnnd thtqepsaqq geevlrqlqt lapkgvnvri avskpsgpqp
      121 qadlqallqs gaqvrmvdmq klthgvlhtk fwvvdqthfy lgsanmdwrs ltqvkelgvv
      181 myncsclard ltkifeaywf lgqagssips twprfydtry nqetpmeicl ngtpalayla
      241 sappplcpsg rtpdlkalln vvdnarsfiy vavmnylptl efshphrfwp aiddglrrat
      301 yergvkvrll iscwghseps mrafllslaa lrdnhthsdi qvklfvvpad eaqaripyar
      361 vnhnkymvte ratyigtsnw sgnyftetag tsllvtqngr gglrsqleai flrdwdspyi
      421 hdldtsadsv gnacrll
//



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1: NP_001210. calumenin precurs...[gi:4502551] Links  


LOCUS       CALU                     315 aa            linear   PRI 31-OCT-2000
DEFINITION  calumenin precursor [Homo sapiens].
ACCESSION   NP_001210
VERSION     NP_001210.1  GI:4502551
DBSOURCE    REFSEQ: aaccession NM_001219.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 315)
  AUTHORS   Yabe,D., Taniwaki,M., Nakamura,T., Kanazawa,N., Tashiro,K. and
            Honjo,T.
  TITLE     Human calumenin gene (CALU): cDNA isolation and chromosomal mapping
            to 7q32
  JOURNAL   Genomics 49 (2), 331-333 (1998)
  MEDLINE   98260687
   PUBMED   9598325
REFERENCE   2  (residues 1 to 315)
  AUTHORS   Vorum,H., Liu,X., Madsen,P., Rasmussen,H.H. and Honore,B.
  TITLE     Molecular cloning of a cDNA encoding human calumenin, expression in
            Escherichia coli and analysis of its Ca2+-binding activity
  JOURNAL   Biochim. Biophys. Acta 1386 (1), 121-131 (1998)
  MEDLINE   98342150
   PUBMED   9675259
REFERENCE   3  (residues 1 to 315)
  AUTHORS   Vorum,H., Hager,H., Christensen,B.M., Nielsen,S. and Honore,B.
  TITLE     Human calumenin localizes to the secretory pathway and is secreted
            to the medium
  JOURNAL   Exp. Cell Res. 248 (2), 473-481 (1999)
  MEDLINE   99240627
   PUBMED   10222138
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF013759.1 and U67280.1.
            Summary: Calumenin (CALU) is a  calcium-binding protein localized
            in the endoplasmic reticulum (ER) and is involved in such ER
            functions as protein folding and sorting. Calumenin is a member of
            the EF-hand superfamily in the ER and Golgi apparatus named CERC.
            CERC is an acronym for its family members Cab-45, reticulocalbin,
            Erc-55, and calumenin. The CALU gene encodes a deduced 315-amino
            acid protein containing 6 EF-hand motifs, 1 potential
            N-glycosylation site, and a C-terminal ER retention signal. The
            human and mouse CALU proteins are 98% identical. CALU mRNA is
            ubiquitously expressed in human tissues and maps to 7q32.
FEATURES             Location/Qualifiers
     source          1..315
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q32"
     Protein         1..315
                     /product="calumenin precursor"
                     /function="Ca2+-binding in the endoplasmic reticulum"
     sig_peptide     1..19
     variation       4
                     /allele="Q"
                     /allele="R"
                     /db_xref="dbSNP:2290228"
     Region          81..92
                     /region_name="EF-hand motif I"
     mat_peptide     116..315
                     /product="calumenin"
     Region          117..128
                     /region_name="EF-hand motif II"
     Region          155..164
                     /region_name="EF-hand motif III"
     Region          200..212
                     /region_name="EF-hand motif IV"
     Region          242..253
                     /region_name="EF-hand motif V"
     Region          268..289
                     /region_name="EF-hand motif VI"
     CDS             1..315
                     /gene="CALU"
                     /coded_by="NM_001219.2:63..1010"
                     /note="member of one subset of EF-hand superfamily that
                     includes reticulocalbin, Erc-55, and Cab-45"
                     /db_xref="LocusID:813"
                     /db_xref="MIM:603420"
ORIGIN      
        1 mdlrqflmcl slctafalsk ptekkdrvhh epqlsdkvhn daqsfdydhd aflgaeeakt
       61 fdqltpeesk erlgkivski dgdkdgfvtv delkdwikfa qkrwiyedve rqwkghdlne
      121 dglvsweeyk natygyvldd pdpddgfnyk qmmvrderrf kmadkdgdli atkeeftafl
      181 hpeeydymkd ivvqetmedi dknadgfidl eeyigdmysh dgntdepewv ktereqfvef
      241 rdknrdgkmd keetkdwilp sdydhaeaea rhlvyesdqn kdgkltkeei vdkydlfvgs
      301 qatdfgealv rhdef
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_000475. amyloid beta (A4)...[gi:4502167] Links  


LOCUS       APP                      770 aa            linear   PRI 27-AUG-2002
DEFINITION  amyloid beta (A4) precursor protein (protease nexin-II, Alzheimer
            disease); Amyloid beta (A4) precursor protein; amyloid beta-peptide
            [Homo sapiens].
ACCESSION   NP_000475
VERSION     NP_000475.1  GI:4502167
DBSOURCE    REFSEQ: aaccession NM_000484.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 770)
  AUTHORS   Tanzi,R.E., Gusella,J.F., Watkins,P.C., Bruns,G.A., St
            George-Hyslop,P., Van Keuren,M.L., Patterson,D., Pagan,S.,
            Kurnit,D.M. and Neve,R.L.
  TITLE     Amyloid beta protein gene: cDNA, mRNA distribution, and genetic
            linkage near the Alzheimer locus
  JOURNAL   Science 235 (4791), 880-884 (1987)
  MEDLINE   87120329
   PUBMED   2949367
REFERENCE   2  (residues 1 to 770)
  AUTHORS   Ponte,P., Gonzalez-DeWhitt,P., Schilling,J., Miller,J., Hsu,D.,
            Greenberg,B., Davis,K., Wallace,W., Lieberburg,I. and Fuller,F.
  TITLE     A new A4 amyloid mRNA contains a domain homologous to serine
            proteinase inhibitors
  JOURNAL   Nature 331 (6156), 525-527 (1988)
  MEDLINE   88122639
   PUBMED   2893289
REFERENCE   3  (residues 1 to 770)
  AUTHORS   La Fauci,G., Lahiri,D.K., Salton,S.R. and Robakis,N.K.
  TITLE     Characterization of the 5'-end region and the first two exons of
            the beta-protein precursor gene
  JOURNAL   Biochem. Biophys. Res. Commun. 159 (1), 297-304 (1989)
  MEDLINE   89165870
   PUBMED   2538123
REFERENCE   4  (residues 1 to 770)
  AUTHORS   de Sauvage,F. and Octave,J.N.
  TITLE     A novel mRNA of the A4 amyloid precursor gene coding for a possibly
            secreted protein
  JOURNAL   Science 245 (4918), 651-653 (1989)
  MEDLINE   89346754
   PUBMED   2569763
REFERENCE   5  (residues 1 to 770)
  AUTHORS   Van Nostrand,W.E., Wagner,S.L., Suzuki,M., Choi,B.H., Farrow,J.S.,
            Geddes,J.W., Cotman,C.W. and Cunningham,D.D.
  TITLE     Protease nexin-II, a potent antichymotrypsin, shows identity to
            amyloid beta-protein precursor
  JOURNAL   Nature 341 (6242), 546-549 (1989)
  MEDLINE   90015171
   PUBMED   2507928
REFERENCE   6  (sites)
  AUTHORS   Yoshikai,S., Sasaki,H., Doh-ura,K., Furuya,H. and Sakaki,Y.
  TITLE     Genomic organization of the human amyloid beta-protein precursor
            gene
  JOURNAL   Gene 87 (2), 257-263 (1990)
  MEDLINE   90236318
   PUBMED   2110105
REFERENCE   7  (residues 1 to 770)
  AUTHORS   Schilling,J., Wang,Y., Lau,K., Smith,L. and Cordell,B.
  TITLE     Synthesis and characterization of the Kunitz protease-inhibitor
            domain of the beta-amyloid precursor protein
  JOURNAL   Gene 98 (2), 225-230 (1991)
  MEDLINE   91200669
   PUBMED   1707846
REFERENCE   8  (residues 1 to 770)
  AUTHORS   Bakker,E., van Broeckhoven,C., Haan,J., Voorhoeve,E., van Hul,W.,
            Levy,E., Lieberburg,I., Carman,M.D., van Ommen,G.J., Frangione,B.
            et al.
  TITLE     DNA diagnosis for hereditary cerebral hemorrhage with amyloidosis
            (Dutch type)
  JOURNAL   Am. J. Hum. Genet. 49 (3), 518-521 (1991)
  MEDLINE   91353566
   PUBMED   1679289
REFERENCE   9  (residues 1 to 770)
  AUTHORS   Multhaup,G., Schlicksupp,A., Hesse,L., Beher,D., Ruppert,T.,
            Masters,C.L. and Beyreuther,K.
  TITLE     The amyloid precursor protein of Alzheimer's disease in the
            reduction of copper(II) to copper(I)
  JOURNAL   Science 271 (5254), 1406-1409 (1996)
  MEDLINE   96173947
   PUBMED   8596911
REFERENCE   10 (residues 1 to 770)
  AUTHORS   Chow,N., Korenberg,J.R., Chen,X.N. and Neve,R.L.
  TITLE     APP-BP1, a novel protein that binds to the carboxyl-terminal region
            of the amyloid precursor protein
  JOURNAL   J. Biol. Chem. 271 (19), 11339-11346 (1996)
  MEDLINE   96212203
   PUBMED   8626687
REFERENCE   11 (residues 1 to 770)
  AUTHORS   Hattori,M., Tsukahara,F., Furuhata,Y., Tanahashi,H., Hirose,M.,
            Saito,M., Tsukuni,S. and Sakaki,Y.
  TITLE     A novel method for making nested deletions and its application for
            sequencing of a 300 kb region of human APP locus
  JOURNAL   Nucleic Acids Res. 25 (9), 1802-1808 (1997)
  MEDLINE   97263807
   PUBMED   9108164
REFERENCE   12 (residues 1 to 770)
  AUTHORS   Hattori,M., Fujiyama,A., Taylor,T.D., Watanabe,H., Yada,T.,
            Park,H.S., Toyoda,A., Ishii,K., Totoki,Y., Choi,D.K., Groner,Y.,
            Soeda,E., Ohki,M., Takagi,T., Sakaki,Y., Taudien,S.,
            Blechschmidt,K., Polley,A., Menzel,U., Delabar,J., Kumpf,K.,
            Lehmann,R., Patterson,D., Reichwald,K., Rump,A., Schillhabel,M.,
            Schudy,A., Zimmermann,W., Rosenthal,A., Kudoh,J., Schibuya,K.,
            Kawasaki,K., Asakawa,S., Shintani,A., Sasaki,T., Nagamine,K.,
            Mitsuyama,S., Antonarakis,S.E., Minoshima,S., Shimizu,N.,
            Nordsiek,G., Hornischer,K., Brant,P., Scharfe,M., Schon,O.,
            Desario,A., Reichelt,J., Kauer,G., Blocker,H., Ramser,J., Beck,A.,
            Klages,S., Hennig,S., Riesselmann,L., Dagand,E., Haaf,T.,
            Wehrmeyer,S., Borzym,K., Gardiner,K., Nizetic,D., Francis,F.,
            Lehrach,H., Reinhardt,R. and Yaspo,M.L.
  TITLE     The DNA sequence of human chromosome 21
  JOURNAL   Nature 405 (6784), 311-319 (2000)
  MEDLINE   20289799
   PUBMED   10830953
REFERENCE   13 (residues 1 to 770)
  AUTHORS   Bruno,V., Copani,A., Besong,G., Scoto,G. and Nicoletti,F.
  TITLE     Neuroprotective activity of chemokines against N-methyl-D-aspartate
            or beta-amyloid-induced toxicity in culture
  JOURNAL   Eur. J. Pharmacol. 399 (2-3), 117-121 (2000)
  MEDLINE   20344774
   PUBMED   10884510
REFERENCE   14 (residues 1 to 770)
  AUTHORS   Xia,W., Ray,W.J., Ostaszewski,B.L., Rahmati,T., Kimberly,W.T.,
            Wolfe,M.S., Zhang,J., Goate,A.M. and Selkoe,D.J.
  TITLE     Presenilin complexes with the C-terminal fragments of amyloid
            precursor protein at the sites of amyloid beta-protein generation
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 97 (16), 9299-9304 (2000)
  MEDLINE   20381377
   PUBMED   10922078
REFERENCE   15 (residues 1 to 770)
  AUTHORS   Walter,J., Schindzielorz,A., Hartung,B. and Haass,C.
  TITLE     Phosphorylation of the beta-amyloid precursor protein at the cell
            surface by ectocasein kinases 1 and 2
  JOURNAL   J. Biol. Chem. 275 (31), 23523-23529 (2000)
  MEDLINE   20378979
   PUBMED   10806211
REFERENCE   16 (residues 1 to 770)
  AUTHORS   Nakagawa,T. and Yuan,J.
  TITLE     Cross-talk between two cysteine protease families. Activation of
            caspase-12 by calpain in apoptosis
  JOURNAL   J. Cell Biol. 150 (4), 887-894 (2000)
  MEDLINE   20411230
   PUBMED   10953012
REFERENCE   17 (residues 1 to 770)
  AUTHORS   Olson,J.M., Goddard,K.A. and Dudek,D.M.
  TITLE     The amyloid precursor protein locus and very-late-onset Alzheimer
            disease
  JOURNAL   Am. J. Hum. Genet. 69 (4), 895-899 (2001)
  MEDLINE   21426327
   PUBMED   11500807
REFERENCE   18 (residues 1 to 770)
  AUTHORS   Kirkitadze,M.D., Condron,M.M. and Teplow,D.B.
  TITLE     Identification and characterization of key kinetic intermediates in
            amyloid beta-protein fibrillogenesis
  JOURNAL   J. Mol. Biol. 312 (5), 1103-1119 (2001)
  MEDLINE   21464908
   PUBMED   11580253
REFERENCE   19 (residues 1 to 770)
  AUTHORS   Kale,L.C., Higgins,G.A., Yoshioka,K., Izumi,R., Oishi,N. and
            Sakaki,Y.
  JOURNAL   Unpublished (1992)
REFERENCE   20 (residues 1 to 770)
  AUTHORS   Yoshioka,K., Izumi,R., Oishi,N. and Sakaki,Y.
  JOURNAL   Unpublished (1992)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M33112.1.
FEATURES             Location/Qualifiers
     source          1..770
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q21.3"
     Protein         1..770
                     /product="amyloid beta (A4) precursor protein (protease
                     nexin-II, Alzheimer disease)"
                     /note="Amyloid beta (A4) precursor protein; amyloid
                     beta-peptide"
     Region          24..188
                     /region_name="pfam02177, A4_EXTRA, Amyloid A4
                     extracellular domain"
     Region          24..188
                     /region_name="smart00006, A4_EXTRA, amyloid A4; amyloid A4
                     precursor of Alzheimers disease"
     Region          291..342
                     /region_name="smart00131, KU, BPTI/Kunitz family of serine
                     protease inhibitors; Serine protease inhibitors. One
                     member of the family is encoded by an
                     alternatively-spliced form of Alzheimer's amyloid
                     beta-protein"
     Region          291..341
                     /region_name="pfam00014, Kunitz_BPTI, Kunitz/Bovine
                     pancreatic trypsin inhibitor domain. Indicative of a
                     protease inhibitor, usually a serine protease inhibitor.
                     Structure is a disulfide rich alpha+beta fold. BPTI
                     (bovine pancreatic trypsin inhibitor) is an extensively
                     studied model structure"
     Region          675..705
                     /region_name="pfam03494, Beta-APP, Beta-amyloid peptide
                     (beta-APP)"
     variation       713
                     /allele="A"
                     /allele="V"
                     /db_xref="dbSNP:1800557"
     CDS             1..770
                     /gene="APP"
                     /coded_by="NM_000484.1:148..2460"
                     /db_xref="LocusID:351"
                     /db_xref="MIM:104760"
ORIGIN      
        1 mlpglallll aawtaralev ptdgnaglla epqiamfcgr lnmhmnvqng kwdsdpsgtk
       61 tcidtkegil qycqevypel qitnvveanq pvtiqnwckr grkqckthph fvipyrclvg
      121 efvsdallvp dkckflhqer mdvcethlhw htvaketcse kstnlhdygm llpcgidkfr
      181 gvefvccpla eesdnvdsad aeeddsdvww ggadtdyadg sedkvvevae eeevaeveee
      241 eadddedded gdeveeeaee pyeeatertt siattttttt esveevvrev cseqaetgpc
      301 ramisrwyfd vtegkcapff yggcggnrnn fdteeycmav cgsamsqsll kttqeplard
      361 pvklpttaas tpdavdkyle tpgdenehah fqkakerlea khrermsqvm reweeaerqa
      421 knlpkadkka viqhfqekve sleqeaaner qqlvethmar veamlndrrr lalenyital
      481 qavpprprhv fnmlkkyvra eqkdrqhtlk hfehvrmvdp kkaaqirsqv mthlrviyer
      541 mnqslsllyn vpavaeeiqd evdellqkeq nysddvlanm iseprisygn dalmpsltet
      601 kttvellpvn gefslddlqp whsfgadsvp antenevepv darpaadrgl ttrpgsgltn
      661 ikteeisevk mdaefrhdsg yevhhqklvf faedvgsnkg aiiglmvggv viatvivitl
      721 vmlkkkqyts ihhgvvevda avtpeerhls kmqqngyenp tykffeqmqn
//



Revised: July 5, 2002.
 
 


Disclaimer | Write to the Help Desk
NCBI | NLM | NIH 

 

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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_001775. CD97 antigen, iso...[gi:17978489] Links  


LOCUS       CD97                     742 aa            linear   PRI 21-DEC-2001
DEFINITION  CD97 antigen, isoform 2 precursor; leukocyte antigen CD97;
            seven-span transmembrane protein [Homo sapiens].
ACCESSION   NP_001775
VERSION     NP_001775.2  GI:17978489
DBSOURCE    REFSEQ: aaccession NM_001784.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 742)
  AUTHORS   Hamann,J., Eichler,W., Hamann,D., Kerstens,H.M., Poddighe,P.J.,
            Hoovers,J.M., Hartmann,E., Strauss,M. and van Lier,R.A.
  TITLE     Expression cloning and chromosomal mapping of the leukocyte
            activation antigen CD97, a new seven-span transmembrane molecule of
            the secretion receptor superfamily with an unusual extracellular
            domain
  JOURNAL   J. Immunol. 155 (4), 1942-1950 (1995)
  MEDLINE   95363161
   PUBMED   7636245
REFERENCE   2  (residues 1 to 742)
  AUTHORS   Hamann,J., Hartmann,E. and van Lier,R.A.
  TITLE     Structure of the human CD97 gene: exon shuffling has generated a
            new type of seven-span transmembrane molecule related to the
            secretin receptor superfamily
  JOURNAL   Genomics 32 (1), 144-147 (1996)
  MEDLINE   96230339
   PUBMED   8786105
REFERENCE   3  (residues 1 to 742)
  AUTHORS   Hamann,J., Vogel,B., van Schijndel,G.M. and van Lier,R.A.
  TITLE     The seven-span transmembrane receptor CD97 has a cellular ligand
            (CD55, DAF)
  JOURNAL   J. Exp. Med. 184 (3), 1185-1189 (1996)
  MEDLINE   97188935
   PUBMED   9064337
REFERENCE   4  (residues 1 to 742)
  AUTHORS   Gray,J.X., Haino,M., Roth,M.J., Maguire,J.E., Jensen,P.N.,
            Yarme,A., Stetler-Stevenson,M.A., Siebenlist,U. and Kelly,K.
  TITLE     CD97 is a processed, seven-transmembrane, heterodimeric receptor
            associated with inflammation
  JOURNAL   J. Immunol. 157 (12), 5438-5447 (1996)
  MEDLINE   97113332
   PUBMED   8955192
REFERENCE   5  (residues 1 to 742)
  AUTHORS   Jaspars,L.H., Vos,W., Aust,G., Van Lier,R.A. and Hamann,J.
  TITLE     Tissue distribution of the human CD97 EGF-TM7 receptor
  JOURNAL   Tissue Antigens 57 (4), 325-331 (2001)
  MEDLINE   21276051
   PUBMED   11380941
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X84700.1.
            On Dec 26, 2001 this sequence version replaced gi:4502691.
            Summary: This gene is a founding member of the EGF-TM7 family of
            class II seven-span transmembrane (7-TM) molecules, likely encoded
            by a gene cluster on the short arm of chromosome 19. The encoded
            product is a glycoprotein that is present on the surface of most
            activated leukocytes and spans the membrane seven times, which is a
            defining feature of G protein-coupled receptors. The protein has an
            extended extracellular region with several N-terminal epidermal
            growth factor (EGF)-like domains, which mediate binding to its
            cellular ligand, decay accelerating factor (DAF, CD55), a
            regulatory protein of the complement cascade. The presence of
            structural features characteristic of extracellular matrix proteins
            and transmembrane proteins suggests that this protein is a receptor
            involved in both cell adhesion and signaling processes early after
            leukocyte activation. Alternative splicing has been observed for
            this gene and two variants have been described.
            Transcript Variant: This variant (2) lacks exons 5 and 6 and
            encodes a shorter isoform (2) compared to variant 1. The missing
            internal region reduces the number of EGF-like domains from 5 to 3,
            compared to the full-length isoform (1).
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13"
     Protein         1..742
                     /product="CD97 antigen, isoform 2 precursor"
                     /note="isoform 2 is encoded by transcript variant 2;
                     leukocyte antigen CD97; seven-span transmembrane protein"
     sig_peptide     1..20
     mat_peptide     21..742
                     /product="CD97 antigen, isoform 2"
     Region          64..98
                     /region_name="Calcium-binding EGF-like domain"
                     /note="EGF_CA"
                     /db_xref="CDD:smart00179"
     Region          116..148
                     /region_name="Calcium-binding EGF-like domain"
                     /note="EGF_CA"
                     /db_xref="CDD:smart00179"
     Region          119..148
                     /region_name="Epidermal growth factor-like domain"
                     /note="EGF"
                     /db_xref="CDD:smart00181"
     variation       274
                     /allele="Q"
                     /allele="R"
                     /db_xref="dbSNP:2252171"
     Region          398..447
                     /region_name="Latrophilin/CL-1-like GPS domain. Domain
                     present in latrophilin/CL-1"
                     /note="GPS"
                     /db_xref="CDD:pfam01825"
     Region          399..449
                     /region_name="G-protein-coupled receptor proteolytic site
                     domain"
                     /note="GPS"
                     /db_xref="CDD:smart00303"
     variation       419
                     /allele="V"
                     /allele="G"
                     /db_xref="dbSNP:3182286"
     Region          451..700
                     /region_name="7 transmembrane receptor (Secretin family)"
                     /note="7tm_2"
                     /db_xref="CDD:pfam00002"
     Region          493..697
                     /region_name="7 transmembrane receptor (rhodopsin family)"
                     /note="7tm_1"
                     /db_xref="CDD:pfam00001"
     Region          592..705
                     /region_name="C. elegans Sre G protein-coupled
                     chemoreceptor. Caenorhabditis elegans Sre proteins are
                     candidate chemosensory receptors. There are four main
                     recognized groups of such receptors: Odr-10"
                     /note="Sre"
                     /db_xref="CDD:pfam03125"
     CDS             1..742
                     /gene="CD97"
                     /coded_by="NM_001784.2:71..2299"
                     /db_xref="LocusID:976"
                     /db_xref="MIM:601211"
                     /db_xref="LocusID:976"
                     /db_xref="MIM:601211"
ORIGIN      
        1 mggrvflafc vwltlpgaet qdsrgcarwc pqnsscvnat acrcnpgfss fseiittpte
       61 tcddinecat pskvscgkfs dcwntegsyd cvcspgyepv sgaktfknes entcqdvdec
      121 ssgqhqcdss tvcfntvgsy scrcrpgwkp rhgipnnqkd tvcedmtfst wtpppgvhsq
      181 tlsrffdkvq dlgrdsktss aevtiqnvik lvdelmeapg dvealappvr hliatqllsn
      241 ledimrilak slpkgpftyi spsnteltlm iqergdknvt mgqssarmkl nwavaagaed
      301 pgpavagils iqnmttllan aslnlhskkq aeleeiyess irgvqlrrls avnsiflshn
      361 ntkelnspil fafshlessd geagrdppak dvmpgprqel lcafwksdsd rgghwategc
      421 qvlgskngst tcqcshlssf ailmahydve dwkltlitrv glalslfcll lciltfllvr
      481 piqgsrttih lhlciclfvg stiflagien eggqvglrcr lvagllhycf laafcwmsle
      541 glelyflvvr vfqgqglstr wlcligygvp llivgvsaai yskgygrpry cwldfeqgfl
      601 wsflgpvtfi ilcnavifvt tvwkltqkfs einpdmkklk karaltitai aqlfllgctw
      661 vfglfifddr slvltyvfti lnclqgafly llhcllnkkv reeyrkwacl vaggskysef
      721 tsttsgtghn qtralrases gi
//



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1: NP_005132. fibrinogen, beta ...[gi:11761631] Links  


LOCUS       FGB                      491 aa            linear   PRI 03-FEB-2001
DEFINITION  fibrinogen, beta chain preproprotein; fibrinogen, B beta
            polypeptide [Homo sapiens].
ACCESSION   NP_005132
VERSION     NP_005132.1  GI:11761631
DBSOURCE    REFSEQ: aaccession NM_005141.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Chung,D.W., Que,B.G., Rixon,M.W., Mace,M. Jr. and Davie,E.W.
  TITLE     Characterization of complementary deoxyribonucleic acid and genomic
            deoxyribonucleic acid for the beta chain of human fibrinogen
  JOURNAL   Biochemistry 22 (13), 3244-3250 (1983)
  MEDLINE   83283433
   PUBMED   6688356
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Chung,D.W., Rixon,M.W., Que,B.G. and Davie,E.W.
  TITLE     Cloning of fibrinogen genes and their cDNA
  JOURNAL   Ann. N. Y. Acad. Sci. 408, 449-456 (1983)
  MEDLINE   83254384
   PUBMED   6575700
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Doolittle,R.F.
  TITLE     Fibrinogen and fibrin
  JOURNAL   Annu. Rev. Biochem. 53, 195-229 (1984)
  MEDLINE   84305751
   PUBMED   6383194
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huber,P., Dalmon,J., Courtois,G., Laurent,M., Assouline,Z. and
            Marguerie,G.
  TITLE     Characterization of the 5'-flanking region for the human fibrinogen
            beta gene
  JOURNAL   Nucleic Acids Res. 15 (4), 1615-1625 (1987)
  MEDLINE   87146483
   PUBMED   3029722
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Herrick,S., Blanc-Brude,O., Gray,A. and Laurent,G.
  TITLE     Fibrinogen
  JOURNAL   Int. J. Biochem. Cell Biol. 31 (7), 741-746 (1999)
  MEDLINE   99397060
   PUBMED   10467729
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from J00129.1 and M64983.1.
            Summary: The protein encoded by this gene is the beta component of
            fibrinogen, a blood-borne glycoprotein comprised of three pairs of
            nonidentical polypeptide chains. Following vascular injury,
            fibrinogen is cleaved by thrombin to form fibrin which is the most
            abundant component of blood clots. In addition, various cleavage
            products of fibrinogen and fibrin regulate cell adhesion and
            spreading, display vasoconstrictor and chemotactic activities, and
            are mitogens for several cell types. Mutations in this gene lead to
            several disorders, including afibrinogenemia, dysfibrinogenemia,
            hypodysfibrinogenemia and thrombotic tendency. S1 mapping studies
            on the 5'-flanking region of this gene revealed three transcription
            initiation points. Transcript variants utilizing alternative polyA
            signals have been described in the literature.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28"
     Protein         1..491
                     /product="fibrinogen, beta chain preproprotein"
                     /note="fibrinogen, B beta polypeptide"
     sig_peptide     1..30
     Proprotein      31..491
     mat_peptide     31..44
                     /product="fibrinopeptide B"
                     /note="processed active peptide"
     mat_peptide     45..491
                     /product="fibrinogen, beta chain"
                     /note="thrombin cleavage product"
     Region          114..222
                     /region_name="Syntaxin N-terminal domain"
                     /note="SynN"
                     /db_xref="CDD:SynN"
     Region          236..487
                     /region_name="Fibrinogen-related domains (FReDs)"
                     /note="FBG"
                     /db_xref="CDD:FBG"
     Region          237..487
                     /region_name="Fibrinogen beta and gamma chains"
                     /note="fibrinogen_C"
                     /db_xref="CDD:pfam00147"
     CDS             1..491
                     /gene="FGB"
                     /coded_by="NM_005141.1:9..1484"
                     /db_xref="LocusID:2244"
                     /db_xref="MIM:134830"
ORIGIN      
        1 mkrmvswsfh klktmkhlll lllcvflvks qgvndneegf fsarghrpld kkreeapslr
       61 papppisggg yrarpakaaa tqkkverkap daggclhadp dlgvlcptgc qlqeallqqe
      121 rpirnsvdel nnnveavsqt ssssfqymyl lkdlwqkrqk qvkdnenvvn eysselekhq
      181 lyidetvnsn iatnlrvlrs ilenlrskiq klesdvsaqm eycrtpctvs cnipvvsgke
      241 ceeiirkgge tsemyliqpd ssvkpyrvyc dmntenggwt viqnrqdgsv dfgrkwdpyk
      301 qgfgnvatnt dgknycglpg eywlgndkis qltrmgptel liemedwkgd kvkahyggft
      361 vqneankyqi svnkyrgtag nalmdgasql mgenrtmtih ngmffstydr dndgwltsdp
      421 rkqcskedgg gwwynrchaa npngryywgg qytwdmakhg tddgvvwmnw kgswysmrkm
      481 smkirpffpq q
//



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1: NP_009016. follistatin-like ...[gi:5901956] Links  


LOCUS       FSTL1                    308 aa            linear   PRI 04-JUN-2002
DEFINITION  follistatin-like 1 precursor; follistatin-related protein [Homo
            sapiens].
ACCESSION   NP_009016
VERSION     NP_009016.1  GI:5901956
DBSOURCE    REFSEQ: aaccession NM_007085.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 308)
  AUTHORS   Zwijsen,A., Blockx,H., Van Arnhem,W., Willems,J., Fransen,L.,
            Devos,K., Raymackers,J., Van de Voorde,A. and Slegers,H.
  TITLE     Characterization of a rat C6 glioma-secreted follistatin-related
            protein (FRP). Cloning and sequence of the human homologue
  JOURNAL   Eur. J. Biochem. 225 (3), 937-946 (1994)
  MEDLINE   95045570
   PUBMED   7957230
REFERENCE   2  (residues 1 to 308)
  AUTHORS   Tanaka,M., Ozaki,S., Osakada,F., Mori,K., Okubo,M. and Nakao,K.
  TITLE     Cloning of follistatin-related protein as a novel autoantigen in
            systemic rheumatic diseases
  JOURNAL   Int. Immunol. 10 (9), 1305-1314 (1998)
  MEDLINE   99000396
   PUBMED   9786430
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC000055.1.
            Summary: This gene encodes a protein with similarity to
            follistatin, an activin-binding protein. Like follistatin, this
            protein binds activin; in constrast to follistatin, it is nuclear
            rather than secreted. It is thought to be an autoantigen associated
            with rheumatoid arthritis.
FEATURES             Location/Qualifiers
     source          1..308
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q13.33"
     Protein         1..308
                     /product="follistatin-like 1 precursor"
                     /note="follistatin-related protein"
     sig_peptide     1..20
     mat_peptide     21..308
                     /product="follistatin-like 1"
     Region          54..98
                     /region_name="Kazal type serine protease inhibitors"
                     /note="KAZAL"
                     /db_xref="CDD:smart00280"
     Region          58..98
                     /region_name="Kazal-type S protease inhibitor domain"
                     /note="kazal"
                     /db_xref="CDD:pfam00050"
     Region          233..271
                     /region_name="von Willebrand factor (vWF) type C domain"
                     /note="VWC_out"
                     /db_xref="CDD:smart00215"
     CDS             1..308
                     /gene="FSTL1"
                     /coded_by="NM_007085.2:92..1018"
                     /db_xref="LocusID:11167"
                     /db_xref="MIM:605547"
ORIGIN      
        1 mwkrwlalal alvavawvra eeelrskski canvfcgagr ecavtekgep tclcieqckp
       61 hkrpvcgsng ktylnhcelh rdacltgski qvdydghcke kksvspsasp vvcyqsnrde
      121 lrrriiqwle aeiipdgwfs kgsnyseild kyfknfdngd srldsseflk fveqnetain
      181 ittypdqenn kllrglcvda lielsdenad wklsfqeflk clnpsfnppe kkcaledety
      241 adgaetevdc nrcvcacgnw vctamtcdgk nqkgaqtqte eemtryvqel qkhqetaekt
      301 krvstkei
//



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1: NP_001144. annexin IV; annex...[gi:4502105] Links  


LOCUS       ANXA4                    321 aa            linear   PRI 31-OCT-2000
DEFINITION  annexin IV; annexin IV (placental anticoagulant protein II);
            placental anticoagulant protein II [Homo sapiens].
ACCESSION   NP_001144
VERSION     NP_001144.1  GI:4502105
DBSOURCE    REFSEQ: aaccession NM_001153.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 321)
  AUTHORS   Grundmann,U., Amann,E., Abel,K.J. and Kupper,H.A.
  TITLE     Isolation and expression of cDNA coding for a new member of the
            phospholipase A2 inhibitor family
  JOURNAL   Behring Inst. Mitt. 82, 59-67 (1988)
  MEDLINE   88309022
   PUBMED   2970257
REFERENCE   2  (residues 1 to 321)
  AUTHORS   Hauptmann,R., Maurer-Fogy,I., Krystek,E., Bodo,G., Andree,H. and
            Reutelingsperger,C.P.
  TITLE     Vascular anticoagulant beta: a novel human Ca2+/phospholipid
            binding protein that inhibits coagulation and phospholipase A2
            activity. Its molecular cloning, expression and comparison with
            VAC-alpha
  JOURNAL   Eur. J. Biochem. 185 (1), 63-71 (1989)
  MEDLINE   90032687
   PUBMED   2530088
REFERENCE   3  (residues 1 to 321)
  AUTHORS   Romisch,J. and Heimburger,N.
  TITLE     Purification and characterization of six annexins from human
            placenta
  JOURNAL   Biol. Chem. Hoppe-Seyler 371 (5), 383-388 (1990)
  MEDLINE   90334740
   PUBMED   2143074
REFERENCE   4  (residues 1 to 321)
  AUTHORS   Romisch,J., Grote,M., Weithmann,K.U., Heimburger,N. and Amann,E.
  TITLE     Annexin proteins PP4 and PP4-X. Comparative characterization of
            biological activities of placental and recombinant proteins
  JOURNAL   Biochem. J. 272 (1), 223-229 (1990)
  MEDLINE   91090718
   PUBMED   2148260
REFERENCE   5  (residues 1 to 321)
  AUTHORS   Tait,J.F., Smith,C., Frankenberry,D.A., Miao,C.H., Adler,D.A. and
            Disteche,C.M.
  TITLE     Chromosomal mapping of the human annexin IV (ANX4) gene
  JOURNAL   Genomics 12 (2), 313-318 (1992)
  MEDLINE   92155721
   PUBMED   1346776
REFERENCE   6  (residues 1 to 321)
  AUTHORS   Satoh,A., Takayama,E., Kojima,K., Ogawa,H., Yamori,T., Sato,S.,
            Kawaguchi,T., Tsuruo,T., Katsura,Y., Kina,T. and Matsumoto,I.
  TITLE     Expression of carbohydrate-binding protein p33/41 in human tumor
            cell lines
  JOURNAL   J. Biochem. 119 (2), 346-353 (1996)
  MEDLINE   97037082
   PUBMED   8882729
REFERENCE   7  (residues 1 to 321)
  AUTHORS   Kojima,K., Yamamoto,K., Irimura,T., Osawa,T., Ogawa,H. and
            Matsumoto,I.
  TITLE     Characterization of carbohydrate-binding protein p33/41: relation
            with annexin IV, molecular basis of the doublet forms (p33 and
            p41), and modulation of the carbohydrate binding activity by
            phospholipids
  JOURNAL   J. Biol. Chem. 271 (13), 7679-7685 (1996)
  MEDLINE   96205957
   PUBMED   8631806
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M82809.1 and D78152.1.
            Summary: Annexin IV (ANX4) belongs to the annexin family of
            calcium-dependent phospholipid binding proteins. Although their
            functions are still not clearly defined, several members of the
            annexin family have been implicated in membrane-related events
            along exocytotic and endocytotic pathways.  ANX4 has 45 to 59%
            identity with other members of its family and shares a similar size
            and exon-intron organization.  Isolated from human placenta, ANX4
            encodes a protein that has possible interactions with ATP, and has
            in vitro anticoagulant activity and also inhibits phospholipase A2
            activity.  ANX4 is almost exclusively expressed in epithelial
            cells.
FEATURES             Location/Qualifiers
     source          1..321
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p13"
     Protein         1..321
                     /product="annexin IV"
                     /note="placental anticoagulant protein II; annexin IV
                     (placental anticoagulant protein II)"
     Region          21..83
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          33..85
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          92..157
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          105..157
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          175..241
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          189..241
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          250..316
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          264..316
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     CDS             1..321
                     /gene="ANXA4"
                     /coded_by="NM_001153.2:74..1039"
                     /note="carbohydrate-binding protein p33/41; protein PP4-X"
                     /db_xref="LocusID:307"
                     /db_xref="MIM:106491"
ORIGIN      
        1 mamatkggtv kaasgfname daqtlrkamk glgtdedaii svlayrntaq rqeirtayks
       61 tigrdliddl kselsgnfeq vivgmmtptv lydvqelrra mkgagtdegc lieilasrtp
      121 eeirrisqty qqqygrsled dirsdtsfmf qrvlvslsag grdegnyldd alvrqdaqdl
      181 yeagekkwgt devkfltvlc srnrnhllhv fdeykrisqk dieqsikset sgsfedalla
      241 ivkcmrnksa yfaeklyksm kglgtddntl irvmvsraei dmldirahfk rlygkslysf
      301 ikgdtsgdyr kvllvlcggd d
//



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1: NP_056453. chromosome 20 ope...[gi:18158416] Links  


LOCUS       C20orf188                797 aa            linear   PRI 09-OCT-2002
DEFINITION  chromosome 20 open reading frame 188 protein; likely ortholog of
            mouse transient receptor potential cation channel, subfamily C,
            member 4 associated protein [Homo sapiens].
ACCESSION   NP_056453
VERSION     NP_056453.1  GI:18158416
DBSOURCE    REFSEQ: aaccession NM_015638.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 797)
  AUTHORS   Andersson,B., Wentland,M.A., Ricafrente,J.Y., Liu,W. and Gibbs,R.A.
  TITLE     A 'double adaptor' method for improved shotgun library construction
  JOURNAL   Anal. Biochem. 236 (1), 107-113 (1996)
  MEDLINE   96207227
   PUBMED   8619474
REFERENCE   2  (residues 1 to 797)
  AUTHORS   Yu,W., Andersson,B., Worley,K.C., Muzny,D.M., Ding,Y., Liu,W.,
            Ricafrente,J.Y., Wentland,M.A., Lennon,G. and Gibbs,R.A.
  TITLE     Large-scale concatenation cDNA sequencing
  JOURNAL   Genome Res. 7 (4), 353-358 (1997)
  MEDLINE   97264341
   PUBMED   9110174
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC013144.1.
FEATURES             Location/Qualifiers
     source          1..797
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q11.21"
                     /clone="MGC:21388 IMAGE:4475866"
                     /tissue_type="Prostate, adenocarcinoma."
                     /clone_lib="NIH_MGC_91"
                     /lab_host="DH10B"
                     /note="Vector: pCMV-SPORT6"
     Protein         1..797
                     /product="chromosome 20 open reading frame 188 protein"
                     /note="likely ortholog of mouse transient receptor
                     potential cation channel, subfamily C, member 4 associated
                     protein"
     CDS             1..797
                     /gene="C20orf188"
                     /coded_by="NM_015638.1:4..2397"
                     /db_xref="LocusID:26133"
ORIGIN      
        1 maaapvaags gagrgrrsaa tvaawggwgg rprpgnillq lrqgqltgrg lvravqftet
       61 flterdkqsk wsgipqlllk lhttshlhsd fvecqnilke ispllsmeam afvteerklt
      121 qettypntyi fdlfggvdll veilmrptis irgqklkisd emskdclsil yntcvctegv
      181 tkrlaekndf viflftlmts kktflqtatl iedilgvkke mirldevpnl sslvsnfdqq
      241 qlanfcrila vtisemdtgn ddkhtllakn aqqkkslslg psaaeinqaa llsipgfver
      301 lcklatrkvs estgtasflq eleewytwld nalvldalmr vaneesehnq asivfpppga
      361 seenglphts artqlpqsmk imheimykle vlyvlcvllm grqrnqvhrm iaefklipgl
      421 nnlfdkliwr khsasalvlh ghnqncdcsp ditlkiqflr llqsfsdhhe nkylllnnqe
      481 lnelsaislk anipeveavl ntdrslvcdg krglltrllq vmkkepaess frfwqarave
      541 sflrgttsya dqmfllkrgl lehilycivd secksrdvlq syfdllgelm kfnvdafkrf
      601 nkyintdakf qvflkqinss lvdsnmlvrc vtlsldrfen qvdmkvaevl secrllayis
      661 qvptqmsflf rliniihvqt ltqenvscln tslvilmlar rkerlplylr llqrmehskk
      721 ypgfllnnfh nllrfwqqhy lhkdkdstcl ensscisfsy wketvsilln pdrqspsalv
      781 syieepymdi drdftee
//



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1: NP_006443. phosphoribosylami...[gi:5453539] Links  


LOCUS       PAICS                    425 aa            linear   PRI 20-OCT-2002
DEFINITION  phosphoribosylaminoimidazole carboxylase,
            phosphoribosylaminoimidazole succinocarboxamide synthetase;
            phosphoribosylaminoimidazole carboxylase,
            phosphoribosylaminoribosylaminoimidazole succinocarboxamide
            synthetase [Homo sapiens].
ACCESSION   NP_006443
VERSION     NP_006443.1  GI:5453539
DBSOURCE    REFSEQ: aaccession NM_006452.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 425)
  AUTHORS   Minet,M. and Lacroute,F.
  TITLE     Cloning and sequencing of a human cDNA coding for a multifunctional
            polypeptide of the purine pathway by complementation of the
            ade2-101 mutant in Saccharomyces cerevisiae
  JOURNAL   Curr. Genet. 18 (4), 287-291 (1990)
  MEDLINE   91070616
   PUBMED   2253271
REFERENCE   2  (residues 1 to 425)
  AUTHORS   Barton,J.W., Hart,I.M. and Patterson,D.
  TITLE     Mapping of a locus correcting lack of phosphoribosylaminoimidazole
            carboxylase activity in Chinese hamster ovary cell Ade-D mutants to
            human chromosome 4
  JOURNAL   Genomics 9 (2), 314-321 (1991)
  MEDLINE   91169536
   PUBMED   2004782
REFERENCE   3  (residues 1 to 425)
  AUTHORS   Brayton,K.A., Chen,Z., Zhou,G., Nagy,P.L., Gavalas,A., Trent,J.M.,
            Deaven,L.L., Dixon,J.E. and Zalkin,H.
  TITLE     Two genes for de novo purine nucleotide synthesis on human
            chromosome 4 are closely linked and divergently transcribed
  JOURNAL   J. Biol. Chem. 269 (7), 5313-5321 (1994)
  MEDLINE   94148998
   PUBMED   8106516
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC010273.1.
FEATURES             Location/Qualifiers
     source          1..425
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4pter-q21"
                     /clone="MGC:5024 IMAGE:2900848"
                     /tissue_type="Placenta, choriocarcinoma"
                     /clone_lib="NIH_MGC_10"
                     /lab_host="DH10B"
                     /note="Vector: pCMV-SPORT6"
     Protein         1..425
                     /product="phosphoribosylaminoimidazole carboxylase,
                     phosphoribosylaminoimidazole succinocarboxamide
                     synthetase"
                     /EC_number="6.3.2.6"
                     /EC_number="4.1.1.21"
                     /note="phosphoribosylaminoimidazole carboxylase,
                     phosphoribosylaminoribosylaminoimidazole
                     succinocarboxamide synthetase"
     Region          9..253
                     /region_name="SAICAR synthetase. Also known as
                     Phosphoribosylaminoimidazole-succinocarboxamide synthase"
                     /note="SAICAR_synt"
                     /db_xref="CDD:pfam01259"
     Region          266..420
                     /region_name="AIR carboxylase. Members of this family
                     catalyse the decarboxylation of
                     1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate
                     (AIR). This family catalyse the sixth step of de novo
                     purine biosynthesis. Some members of this family contain
                     two copies of this domain"
                     /note="AIRC"
                     /db_xref="CDD:pfam00731"
     CDS             1..425
                     /gene="PAICS"
                     /coded_by="NM_006452.2:206..1483"
                     /db_xref="LocusID:10606"
                     /db_xref="MIM:172439"
ORIGIN      
        1 mataevlnig kklyegktke vyelldspgk vllqskdqit agnaarknhl egkaaisnki
       61 tscifqllqe agiktaftrk cgetafiapq cemipiewvc rriatgsflk rnpgvkegyk
      121 fyppkvelff kddanndpqw seeqliaakf cfaglligqt evdimshatq aifeileksw
      181 lpqnctlvdm kiefgvdvtt keivladvid ndswrlwpsg drsqqkdkqs yrdlkevtpe
      241 glqmvkknfe wvaervelll ksesqcrvvv lmgstsdlgh cekikkacgn fgipcelrvt
      301 sahkgpdetl rikaeyegdg iptvfvavag rsnglgpvms gntaypvisc ppltpdwgvq
      361 dvwsslrlps glgcstvlsp egsaqfaaqi fglsnhlvws klrasilntw islkqadkki
      421 recnl
//



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1: NP_005302. growth factor rec...[gi:19923303] Links  


LOCUS       GRB10                    588 aa            linear   PRI 04-APR-2002
DEFINITION  growth factor receptor-bound protein 10 [Homo sapiens].
ACCESSION   NP_005302
VERSION     NP_005302.2  GI:19923303
DBSOURCE    REFSEQ: aaccession NM_005311.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 588)
  AUTHORS   Ohara,O., Nagase,T., Kikuno,R. and Nomura,N.
  TITLE     Homo sapiens growth factor receptor-bound protein 10 (GRB10), mRNA
  JOURNAL   Unpublished (1996)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D86962.1.
            On Apr 4, 2002 this sequence version replaced gi:4885353.
FEATURES             Location/Qualifiers
     source          1..588
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p12-p11.2"
                     /sex="male"
                     /cell_line="KG-1"
                     /cell_type="myeloblast"
     Protein         1..588
                     /product="growth factor receptor-bound protein 10"
     Region          164..244
                     /region_name="Ras association (RalGDS/AF-6) domain"
                     /note="RA"
                     /db_xref="CDD:smart00314"
     Region          164..243
                     /region_name="Band 4.1 homologues"
                     /note="B41"
                     /db_xref="CDD:smart00295"
     Region          285..393
                     /region_name="PH domain"
                     /note="PH"
                     /db_xref="CDD:pfam00169"
     Region          285..389
                     /region_name="Pleckstrin homology domain."
                     /note="PH"
                     /db_xref="CDD:smart00233"
     Region          485..572
                     /region_name="Src homology 2 domains"
                     /note="SH2"
                     /db_xref="CDD:smart00252"
     Region          487..568
                     /region_name="SH2 domain"
                     /note="SH2"
                     /db_xref="CDD:pfam00017"
     CDS             1..588
                     /gene="GRB10"
                     /coded_by="NM_005311.2:782..2548"
                     /db_xref="LocusID:2887"
                     /db_xref="MIM:601523"
ORIGIN      
        1 mqaagplfrs kdkveqtprs qqdpagpglp aqsdrlanhq eddvdlealv ndmnaslesl
       61 ysacsmqsdt vpllqngqha rsqprasgpp rsiqpqvspr qrvqrsqpvh ilavrrlqee
      121 dqqfrtsslp aipnpfpelc gpgspavltp gslppsqaaa kqdvkvfsed gtskvveila
      181 dmtardlcql lvykshcvdd nswtlvehhp hlglercled helvvqvest maseskflfr
      241 knyakyeffk npmnffpeqm vtwcqqsngs qtqllqnfln ssscpeiqgf lhvkelgkks
      301 wkklyvclrr sglycstkgt skeprhlqll adledsnifs liagrkqyna ptdhglcikp
      361 nkvrnetkel rllcaedeqt rtcwmtafrl lkygmllyqn yripqqrkal lspfstpvrs
      421 vsenslvamd fsgqtgrvie npaeaqsaal eeghawrkrs trmnilgsqs plhpstlstv
      481 ihrtqhwfhg risreeshri ikqqglvdgl fllrdsqsnp kafvltlchh qkiknfqilp
      541 ceddgqtffs lddgntkfsd liqlvdfyql nkgvlpcklk hhcirval
//



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1: NP_000652. ribosomal protein...[gi:15431303] Links  


LOCUS       RPL9                     192 aa            linear   PRI 04-SEP-2001
DEFINITION  ribosomal protein L9; 60S ribosomal protein L9 [Homo sapiens].
ACCESSION   NP_000652
VERSION     NP_000652.2  GI:15431303
DBSOURCE    REFSEQ: aaccession NM_000661.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 192)
  AUTHORS   Hori,N., Murakawa,K., Matoba,R., Fukushima,A., Okubo,K. and
            Matsubara,K.
  TITLE     A new human ribosomal protein sequence, homologue of rat L9
  JOURNAL   Nucleic Acids Res. 21 (18), 4395 (1993)
  MEDLINE   94021394
   PUBMED   8415001
REFERENCE   2  (residues 1 to 192)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem. Cell Biol. 73 (11-12), 933-947 (1995)
  MEDLINE   96282697
   PUBMED   8722009
  REMARK    This reference focuses primarily on rat ribosomal proteins, but it
            compares them to human ribosomal proteins.
REFERENCE   3  (residues 1 to 192)
  AUTHORS   Mazuruk,K., Schoen,T.J., Chader,G.J., Iwata,T. and Rodriguez,I.R.
  TITLE     Structural organization and chromosomal localization of the human
            ribosomal protein L9 gene
  JOURNAL   Biochim. Biophys. Acta 1305 (3), 151-162 (1996)
  MEDLINE   96180319
   PUBMED   8597601
REFERENCE   4  (residues 1 to 192)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res. 8 (5), 509-523 (1998)
  MEDLINE   98248690
   PUBMED   9582194
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U09953.1 and BG829769.1.
            On Sep 5, 2001 this sequence version replaced gi:4506665.
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L6P family of ribosomal proteins. It is located in the
            cytoplasm. As is typical for genes encoding ribosomal proteins,
            there are multiple processed pseudogenes of this gene dispersed
            through the genome.
FEATURES             Location/Qualifiers
     source          1..192
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4p13"
     Protein         1..192
                     /product="ribosomal protein L9"
                     /note="60S ribosomal protein L9"
     Region          12..190
                     /region_name="Ribosomal protein L6"
                     /note="Ribosomal_L6"
                     /db_xref="CDD:pfam00347"
     CDS             1..192
                     /gene="RPL9"
                     /coded_by="NM_000661.2:29..607"
                     /db_xref="LocusID:6133"
                     /db_xref="MIM:603686"
                     /db_xref="LocusID:6133"
                     /db_xref="MIM:603686"
ORIGIN      
        1 mktilsnqtv dipenvditl kgrtvivkgp rgtlrrdfnh invelsllgk kkkrlrvdkw
       61 wgnrkelatv rticshvqnm ikgvtlgfry kmrsvyahfp invviqengs lveirnflge
      121 kyirrvrmrp gvacsvsqaq kdelilegnd ielvsnsaal iqqattvknk dirkfldgiy
      181 vsekgtvqqa de
//



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1: NP_002928. ribonuclease, RNa...[gi:4506557] Links  


LOCUS       RNASE4                   147 aa            linear   PRI 27-AUG-2002
DEFINITION  ribonuclease, RNase A family, 4 [Homo sapiens].
ACCESSION   NP_002928
VERSION     NP_002928.1  GI:4506557
DBSOURCE    REFSEQ: aaccession NM_002937.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 147)
  AUTHORS   Seno,M., Futami,J., Tsushima,Y., Akutagawa,K., Kosaka,M., Tada,H.
            and Yamada,H.
  TITLE     Molecular cloning and expression of human ribonuclease 4 cDNA
  JOURNAL   Biochim. Biophys. Acta 1261 (3), 424-426 (1995)
  MEDLINE   95260866
   PUBMED   7742370
REFERENCE   2  (residues 1 to 147)
  AUTHORS   Rosenberg,H.F. and Dyer,K.D.
  TITLE     Human ribonuclease 4 (RNase 4): coding sequence, chromosomal
            localization and identification of two distinct transcripts in
            human somatic tissues
  JOURNAL   Nucleic Acids Res. 23 (21), 4290-4295 (1995)
  MEDLINE   96091174
   PUBMED   7501448
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC015520.1.
FEATURES             Location/Qualifiers
     source          1..147
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q11.1"
                     /clone="MGC:9306 IMAGE:3905439"
                     /tissue_type="Pancreas, epithelioid carcinoma"
                     /clone_lib="NIH_MGC_70"
                     /lab_host="DH10B"
                     /note="Vector: pCMV-SPORT6"
     Protein         1..147
                     /product="ribonuclease, RNase A family, 4"
     Region          29..147
                     /region_name="pfam00074, rnaseA, Pancreatic ribonuclease.
                     Ribonucleases. Members include pancreatic RNAase A and
                     angiogenins. Structure is an alpha+beta fold -- long
                     curved beta sheet and three helices"
     Region          29..147
                     /region_name="smart00092, RNAse_Pc, Pancreatic
                     ribonuclease"
     CDS             1..147
                     /gene="RNASE4"
                     /coded_by="NM_002937.2:173..616"
                     /db_xref="LocusID:6038"
                     /db_xref="MIM:601030"
ORIGIN      
        1 malqrthsll llllltllgl glvqpsygqd gmyqrflrqh vhpeetggsd rycnlmmqrr
       61 kmtlyhckrf ntfihediwn irsicsttni qckngkmnch egvvkvtdcr dtgssrapnc
      121 ryraiastrr vviacegnpq vpvhfdg
//



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1: NP_002334. lactotransferrin ...[gi:4505043] Links  


LOCUS       LTF                      711 aa            linear   PRI 31-OCT-2000
DEFINITION  lactotransferrin [Homo sapiens].
ACCESSION   NP_002334
VERSION     NP_002334.1  GI:4505043
DBSOURCE    REFSEQ: aaccession NM_002343.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 711)
  AUTHORS   Rado TA, Wei XP and Benz EJ Jr.
  TITLE     Isolation of lactoferrin cDNA from a human myeloid library and
            expression of mRNA during normal and leukemic myelopoiesis
  JOURNAL   Blood 70 (4), 989-993 (1987)
  MEDLINE   88001031
   PUBMED   3477300
REFERENCE   2  (residues 1 to 711)
  AUTHORS   McCombs JL, Teng CT, Pentecost BT, Magnuson VL, Moore CM and McGill
            JR.
  TITLE     Chromosomal localization of human lactotransferrin gene (LTF) by in
            situ hybridization
  JOURNAL   Cytogenet. Cell Genet. 47 (1-2), 16-17 (1988)
  MEDLINE   88185118
   PUBMED   3356163
REFERENCE   3  (residues 1 to 711)
  AUTHORS   Powell MJ and Ogden JE.
  TITLE     Nucleotide sequence of human lactoferrin cDNA
  JOURNAL   Nucleic Acids Res. 18 (13), 4013 (1990)
  MEDLINE   90326549
   PUBMED   2374734
REFERENCE   4  (residues 1 to 711)
  AUTHORS   Rey,M.W., Woloshuk,S.L., deBoer,H.A. and Pieper,F.R.
  TITLE     Complete nucleotide sequence of human mammary gland lactoferrin
  JOURNAL   Nucleic Acids Res. 18 (17), 5288 (1990)
  MEDLINE   90384839
   PUBMED   2402455
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X53961.1.
FEATURES             Location/Qualifiers
     source          1..711
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21-q23"
                     /clone="HLF-1"
                     /cell_type="epithelial"
                     /tissue_type="mammary gland"
                     /clone_lib="lambda gt11"
     Protein         1..711
                     /product="lactotransferrin"
     sig_peptide     1..19
     mat_peptide     20..711
                     /product="lactotransferrin"
     Region          26..354
                     /region_name="Transferrin"
                     /note="TR_FER"
                     /db_xref="CDD:TR_FER"
     Region          26..353
                     /region_name="Transferrin"
                     /note="transferrin"
                     /db_xref="CDD:pfam00405"
     Region          367..711
                     /region_name="Transferrin"
                     /note="TR_FER"
                     /db_xref="CDD:TR_FER"
     Region          367..696
                     /region_name="Transferrin"
                     /note="transferrin"
                     /db_xref="CDD:pfam00405"
     CDS             1..711
                     /gene="LTF"
                     /coded_by="NM_002343.1:295..2430"
                     /db_xref="LocusID:4057"
                     /db_xref="MIM:150210"
ORIGIN      
        1 mklvflvllf lgalglclag rrrrsvqwca vsqpeatkcf qwqrnmrkvr gppvscikrd
       61 spiqciqaia enradavtld ggfiyeagla pyklrpvaae vygterqprt hyyavavvkk
      121 ggsfqlnelq glkschtglr rtagwnvptg tlrpflnwtg ppepieaava rffsascvpg
      181 adkgqfpnlc rlcagtgenk cafssqepyf sysgafkclr dgagdvafir estvfedlsd
      241 eaerdeyell cpdntrkpvd kfkdchlarv pshavvarsv ngkedaiwnl lrqaqekfgk
      301 dkspkfqlfg spsgqkdllf kdsaigfsrv ppridsglyl gsgyftaiqn lrkseeevaa
      361 rrarvvwcav geqelrkcnq wsglsegsvt cssasttedc ialvlkgead amsldggyvy
      421 tackcglvpv laenyksqqs sdpdpncvdr pvegylavav vrrsdtsltw nsvkgkksch
      481 tavdrtagwn ipmgllfnqt gsckfdeyfs qscapgsdpr snlcalcigd eqgenkcvpn
      541 sneryygytg afrclaenag dvafvkdvtv lqntdgnnne awakdlklad fallcldgkr
      601 kpvtearsch lamapnhavv srmdkverlk qvllhqqakf grngsdcpdk fclfqsetkn
      661 llfndntecl arlhgkttye kylgpqyvag itnlkkcsts plleaceflr k
//



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1: NP_001146. annexin VI isofor...[gi:4502109] Links  


LOCUS       ANXA6                    673 aa            linear   PRI 03-FEB-2001
DEFINITION  annexin VI isoform 1; annexin VI (p68); calcium-binding protein
            p68; calphobindin II; calelectrin [Homo sapiens].
ACCESSION   NP_001146
VERSION     NP_001146.1  GI:4502109
DBSOURCE    REFSEQ: aaccession NM_001155.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 673)
  AUTHORS   Crompton,M.R., Owens,R.J., Totty,N.F., Moss,S.E., Waterfield,M.D.
            and Crumpton,M.J.
  TITLE     Primary structure of the human, membrane-associated Ca2+-binding
            protein p68 a novel member of a protein family
  JOURNAL   EMBO J. 7 (1), 21-27 (1988)
  MEDLINE   88196081
   PUBMED   3258820
REFERENCE   2  (residues 1 to 673)
  AUTHORS   Sudhof,T.C., Slaughter,C.A., Leznicki,I., Barjon,P. and
            Reynolds,G.A.
  TITLE     Human 67-kDa calelectrin contains a duplication of four repeats
            found in 35-kDa lipocortins
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 85 (3), 664-668 (1988)
  MEDLINE   88124902
   PUBMED   2963335
REFERENCE   3  (residues 1 to 673)
  AUTHORS   Iwasaki,A., Suda,M., Watanabe,M., Nakao,H., Hattori,Y., Nagoya,T.,
            Saino,Y., Shidara,Y. and Maki,M.
  TITLE     Structure and expression of cDNA for calphobindin II, a human
            placental coagulation inhibitor
  JOURNAL   J. Biochem. 106 (1), 43-49 (1989)
  MEDLINE   89380132
   PUBMED   2528541
REFERENCE   4  (residues 1 to 673)
  AUTHORS   Smith,P.D., Davies,A., Crumpton,M.J. and Moss,S.E.
  TITLE     Structure of the human annexin VI gene
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 91 (7), 2713-2717 (1994)
  MEDLINE   94195813
   PUBMED   8146179
REFERENCE   5  (residues 1 to 673)
  AUTHORS   Warrington,J.A. and Bengtsson,U.
  TITLE     High-resolution physical mapping of human 5q31-q33 using three
            methods: radiation hybrid mapping, interphase fluorescence in situ
            hybridization, and pulsed-field gel electrophoresis
  JOURNAL   Genomics 24 (2), 395-398 (1994)
  MEDLINE   95213037
   PUBMED   7698768
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from J03578.1 and X77673.1.
            Summary: Annexin VI belongs to a family of calcium-dependent
            membrane and phospholipid binding proteins. Although their
            functions are still not clearly defined, several members of the
            annexin family have been implicated in membrane-related events
            along exocytotic and endocytotic pathways. The annexin VI gene is
            approximately 60 kbp long and contains 26 exons.  It encodes a
            protein of about 68 kDa that consists of eight 68-amino acid
            repeats separated by linking sequences of variable lengths. It is
            highly similar to human annexins I and II sequences, each of which
            contain four such repeats.  Exon 21 of annexin VI is alternatively
            spliced, giving rise to two isoforms that differ by a 6-amino acid
            insertion at the start of the seventh repeat.  Annexin VI has been
            implicated in mediating the endosome aggregation and vesicle fusion
            in secreting epithelia during exocytosis.
            Transcript Variant: ANX6a transcript includes all 26 exons.
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..673
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32-q34"
     Protein         1..673
                     /product="annexin VI isoform 1"
                     /note="calphobindin II, calelectrin, calcium-binding
                     protein p68, p68, splice variant 1, protein isoform 1;
                     annexin VI (p68)"
     Region          22..89
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          37..89
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          97..161
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          109..161
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          179..245
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          193..245
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          253..320
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          268..320
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          365..432
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          393..432
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          439..504
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          452..504
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          544..593
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          544..593
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     Region          601..668
                     /region_name="Annexin"
                     /note="annexin"
                     /db_xref="CDD:pfam00191"
     Region          616..668
                     /region_name="Annexin repeats"
                     /note="ANX"
                     /db_xref="CDD:ANX"
     CDS             1..673
                     /gene="ANXA6"
                     /coded_by="NM_001155.2:171..2192"
                     /db_xref="LocusID:309"
                     /db_xref="MIM:114070"
ORIGIN      
        1 makpaqgaky rgsihdfpgf dpnqdaealy tamkgfgsdk eaildiitsr snrqrqevcq
       61 sykslygkdl iadlkyeltg kferlivglm rppaycdake ikdaisgigt dekclieila
      121 srtneqmhql vaaykdayer dleadiigdt sghfqkmlvv llqgtreedd vvsedlvqqd
      181 vqdlyeagel kwgtdeaqfi yilgnrskqh lrlvfdeylk ttgkpmkasi rgelsgdfek
      241 lmlavvkcir stpeyfaerl fkamkglgtr dntlirimvs rseldmldir eifrtkyeks
      301 lysmikndts geykktllkl sggdddaagq ffpeaaqvay qmwelsavar velkgtvrpa
      361 ndfnpdadak alrkamkglg tdedtiidii thrsnvqrqq irqtfkshfg rdlmtdlkse
      421 isgdlarlil glmmppahyd akqlkkameg agtdekalie ilatrtnaei raineayked
      481 yhksledals sdtsghfrri lislatghre eggenldqar edaqvaaeil eiadtpsgdk
      541 tsletrfmti lctrtyphlr rvfqefikmt nydvehtikk emsgdvrdaf vaivqsvknk
      601 plffadklyk smkgagtdek tltrimvsrs eidllnirre fiekydkslh qaiegdtsgd
      661 flkallalcg ged
//



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1: NP_002722. protein kinase, c...[gi:4506057] Links  


LOCUS       PRKACB                   351 aa            linear   PRI 27-AUG-2002
DEFINITION  protein kinase, cAMP-dependent, catalytic, beta [Homo sapiens].
ACCESSION   NP_002722
VERSION     NP_002722.1  GI:4506057
DBSOURCE    REFSEQ: aaccession NM_002731.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 351)
  AUTHORS   Beebe,S.J., Oyen,O., Sandberg,M., Froysa,A., Hansson,V. and
            Jahnsen,T.
  TITLE     Molecular cloning of a tissue-specific protein kinase (C gamma)
            from human testis--representing a third isoform for the catalytic
            subunit of cAMP-dependent protein kinase
  JOURNAL   Mol. Endocrinol. 4 (3), 465-475 (1990)
  MEDLINE   90258940
   PUBMED   2342480
REFERENCE   2  (residues 1 to 351)
  AUTHORS   Simard,J., Berube,D., Sandberg,M., Grzeschik,K.H., Gagne,R.,
            Hansson,V. and Jahnsen,T.
  TITLE     Assignment of the gene encoding the catalytic subunit C beta of
            cAMP-dependent protein kinase to the p36 band on chromosome 1
  JOURNAL   Hum. Genet. 88 (6), 653-657 (1992)
  MEDLINE   92201831
   PUBMED   1551670
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M34181.1.
FEATURES             Location/Qualifiers
     source          1..351
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.1"
                     /tissue_type="testis"
     Protein         1..351
                     /product="protein kinase, cAMP-dependent, catalytic, beta"
                     /EC_number="2.7.1.37"
     Region          44..298
                     /region_name="pfam00069, pkinase, Protein kinase domain"
     Region          44..298
                     /region_name="smart00220, S_TKc, erine/Threonine protein
                     kinases, catalytic domain; Phosphotransferases. Serine or
                     threonine-specific kinase subfamily"
     Region          47..281
                     /region_name="smart00219, TyrKc, Tyrosine kinase,
                     catalytic domain; Phosphotransferases. Tyrosine-specific
                     kinase subfamily"
     Region          301..351
                     /region_name="smart00133, S_TK_X, Extension to
                     Ser/Thr-type protein kinases"
     Region          302..330
                     /region_name="pfam00433, pkinase_C, Protein kinase C
                     terminal domain"
     CDS             1..351
                     /gene="PRKACB"
                     /coded_by="NM_002731.1:48..1103"
                     /note="C-beta isoform"
                     /db_xref="LocusID:5567"
                     /db_xref="MIM:176892"
ORIGIN      
        1 mgnaatakkg sevesvkefl akakedflkk wenptqnnag ledferkktl gtgsfgrvml
       61 vkhkateqyy amkildkqkv vklkqiehtl nekrilqavn fpflvrleya fkdnsnlymv
      121 meyvpggemf shlrrigrfs epharfyaaq ivltfeylhs ldliyrdlkp enllidhqgy
      181 iqvtdfgfak rvkgrtwtlc gtpeylapei ilskgynkav dwwalgvliy emaagyppff
      241 adqpiqiyek ivsgkvrfps hfssdlkdll rnllqvdltk rfgnlkngvs dikthkwfat
      301 tdwiaiyqrk veapfipkfr gsgdtsnfdd yeeedirvsi tekcakefge f
//



Revised: July 5, 2002.
 
 


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1: NP_001378. dihydropyrimidina...[gi:4503379] Links  


LOCUS       DPYSL3                   570 aa            linear   PRI 31-OCT-2000
DEFINITION  dihydropyrimidinase-like 3 [Homo sapiens].
ACCESSION   NP_001378
VERSION     NP_001378.1  GI:4503379
DBSOURCE    REFSEQ: aaccession NM_001387.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (sites)
  AUTHORS   Hamajima,N., Matsuda,K., Sakata,S., Tamaki,N., Sasaki,M. and
            Nonaka,M.
  TITLE     A novel gene family defined by human dihydropyrimidinase and three
            related proteins with differential tissue distribution
  JOURNAL   Gene 180 (1-2), 157-163 (1996)
  MEDLINE   97128821
   PUBMED   8973361
REFERENCE   2  (residues 1 to 570)
  AUTHORS   Gaetano C, Matsuo T and Thiele CJ.
  TITLE     Identification and characterization of a retinoic acid-regulated
            human homologue of the unc-33-like phosphoprotein gene (hUlip) from
            neuroblastoma cells
  JOURNAL   J. Biol. Chem. 272 (18), 12195-12201 (1997)
  MEDLINE   97277371
   PUBMED   9115293
REFERENCE   3  (residues 1 to 570)
  AUTHORS   Matsuo T, Stauffer JK, Walker RL, Meltzer P and Thiele CJ.
  TITLE     Structure and promoter analysis of the human unc-33-like
            phosphoprotein gene. E-box required for maximal expression in
            neuroblastoma and myoblasts
  JOURNAL   J. Biol. Chem. 275 (22), 16560-16568 (2000)
  MEDLINE   20287517
   PUBMED   10748015
  REMARK    Erratum:[[published erratum appears in J Biol Chem 2000 Aug
            11;275(32):25052-3]]
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D78014.1.
FEATURES             Location/Qualifiers
     source          1..570
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
                     /tissue_type="brain"
                     /dev_stage="fetus"
     Protein         1..570
                     /product="dihydropyrimidinase-like 3"
     Region          17..104
                     /region_name="Urease"
                     /note="urease"
                     /db_xref="CDD:pfam00449"
     Region          19..105
                     /region_name="Adenine deaminase"
                     /note="Adenine_deam"
                     /db_xref="CDD:pfam01979"
     Region          36..186
                     /region_name="Cellulase (glycosyl hydrolase family 5)"
                     /note="cellulase"
                     /db_xref="CDD:pfam00150"
     Region          56..452
                     /region_name="Dihydroorotase-like"
                     /note="Dihydrooratase"
                     /db_xref="CDD:pfam00744"
     variation       442
                     /allele="A"
                     /allele="S"
                     /db_xref="dbSNP:2304044"
     variation       517
                     /allele="V"
                     /allele="G"
                     /db_xref="dbSNP:1803521"
     CDS             1..570
                     /gene="DPYSL3"
                     /coded_by="NM_001387.1:111..1823"
                     /db_xref="LocusID:1809"
                     /db_xref="MIM:601168"
ORIGIN      
        1 msyqgkknip ritsdrllik ggrivnddqs fyadiymedg likqigdnli vpggvktiea
       61 ngkmvipggi dvhthfqmpy kgmttvddff qgtkaalagg ttmiidhvvp epesslteay
      121 ekwrewadgk sccdyalhvd ithwndsvkq evqnlikdkg vnsfmvymay kdlyqvsnte
      181 lyeiftclge lgaiaqvhae ngdiiaqeqt rmlemgitgp eghvlsrpee leaeavfrai
      241 tiasqtncpl yvtkvmsksa adlisqarkk gnvvfgepit aslgidgthy wsknwakaaa
      301 fvtspplspd pttpdyinsl lasgdlqlsg sahctfstaq kaigkdnfta ipegtngvee
      361 rmsviwdkav atgkmdenqf vavtstnaak ifnlyprkgr isvgsdsdlv iwdpdavkiv
      421 saknhqsaae ynifegmelr gaplvvicqg kimledgnlh vtqgagrfip cspfsdyvyk
      481 rikarrkmad lhavprgmyd gpvfdltttp kggtpagsar gsptrpnppv rnlhqsgfsl
      541 sgtqvdegvr saskrivapp ggrsnitsls
//



Revised: July 5, 2002.
 
 


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1: NP_003913. guanine nucleotid...[gi:4557026] Links  


LOCUS       HERC1                   4861 aa            linear   PRI 16-NOV-2000
DEFINITION  guanine nucleotide exchange factor p532 [Homo sapiens].
ACCESSION   NP_003913
VERSION     NP_003913.1  GI:4557026
DBSOURCE    REFSEQ: aaccession NM_003922.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 4861)
  AUTHORS   Rosa,J.L., Casaroli-Marano,R.P., Buckler,A.J., Vilaro,S. and
            Barbacid,M.
  TITLE     p619, a giant protein related to the chromosome condensation
            regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and
            Rab proteins
  JOURNAL   EMBO J. 15 (16), 4262-4273 (1996)
  MEDLINE   97015127
   PUBMED   8861955
REFERENCE   2  (residues 1 to 4861)
  AUTHORS   Rosa,J.L. and Barbacid,M.
  TITLE     A giant protein that stimulates guanine nucleotide exchange on ARF1
            and Rab proteins forms a cytosolic ternary complex with clathrin
            and Hsp70
  JOURNAL   Oncogene 15 (1), 1-6 (1997)
  MEDLINE   97377001
   PUBMED   9233772
REFERENCE   3  (residues 1 to 4861)
  AUTHORS   Ji,Y., Walkowicz,M.J., Buiting,K., Johnson,D.K., Tarvin,R.E.,
            Rinchik,E.M., Horsthemke,B., Stubbs,L. and Nicholls,R.D.
  TITLE     The ancestral gene for transcribed, low-copy repeats in the
            Prader-Willi/Angelman region encodes a large protein implicated in
            protein trafficking, which is deficient in mice with neuromuscular
            and spermiogenic abnormalities
  JOURNAL   Hum. Mol. Genet. 8 (3), 533-542 (1999)
  MEDLINE   99138701
   PUBMED   9949213
REFERENCE   4  (residues 1 to 4861)
  AUTHORS   Cruz,C., Paladugu,A., Ventura,F., Bartrons,R., Aldaz,M. and
            Rosa,J.L.
  TITLE     Assignment of the human P532 gene (HERC1) to chromosome 15q22 by
            fluorescence in situ hybridization
  JOURNAL   Cytogenet. Cell Genet. 86 (1), 68-69 (1999)
  MEDLINE   99447611
   PUBMED   10516438
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U50078.1.
            Summary: The protein encoded by this gene stimulates guanine
            nucleotide exchange on ARF1 and Rab proteins. This protein is
            throught to be involved in membrane transport processes.
FEATURES             Location/Qualifiers
     source          1..4861
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q22"
     Protein         1..4861
                     /product="guanine nucleotide exchange factor p532"
     Region          476..527
                     /region_name="Regulator of chromosome condensation (RCC1)"
                     /note="RCC1"
                     /db_xref="CDD:pfam00415"
     Region          529..578
                     /region_name="Regulator of chromosome condensation (RCC1)"
                     /note="RCC1"
                     /db_xref="CDD:pfam00415"
     Region          2069..2147
                     /region_name="Domain in SPla and the RYanodine Receptor."
                     /note="SPRY"
                     /db_xref="CDD:SPRY"
     Region          2100..2186
                     /region_name="SPRY domain"
                     /note="SPRY"
                     /db_xref="CDD:pfam00622"
     Region          4100..4150
                     /region_name="Regulator of chromosome condensation (RCC1)"
                     /note="RCC1"
                     /db_xref="CDD:pfam00415"
     Region          4152..4203
                     /region_name="Regulator of chromosome condensation (RCC1)"
                     /note="RCC1"
                     /db_xref="CDD:pfam00415"
     Region          4310..4360
                     /region_name="Regulator of chromosome condensation (RCC1)"
                     /note="RCC1"
                     /db_xref="CDD:pfam00415"
     Region          4501..4848
                     /region_name="Domain Homologous to E6-AP Carboxyl Terminus
                     with"
                     /note="HECTc"
                     /db_xref="CDD:HECTc"
     Region          4543..4836
                     /region_name="HECT-domain (ubiquitin-transferase)"
                     /note="HECT"
                     /db_xref="CDD:pfam00632"
     CDS             1..4861
                     /gene="HERC1"
                     /coded_by="NM_003922.1:97..14682"
                     /db_xref="LocusID:8925"
                     /db_xref="MIM:605109"
                     /db_xref="LocusID:8925"
                     /db_xref="MIM:605109"
ORIGIN      
        1 matmippvkl kwlehlnssw itedsesiat regvavlysk lvsnkevvpl pqqvlclkgp
       61 qlpdferesl ssdeqdhyld allssqlala kmvcsdspfa galrkrllvl qrvfyalsnk
      121 yhdkgkvkqq qhspesssgs advhsvserp rsstdaliem gvrtglsllf allrqswmmp
      181 vsgpglslcn dvihtaievv sslpplslan eskippmgld clsqvttflk gvtipnsgad
      241 tlgrrlasel llglaaqrgs lryllewiem algasavvht mekgkllssq egmisfdcfm
      301 tilmqmrrsl gssadrsqwr eptrtsdglc slyeaalclf eevcrmasdy srtcaspdsi
      361 qtgdapivse tcevyvwgsn sshqlvegtq ekilqpklap sfsdaqtiea gqyctfvist
      421 dgsvracgkg sygrlglgds nnqstlkklt fephrsikkv ssskgsdght lafttegevf
      481 swgdgdygkl ghgnsstqky pkliqgplqg kvvvcvsagy rhsaavtedg elytwgegdf
      541 grlghgdsns rniptlvkdi snvgevscgs shtialskdg rtvwsfgggd ngklghgdtn
      601 rvykpkviea lqgmfirkvc agsqsslalt stgqvyawgc gaclgcgsse atalrpklie
      661 elaatrivdv sigdshclal shdnevyawg nnsmgqcgqg nstgpitkpk kvsgldgiai
      721 qqisagtshs lawtalprdr qvvawhrpyc vdleestfsh lrsflerycd kinseipplp
      781 fpssrehhsf lklclkllsn hlalalaggv atsilgrqag plrnllfrlm dstvpdeiqe
      841 vvietlsvga tmllpplrer mellhsllpq gpdrweslsk gqrmqldiil tslqdhthva
      901 sllgysspsd aadlssvctg ygnlsdqpyg tqschpdthl aeilmktllr nlgfytdqaf
      961 geleknsdkf llgtsssens qpahlhellc slqkqllafc hinnisenss svallhkhlq
     1021 lllphatdiy srsanllkes pwngsvgekl rdviyvsaag smlcqivnsl lllpvsvarp
     1081 llsylldllp pldclnrllp aadlledqel qwplhggpel idpaglplpq paqswvwlvd
     1141 lertiallig rclggmlqgs pvspeeqdta ywmktplfsd gvemdtpqld kcmsclleva
     1201 lsgneeqkpf dyklrpeiav yvdlalgcsk eparslwism qdyavskdwd satlsnesll
     1261 dtvsrfvlaa llkhtnllsq acgesryqpg khlsevyrcv ykvrsrllac knleliqtrs
     1321 ssrdrwisen qdsadvdpqe hsftrtidee aemeeqaerd reeghpeped eeeerehevm
     1381 tagkifqcfl sarevarsrd rdrmnsgags garaddpppq sqqerrvstd lpegqdvyta
     1441 acnsvihrca llilgvspvi delqkrreeg qlqqpstsas eggglmtrse sltaesrlvh
     1501 tspnyrliks rsesdlsqpe sdeegyalsg rqnvdldlaa shrkrgpmhs qleslsdswa
     1561 rlkhsrdwlc nssysfesdf dltkslgvht lienvvsfvs gdvgnapgfk epeesmstsp
     1621 qasiiameqq qlraelrlea lhqilvllsg meekgsisla gsrlssgfqs stlltsvrlq
     1681 flagcfglgt vghtgakges grlhhyqdgi raakrniqie iqvavhkiyq qlsatleral
     1741 qankhhieaq qrlllvtvfa lsvhyqpvdv slaistglln vlsqlcgtdt mlgqplqllp
     1801 ktgvsqlsta lkvastrllq ilaittgtya dklspkvvqs lldllcsqlk nllsqtgvlh
     1861 masfgegeqe dgeeeekkvd ssgetekkdf raalrkqhaa elhlgdflvf lrrvvsskai
     1921 qskmaspkwt evllniasqk cssgiplvgn lrtrllalhv leavlpaces gveddqmaqi
     1981 verlfsllsd cmwetpiaqa khaiqikeke qeiklqkqge leeedenlpi qevsfdpeka
     2041 qcclvengqi lthgsggkgy glastgvtsg cyqwkfyivk enrgnegtcv gvsrwpvhdf
     2101 nhrttsdmwl yraysgnlyh ngeqtltlss ftqgdfitcv ldmeartisf gkngeepkla
     2161 fedvdaaely pcvmfyssnp gekvkicdmq mrgtprdllp gdpicspvaa vlaeatiqlv
     2221 rilhrtdrwt ycinkkmmer lhkikicike sgqklkksrs vqsreenemr eekeskeeek
     2281 gkhtrhglad lselqlrtlc ievwpvlavi ggvdaglrvg grcvhkqtgr hatllgvvke
     2341 gstsakvqwd eaeitisfpt fwspsdtply nlepceplpf dvarfrglta svlldltylt
     2401 gvhedmgkqs tkrhekkhrh eseekgdveq kpesesaldm rtgltsddvk sqsttsskse
     2461 neiasfsldp tlpsvesqhq itegkrknhe hmsknhdvaq seiravqlsy lylgamksls
     2521 allgcskyae lllipkvlae nghnsdcass pvvhedvemr aalqflmrhm vkravmrspi
     2581 kralgladle raqamiyklv vhglledqfg gkikqeidqq aeesdpaqqa qtpvttspsa
     2641 ssttsfmsss ledtttattp vtdtetvpas espgvmplsl lrqmfssypt ttvlptrraq
     2701 tppisslpts psdevgrrqs ltspdsqsar panrtalsdp ssrlstsppp paiavpllem
     2761 gfslrqiaka meatgargea daqnitvlam wmiehpghed eeepqsgsta dsrpgaavlg
     2821 sggksndpcy lqspgdipsa daaemeegfs espdnldhte naasgsgpsa rgrsavtrrh
     2881 kfdlaartll araaglyrsv qahrnqsrre gislqqdpga lydfnldeel eidlddeame
     2941 amfgqdltsd ndilgmwipe vldwptwhvc esedreevvv celcecsvvs fnqhmkrnhp
     3001 gcgrsanrqg yrsngsyvdg wfggecgsgn pyyllcgtcr ekylamktks kstsserykg
     3061 qapdligkqd svyeedwdml dvdedekltg eeefellagp lglndrrivp epvqfpdsdp
     3121 lgasvamvta tnsmeetlmq igchgsveks ssgritlgeq aaalanphdr vvalrrvtaa
     3181 aqvllartmv mralsllsvs gsscslaagl eslgltdirt lvrlmclaaa graglstsps
     3241 amastsersr gghskankpi sclaylstav gclasnapsa akllvqlctq nlisaatgvn
     3301 lttvddsiqr kflpsflrgi aeenklvtsp nfvvtqalva lladkgaklr pnydksevek
     3361 kgplelanal aacclssrls sqhrqwaaqq lvrtlaahdr dnqttlqtla dmggdlrkcs
     3421 fikleahqnr vmtcvwcnkk gllatsgndg tirvwnvtkk qyslqqtcvf nrlegdaees
     3481 lgspsdpsfs pvswsisgky lagalekmvn iwqvnggkgl vdiqphwvsa lawpeegpat
     3541 awsgespell lvgrmdgslg lievvdvstm hrrelehcyr kdvsvtciaw fsedrpfavg
     3601 yfdgklllgt keplekggiv lidahkdtli smkwdptghi lmtcakedsv klwgsisgcw
     3661 cclhslchps ivngiawcrl pgkgsklqll matgcqsglv cvwripqdtt qtnvtsaegw
     3721 wdqesncqdg yrkssgakcv yqlrghitpv rtvafssdgl alvsgglggl mniwslrdgs
     3781 vlqtvvigsg aiqttvwipe vgvaacsnrs kdvlvvncta ewaaanhvla tcrtalkqqg
     3841 vlglnmapcm raflerlpmm lqeqyayekp hvvcgdqlvh spymqclasl avglhldqll
     3901 cnppvpphhq nclpdpaswn pnewawlecf sttikaaeal tngaqfpesf tvpdlepvpe
     3961 delvflmdns kwingmdeqi mswatsrped whlggkcdvy lwgagrhgql aeagrnvmvp
     4021 aaapsfsqaq qvicgqnctf viqangtvla cgegsygrlg qgnsddlhvl tvisalqgfv
     4081 vtqlvtscgs dghsmaltes gevfswgdgd ygklghgnsd rqrrprqiea lqgeevvqms
     4141 cgfkhsavvt sdgklftfgn gdygrlglgn tsnkklperv talegyqigq vacglnhtla
     4201 vsadgsmvwa fgdgdygklg lgnstakssp qkidvlcgig ikkvacgtqf svaltkdghv
     4261 ytfgqdrlig lpegrarnhn rpqqipvlag viiedvavga ehtlalasng dvyawgsnse
     4321 gqlglghtnh vreptlvtgl qgknvrqisa grchsaawta ppvpprapgv svplqlglpd
     4381 tvppqygalr evsihtvrar lrllyhfsdl mysswrllnl spnnqnstsh ynagtwgivq
     4441 gqlrpllapr vytlpmvrsi gktmvqgkny gpqitvkris trgrkckpif vqiarqvvkl
     4501 nasdlrlpsr awkvklvgeg addaggvfdd titemcqele tgivdllips pnataevgyn
     4561 rdrflfnpsa cldehlmqfk flgilmgvai rtkkpldlhl aplvwkqlcc vpltledlee
     4621 vdllyvqtln silhiedsgi teesfhemip ldsfvgqsad gkmvpiipgg nsipltfsnr
     4681 keyveraiey rlhemdrqva avregmswiv pvpllsllta kqleqmvcgm peisvevlkk
     4741 vvryrevdeq hqlvqwfwht leefsneerv lfmrfvsgrs rlpantadis qrfqimkvdr
     4801 pydslptsqt cffqlrlppy ssqlvmaerl ryainncrsi dmdnymlsrn vdnaegsdtd
     4861 y
//



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1: NP_005597. legumain; proteas...[gi:21914881] Links  


LOCUS       LGMN                     433 aa            linear   PRI 22-JUL-2002
DEFINITION  legumain; protease, cysteine, 1 (legumain) [Homo sapiens].
ACCESSION   NP_005597
VERSION     NP_005597.2  GI:21914881
DBSOURCE    REFSEQ: aaccession NM_005606.3
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 433)
  AUTHORS   Tanaka,T., Inazawa,J. and Nakamura,Y.
  TITLE     Molecular cloning of a human cDNA encoding putative cysteine
            protease (PRSC1) and its chromosome assignment to 14q32.1
  JOURNAL   Cytogenet. Cell Genet. 74 (1-2), 120-123 (1996)
  MEDLINE   97049087
   PUBMED   8893817
REFERENCE   2  (residues 1 to 433)
  AUTHORS   Chen,J.M., Dando,P.M., Rawlings,N.D., Brown,M.A., Young,N.E.,
            Stevens,R.A., Hewitt,E., Watts,C. and Barrett,A.J.
  TITLE     Cloning, isolation, and characterization of mammalian legumain, an
            asparaginyl endopeptidase
  JOURNAL   J. Biol. Chem. 272 (12), 8090-8098 (1997)
  MEDLINE   97218252
   PUBMED   9065484
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC003061.1.
            On Jul 22, 2002 this sequence version replaced gi:5031991.
FEATURES             Location/Qualifiers
     source          1..433
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q32.1"
                     /clone="MGC:1395 IMAGE:3504506"
                     /tissue_type="Placenta, choriocarcinoma"
                     /clone_lib="NIH_MGC_21"
                     /lab_host="DH10B-R"
                     /note="Vector: pOTB7"
     Protein         1..433
                     /product="legumain"
                     /note="protease, cysteine, 1 (legumain)"
     Region          6..327
                     /region_name="pfam01650, Peptidase_C13, Peptidase C13
                     family. This family of peptidases is known as the
                     hemoglobinase family because it contains a globin
                     degrading enzyme from blood parasites. However relatives
                     are found in plants and other organisms that have other
                     functions. Members of this family are asparaginyl
                     peptidases"
     CDS             1..433
                     /gene="LGMN"
                     /coded_by="NM_005606.3:142..1443"
                     /db_xref="LocusID:5641"
                     /db_xref="MIM:602620"
ORIGIN      
        1 mvwkvavfls valgigaipi ddpedggkhw vvivagsngw ynyrhqadac hayqiihrng
       61 ipdeqivvmm yddiaysedn ptpgivinrp ngtdvyqgvp kdytgedvtp qnflavlrgd
      121 aeavkgigsg kvlksgpqdh vfiyftdhgs tgilvfpned lhvkdlneti hymykhkmyr
      181 kmvfyieace sgsmmnhlpd ninvyattaa npressyacy ydekrstylg dwysvnwmed
      241 sdvedltket lhkqyhlvks htntshvmqy gnktistmkv mqfqgmkrka sspvplppvt
      301 hldltpspdv pltimkrklm ntndleesrq lteeiqrhld arhlieksvr kivsllaase
      361 aeveqllser apltghscyp eallhfrthc fnwhsptyey alrhlyvlvn lcekpyplhr
      421 iklsmdhvcl ghy
//



Revised: July 5, 2002.
 
 


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1: NP_005859. Golgi vesicular m...[gi:5031611] Links  


LOCUS       BET1                     118 aa            linear   PRI 20-DEC-2001
DEFINITION  Golgi vesicular membrane trafficking protein p18; Bet1 (S.
            cerevisiae) homolog; Bet1p homolog [Homo sapiens].
ACCESSION   NP_005859
VERSION     NP_005859.1  GI:5031611
DBSOURCE    REFSEQ: aaccession NM_005868.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 118)
  AUTHORS   Hay,J.C., Hirling,H. and Scheller,R.H.
  TITLE     Mammalian vesicle trafficking proteins of the endoplasmic reticulum
            and Golgi apparatus
  JOURNAL   J. Biol. Chem. 271 (10), 5671-5679 (1996)
  MEDLINE   96215028
   PUBMED   8621431
REFERENCE   2  (residues 1 to 118)
  AUTHORS   Zhang,T., Wong,S.H., Tang,B.L., Xu,Y., Peter,F., Subramaniam,V.N.
            and Hong,W.
  TITLE     The mammalian protein (rbet1) homologous to yeast Bet1p is
            primarily associated with the pre-Golgi intermediate compartment
            and is involved in vesicular transport from the endoplasmic
            reticulum to the Golgi apparatus
  JOURNAL   J. Cell Biol. 139 (5), 1157-1168 (1997)
  MEDLINE   98044220
   PUBMED   9382863
REFERENCE   3  (residues 1 to 118)
  AUTHORS   Waters,M.G. and Pfeffer,S.R.
  TITLE     Membrane tethering in intracellular transport
  JOURNAL   Curr. Opin. Cell Biol. 11 (4), 453-459 (1999)
  MEDLINE   99379903
   PUBMED   10449330
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF007551.1.
            Summary: The protein encoded by this gene is a homolog of yeast
            Bet1 protein which is a golgi-associated protein that participates
            in vesicular transport from the endoplasmic reticulum (ER) to the
            Golgi apparatus. Studies with the rat homolog suggest that it is
            localized in the vesicular structures, and may be involved in the
            docking process of ER-derived vesicles with the cis-Golgi membrane.
FEATURES             Location/Qualifiers
     source          1..118
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q21.1-q22"
     Protein         1..118
                     /product="Golgi vesicular membrane trafficking protein
                     p18"
                     /note="Bet1 (S. cerevisiae) homolog; Bet1p homolog"
     Region          29..86
                     /region_name="Helical region found in SNAREs"
                     /note="t_SNARE"
                     /db_xref="CDD:smart00397"
     CDS             1..118
                     /gene="BET1"
                     /coded_by="NM_005868.2:120..476"
                     /db_xref="LocusID:10282"
                     /db_xref="MIM:605456"
ORIGIN      
        1 mrraglgegv ppgnygnygy ansgysacee enerlteslr skvtaiksls ieighevktq
       61 nkllaemdsq fdsttgflgk tmgklkilsr gsqtkllcym mlfslfvffi iywiiklr
//



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1: NP_004521. matrix metallopro...[gi:11342666] Links  


LOCUS       MMP2                     660 aa            linear   PRI 07-SEP-2002
DEFINITION  matrix metalloproteinase 2 preproprotein; gelatinase A; 72kD type
            IV collagenase; gelatinase neutrophil [Homo sapiens].
ACCESSION   NP_004521
VERSION     NP_004521.1  GI:11342666
DBSOURCE    REFSEQ: aaccession NM_004530.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 660)
  AUTHORS   Collier,I.E., Wilhelm,S.M., Eisen,A.Z., Marmer,B.L., Grant,G.A.,
            Seltzer,J.L., Kronberger,A., He,C.S., Bauer,E.A. and Goldberg,G.I.
  TITLE     H-ras oncogene-transformed human bronchial epithelial cells (TBE-1)
            secrete a single metalloprotease capable of degrading basement
            membrane collagen
  JOURNAL   J. Biol. Chem. 263 (14), 6579-6587 (1988)
  MEDLINE   88198218
   PUBMED   2834383
REFERENCE   2  (residues 1 to 660)
  AUTHORS   Huhtala,P., Eddy,R.L., Fan,Y.S., Byers,M.G., Shows,T.B. and
            Tryggvason,K.
  TITLE     Completion of the primary structure of the human type IV
            collagenase preproenzyme and assignment of the gene (CLG4) to the
            q21 region of chromosome 16
  JOURNAL   Genomics 6 (3), 554-559 (1990)
  MEDLINE   90228972
   PUBMED   2158484
REFERENCE   3  (residues 1 to 660)
  AUTHORS   Huhtala,P., Chow,L.T. and Tryggvason,K.
  TITLE     Structure of the human type IV collagenase gene
  JOURNAL   J. Biol. Chem. 265 (19), 11077-11082 (1990)
  MEDLINE   90293047
   PUBMED   2162831
REFERENCE   4  (residues 1 to 660)
  AUTHORS   Levy,A.T., Cioce,V., Sobel,M.E., Garbisa,S., Grigioni,W.F.,
            Liotta,L.A. and Stetler-Stevenson,W.G.
  TITLE     Increased expression of the Mr 72,000 type IV collagenase in human
            colonic adenocarcinoma
  JOURNAL   Cancer Res. 51 (1), 439-444 (1991)
  MEDLINE   91105673
   PUBMED   1846313
REFERENCE   5  (residues 1 to 660)
  AUTHORS   Collier,I.E., Bruns,G.A., Goldberg,G.I. and Gerhard,D.S.
  TITLE     On the structure and chromosome location of the 72- and 92-kDa
            human type IV collagenase genes
  JOURNAL   Genomics 9 (3), 429-434 (1991)
  MEDLINE   91236162
   PUBMED   1851724
REFERENCE   6  (residues 1 to 660)
  AUTHORS   Chen, L.Z., Harris, P.C., Apostolou, S., Baker, E., Holman, K.,
            Lane, S.A., Nancarrow, J.K., Whitmore, S.A., Stallings, R.L.,
            Hildebrand, C.E. et al.
  TITLE     A refined physical map of the long arm of human chromosome 16
  JOURNAL   Genomics 10 (2), 308-312 (1991)
  MEDLINE   91301684
   PUBMED   2071140
REFERENCE   7  (residues 1 to 660)
  AUTHORS   Devarajan,P., Johnston,J.J., Ginsberg,S.S., Van Wart,H.E. and
            Berliner,N.
  TITLE     Structure and expression of neutrophil gelatinase cDNA. Identity
            with type IV collagenase from HT1080 cells
  JOURNAL   J. Biol. Chem. 267 (35), 25228-25232 (1992)
  MEDLINE   93094232
   PUBMED   1460022
REFERENCE   8  (residues 1 to 660)
  AUTHORS   Libson,A.M., Gittis,A.G., Collier,I.E., Marmer,B.L., Goldberg,G.I.
            and Lattman,E.E.
  TITLE     Crystal structure of the haemopexin-like C-terminal domain of
            gelatinase A
  JOURNAL   Nat. Struct. Biol. 2 (11), 938-942 (1995)
  MEDLINE   96069777
   PUBMED   7583664
REFERENCE   9  (residues 1 to 660)
  AUTHORS   Massova,I., Kotra,L.P., Fridman,R. and Mobashery,S.
  TITLE     Matrix metalloproteinases: structures, evolution, and
            diversification
  JOURNAL   FASEB J. 12 (12), 1075-1095 (1998)
  MEDLINE   98407729
   PUBMED   9737711
REFERENCE   10 (residues 1 to 660)
  AUTHORS   Morgunova,E., Tuuttila,A., Bergmann,U., Isupov,M., Lindqvist,Y.,
            Schneider,G. and Tryggvason,K.
  TITLE     Structure of human pro-matrix metalloproteinase-2: activation
            mechanism revealed
  JOURNAL   Science 284 (5420), 1667-1670 (1999)
  MEDLINE   99286304
   PUBMED   10356396
REFERENCE   11 (residues 1 to 660)
  AUTHORS   Nagase,H. and Woessner,J.F. Jr.
  TITLE     Matrix metalloproteinases
  JOURNAL   J. Biol. Chem. 274 (31), 21491-21494 (1999)
  MEDLINE   99348265
   PUBMED   10419448
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M58552.1.
            Summary: Proteins of the matrix metalloproteinase (MMP) family are
            involved in the breakdown of extracellular matrix in normal
            physiological processes, such as embryonic development,
            reproduction, and tissue remodeling,as well as in disease
            processes, such as arthritis and metastasis. Most MMP's are
            secreted as inactive proproteins which are activated when cleaved
            by extracellular proteinases. This gene encodes an enzyme which
            degrades type IV collagen, the major structural component of
            basement membranes. The enzyme plays a role in endometrial
            menstrual breakdown, regulation of vascularization and the
            inflammatory response.
FEATURES             Location/Qualifiers
     source          1..660
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q13-q21"
     Protein         1..660
                     /product="matrix metalloproteinase 2 preproprotein"
                     /EC_number="3.4.24.24"
                     /note="gelatinase A; 72kD type IV collagenase; gelatinase
                     neutrophil"
     Protein         1..660
                     /product="matrix metalloproteinase 2 preproprotein"
                     /EC_number="3.4.24.24"
                     /note="gelatinase A; matrix metalloproteinase 2
                     (gelatinase A, 72kD gelatinase, 72kD type IV collagenase);
                     gelatinase neutrophil"
     sig_peptide     1..29
     variation       27
                     /allele="A"
                     /allele="S"
                     /db_xref="dbSNP:243863"
     Region          32..106
                     /region_name="pfam03933, Peptidase_M10_N, Matrix
                     metalloprotease, N-terminal domain. This family is found
                     N-terminal to the catalytic domain of matrixin"
     mat_peptide     110..660
                     /product="matrix metalloproteinase 2"
     Region          112..218
                     /region_name="pfam00413, Peptidase_M10, Matrixin. The
                     members of this family are enzymes that cleave peptides.
                     These proteases require zinc for catalysis"
     Region          115..230
                     /region_name="smart00235, ZnMc, Zinc-dependent
                     metalloprotease; Neutral zinc metallopeptidases. This
                     alignment represents a subset of known subfamilies.
                     Highest similarity occurs in the HExxH zinc-binding site/
                     active site"
     Region          226..274
                     /region_name="smart00059, FN2, Fibronectin type 2 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Also occurs in coagulation factor
                     XII, 2 type IV collagenases, PDC-109, and
                     cation-independent mannose-6-phosphate and secretory
                     phospholipase A2 receptors. In fibronectin, PDC-109, and
                     the collagenases, this domain contributes to
                     collagen-binding function"
     Region          233..274
                     /region_name="pfam00040, fn2, Fibronectin type II domain"
     Region          284..332
                     /region_name="smart00059, FN2, Fibronectin type 2 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Also occurs in coagulation factor
                     XII, 2 type IV collagenases, PDC-109, and
                     cation-independent mannose-6-phosphate and secretory
                     phospholipase A2 receptors. In fibronectin, PDC-109, and
                     the collagenases, this domain contributes to
                     collagen-binding function"
     Region          291..332
                     /region_name="pfam00040, fn2, Fibronectin type II domain"
     Region          342..390
                     /region_name="smart00059, FN2, Fibronectin type 2 domain;
                     One of three types of internal repeat within the plasma
                     protein, fibronectin. Also occurs in coagulation factor
                     XII, 2 type IV collagenases, PDC-109, and
                     cation-independent mannose-6-phosphate and secretory
                     phospholipase A2 receptors. In fibronectin, PDC-109, and
                     the collagenases, this domain contributes to
                     collagen-binding function"
     Region          349..390
                     /region_name="pfam00040, fn2, Fibronectin type II domain"
     Region          383..447
                     /region_name="smart00235, ZnMc, Zinc-dependent
                     metalloprotease; Neutral zinc metallopeptidases. This
                     alignment represents a subset of known subfamilies.
                     Highest similarity occurs in the HExxH zinc-binding site/
                     active site"
     Region          475..517
                     /region_name="smart00120, HX, Hemopexin-like repeats;
                     Hemopexin is a heme-binding protein that transports heme
                     to the liver. Hemopexin-like repeats occur in vitronectin
                     and some matrix metalloproteinases family (matrixins). The
                     HX repeats of some matrixins bind tissue inhibitor of
                     metalloproteinases (TIMPs)"
     Region          475..513
                     /region_name="pfam00045, hemopexin, Hemopexin. Hemopexin
                     is a heme-binding protein that transports heme to the
                     liver. Hemopexin-like repeats occur in vitronectin and
                     some matrix metallopeptidases family (matrixins). The HX
                     repeats of some matrixins bind tissue inhibitor of
                     metallopeptidases (TIMPs)"
     Region          520..563
                     /region_name="pfam00045, hemopexin, Hemopexin. Hemopexin
                     is a heme-binding protein that transports heme to the
                     liver. Hemopexin-like repeats occur in vitronectin and
                     some matrix metallopeptidases family (matrixins). The HX
                     repeats of some matrixins bind tissue inhibitor of
                     metallopeptidases (TIMPs)"
     Region          568..614
                     /region_name="smart00120, HX, Hemopexin-like repeats;
                     Hemopexin is a heme-binding protein that transports heme
                     to the liver. Hemopexin-like repeats occur in vitronectin
                     and some matrix metalloproteinases family (matrixins). The
                     HX repeats of some matrixins bind tissue inhibitor of
                     metalloproteinases (TIMPs)"
     Region          568..610
                     /region_name="pfam00045, hemopexin, Hemopexin. Hemopexin
                     is a heme-binding protein that transports heme to the
                     liver. Hemopexin-like repeats occur in vitronectin and
                     some matrix metallopeptidases family (matrixins). The HX
                     repeats of some matrixins bind tissue inhibitor of
                     metallopeptidases (TIMPs)"
     CDS             1..660
                     /gene="MMP2"
                     /coded_by="NM_004530.1:290..2272"
                     /db_xref="LocusID:4313"
                     /db_xref="MIM:120360"
ORIGIN      
        1 mealmargal tgplralcll gcllshaaaa pspiikfpgd vapktdkela vqylntfygc
       61 pkescnlfvl kdtlkkmqkf fglpqtgdld qntietmrkp rcgnpdvany nffprkpkwd
      121 knqityriig ytpdldpetv ddafarafqv wsdvtplrfs rihdgeadim infgrwehgd
      181 gypfdgkdgl lahafapgtg vggdshfddd elwtlgegqv vrvkygnadg eyckfpflfn
      241 gkeynsctdt grsdgflwcs ttynfekdgk ygfcphealf tmggnaegqp ckfpfrfqgt
      301 sydscttegr tdgyrwcgtt edydrdkkyg fcpetamstv ggnsegapcv fpftflgnky
      361 esctsagrsd gkmwcattan ydddrkwgfc pdqgyslflv aahefghamg lehsqdpgal
      421 mapiytytkn frlsqddikg iqelygaspd idlgtgptpt lgpvtpeick qdivfdgiaq
      481 irgeifffkd rfiwrtvtpr dkpmgpllva tfwpelpeki davyeapqee kavffagney
      541 wiysastler gypkpltslg lppdvqrvda afnwsknkkt yifagdkfwr ynevkkkmdp
      601 gfpkliadaw naipdnldav vdlqggghsy ffkgayylkl enqslksvkf gsiksdwlgc
//



Revised: July 5, 2002.
 
 


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NCBI | NLM | NIH 

 

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&&&&&&&


    
 
PubMed Nucleotide Protein Genome Structure PopSet Taxonomy OMIM Books 
 
   Search PubMed Protein Nucleotide PopSet Taxonomy Genome OMIM Structure Domains GEO Books Books2 MapViewDr TestDb UniSTS CDD SNP Journals UniGene  for        
 
    Limits  Preview/Index  History  Clipboard  Details  
 
 
  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_003239. thrombospondin 4 ...[gi:4507489] Links  


LOCUS       THBS4                    961 aa            linear   PRI 27-AUG-2002
DEFINITION  thrombospondin 4 [Homo sapiens].
ACCESSION   NP_003239
VERSION     NP_003239.1  GI:4507489
DBSOURCE    REFSEQ: aaccession NM_003248.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 961)
  AUTHORS   Lawler,J., McHenry,K., Duquette,M. and Derick,L.
  TITLE     Characterization of human thrombospondin-4
  JOURNAL   J. Biol. Chem. 270 (6), 2809-2814 (1995)
  MEDLINE   95155352
   PUBMED   7852353
REFERENCE   2  (residues 1 to 961)
  AUTHORS   Arber,S. and Caroni,P.
  TITLE     Thrombospondin-4, an extracellular matrix protein expressed in the
            developing and adult nervous system promotes neurite outgrowth
  JOURNAL   J. Cell Biol. 131 (4), 1083-1094 (1995)
  MEDLINE   96074771
   PUBMED   7490284
REFERENCE   3  (residues 1 to 961)
  AUTHORS   Newton,G., Weremowicz,S., Morton,C.C., Jenkins,N.A., Gilbert,D.J.,
            Copeland,N.G. and Lawler,J.
  TITLE     The thrombospondin-4 gene
  JOURNAL   Mamm. Genome 10 (10), 1010-1016 (1999)
  MEDLINE   99431670
   PUBMED   10501972
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from Z19585.1.
FEATURES             Location/Qualifiers
     source          1..961
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13"
                     /tissue_type="heart"
                     /clone_lib="human heart"
                     /dev_stage="adult"
     Protein         1..961
                     /product="thrombospondin 4"
                     /function="unknown"
     sig_peptide     1..21
     mat_peptide     22..961
                     /product="thrombospondin 4"
                     /standard_name="thrombospondin-4"
     Region          24..192
                     /region_name="pfam02210, TSPN, Thrombospondin N-terminal
                     -like domain"
     Region          24..192
                     /region_name="smart00210, TSPN, Thrombospondin N-terminal
                     -like domains; Heparin-binding and cell adhesion domain of
                     thrombospondin"
     Region          290..325
                     /region_name="smart00179, EGF_CA, Calcium-binding EGF-like
                     domain"
     Region          326..360
                     /region_name="smart00179, EGF_CA, Calcium-binding EGF-like
                     domain"
     Region          379..413
                     /region_name="smart00179, EGF_CA, Calcium-binding EGF-like
                     domain"
     CDS             1..961
                     /gene="THBS4"
                     /coded_by="NM_003248.1:28..2913"
                     /db_xref="LocusID:7060"
                     /db_xref="MIM:600715"
ORIGIN      
        1 mlaprgaavl llhlvlqrwl aagaqatpqv fdllpsssqr lnpgallpvl tdpalndlyv
       61 istfklqtks satifglyss tdnskyfeft vmgrlskail rylkndgkvh lvvfnnlqla
      121 dgrrhrillr lsnlqrgags lelyldciqv dsvhnlpraf agpsqkpeti elrtfqrkpq
      181 dfleelklvv rgslfqvasl qdcflqqsep laatgtgdfn rqflgqmtql nqllgevkdl
      241 lrqqvketsf lrntiaecqa cgplkfqspt pstvvapapp apptrpprrc dsnpcfrgvq
      301 ctdsrdgfqc gpcpegytgn gitcidvdec kyhpcypgvh cinlspgfrc dacpvgftgp
      361 mvqgvgisfa ksnkqvctdi decrngacvp nsicvntlgs yrcgpckpgy tgdqirgckv
      421 erncrnpeln pcsvnaqcie erqgdvtcvc gvgwagdgyi cgkdvdidsy pdeelpcsar
      481 nckkdnckyv pnsgqedadr dgigdacded adgdgilneq dncvlihnvd qrnsdkdifg
      541 dacdnclsvl nndqkdtdgd grgdacdddm dgdgiknild ncpkfpnrdq rdkdgdgvgd
      601 acdscpdvsn pnqsdvdndl vgdscdtnqd sdgdghqdst dncptvinsa qldtdkdgig
      661 decdddddnd gipdlvppgp dncrlvpnpa qedsnsdgvg dicesdfdqd qvidridvcp
      721 enaevtltdf rayqtvgldp egdaqidpnw vvlnqgmeiv qtmnsdpgla vgytafngvd
      781 fegtfhvntq tdddyagfif gyqdsssfyv vmwkqteqty wqatpfrava epgiqlkavk
      841 sktgpgehlr nslwhtgdts dqvrllwkds rnvgwkdkvs yrwflqhrpq vgyirvrfye
      901 gselvadsgv tidttmrggr lgvfcfsqen iiwsnlkyrc ndtipedfqe fqtqnfdrfd
      961 n
//



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1: NP_000079. alpha 1 type I co...[gi:4502945] Links  


LOCUS       COL1A1                  1464 aa            linear   PRI 27-AUG-2002
DEFINITION  alpha 1 type I collagen preproprotein; Collagen I, alpha-1
            polypeptide; osteogenesis imperfecta type IV; collagen of skin,
            tendon and bone, alpha-1 chain [Homo sapiens].
ACCESSION   NP_000079
VERSION     NP_000079.1  GI:4502945
DBSOURCE    REFSEQ: aaccession NM_000088.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1464)
  AUTHORS   Chu ML, Myers JC, Bernard MP, Ding JF and Ramirez F.
  TITLE     Cloning and characterization of five overlapping cDNAs specific for
            the human pro alpha 1(I) collagen chain
  JOURNAL   Nucleic Acids Res. 10 (19), 5925-5934 (1982)
  MEDLINE   83064528
   PUBMED   6183642
REFERENCE   2  (residues 1 to 1464)
  AUTHORS   Bernard,M.P., Chu,M.L., Myers,J.C., Ramirez,F., Eikenberry,E.F. and
            Prockop,D.J.
  TITLE     Nucleotide sequences of complementary deoxyribonucleic acids for
            the pro alpha 1 chain of human type I procollagen. Statistical
            evaluation of structures that are conserved during evolution
  JOURNAL   Biochemistry 22 (22), 5213-5223 (1983)
  MEDLINE   84080385
   PUBMED   6689127
REFERENCE   3  (residues 1 to 1464)
  AUTHORS   Chu,M.L., de Wet,W., Bernard,M. and Ramirez,F.
  TITLE     Fine structural analysis of the human pro-alpha 1 (I) collagen
            gene. Promoter structure, AluI repeats, and polymorphic transcripts
  JOURNAL   J. Biol. Chem. 260 (4), 2315-2320 (1985)
  MEDLINE   85130970
   PUBMED   2857713
REFERENCE   4  (residues 1 to 1464)
  AUTHORS   Retief,E., Parker,M.I. and Retief,A.E.
  TITLE     Regional chromosome mapping of human collagen genes alpha 2(I) and
            alpha 1(I) (COLIA2 and COLIA1)
  JOURNAL   Hum. Genet. 69 (4), 304-308 (1985)
  MEDLINE   85181198
   PUBMED   3857213
REFERENCE   5  (residues 1 to 1464)
  AUTHORS   Makela JK, Raassina M, Virta A and Vuorio E.
  TITLE     Human pro alpha 1(I) collagen: cDNA sequence for the C-propeptide
            domain
  JOURNAL   Nucleic Acids Res. 16 (1), 349 (1988)
  MEDLINE   88124208
   PUBMED   3340531
REFERENCE   6  (residues 1 to 1464)
  AUTHORS   D'Alessio,M., Bernard,M., Pretorius,P.J., de Wet,W., Ramirez,F. and
            Pretorious,P.J.
  TITLE     Complete nucleotide sequence of the region encompassing the first
            twenty-five exons of the human pro alpha 1(I) collagen gene
            (COL1A1)
  JOURNAL   Gene 67 (1), 105-115 (1988)
  MEDLINE   88329734
   PUBMED   2843432
REFERENCE   7  (residues 1 to 1464)
  AUTHORS   Tromp,G., Kuivaniemi,H., Stacey,A., Shikata,H., Baldwin,C.T.,
            Jaenisch,R. and Prockop,D.J.
  TITLE     Structure of a full-length cDNA clone for the prepro alpha 1(I)
            chain of human type I procollagen
  JOURNAL   Biochem. J. 253 (3), 919-922 (1988)
  MEDLINE   89025644
   PUBMED   3178743
REFERENCE   8  (residues 1 to 1464)
  AUTHORS   Willing,M.C., Cohn,D.H. and Byers,P.H.
  TITLE     Frameshift mutation near the 3' end of the COL1A1 gene of type I
            collagen predicts an elongated Pro alpha 1(I) chain and results in
            osteogenesis imperfecta type I
  JOURNAL   J. Clin. Invest. 85 (1), 282-290 (1990)
  MEDLINE   90110490
   PUBMED   2295701
REFERENCE   9  (residues 1 to 1464)
  AUTHORS   Maatta,A., Bornstein,P. and Penttinen,R.P.
  TITLE     Highly conserved sequences in the 3'-untranslated region of the
            COL1A1 gene bind cell-specific nuclear proteins
  JOURNAL   FEBS Lett. 279 (1), 9-13 (1991)
  MEDLINE   91138770
   PUBMED   1995349
REFERENCE   10 (residues 1 to 1464)
  AUTHORS   Tsuneyoshi,T., Westerhausen,A., Constantinou,C.D. and Prockop,D.J.
  TITLE     Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of
            type I procollagen in lethal osteogenesis imperfecta. The
            conformational strain on the triple helix introduced by a glycine
            substitution can be transmitted along the helix
  JOURNAL   J. Biol. Chem. 266 (24), 15608-15613 (1991)
  MEDLINE   91340689
   PUBMED   1874719
REFERENCE   11 (residues 1 to 1464)
  AUTHORS   Westerhausen,A., Constantinou,C.D., Pack,M., Peng,M.Z., Hanning,C.,
            Olsen,A.S. and Prockop,D.J.
  TITLE     Completion of the last half of the structure of the human gene for
            the Pro alpha 1 (I) chain of type I procollagen (COL1A1)
  JOURNAL   Matrix 11 (6), 375-379 (1991)
  MEDLINE   92157916
   PUBMED   1787829
REFERENCE   12 (residues 1 to 1464)
  AUTHORS   Nusgens,B.V., Verellen-Dumoulin,C., Hermanns-Le,T., De Paepe,A.,
            Nuytinck,L., Pierard,G.E. and Lapiere,C.M.
  TITLE     Evidence for a relationship between Ehlers-Danlos type VII C in
            humans and bovine dermatosparaxis
  JOURNAL   Nat. Genet. 1 (3), 214-217 (1992)
  MEDLINE   93265106
   PUBMED   1303238
REFERENCE   13 (residues 1 to 1464)
  AUTHORS   Grant,S.F., Reid,D.M., Blake,G., Herd,R., Fogelman,I. and
            Ralston,S.H.
  TITLE     Reduced bone density and osteoporosis associated with a polymorphic
            Sp1 binding site in the collagen type I alpha 1 gene
  JOURNAL   Nat. Genet. 14 (2), 203-205 (1996)
  MEDLINE   96438861
   PUBMED   8841196
REFERENCE   14 (residues 1 to 1464)
  AUTHORS   Dalgleish,R.
  TITLE     The human type I collagen mutation database
  JOURNAL   Nucleic Acids Res. 25 (1), 181-187 (1997)
  MEDLINE   97169389
   PUBMED   9016532
REFERENCE   15 (residues 1 to 1464)
  AUTHORS   Chambers,R.C., Dabbagh,K., McAnulty,R.J., Gray,A.J.,
            Blanc-Brude,O.P. and Laurent,G.J.
  TITLE     Thrombin stimulates fibroblast procollagen production via
            proteolytic activation of protease-activated receptor 1
  JOURNAL   Biochem. J. 333 (Pt 1), 121-127 (1998)
  MEDLINE   98306062
   PUBMED   9639571
REFERENCE   16 (residues 1 to 1464)
  AUTHORS   Pace,J.M., Kuslich,C.D., Willing,M.C. and Byers,P.H.
  TITLE     Disruption of one intra-chain disulphide bond in the
            carboxyl-terminal propeptide of the proalpha1(I) chain of type I
            procollagen permits slow assembly and secretion of overmodified,
            but stable procollagen trimers and results in mild osteogenesis
            imperfecta
  JOURNAL   J. Med. Genet. 38 (7), 443-449 (2001)
  MEDLINE   21326303
   PUBMED   11432962
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Z74615.1.
            Summary: This gene encodes the major component of type I collagen,
            the fibrillar collagen found in most connective tissues, and the
            only component of the collagen found in cartilage. Mutations in
            this gene are associated with osteogenesis imperfecta,
            Ehlers-Danlos syndrome, and idiopathic osteoporosis. Reciprocal
            translocations between chromosomes 17 and 22, where this gene and
            the gene for platelet-derived growth factor beta are located, are
            associated with a particular type of skin tumor called
            dermatofibrosarcoma protuberans, resulting from unregulated
            expression of the growth factor. Two transcripts, resulting from
            the use of alternate polyadenylation signals, have been identified
            for this gene.
FEATURES             Location/Qualifiers
     source          1..1464
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q21.3-q22.1"
     Protein         1..1464
                     /product="alpha 1 type I collagen preproprotein"
                     /note="Collagen I, alpha-1 polypeptide; osteogenesis
                     imperfecta type IV; collagen of skin, tendon and bone,
                     alpha-1 chain"
     sig_peptide     1..22
     Region          23..1464
                     /region_name="alpha one type I collagen proprotein"
     Region          40..95
                     /region_name="pfam00093, vwc, von Willebrand factor type C
                     domain. The high cutoff was used to prevent overlap with
                     pfam00094"
     Region          40..95
                     /region_name="smart00214, VWC, von Willebrand factor (vWF)
                     type C domain"
     mat_peptide     179..1218
                     /product="alpha 1 type I collagen"
     Region          1230..1464
                     /region_name="smart00038, COLFI, Fibrillar collagens
                     C-terminal domain; Found at C-termini of fibrillar
                     collagens: Ephydatia muelleri procollagen EMF1alpha,
                     vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V
                     etc"
     Region          1245..1463
                     /region_name="pfam01410, COLFI, Fibrillar collagen
                     C-terminal domain. Found at C-termini of fibrillar
                     collagens: Ephydatia muelleri procollagen EMF1 alpha,
                     vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V
                     etc"
     CDS             1..1464
                     /gene="COL1A1"
                     /coded_by="NM_000088.2:120..4514"
                     /db_xref="LocusID:1277"
                     /db_xref="MIM:120150"
ORIGIN      
        1 mfsfvdlrll lllaatallt hgqeegqveg qdedippitc vqnglryhdr dvwkpepcri
       61 cvcdngkvlc ddvicdetkn cpgaevpege ccpvcpdgse sptdqettgv egpkgdtgpr
      121 gprgpagppg rdgipgqpgl pgppgppgpp gppglggnfa pqlsygydek stggisvpgp
      181 mgpsgprglp gppgapgpqg fqgppgepge pgasgpmgpr gppgppgkng ddgeagkpgr
      241 pgergppgpq garglpgtag lpgmkghrgf sgldgakgda gpagpkgepg spgengapgq
      301 mgprglpger grpgapgpag argndgatga agppgptgpa gppgfpgavg akgeagpqgp
      361 rgsegpqgvr gepgppgpag aagpagnpga dgqpgakgan gapgiagapg fpgargpsgp
      421 qgpggppgpk gnsgepgapg skgdtgakge pgpvgvqgpp gpageegkrg argepgptgl
      481 pgppgerggp gsrgfpgadg vagpkgpage rgspgpagpk gspgeagrpg eaglpgakgl
      541 tgspgspgpd gktgppgpag qdgrpgppgp pgargqagvm gfpgpkgaag epgkagergv
      601 pgppgavgpa gkdgeagaqg ppgpagpage rgeqgpagsp gfqglpgpag ppgeagkpge
      661 qgvpgdlgap gpsgargerg fpgergvqgp pgpagprgan gapgndgakg dagapgapgs
      721 qgapglqgmp gergaaglpg pkgdrgdagp kgadgspgkd gvrgltgpig ppgpagapgd
      781 kgesgpsgpa gptgargapg drgepgppgp agfagppgad gqpgakgepg dagakgdagp
      841 pgpagpagpp gpignvgapg akgargsagp pgatgfpgaa grvgppgpsg nagppgppgp
      901 agkeggkgpr getgpagrpg evgppgppgp agekgspgad gpagapgtpg pqgiagqrgv
      961 vglpgqrger gfpglpgpsg epgkqgpsga sgergppgpm gppglagppg esgregapaa
     1021 egspgrdgsp gakgdrgetg pagppgapga pgapgpvgpa gksgdrgetg pagpagpvgp
     1081 vgargpagpq gprgdkgetg eqgdrgikgh rgfsglqgpp gppgspgeqg psgasgpagp
     1141 rgppgsagap gkdglnglpg pigppgprgr tgdagpvgpp gppgppgppg ppsagfdfsf
     1201 lpqppqekah dggryyradd anvvrdrdle vdttlkslsq qienirspeg srknpartcr
     1261 dlkmchsdwk sgeywidpnq gcnldaikvf cnmetgetcv yptqpsvaqk nwyisknpkd
     1321 krhvwfgesm tdgfqfeygg qgsdpadvai qltflrlmst easqnityhc knsvaymdqq
     1381 tgnlkkalll kgsneieira egnsrftysv tvdgctshtg awgktvieyk ttkssrlpii
     1441 dvapldvgap dqefgfdvgp vcfl
//



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1: NP_002336. lumican [Homo sap...[gi:4505047] Links  


LOCUS       LUM                      338 aa            linear   PRI 09-JUN-2002
DEFINITION  lumican [Homo sapiens].
ACCESSION   NP_002336
VERSION     NP_002336.1  GI:4505047
DBSOURCE    REFSEQ: aaccession NM_002345.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 338)
  AUTHORS   Strausberg,R.
  TITLE     Homo sapiens lumican (LUM), mRNA
  JOURNAL   Unpublished (2001)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC007038.1.
FEATURES             Location/Qualifiers
     source          1..338
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q21.3-q22"
                     /clone="MGC:12410 IMAGE:3950745"
                     /tissue_type="Prostate"
                     /clone_lib="NIH_MGC_83"
                     /lab_host="DH10B"
                     /note="Vector: pDNR-LIB"
     Protein         1..338
                     /product="lumican"
     Region          37..71
                     /region_name="Leucine rich repeat N-terminal domain"
                     /note="LRRNT"
                     /db_xref="CDD:smart00013"
     Region          37..66
                     /region_name="Leucine rich repeat N-terminal domain"
                     /note="LRRNT"
                     /db_xref="CDD:pfam01462"
     variation       313
                     /allele="C"
                     /allele="G"
                     /db_xref="dbSNP:1802743"
     CDS             1..338
                     /gene="LUM"
                     /coded_by="NM_002345.2:142..1158"
                     /db_xref="LocusID:4060"
                     /db_xref="MIM:600616"
ORIGIN      
        1 mslsaftlfl aliggtsgqy ydydfplsiy gqsspncape cncpesypsa mycdelklks
       61 vpmvppgiky lylrnnqidh idekafenvt dlqwlildhn llenskikgr vfsklkqlkk
      121 lhinhnnlte svgplpksle dlqlthnkit klgsfeglvn ltfihlqhnr lkedavsaaf
      181 kglksleyld lsfnqiarlp sglpvslltl yldnnkisni pdeyfkrfna lqylrlshne
      241 ladsgipgns fnvsslveld lsynklknip tvnenlenyy levnqlekfd iksfckilgp
      301 lsyskikhlr ldgnrisets lppdmyeclr vanevtln
//



Revised: July 5, 2002.
 
 


Disclaimer | Write to the Help Desk
NCBI | NLM | NIH 

 

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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_000081. alpha 1 type III ...[gi:4502951] Links  


LOCUS       COL3A1                  1466 aa            linear   PRI 27-AUG-2002
DEFINITION  alpha 1 type III collagen preproprotein; collagen, fetal [Homo
            sapiens].
ACCESSION   NP_000081
VERSION     NP_000081.1  GI:4502951
DBSOURCE    REFSEQ: aaccession NM_000090.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1466)
  AUTHORS   Loidl,H.R., Brinker,J.M., May,M., Pihlajaniemi,T., Morrow,S.,
            Rosenbloom,J. and Myers,J.C.
  TITLE     Molecular cloning and carboxyl-propeptide analysis of human type
            III procollagen
  JOURNAL   Nucleic Acids Res. 12 (24), 9383-9394 (1984)
  MEDLINE   85087944
   PUBMED   6096827
REFERENCE   2  (residues 1 to 1466)
  AUTHORS   Emanuel,B.S., Cannizzaro,L.A., Seyer,J.M. and Myers,J.C.
  TITLE     Human alpha 1(III) and alpha 2(V) procollagen genes are located on
            the long arm of chromosome 2
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 82 (10), 3385-3389 (1985)
  MEDLINE   85216505
   PUBMED   3858826
REFERENCE   3  (residues 1 to 1466)
  AUTHORS   Miskulin,M., Dalgleish,R., Kluve-Beckerman,B., Rennard,S.I.,
            Tolstoshev,P., Brantly,M. and Crystal,R.G.
  TITLE     Human type III collagen gene expression is coordinately modulated
            with the type I collagen genes during fibroblast growth
  JOURNAL   Biochemistry 25 (6), 1408-1413 (1986)
  MEDLINE   86187804
   PUBMED   3754462
REFERENCE   4  (residues 1 to 1466)
  AUTHORS   Mankoo,B.S. and Dalgleish,R.
  TITLE     Human pro alpha 1(III) collagen: cDNA sequence for the 3' end
  JOURNAL   Nucleic Acids Res. 16 (5), 2337 (1988)
  MEDLINE   88189827
   PUBMED   3357782
REFERENCE   5  (residues 1 to 1466)
  AUTHORS   Toman,P.D., Ricca,G.A. and de Crombrugghe,B.
  TITLE     Nucleotide sequence of a cDNA coding for the amino-terminal region
            of human prepro alpha 1(III) collagen
  JOURNAL   Nucleic Acids Res. 16 (14B), 7201 (1988)
  MEDLINE   88303360
   PUBMED   3405773
REFERENCE   6  (residues 1 to 1466)
  AUTHORS   Molyneux,K. and Dalgleish,R.
  TITLE     Human type III collagen 'variant' is a cDNA cloning artefact
  JOURNAL   Nucleic Acids Res. 16 (24), 11833 (1988)
  MEDLINE   89098346
   PUBMED   3211760
REFERENCE   7  (residues 1 to 1466)
  AUTHORS   Ala-Kokko,L., Kontusaari,S., Baldwin,C.T., Kuivaniemi,H. and
            Prockop,D.J.
  TITLE     Structure of cDNA clones coding for the entire prepro alpha 1 (III)
            chain of human type III procollagen. Differences in protein
            structure from type I procollagen and conservation of codon
            preferences
  JOURNAL   Biochem. J. 260 (2), 509-516 (1989)
  MEDLINE   89350838
   PUBMED   2764886
REFERENCE   8  (residues 1 to 1466)
  AUTHORS   Janeczko,R.A. and Ramirez,F.
  TITLE     Nucleotide and amino acid sequences of the entire human alpha 1
            (III) collagen
  JOURNAL   Nucleic Acids Res. 17 (16), 6742 (1989)
  MEDLINE   89386015
   PUBMED   2780304
REFERENCE   9  (residues 1 to 1466)
  AUTHORS   Cutting,G.R., McGinniss,M.J., Kasch,L.M., Tsipouras,P. and
            Antonarakis,S.E.
  TITLE     Physical mapping by PFGE localizes the COL3A1 and COL5A2 genes to a
            35-kb region on human chromosome 2
  JOURNAL   Genomics 8 (2), 407-410 (1990)
  MEDLINE   91065664
   PUBMED   1979060
REFERENCE   10 (residues 1 to 1466)
  AUTHORS   Cole,W.G., Chiodo,A.A., Lamande,S.R., Janeczko,R., Ramirez,F.,
            Dahl,H.H., Chan,D. and Bateman,J.F.
  TITLE     A base substitution at a splice site in the COL3A1 gene causes exon
            skipping and generates abnormal type III procollagen in a patient
            with Ehlers-Danlos syndrome type IV
  JOURNAL   J. Biol. Chem. 265 (28), 17070-17077 (1990)
  MEDLINE   91009133
   PUBMED   2145268
REFERENCE   11 (residues 1 to 1466)
  AUTHORS   Chiodo,A.A., Sillence,D.O., Cole,W.G. and Bateman,J.F.
  TITLE     Abnormal type III collagen produced by an exon-17-skipping mutation
            of the COL3A1 gene in Ehlers-Danlos syndrome type IV is not
            incorporated into the extracellular matrix
  JOURNAL   Biochem. J. 311 (Pt 3), 939-943 (1995)
  MEDLINE   96067614
   PUBMED   7487954
REFERENCE   12 (residues 1 to 1466)
  AUTHORS   Limongi,M.Z., Pelliccia,F. and Rocchi,A.
  TITLE     Assignment of the human nebulin gene (NEB) to chromosome band
            2q24.2 and the alpha 1 (III) collagen gene (COL3A1) to chromosome
            band 2q32.2 by in situ hybridization; the FRA2G common fragile site
            lies between the two genes in the 2q31 band
  JOURNAL   Cytogenet. Cell Genet. 77 (3-4), 259-260 (1997)
  MEDLINE   97430831
   PUBMED   9284930
REFERENCE   13 (residues 1 to 1466)
  AUTHORS   Schwarze,U., Schievink,W.I., Petty,E., Jaff,M.R.,
            Babovic-Vuksanovic,D., Cherry,K.J., Pepin,M. and Byers,P.H.
  TITLE     Haploinsufficiency for one COL3A1 allele of type III procollagen
            results in a phenotype similar to the vascular form of
            Ehlers-Danlos syndrome, Ehlers-Danlos syndrome type IV
  JOURNAL   Am. J. Hum. Genet. 69 (5), 989-1001 (2001)
  MEDLINE   21473749
   PUBMED   11577371
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X14420.1, AI755052.1 and
            M26939.1.
            Summary: This gene encodes a fibrillar collagen that is found in
            extensible connective tissues such as skin, lung, and the vascular
            system, frequently in association with type I collagen. Mutations
            in this gene are associated with Ehlers-Danlos syndrome type IV,
            and with aortic and arterial aneurysms. Although alternate
            transcripts have been detected for this gene, they are the result
            of mutations; these mutations alter splicing, often leading to the
            exclusion of multiple exons.
FEATURES             Location/Qualifiers
     source          1..1466
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q31"
     Protein         1..1466
                     /product="alpha 1 type III collagen"
                     /note="Collagen III, alpha-1 polypeptide; collagen, fetal"
     Proprotein      1..1466
                     /note="collagen, fetal"
     sig_peptide     1..23
     Proprotein      24..1466
     Region          32..88
                     /region_name="pfam00093, vwc, von Willebrand factor type C
                     domain. The high cutoff was used to prevent overlap with
                     pfam00094"
     Region          32..88
                     /region_name="smart00214, VWC, von Willebrand factor (vWF)
                     type C domain"
     mat_peptide     149..1205
                     /product="alpha 1 type III collagen"
     Region          1231..1466
                     /region_name="smart00038, COLFI, Fibrillar collagens
                     C-terminal domain; Found at C-termini of fibrillar
                     collagens: Ephydatia muelleri procollagen EMF1alpha,
                     vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V
                     etc"
     Region          1248..1465
                     /region_name="pfam01410, COLFI, Fibrillar collagen
                     C-terminal domain. Found at C-termini of fibrillar
                     collagens: Ephydatia muelleri procollagen EMF1 alpha,
                     vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V
                     etc"
     CDS             1..1466
                     /gene="COL3A1"
                     /coded_by="NM_000090.2:118..4518"
                     /db_xref="LocusID:1281"
                     /db_xref="MIM:120180"
ORIGIN      
        1 mmsfvqkgsw lllallhpti ilaqqeaveg gcshlgqsya drdvwkpepc qicvcdsgsv
       61 lcddiicddq eldcpnpeip fgeccavcpq pptaptrppn gqgpqgpkgd pgppgipgrn
      121 gdpgipgqpg spgspgppgi cescptgpqn yspqydsydv ksgvavggla gypgpagppg
      181 ppgppgtsgh pgspgspgyq gppgepgqag psgppgppga igpsgpagkd gesgrpgrpg
      241 erglpgppgi kgpagipgfp gmkghrgfdg rngekgetga pglkgenglp gengapgpmg
      301 prgapgergr pglpgaagar gndgargsdg qpgppgppgt agfpgspgak gevgpagspg
      361 sngapgqrge pgpqghagaq gppgppging spggkgemgp agipgapglm gargppgpag
      421 angapglrgg agepgkngak gepgprgerg eagipgvpga kgedgkdgsp gepganglpg
      481 aagergapgf rgpagpngip gekgpagerg apgpagprga agepgrdgvp ggpgmrgmpg
      541 spggpgsdgk pgppgsqges grpgppgpsg prgqpgvmgf pgpkgndgap gkngerggpg
      601 gpgpqgppgk ngetgpqgpp gptgpggdkg dtgppgpqgl qglpgtggpp gengkpgepg
      661 pkgdagapga pggkgdagap gergppglag apglrggagp pgpeggkgaa gppgppgaag
      721 tpglqgmpge rgglgspgpk gdkgepggpg adgvpgkdgp rgptgpigpp gpagqpgdkg
      781 eggapglpgi agprgspger getgppgpag fpgapgqnge pggkgergap gekgeggppg
      841 vagppggsgp agppgpqgvk gergspggpg aagfpgargl pgppgsngnp gppgpsgspg
      901 kdgppgpagn tgapgspgvs gpkgdagqpg ekgspgaqgp pgapgplgia gitgarglag
      961 ppgmpgprgs pgpqgvkges gkpganglsg ergppgpqgl pglagtagep grdgnpgsdg
     1021 lpgrdgspgg kgdrgengsp gapgapghpg ppgpvgpagk sgdrgesgpa gpagapgpag
     1081 srgapgpqgp rgdkgetger gaagikghrg fpgnpgapgs pgpagqqgai gspgpagprg
     1141 pvgpsgppgk dgtsghpgpi gppgprgnrg ergsegspgh pgqpgppgpp gapgpccggv
     1201 gaaaiagigg ekaggfapyy gdepmdfkin tdeimtslks vngqieslis pdgsrknpar
     1261 ncrdlkfchp elksgeywvd pnqgckldai kvfcnmetge tcisanplnv prkhwwtdss
     1321 aekkhvwfge smdggfqfsy gnpelpedvl dvqlaflrll ssrasqnity hcknsiaymd
     1381 qasgnvkkal klmgsnegef kaegnskfty tvledgctkh tgewsktvfe yrtrkavrlp
     1441 ivdiapydig gpdqefgvdv gpvcfl
//



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1: NP_009201. FK506 binding pro...[gi:24307927] Links  


LOCUS       FKBP9                    142 aa            linear   PRI 24-OCT-2002
DEFINITION  FK506 binding protein 9, 63 kDa; FK506-binding protein 9 (63 kD);
            FK506 binding protein 9 (63 kD) [Homo sapiens].
ACCESSION   NP_009201
VERSION     NP_009201.1  GI:24307927
DBSOURCE    REFSEQ: aaccession NM_007270.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 142)
  AUTHORS   Patterson,C.E., Gao,J., Rooney,A.P. and Davis,E.C.
  TITLE     Genomic organization of mouse and human 65 kDa FK506-binding
            protein genes and evolution of the FKBP multigene family
  JOURNAL   Genomics 79 (6), 881-889 (2002)
  MEDLINE   22032991
   PUBMED   12036304
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC011872.1.
FEATURES             Location/Qualifiers
     source          1..142
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p11.1"
                     /clone="MGC:20531 IMAGE:3028515"
                     /tissue_type="Muscle, rhabdomyosarcoma"
                     /clone_lib="NIH_MGC_17"
                     /lab_host="DH10B-R"
                     /note="Vector: pOTB7"
     Protein         1..142
                     /product="FK506 binding protein 9, 63 kDa"
                     /note="FK506-binding protein 9 (63 kD); FK506 binding
                     protein 9 (63 kD)"
     Region          4..46
                     /region_name="FKBP-type peptidyl-prolyl cis-trans
                     isomerase"
                     /note="FKBP"
                     /db_xref="CDD:pfam00254"
     CDS             1..142
                     /gene="FKBP9"
                     /coded_by="NM_007270.1:457..885"
                     /db_xref="LocusID:11328"
ORIGIN      
        1 mdmglremcv gekrtviipp hlgygeagvd gevpgsavlv fdiellelva glpegymfiw
       61 ngevspnlfe eidkdgngev lleefseyih aqvasgkgkl apgfdaeliv knmftnqdrn
      121 gdgkvtaeef klkdqeakqd el
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_000465. twist; TWIST, dro...[gi:4507741] Links  


LOCUS       TWIST                    202 aa            linear   PRI 27-AUG-2002
DEFINITION  twist; TWIST, drosophila, homolog of; acrocephalosyndactyly 3
            (Saethre-Chotzen syndrome); Blepharophimosis, epicanthus inversus,
            and ptosis 2; Blepharophimosis, epicanthus inversus, and ptosis 3;
            blepharophimosis, epicanthus inversus and ptosis 3 [Homo sapiens].
ACCESSION   NP_000465
VERSION     NP_000465.1  GI:4507741
DBSOURCE    REFSEQ: aaccession NM_000474.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 202)
  AUTHORS   Bianchi,D.W., Cirillo-Silengo,M., Luzzatti,L. and Greenstein,R.M.
  TITLE     Interstitial deletion of the short arm of chromosome 7 without
            craniosynostosis
  JOURNAL   Clin. Genet. 19 (6), 456-461 (1981)
  MEDLINE   82049227
   PUBMED   7296937
REFERENCE   2  (residues 1 to 202)
  AUTHORS   Brueton,L.A., van Herwerden,L., Chotai,K.A. and Winter,R.M.
  TITLE     The mapping of a gene for craniosynostosis: evidence for linkage of
            the Saethre-Chotzen syndrome to distal chromosome 7p
  JOURNAL   J. Med. Genet. 29 (10), 681-685 (1992)
  MEDLINE   93059268
   PUBMED   1433226
REFERENCE   3  (residues 1 to 202)
  AUTHORS   Rose,C.S., King,A.A., Summers,D., Palmer,R., Yang,S., Wilkie,A.O.,
            Reardon,W., Malcolm,S. and Winter,R.M.
  TITLE     Localization of the genetic locus for Saethre-Chotzen syndrome to a
            6 cM region of chromosome 7 using four cases with apparently
            balanced translocations at 7p21.2
  JOURNAL   Hum. Mol. Genet. 3 (8), 1405-1408 (1994)
  MEDLINE   95078849
   PUBMED   7987323
REFERENCE   4  (residues 1 to 202)
  AUTHORS   Maw,M., Kar,B., Biswas,J., Biswas,P., Nancarrow,D., Bridges,R.,
            Kumaramanickavel,G., Denton,M. and Badrinath,S.S.
  TITLE     Linkage of blepharophimosis syndrome in a large Indian pedigree to
            chromosome 7p
  JOURNAL   Hum. Mol. Genet. 5 (12), 2049-2054 (1996)
  MEDLINE   97123515
   PUBMED   8968762
REFERENCE   5  (residues 1 to 202)
  AUTHORS   Bourgeois,P., Stoetzel,C., Bolcato-Bellemin,A.L., Mattei,M.G. and
            Perrin-Schmitt,F.
  TITLE     The human H-twist gene is located at 7p21 and encodes a B-HLH
            protein that is 96% similar to its murine M-twist counterpart
  JOURNAL   Mamm. Genome 7 (12), 915-917 (1996)
  MEDLINE   97148940
   PUBMED   8995765
REFERENCE   6  (residues 1 to 202)
  AUTHORS   Howard,T.D., Paznekas,W.A., Green,E.D., Chiang,L.C., Ma,N., Ortiz
            de Luna,R.I., Garcia Delgado,C., Gonzalez-Ramos,M., Kline,A.D. and
            Jabs,E.W.
  TITLE     Mutations in TWIST, a basic helix-loop-helix transcription factor,
            in Saethre-Chotzen syndrome
  JOURNAL   Nat. Genet. 15 (1), 36-41 (1997)
  MEDLINE   97141916
   PUBMED   8988166
REFERENCE   7  (residues 1 to 202)
  AUTHORS   el Ghouzzi,V., Le Merrer,M., Perrin-Schmitt,F., Lajeunie,E.,
            Benit,P., Renier,D., Bourgeois,P., Bolcato-Bellemin,A.L.,
            Munnich,A. and Bonaventure,J.
  TITLE     Mutations of the TWIST gene in the Saethre-Chotzen syndrome
  JOURNAL   Nat. Genet. 15 (1), 42-46 (1997)
  MEDLINE   97141917
   PUBMED   8988167
REFERENCE   8  (residues 1 to 202)
  AUTHORS   Wang,S.M., Coljee,V.W., Pignolo,R.J., Rotenberg,M.O.,
            Cristofalo,V.J. and Sierra,F.
  TITLE     Cloning of the human twist gene: its expression is retained in
            adult mesodermally-derived tissues
  JOURNAL   Gene 187 (1), 83-92 (1997)
  MEDLINE   97225800
   PUBMED   9073070
REFERENCE   9  (residues 1 to 202)
  AUTHORS   Krebs,I., Weis,I., Hudler,M., Rommens,J.M., Roth,H., Scherer,S.W.,
            Tsui,L.C., Fuchtbauer,E.M., Grzeschik,K.H., Tsuji,K. and Kunz,J.
  TITLE     Translocation breakpoint maps 5 kb 3' from TWIST in a patient
            affected with Saethre-Chotzen syndrome
  JOURNAL   Hum. Mol. Genet. 6 (7), 1079-1086 (1997)
  MEDLINE   97358582
   PUBMED   9215678
REFERENCE   10 (residues 1 to 202)
  AUTHORS   Hamamori,Y., Sartorelli,V., Ogryzko,V., Puri,P.L., Wu,H.Y.,
            Wang,J.Y., Nakatani,Y. and Kedes,L.
  TITLE     Regulation of histone acetyltransferases p300 and PCAF by the bHLH
            protein twist and adenoviral oncoprotein E1A
  JOURNAL   Cell 96 (3), 405-413 (1999)
  MEDLINE   99148273
   PUBMED   10025406
REFERENCE   11 (residues 1 to 202)
  AUTHORS   Lee,M.S., Lowe,G., Flanagan,S., Kuchler,K. and Glackin,C.A.
  TITLE     Human Dermo-1 has attributes similar to twist in early bone
            development
  JOURNAL   Bone 27 (5), 591-602 (2000)
  MEDLINE   20517301
   PUBMED   11062344
REFERENCE   12 (residues 1 to 202)
  AUTHORS   Dollfus,H., Kumaramanickavel,G., Biswas,P., Stoetzel,C.,
            Quillet,R., Denton,M., Maw,M. and Perrin-Schmitt,F.
  TITLE     Identification of a new TWIST mutation (7p21) with variable eyelid
            manifestations supports locus homogeneity of BPES at 3q22
  JOURNAL   J. Med. Genet. 38 (7), 470-472 (2001)
  MEDLINE   21367233
   PUBMED   11474656
REFERENCE   13 (residues 1 to 202)
  AUTHORS   Dollfus,H., Biswas,P., Kumaramanickavel,G., Stoetzel,C.,
            Quillet,R., Biswas,J., Lajeunie,E., Renier,D. and Perrin-Schmitt,F.
  TITLE     Saethre-Chotzen syndrome: notable intrafamilial phenotypic
            variability in a large family with Q28X TWIST mutation
  JOURNAL   Am. J. Med. Genet. 109 (3), 218-225 (2002)
  MEDLINE   22020455
   PUBMED   11977182
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U80998.1 and X99268.1.
            Summary: Basic helix-loop-helix (bHLH) transcription factors have
            been implicated in cell lineage determination and differentiation.
            The protein encoded by this gene is a bHLH transcription factor and
            shares similarity with another bHLH transcription factor, Dermo1.
            The strongest expression of this mRNA is in placental tissue; in
            adults, mesodermally derived tissues express this mRNA
            preferentially. Mutations in this gene have been found in patients
            with Saethre-Chotzen syndrome.
FEATURES             Location/Qualifiers
     source          1..202
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7p21.2"
     Protein         1..202
                     /product="twist"
                     /note="TWIST, drosophila, homolog of;
                     acrocephalosyndactyly 3 (Saethre-Chotzen syndrome);
                     Blepharophimosis, epicanthus inversus, and ptosis 2;
                     Blepharophimosis, epicanthus inversus, and ptosis 3;
                     blepharophimosis, epicanthus inversus and ptosis 3"
     variation       31
                     /allele="S"
                     /allele="G"
                     /db_xref="dbSNP:1800126"
     variation       41
                     /allele="R"
                     /allele="S"
                     /db_xref="dbSNP:2522203"
     variation       41
                     /allele="S"
                     /allele="T"
                     /db_xref="dbSNP:2522204"
     variation       45
                     /allele="R"
                     /allele="S"
                     /db_xref="dbSNP:2522201"
     variation       45
                     /allele="S"
                     /allele="T"
                     /db_xref="dbSNP:2522202"
     Region          109..159
                     /region_name="pfam00010, HLH, Helix-loop-helix DNA-binding
                     domain"
     Region          114..165
                     /region_name="smart00353, HLH, helix loop helix domain"
     CDS             1..202
                     /gene="TWIST"
                     /coded_by="NM_000474.2:82..690"
                     /db_xref="LocusID:7291"
                     /db_xref="MIM:601622"
ORIGIN      
        1 mmqdvssspv spaddslsns eeepdrqqpp sgkrggrkrr ssrrsaggga gpggaagggv
       61 gggdepgspa qgkrgkksag cgggggaggg ggsssgggsp qsyeelqtqr vmanvrerqr
      121 tqslneafaa lrkiiptlps dklskiqtlk laaryidfly qvlqsdelds kmascsyvah
      181 erlsyafsvw rmegawsmsa sh
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_001845. alpha 1 type XI c...[gi:18375518] Links  


LOCUS       COL11A1                 1806 aa            linear   PRI 25-JAN-2002
DEFINITION  alpha 1 type XI collagen, isoform A preproprotein; collagen XI,
            alpha-1 polypeptide [Homo sapiens].
ACCESSION   NP_001845
VERSION     NP_001845.2  GI:18375518
DBSOURCE    REFSEQ: aaccession NM_001854.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1806)
  AUTHORS   Bernard,M., Yoshioka,H., Rodriguez,E., Van der Rest,M., Kimura,T.,
            Ninomiya,Y., Olsen,B.R. and Ramirez,F.
  TITLE     Cloning and sequencing of pro-alpha 1 (XI) collagen cDNA
            demonstrates that type XI belongs to the fibrillar class of
            collagens and reveals that the expression of the gene is not
            restricted to cartilagenous tissue
  JOURNAL   J. Biol. Chem. 263 (32), 17159-17166 (1988)
  MEDLINE   89034222
   PUBMED   3182841
REFERENCE   2  (residues 1 to 1806)
  AUTHORS   Yoshioka,H., Greenwel,P., Inoguchi,K., Truter,S., Inagaki,Y.,
            Ninomiya,Y. and Ramirez,F.
  TITLE     Structural and functional analysis of the promoter of the human
            alpha 1(XI) collagen gene
  JOURNAL   J. Biol. Chem. 270 (1), 418-424 (1995)
  MEDLINE   95113862
   PUBMED   7814404
REFERENCE   3  (residues 1 to 1806)
  AUTHORS   Zhidkova,N.I., Justice,S.K. and Mayne,R.
  TITLE     Alternative mRNA processing occurs in the variable region of the
            pro-alpha 1(XI) and pro-alpha 2(XI) collagen chains
  JOURNAL   J. Biol. Chem. 270 (16), 9486-9493 (1995)
  MEDLINE   95238468
   PUBMED   7721876
REFERENCE   4  (residues 1 to 1806)
  AUTHORS   Richards,A.J., Yates,J.R., Williams,R., Payne,S.J., Pope,F.M.,
            Scott,J.D. and Snead,M.P.
  TITLE     A family with Stickler syndrome type 2 has a mutation in the
            COL11A1 gene resulting in the substitution of glycine 97 by valine
            in alpha 1 (XI) collagen
  JOURNAL   Hum. Mol. Genet. 5 (9), 1339-1343 (1996)
  MEDLINE   97026296
   PUBMED   8872475
REFERENCE   5  (residues 1 to 1806)
  AUTHORS   Annunen,S., Korkko,J., Czarny,M., Warman,M.L., Brunner,H.G.,
            Kaariainen,H., Mulliken,J.B., Tranebjaerg,L., Brooks,D.G.,
            Cox,G.F., Cruysberg,J.R., Curtis,M.A., Davenport,S.L.,
            Friedrich,C.A., Kaitila,I., Krawczynski,M.R., Latos-Bielenska,A.,
            Mukai,S., Olsen,B.R., Shinno,N., Somer,M., Vikkula,M.,
            Zlotogora,J., Prockop,D.J. and Ala-Kokko,L.
  TITLE     Splicing mutations of 54-bp exons in the COL11A1 gene cause
            Marshall syndrome, but other mutations cause overlapping
            Marshall/Stickler phenotypes
  JOURNAL   Am. J. Hum. Genet. 65 (4), 974-983 (1999)
  MEDLINE   20455728
   PUBMED   10486316
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from J04177.1, U12139.1 and
            AU118365.1.
            On Jan 25, 2002 this sequence version replaced gi:4502939.
            Summary: This gene encodes one of the two alpha chains of type XI
            collagen, a minor fibrillar collagen. Type XI collagen is a
            heterotrimer but the third alpha chain is a post-translationally
            modified alpha 1 type II chain. Mutations in this gene are
            associated with type II Stickler syndrome and with Marshall
            syndrome. Three transcript variants encoding different isoforms
            have been identified for this gene.
            Transcript Variant: This variant (A) utilizes alternate exon 6,
            designated exon 6A. The encoded isoform (A) has a 39 aa region
            specified by exon 6A, that differs from the corresponding 51 aa
            region encoded by exon 6B in isoform B.
FEATURES             Location/Qualifiers
     source          1..1806
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p21"
     Protein         1..1806
                     /product="alpha 1 type XI collagen, isoform A
                     preproprotein"
                     /note="isoform A is encoded by transcript variant A;
                     collagen XI, alpha-1 polypeptide"
     sig_peptide     1..36
     Proprotein      37..1806
     Region          38..229
                     /region_name="Thrombospondin N-terminal -like domain"
                     /note="TSPN"
                     /db_xref="CDD:pfam02210"
     Region          38..229
                     /region_name="Thrombospondin N-terminal -like domains."
                     /note="TSPN"
                     /db_xref="CDD:smart00210"
     Region          98..227
                     /region_name="Laminin G domain"
                     /note="LamG"
                     /db_xref="CDD:smart00282"
     mat_peptide     512..1563
                     /product="alpha 1 type XI collagen, isoform A"
     Region          765..821
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          766..825
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          769..827
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          772..831
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          775..833
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          781..840
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          784..843
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          787..846
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          790..847
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          793..851
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          796..853
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          799..856
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          802..859
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          805..864
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          808..866
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          811..870
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          814..871
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          826..873
                     /region_name="Collagen triple helix repeat (20 copies)"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          1576..1805
                     /region_name="Fibrillar collagens C-terminal domain"
                     /note="COLFI"
                     /db_xref="CDD:smart00038"
     Region          1593..1804
                     /region_name="Fibrillar collagen C-terminal domain"
                     /note="COLFI"
                     /db_xref="CDD:pfam01410"
     CDS             1..1806
                     /gene="COL11A1"
                     /coded_by="NM_001854.2:319..5739"
                     /db_xref="LocusID:1301"
                     /db_xref="MIM:120280"
                     /db_xref="LocusID:1301"
                     /db_xref="MIM:120280"
ORIGIN      
        1 mepwssrwkt krwlwdftvt tlaltflfqa revrgaapvd vlkaldfhns pegiskttgf
       61 ctnrknskgs dtayrvskqa qlsaptkqlf pggtfpedfs ilftvkpkkg iqsfllsiyn
      121 ehgiqqigve vgrspvflfe dhtgkpaped yplfrtvnia dgkwhrvais vekktvtmiv
      181 dckkkttkpl drseraivdt ngitvfgtri ldeevfegdi qqflitgdpk aaydycehys
      241 pdcdssapka aqaqepqide yapediieyd yeygeaeyke aesvtegptv teetiaqtea
      301 nivddfqeyn ygtmesyqte aprhvsgtne pnpveeifte eyltgedyds qrknsedtly
      361 enkeidgrds dllvdgdlge ydfyeykeye dkptsppnee fgpgvpaetd itetsinghg
      421 aygekgqkge pavvepgmlv egppgpagpa gimgppglqg ptgppgdpgd rgppgrpglp
      481 gadglpgppg tmlmlpfryg gdgskgptis aqeaqaqail qqarialrgp pgpmgltgrp
      541 gpvggpgssg akgesgdpgp qgprgvqgpp gptgkpgkrg rpgadggrgm pgepgakgdr
      601 gfdglpglpg dkghrgergp qgppgppgdd gmrgedgeig prglpgeagp rgllgprgtp
      661 gapgqpgmag vdgppgpkgn mgpqgepgpp gqqgnpgpqg lpgpqgpigp pgekgpqgkp
      721 glaglpgadg ppghpgkegq sgekgalgpp gpqgpigypg prgvkgadgv rglkgskgek
      781 gedgfpgfkg dmglkgdrge vgqigprged gpegpkgrag ptgdpgpsgq agekgklgvp
      841 glpgypgrqg pkgstgfpgf pgangekgar gvagkpgprg qrgptgprgs rgargptgkp
      901 gpkgtsggdg ppgppgergp qgpqgpvgfp gpkgppgppg rmgcpghpgq rgetgfqgkt
      961 gppgpggvvg pqgptgetgp igerghpgpp gppgeqglpg aagkegakgd pgpqgisgkd
     1021 gpaglrgfpg erglpgaqga pglkggegpq gppgpvgspg ergsagtagp iglpgrpgpq
     1081 gppgpagekg apgekgpqgp agrdgvqgpv glpgpagpag spgedgdkge igepgqkgsk
     1141 gdkgengppg ppglqgpvga pgiaggdgep gprgqqgmfg qkgdegargf pgppgpiglq
     1201 glpgppgekg engdvgpwgp pgppgprgpq gpngadgpqg ppgsvgsvgg vgekgepgea
     1261 gnpgppgeag vggpkgerge kgeagppgaa gppgakgppg ddgpkgnpgp vgfpgdpgpp
     1321 gelgpagqdg vggdkgedgd pgqpgppgps geagppgppg krgppgaaga egrqgekgak
     1381 geagaegppg ktgpvgpqgp agkpgpeglr gipgpvgeqg lpgaagqdgp pgpmgppglp
     1441 glkgdpgskg ekghpgligl igppgeqgek gdrglpgtqg spgakgdggi pgpagplgpp
     1501 gppglpgpqg pkgnkgstgp agqkgdsglp gppgppgppg eviqplpils skktrrhteg
     1561 mqadaddnil dysdgmeeif gslnslkqdi ehmkfpmgtq tnpartckdl qlshpdfpdg
     1621 eywidpnqgc sgdsfkvycn ftsggetciy pdkksegvri sswpkekpgs wfsefkrgkl
     1681 lsyldvegns inmvqmtflk lltasarqnf tyhchqsaaw ydvssgsydk alrflgsnde
     1741 emsydnnpfi ktlydgctsr kgyektviei ntpkidqvpi vdvmindfgd qnqkfgfevg
     1801 pvcflg
//



Revised: July 5, 2002.
 
 


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1: NP_002204. integrin, beta 5 ...[gi:20127446] Links  


LOCUS       ITGB5                    799 aa            linear   PRI 14-MAY-2002
DEFINITION  integrin, beta 5 [Homo sapiens].
ACCESSION   NP_002204
VERSION     NP_002204.2  GI:20127446
DBSOURCE    REFSEQ: aaccession NM_002213.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 799)
  AUTHORS   Strausberg,R.
  TITLE     Homo sapiens integrin, beta 5 (ITGB5), mRNA
  JOURNAL   Unpublished (2001)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC006541.1.
            On Apr 10, 2002 this sequence version replaced gi:4504773.
FEATURES             Location/Qualifiers
     source          1..799
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3q21.3"
                     /clone="MGC:2338 IMAGE:2958666"
                     /tissue_type="Kidney, renal cell adenocarcinoma"
                     /clone_lib="NIH_MGC_14"
                     /lab_host="DH10B-R"
                     /note="Vector: pOTB7"
     Protein         1..799
                     /product="integrin, beta 5"
     Region          35..463
                     /region_name="Integrin beta subunits (N-terminal portion
                     of extracellular region)"
                     /note="INB"
                     /db_xref="CDD:smart00187"
     Region          35..463
                     /region_name="Integrins, beta chain"
                     /note="integrin_B"
                     /db_xref="CDD:pfam00362"
     CDS             1..799
                     /gene="ITGB5"
                     /coded_by="NM_002213.2:307..2706"
                     /db_xref="LocusID:3693"
                     /db_xref="MIM:147561"
ORIGIN      
        1 mprapaplya cllglcallp rlaglnicts gsatsceecl lihpkcawcs kedfgsprsi
       61 tsrcdlranl vkngcggeie spassfhvlr slplsskgsg sagwdviqmt pqeiavnlrp
      121 gdkttfqlqv rqvedypvdl yylmdlslsm kddldnirsl gtklaeemrk ltsnfrlgfg
      181 sfvdkdispf sytapryqtn pcigyklfpn cvpsfgfrhl lpltdrvdsf neevrkqrvs
      241 rnrdapeggf davlqaavck ekigwrkdal hllvfttddv phialdgklg glvqphdgqc
      301 hlneaneyta snqmdypsla llgeklaenn inlifavtkn hymlyknfta lipgttveil
      361 dgdskniiql iinaynsirs kvelsvwdqp edlnlfftat cqdgvsypgq rkceglkigd
      421 tasfevslea rscpsrhteh vfalrpvgfr dslevgvtyn ctcgcsvgle pnsarcngsg
      481 tyvcglcecs pgylgtrcec qdgenqsvyq nlcreaegkp lcsgrgdcsc nqcscfesef
      541 gkiygpfcec dnfscarnkg vlcsghgech cgeckchagy igdncncstd istcrgrdgq
      601 icserghclc gqcqctepga fgemcekcpt cpdacstkrd cveclllhsg kpdnqtchsl
      661 crdevitwvd tivkddqeav lcfyktakdc vmmftyvelp sgksnltvlr epecgntpna
      721 mtillavvgs illvglalla iwkllvtihd rrefakfqse rsraryemas nplyrkpist
      781 htvdftfnkf nksyngtvd
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_000384. alpha 2 type V co...[gi:4502959] Links  


LOCUS       COL5A2                  1496 aa            linear   PRI 31-OCT-2001
DEFINITION  alpha 2 type V collagen preproprotein; collagen V, alpha-2
            polypeptide; AB collagen; collagen, fetal membrane, A polypeptide
            [Homo sapiens].
ACCESSION   NP_000384
VERSION     NP_000384.1  GI:4502959
DBSOURCE    REFSEQ: aaccession NM_000393.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1496)
  AUTHORS   Myers,J.C., Loidl,H.R., Seyer,J.M. and Dion,A.S.
  TITLE     Complete primary structure of the human alpha 2 type V procollagen
            COOH-terminal propeptide
  JOURNAL   J. Biol. Chem. 260 (20), 11216-11222 (1985)
  MEDLINE   85289337
   PUBMED   2411731
REFERENCE   2  (residues 1 to 1496)
  AUTHORS   Weil,D., Bernard,M., Gargano,S. and Ramirez,F.
  TITLE     The pro alpha 2(V) collagen gene is evolutionarily related to the
            major fibrillar-forming collagens
  JOURNAL   Nucleic Acids Res. 15 (1), 181-198 (1987)
  MEDLINE   87146331
   PUBMED   3029669
REFERENCE   3  (residues 1 to 1496)
  AUTHORS   Woodbury,D., Benson-Chanda,V. and Ramirez,F.
  TITLE     Amino-terminal propeptide of human pro-alpha 2(V) collagen conforms
            to the structural criteria of a fibrillar procollagen molecule
  JOURNAL   J. Biol. Chem. 264 (5), 2735-2738 (1989)
  MEDLINE   89123368
   PUBMED   2914927
REFERENCE   4  (residues 1 to 1496)
  AUTHORS   Greenspan,D.S., Lee,S.T., Lee,B.S. and Hoffman,G.G.
  TITLE     Homology between alpha 2(V) and alpha 1(III) collagen promoters and
            evidence for negatively acting elements in the alpha 2(V) first
            intron and 5' flanking sequences
  JOURNAL   Gene Expr. 1 (1), 29-39 (1991)
  MEDLINE   92314691
   PUBMED   1820205
REFERENCE   5  (residues 1 to 1496)
  AUTHORS   Michalickova,K., Susic,M., Willing,M.C., Wenstrup,R.J. and
            Cole,W.G.
  TITLE     Mutations of the alpha2(V) chain of type V collagen impair matrix
            assembly and produce ehlers-danlos syndrome type I
  JOURNAL   Hum. Mol. Genet. 7 (2), 249-255 (1998)
  MEDLINE   98087576
   PUBMED   9425231
REFERENCE   6  (residues 1 to 1496)
  AUTHORS   Valkkila,M., Melkoniemi,M., Kvist,L., Kuivaniemi,H., Tromp,G. and
            Ala-Kokko,L.
  TITLE     Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2
            has evolved differently than the other minor fibrillar collagen
            genes
  JOURNAL   Matrix Biol. 20 (5-6), 357-366 (2001)
  MEDLINE   21451029
   PUBMED   11566270
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from Y14690.1, BC015705.1 and
            M58529.1.
            Summary: This gene encodes an alpha chain for one of the low
            abundance fibrillar collagens. Fibrillar collagen molecules are
            trimers that can be composed of one or more types of alpha chains.
            Type V collagen is found in tissues containing type I collagen and
            appears to regulate the assembly of heterotypic fibers composed of
            both type I and type V collagen. This gene product is closely
            related to type XI collagen and it is possible that the collagen
            chains of types V and XI constitute a single collagen type with
            tissue-specific chain combinations. Mutations in this gene are
            associated with Ehlers-Danlos syndrome, types I and II. Two
            transcripts that differ in the length of the 3'UTR due to the use
            of alternative polyadenylation signals have been identified for
            this gene.
FEATURES             Location/Qualifiers
     source          1..1496
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q14-q32"
     Protein         1..1496
                     /product="alpha 2 type V collagen preproprotein"
                     /note="collagen V, alpha-2 polypeptide; AB collagen;
                     collagen, fetal membrane, A polypeptide"
     sig_peptide     1..26
     Proprotein      27..1496
     mat_peptide     27..1226
                     /product="alpha 2 type V collagen"
     Region          41..96
                     /region_name="von Willebrand factor (vWF) type C domain"
                     /note="VWC"
                     /db_xref="CDD:smart00214"
     Region          41..96
                     /region_name="von Willebrand factor type C domain. The
                     high cutoff was used to prevent overlap with pfam00094"
                     /note="vwc"
                     /db_xref="CDD:pfam00093"
     Region          510..568
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          510..566
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          543..600
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          843..902
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          1262..1495
                     /region_name="Fibrillar collagens C-terminal domain"
                     /note="COLFI"
                     /db_xref="CDD:smart00038"
     Region          1279..1495
                     /region_name="Fibrillar collagen C-terminal domain. Found
                     at C-termini of fibrillar collagens: Ephydatia muelleri
                     procollagen EMF1 alpha"
                     /note="COLFI"
                     /db_xref="CDD:pfam01410"
     CDS             1..1496
                     /gene="COL5A2"
                     /coded_by="NM_000393.2:158..4648"
                     /db_xref="LocusID:1290"
                     /db_xref="MIM:120190"
                     /db_xref="LocusID:1290"
                     /db_xref="MIM:120190"
ORIGIN      
        1 mmanwaearp llilivllgq fvsikaqeed edegygeeia ctqngqmyln rdiwkpapcq
       61 icvcdngail cdkiecqdvl dcadpvtppg eccpvcsqtp gggntnfgrg rkgqkgepgl
      121 vpvvtgirgr pgpagppgsq gprgergpkg rpgprgpqgi dgepgvpgqp gapgppghps
      181 hpgpdglsrp fsaqmaglde ksglgsqvgl mpgsvgpvgp rgpqglqgqq ggagptgppg
      241 epgdpgpmgp igsrgpegpp gkpgedgepg rngnpgevgf agspgargfp gapglpglkg
      301 hrghkglegp kgevgapgsk geagptgpmg amgplgprgm pgergrlgpq gapgqrgahg
      361 mpgkpgpmgp lgipgssgfp gnpgmkgeag ptgargpegp qgqrgetgpp gpvgspglpg
      421 aigtdgtpgp kgptgspgts gppgsagppg spgpqgstgp qgnsglpgdp gfkgeagpkg
      481 epgphgiqgp igppgeegkr gprgdpgtlg ppgpvgerga pgnrgfpgsd glpgpkgaqg
      541 ergpvgssgp kgsqgdpgrp gepglpgarg ltgnpgvqgp egklgplgap gedgrpgppg
      601 sigikgqpgt mglpgpkgsn gdpgkpgeag npgvpgqrga pgkdgkvgpy gppgppglrg
      661 ergeqgppgp tgfqghpgpp gppgeggkpg dqgvpggpga vgplgprger gnpgergepg
      721 itglpgekgm agghgpdgpk gspgpsgtpg dtgppglqgm pgergiagtp gpkgdrggig
      781 ekgaegtagn dgagglpgpl gppgpagllg ekgepgprgl vgppgsrgnp gsrgengptg
      841 avgfagpqgs dgqpgvkgep gepgqkgdag spgpqglags pgphgpngvp glkggrgtqg
      901 ppgatgfpgs agrvgppgpa gapgpagplg epgkegppgp rgdpgshgrv gvrgpagppg
      961 gpgdkgdpge dgqpgpdgpp gpagttgqrg ivgmpgqrge rgmpglpgpa gtpgkvgptg
     1021 atgdkgppgp vgppgsngpv gepgpegpag ndgtpgrdga vgergdrgdp gpaglpgsqg
     1081 apgtpgpvga pgdagqrgdp gsrgpighlg ragkrglpgp qgprgdkgdh gdrgdrgqkg
     1141 hrgftglqgl pgppgpngeq gsagipgpfg prgppgpvgp sgkegnpgpl gplgppgvrg
     1201 svgeagpegp pgepgppgpp gppghltaal gdimghydes mpdplpefte dqaapddknk
     1261 tdpgvhatlk slssqietmr spdgskkhpa rtcddlklch sakqsgeywi dpnqgsveda
     1321 ikvycnmetg etcisanpss vprktwwask spdnkpvwyg ldmnrgsqfa ygdhqspnta
     1381 itqmtflrll skeasqnity icknsvgymd dqaknlkkav vlkgandldi kaegnirfry
     1441 ivlqdtcskr ngnvgktvfe yrtqnvarlp iidlapvdvg gtdqefgvei gpvcfv
//



Revised: July 5, 2002.
 
 


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1: NP_003471. Microfibril-assoc...[gi:4505089] Links  


LOCUS       MAGP2                    173 aa            linear   PRI 01-NOV-2000
DEFINITION  Microfibril-associated glycoprotein-2 [Homo sapiens].
ACCESSION   NP_003471
VERSION     NP_003471.1  GI:4505089
DBSOURCE    REFSEQ: aaccession NM_003480.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 173)
  AUTHORS   Gibson,M.A., Hatzinikolas,G., Kumaratilake,J.S., Sandberg,L.B.,
            Nicholl,J.K., Sutherland,G.R. and Cleary,E.G.
  TITLE     Further characterization of proteins associated with elastic fiber
            microfibrils including the molecular cloning of MAGP-2 (MP25)
  JOURNAL   J. Biol. Chem. 271 (2), 1096-1103 (1996)
  MEDLINE   96132851
   PUBMED   8557636
REFERENCE   2  (residues 1 to 173)
  AUTHORS   Hatzinikolas,G. and Gibson,M.A.
  TITLE     The exon structure of the human MAGP-2 gene. Similarity with the
            MAGP-1 gene is confined to two exons encoding a cysteine-rich
            region
  JOURNAL   J. Biol. Chem. 273 (45), 29309-29314 (1998)
  MEDLINE   99009031
   PUBMED   9792630
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF084927.1.
            Summary: This gene encodes a 25-kD microfibril-associated
            glycoprotein which is rich in serine and threonine residues. It
            lacks proline-, glutamine-, and tyrosine-rich sequences and a
            hydrophobic carboxyl terminus, which are characteristics of the
            related MFAP2 (MAGP1) molecule, a 31-kDa microfibril-associated
            glycoprotein. The close similarity between these two proteins is
            confined to a central region of 60 amino acids where there is
            precise alignment of 7 cystein residues. The structural differences
            suggest that MAGP2 has some functions that are distinct from those
            of MFAP2.
FEATURES             Location/Qualifiers
     source          1..173
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12p13.1-p12.3"
     Protein         1..173
                     /product="Microfibril-associated glycoprotein-2"
     CDS             1..173
                     /gene="MAGP2"
                     /coded_by="NM_003480.1:214..735"
                     /db_xref="LocusID:8076"
                     /db_xref="MIM:601103"
ORIGIN      
        1 msllgpkvll flaafiitsd wiplgvnsqr gddvtqatpe tftedpnlvn dpatdetvla
       61 vladiapstd dlaslseknt taecwdekft ctrlysvhrp vkqcihqlcf tslrrmyivn
      121 keicsrlvck eheamkdelc rqmaglpprr lrrsnyfrlp pcenvdlqrp ngl
//



Revised: July 5, 2002.
 
 


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1: NP_004360. alpha 3 type VI c...[gi:4758028] Links  


LOCUS       COL6A3                  3176 aa            linear   PRI 29-NOV-2001
DEFINITION  alpha 3 type VI collagen, isoform 1 precursor; collagen VI, alpha-3
            polypeptide [Homo sapiens].
ACCESSION   NP_004360
VERSION     NP_004360.1  GI:4758028
DBSOURCE    REFSEQ: aaccession NM_004369.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 3176)
  AUTHORS   Weil,D., Mattei,M.G., Passage,E., N'Guyen,V.C., Pribula-Conway,D.,
            Mann,K., Deutzmann,R., Timpl,R. and Chu,M.L.
  TITLE     Cloning and chromosomal localization of human genes encoding the
            three chains of type VI collagen
  JOURNAL   Am. J. Hum. Genet. 42 (3), 435-445 (1988)
  MEDLINE   88161046
   PUBMED   3348212
REFERENCE   2  (residues 1 to 3176)
  AUTHORS   Chu,M.L., Zhang,R.Z., Pan,T.C., Stokes,D., Conway,D., Kuo,H.J.,
            Glanville,R., Mayer,U., Mann,K., Deutzmann,R. and Timpl,R.
  TITLE     Mosaic structure of globular domains in the human type VI collagen
            alpha 3 chain: similarity to von Willebrand factor, fibronectin,
            actin, salivary proteins and aprotinin type protease inhibitors
  JOURNAL   EMBO J. 9 (2), 385-393 (1990)
  MEDLINE   90151612
   PUBMED   1689238
REFERENCE   3  (residues 1 to 3176)
  AUTHORS   Zanussi,S., Doliana,R., Segat,D., Bonaldo,P. and Colombatti,A.
  TITLE     The human type VI collagen gene. mRNA and protein variants of the
            alpha 3 chain generated by alternative splicing of an additional
            5-end exon
  JOURNAL   J. Biol. Chem. 267 (33), 24082-24089 (1992)
  MEDLINE   93054780
   PUBMED   1339440
REFERENCE   4  (residues 1 to 3176)
  AUTHORS   Jobsis,G.J., Keizers,H., Vreijling,J.P., de Visser,M., Speer,M.C.,
            Wolterman,R.A., Baas,F. and Bolhuis,P.A.
  TITLE     Type VI collagen mutations in Bethlem myopathy, an autosomal
            dominant myopathy with contractures
  JOURNAL   Nat. Genet. 14 (1), 113-115 (1996)
  MEDLINE   96376983
   PUBMED   8782832
REFERENCE   5  (residues 1 to 3176)
  AUTHORS   Lamande,S.R., Sigalas,E., Pan,T.C., Chu,M.L., Dziadek,M., Timpl,R.
            and Bateman,J.F.
  TITLE     The role of the alpha3(VI) chain in collagen VI assembly.
            Expression of an alpha3(VI) chain lacking N-terminal modules N10-N7
            restores collagen VI assembly, secretion, and matrix deposition in
            an alpha3(VI)-deficient cell line
  JOURNAL   J. Biol. Chem. 273 (13), 7423-7430 (1998)
  MEDLINE   98184847
   PUBMED   9516440
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X52022.1.
            Summary: This gene encodes the alpha 3 chain, one of the three
            alpha chains of type VI collagen, a beaded filament collagen found
            in most connective tissues. The alpha 3 chain of type VI collagen
            is much larger than the alpha 1 and 2 chains. This difference in
            size is largely due to an increase in the number of subdomains,
            similar to von Willebrand Factor type A domains, found in the amino
            terminal globular domain of all the alpha chains. These domains
            have been shown to bind extracellular matrix proteins, an
            interaction that explains the importance of this collagen in
            organizing matrix components. Mutations in the type VI collagen
            genes are associated with Bethlem myopathy. In addition to the full
            length transcript, four transcript variants have been identified
            that encode proteins with N-terminal globular domains of varying
            sizes.
            Transcript Variant: This variant (1) encodes the full length
            isoform.
FEATURES             Location/Qualifiers
     source          1..3176
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q37"
     Protein         1..3176
                     /product="alpha 3 type VI collagen, isoform 1 precursor"
                     /note="collagen VI, alpha-3 polypeptide"
     sig_peptide     1..25
     mat_peptide     26..3176
                     /product="alpha 3 type VI collagen, isoform 1"
     Region          38..207
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          39..213
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          241..416
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          242..415
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          443..609
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          445..612
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          637..804
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          639..804
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          835..1010
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          837..990
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          1027..1194
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          1029..1199
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          1231..1406
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          1233..1404
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          1435..1602
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          1436..1607
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          1637..1799
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          1639..1801
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          1837..1991
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          2080..2160
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2086..2172
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2126..2174
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2128..2174
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2315..2338
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2316..2355
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2316..2355
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2316..2355
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2316..2354
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2316..2354
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2316..2353
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2316..2349
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2317..2353
                     /region_name="Collagen triple helix repeat (20 copies).
                     Members of this family belong to the collagen superfamily.
                     Collagens are generally extracellular structural proteins
                     involved in formation of connective tissue structure. The
                     alignment contains 20 copies of the G-X-Y repeat that
                     forms a triple helix. The first position of the repeat is
                     G"
                     /note="Collagen"
                     /db_xref="CDD:pfam01391"
     Region          2400..2574
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          2402..2581
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          2619..2804
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     Region          2619..2795
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          2992..3060
                     /region_name="Fibronectin type 3 domain"
                     /note="FN3"
                     /db_xref="CDD:smart00060"
     Region          3109..3161
                     /region_name="BPTI/Kunitz family of serine protease
                     inhibitors."
                     /note="KU"
                     /db_xref="CDD:smart00131"
     Region          3111..3161
                     /region_name="Kunitz/Bovine pancreatic trypsin inhibitor
                     domain. Indicative of a protease inhibitor"
                     /note="Kunitz_BPTI"
                     /db_xref="CDD:pfam00014"
     CDS             1..3176
                     /gene="COL6A3"
                     /coded_by="NM_004369.1:256..9786"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="LocusID:1293"
                     /db_xref="MIM:120250"
                     /db_xref="LocusID:1293"
                     /db_xref="MIM:120250"
ORIGIN      
        1 mrkhrhlplv avfclflsgf ptthaqqqqa dvkngaaadi iflvdsswti geehfqlvre
       61 flydvvksla vgendfhfal vqfngnphte fllntyrtkq evlshisnms yiggtnqtgk
      121 gleyimqshl tkaagsragd gvpqvivvlt dghskdglal psaelksadv nvfaigveda
      181 degalkeias eplnmhmfnl enftslhdiv gnlvscvhss vsperagdte tlkditaqds
      241 adiiflidgs nntgsvnfav ildflvnlle klpigtqqir vgvvqfsdep rtmfsldtys
      301 tkaqvlgavk algfaggela niglaldfvv enhftraggs rveegvpqvl vlisagpssd
      361 eirygvvalk qasvfsfglg aqaasraelq hiatddnlvf tvpefrsfgd lqekllpyiv
      421 gvaqrhivlk pptivtqvie vnkrdivflv dgssalglan fnairdfiak viqrleigqd
      481 liqvavaqya dtvrpefyfn thptkrevit avrkmkpldg salytgsald fvrnnlftss
      541 agyraaegip kllvlitggk sldeisqpaq elkrssimaf aignkgadqa eleeiafdss
      601 lvfipaefra aplqgmlpgl laplrtlsgt pevhsnkrdi iflldgsanv gktnfpyvrd
      661 fvmnlvnsld igndnirvgl vqfsdtpvte fslntyqtks dilghlrqlq lqggsglntg
      721 salsyvyanh fteaggsrir ehvpqlllll tagqsedsyl qaanaltrag iltfcvgasq
      781 ankaeleqia fnpslvylmd dfsslpalpq qliqplttyv sggveevpla qpeskrdilf
      841 lfdgsanlvg qfpvvrdfly kiidelnvkp egtriavaqy sddvkvesrf dehqskpeil
      901 nlvkrmkikt gkalnlgyal dyaqryifvk sagsriedgv lqflvllvag rssdrvdgpa
      961 snlkqsgvvp fifqaknadp aeleqivlsp afilaaeslp kigdlhpqiv nllksvhnga
     1021 papvsgekdv vflldgsegv rsgfpllkef vqrvvesldv gqdrvrvavv qysdrtrpef
     1081 ylnsymnkqd vvnavrqltl lggptpntga alefvlrnil vssagsrite gvpqllivlt
     1141 adrsgddvrn psvvvkrgga vpigigigna ditemqtisf ipdfavaipt frqlgtvqqv
     1201 iservtqltr eelsrlqpvl qplpspgvgg krdvvflidg sqsagpefqy vrtlierlvd
     1261 yldvgfdttr vaviqfsddp kaefllnahs skdevqnavq rlrpkggrqi nvgnaleyvs
     1321 rnifkrplgs rieegvpqfl vlissgksdd evvvpavelk qfgvapftia rnadqeelvk
     1381 islspeyvfs vstfrelpsl eqklltpitt ltseqiqkll astrypppav esdaadivfl
     1441 idssegvrpd gfahirdfvs rivrrlnigp skvrvgvvqf sndvfpefyl ktyrsqapvl
     1501 dairrlrlrg gsplntgkal efvarnlfvk sagsriedgv pqhlvlvlgg ksqddvsrfa
     1561 qvirssgivs lgvgdrnidr telqtitndp rlvftvrefr elpnieerim nsfgpsaatp
     1621 appgvdtppp srpekkkadi vflldgsinf rrdsfqevlr fvseivdtvy edgdsiqvgl
     1681 vqynsdptde fflkdfstkr qiidainkvv ykggrhantk vglehlrvnh fvpeagsrld
     1741 qrvpqiafvi tggksvedaq dvslaltqrg vkvfavgvrn idseevgkia snsatafrvg
     1801 nvqelselse qvletlhdam hetlcpgvtd aakacnldvi lgfdgsrdqn vfvaqkgfes
     1861 kvdailnris qmhrvscsgg rsptvrvsvv antpsgpvea fdfdeyqpem lekfrnmrsq
     1921 hpyvltedtl kvylnkfrqs spdsvkvvih ftdgadgdla dlhrasenlr qegvralilv
     1981 glervvnler lmhlefgrgf mydrplrlnl ldldyelaeq ldniaekacc gvpckcsgqr
     2041 gdrgpigsig pkgipgedgy rgypgdeggp gergppgvng tqgfqgcpgq rgvkgsrgfp
     2101 gekgevgeig ldgldgedgd kglpgssgek gnpgrrgdkg prgekgergd vgirgdpgnp
     2161 gqdsqergpk getgdlgpmg vpgrdgvpgg pgetgknggf grrgppgakg nkggpgqpgf
     2221 egeqgtrgaq gpagpagppg ligeqgisgp rgsggargap gergrtgplg rkgepgepgp
     2281 kggignpgpr getgddgrdg vgsegrrgkk gergfpgypg pkgnpgepgl ngttgpkgir
     2341 grrgnsgppg ivgqkgrpgy pgpagprgnr gdsidqcali qsikdkcpcc ygplecpvfp
     2401 telafaldts egvnqdtfgr mrdvvlsivn vltiaesncp tgarvavvty nnevtteirf
     2461 adskrksvll dkiknlqval tskqqsleta msfvarntfk rvrngflmrk vavffsntpt
     2521 raspqlreav lklsdagitp lfltrqedrq linalqinnt avghalvlpa grdltdflen
     2581 vltchvcldi cnidpscgfg swrpsfrdrr aagsdvdidm afildsaett tlfqfnemkk
     2641 yiaylvrqld mspdpkasqh farvavvqha psesvdnasm ppvkvefslt dygskeklvd
     2701 flsrgmtqlq gtralgsaie ytienvfesa pnprdlkivv lmltgevpeq qleeaqrvil
     2761 qakckgyffv vlgigrkvni kevytfasep ndvffklvdk stelneeplm rfgrllpsfv
     2821 ssenafylsp dirkqcdwfq gdqptknlvk fghkqvnvpn nvtssptsnp vtttkpvttt
     2881 kpvttttkpv ttttkpvtii nqpsvkpaaa kpapakpvaa kpvatktatv rppvavkpat
     2941 aakpvaakpa avrppaaaak pvatkpevpr pqaakpaatk pattkpvvkm lrevqvfeit
     3001 ensaklhwer peppgpyfyd ltvtsahdqs lvlkqnltvt drviggllag qtyhvavvcy
     3061 lrsqvratyh gsfstkksqp pppqparsas sstinlmvst eplaltetdi cklpkdegtc
     3121 rdfilkwyyd pntkscarfw yggcggnenk fgsqkecekv capvlakpgv isvmgt
//



Revised: July 5, 2002.
 
 


Disclaimer | Write to the Help Desk
NCBI | NLM | NIH 

 

Oct 21 2002 11:56:56 

BLinkBLinkRelated SequencesRelated SequencesDomain RelativesDomain RelativesDomainsDomainsMap ViewerMap ViewerNucleotideNucleotideOMIMOMIMPubMedPubMedSNPSNPTaxonomyTaxonomyLinkOutLinkOutHelpHelp  


&&&&&&&


    
 
PubMed Nucleotide Protein Genome Structure PopSet Taxonomy OMIM Books 
 
   Search PubMed Protein Nucleotide PopSet Taxonomy Genome OMIM Structure Domains GEO Books Books2 MapViewDr TestDb UniSTS CDD SNP Journals UniGene  for        
 
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1: NP_004858. integral membrane...[gi:4758224] Links  


LOCUS       ITM2A                    263 aa            linear   PRI 01-NOV-2000
DEFINITION  integral membrane protein 2A [Homo sapiens].
ACCESSION   NP_004858
VERSION     NP_004858.1  GI:4758224
DBSOURCE    REFSEQ: aaccession NM_004867.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 263)
  AUTHORS   Deleersnijder,W., Hong,G., Cortvrindt,R., Poirier,C.,
            Tylzanowski,P., Pittois,K., Van Marck,E. and Merregaert,J.
  TITLE     Isolation of markers for chondro-osteogenic differentiation using
            cDNA library subtraction. Molecular cloning and characterization of
            a gene belonging to a novel multigene family of integral membrane
            proteins
  JOURNAL   J. Biol. Chem. 271 (32), 19475-19482 (1996)
  MEDLINE   96325063
   PUBMED   8702637
REFERENCE   2  (residues 1 to 263)
  AUTHORS   Mao,M., Fu,G., Wu,J.-S., Zhang,Q.-H., Zhou,J., Kan,L.-X.,
            Huang,Q.-H., He,K.-L., Gu,B.-W., Han,Z.-G., Shen,Y., Gu,J.,
            Yu,Y.-P., Xu,S.-H., Wang,Y., Chen,S.-J. and Chen,Z.
  TITLE     Identification of genes expressed in human CD34(+) hematopoietic
            stem/progenitor cells by expressed sequence tags and efficient
            full-length cDNA cloning
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 95 (14), 8175-8180 (1998)
  MEDLINE   98318631
   PUBMED   9653160
REFERENCE   3  (residues 1 to 263)
  AUTHORS   Pittois,K., Wauters,J., Bossuyt,P., Deleersnijder,W. and
            Merregaert,J.
  TITLE     Genomic organization and chromosomal localization of the Itm2a gene
  JOURNAL   Mamm. Genome 10 (1), 54-56 (1999)
  MEDLINE   99111395
   PUBMED   9892734
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF038953.1.
FEATURES             Location/Qualifiers
     source          1..263
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.3-Xq21.2"
                     /cell_type="CD34+ cell"
                     /tissue_type="cord blood"
     Protein         1..263
                     /product="integral membrane protein 2A"
     variation       225
                     /allele="F"
                     /allele="V"
                     /db_xref="dbSNP:3180833"
     variation       226
                     /allele="P"
                     /allele="R"
                     /db_xref="dbSNP:3180834"
     CDS             1..263
                     /gene="ITM2A"
                     /coded_by="NM_004867.1:140..931"
                     /db_xref="LocusID:9452"
                     /db_xref="MIM:300222"
ORIGIN      
        1 mvkiafntpt avqkeearqd veallsrtvr tqiltgkelr vatqekegss grcmltllgl
       61 sfilaglivg gaciykyfmp kstiyrgemc ffdsedpans lrggepnflp vteeadired
      121 dniaiidvpv psfsdsdpaa iihdfekgmt ayldlllgnc ylmplntsiv mppknlvelf
      181 gklasgrylp qtyvvredlv aveeirdvsn lgifiyqlcn nrksfrlrrr dlllgfnkra
      241 idkcwkirhf pnefivetki cqe
//



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1: NP_000958. ribosomal protein...[gi:4506649] Links  


LOCUS       RPL3                     403 aa            linear   PRI 27-AUG-2002
DEFINITION  ribosomal protein L3; 60S ribosomal protein L3; HIV-1 TAR
            RNA-binding protein B [Homo sapiens].
ACCESSION   NP_000958
VERSION     NP_000958.1  GI:4506649
DBSOURCE    REFSEQ: aaccession NM_000967.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 403)
  AUTHORS   Reddy,T.R., Suhasini,M., Rappaport,J., Looney,D.J., Kraus,G. and
            Wong-Staal,F.
  TITLE     Molecular cloning and characterization of a TAR-binding nuclear
            factor from T cells
  JOURNAL   AIDS Res. Hum. Retroviruses 11 (6), 663-669 (1995)
  MEDLINE   96078226
   PUBMED   7576925
REFERENCE   2  (residues 1 to 403)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem. Cell Biol. 73 (11-12), 933-947 (1995)
  MEDLINE   96282697
   PUBMED   8722009
  REMARK    This review focuses primarily on rat ribosomal proteins, but it
            compares them to human ribosomal proteins.
REFERENCE   3  (residues 1 to 403)
  AUTHORS   Kenmochi,N., Kawaguchi,T., Rozen,S., Davis,E., Goodman,N.,
            Hudson,T.J., Tanaka,T. and Page,D.C.
  TITLE     A map of 75 human ribosomal protein genes
  JOURNAL   Genome Res. 8 (5), 509-523 (1998)
  MEDLINE   98248690
   PUBMED   9582194
REFERENCE   4  (residues 1 to 403)
  AUTHORS   Duga,S., Asselta,R., Malcovati,M., Tenchini,M.L., Ronchi,S. and
            Simonic,T.
  TITLE     The intron-containing L3 ribosomal protein gene (RPL3): sequence
            analysis and identification of U43 and of two novel intronic small
            nucleolar RNAs
  JOURNAL   Biochim. Biophys. Acta 1490 (3), 225-236 (2000)
  MEDLINE   20149844
   PUBMED   10684968
REFERENCE   5  (residues 1 to 403)
  AUTHORS   Uechi,T., Tanaka,T. and Kenmochi,N.
  TITLE     A complete map of the human ribosomal protein genes: assignment of
            80 genes to the cytogenetic map and implications for human
            disorders
  JOURNAL   Genomics 72 (3), 223-230 (2001)
  MEDLINE   21295043
   PUBMED   11401437
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC012146.1 and BC008492.1.
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            protein that is a component of the 60S subunit. The protein belongs
            to the L3P family of ribosomal proteins. It is located in the
            cytoplasm. The protein can bind to the HIV-1 TAR mRNA, and it has
            been suggested that the protein contributes to tat-mediated
            transactivation. This gene is co-transcribed with the small
            nucleolar RNA genes U43, U86, U83a, and U83b, which are located in
            its first, third, fifth, and seventh introns, respectively. As is
            typical for genes encoding ribosomal proteins, there are multiple
            processed pseudogenes of this gene dispersed through the genome.
FEATURES             Location/Qualifiers
     source          1..403
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13"
     Protein         1..403
                     /product="ribosomal protein L3"
                     /note="60S ribosomal protein L3; HIV-1 TAR RNA-binding
                     protein B"
     Region          50..347
                     /region_name="pfam00297, Ribosomal_L3, Ribosomal protein
                     L3"
     variation       390
                     /allele="V"
                     /allele="G"
                     /db_xref="dbSNP:2014840"
     CDS             1..403
                     /gene="RPL3"
                     /coded_by="NM_000967.2:27..1238"
                     /db_xref="LocusID:6122"
                     /db_xref="MIM:604163"
ORIGIN      
        1 mshrkfsapr hgslgflprk rssrhrgkvk sfpkddpskp vhltaflgyk agmthivrev
       61 drpgskvnkk evveavtive tppmvvvgiv gyvetprglr tfktvfaehi sdeckrrfyk
      121 nwhkskkkaf tkyckkwqde dgkkqlekdf ssmkkycqvi rviahtqmrl lplrqkkahl
      181 meiqvnggtv aekldwarer leqqvpvnqv fgqdemidvi gvtkgkgykg vtsrwhtkkl
      241 prkthrglrk vacigawhpa rvafsvarag qkgyhhrtei nkkiykigqg ylikdgklik
      301 nnastdydls dksinplggf vhygevtndf vmlkgcvvgt kkrvltlrks llvqtkrral
      361 ekidlkfidt tskfghgrfq tmeekkafmg plkkdriake ega
//



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1: NP_000573. secreted phosphop...[gi:4759166] Links  


LOCUS       SPP1                     300 aa            linear   PRI 27-AUG-2002
DEFINITION  secreted phosphoprotein 1 (osteopontin, bone sialoprotein I, early
            T-lymphocyte activation 1); Secreted phosphoprotein-1 (osteopontin,
            bone sialoprotein) [Homo sapiens].
ACCESSION   NP_000573
VERSION     NP_000573.1  GI:4759166
DBSOURCE    REFSEQ: aaccession NM_000582.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 300)
  AUTHORS   Kiefer,M.C., Bauer,D.M. and Barr,P.J.
  TITLE     The cDNA and derived amino acid sequence for human osteopontin
  JOURNAL   Nucleic Acids Res. 17 (8), 3306 (1989)
  MEDLINE   89263749
   PUBMED   2726470
REFERENCE   2  (residues 1 to 300)
  AUTHORS   Fisher,L.W., McBride,O.W., Termine,J.D. and Young,M.F.
  TITLE     Human bone sialoprotein. Deduced protein sequence and chromosomal
            localization
  JOURNAL   J. Biol. Chem. 265 (4), 2347-2351 (1990)
  MEDLINE   90130496
   PUBMED   2404984
REFERENCE   3  (residues 1 to 300)
  AUTHORS   Young,M.F., Kerr,J.M., Termine,J.D., Wewer,U.M., Wang,M.G.,
            McBride,O.W. and Fisher,L.W.
  TITLE     cDNA cloning, mRNA distribution and heterogeneity, chromosomal
            location, and RFLP analysis of human osteopontin (OPN)
  JOURNAL   Genomics 7 (4), 491-502 (1990)
  MEDLINE   90353945
   PUBMED   1974876
REFERENCE   4  (residues 1 to 300)
  AUTHORS   Shiraga,H., Min,W., VanDusen,W.J., Clayman,M.D., Miner,D.,
            Terrell,C.H., Sherbotie,J.R., Foreman,J.W., Przysiecki,C.,
            Neilson,E.G. et al.
  TITLE     Inhibition of calcium oxalate crystal growth in vitro by uropontin:
            another member of the aspartic acid-rich protein superfamily
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 89 (1), 426-430 (1992)
  MEDLINE   92108068
   PUBMED   1729712
REFERENCE   5  (residues 1 to 300)
  AUTHORS   Kohri,K., Suzuki,Y., Yoshida,K., Yamamoto,K., Amasaki,N.,
            Yamate,T., Umekawa,T., Iguchi,M., Sinohara,H. and Kurita,T.
  TITLE     Molecular cloning and sequencing of cDNA encoding urinary stone
            protein, which is identical to osteopontin
  JOURNAL   Biochem. Biophys. Res. Commun. 184 (2), 859-864 (1992)
  MEDLINE   92246977
   PUBMED   1575754
REFERENCE   6  (residues 1 to 300)
  AUTHORS   Crosby,A.H., Edwards,S.J., Murray,J.C. and Dixon,M.J.
  TITLE     Genomic organization of the human osteopontin gene: exclusion of
            the locus from a causative role in the pathogenesis of
            dentinogenesis imperfecta type II
  JOURNAL   Genomics 27 (1), 155-160 (1995)
  MEDLINE   95394452
   PUBMED   7665163
REFERENCE   7  (residues 1 to 300)
  AUTHORS   Crosby,A.H., Lyu,M.S., Lin,K., McBride,O.W., Kerr,J.M., Aplin,H.M.,
            Fisher,L.W., Young,M.F., Kozak,C.A. and Dixon,M.J.
  TITLE     Mapping of the human and mouse bone sialoprotein and osteopontin
            loci
  JOURNAL   Mamm. Genome 7 (2), 149-151 (1996)
  MEDLINE   96432468
   PUBMED   8835534
REFERENCE   8  (residues 1 to 300)
  AUTHORS   Andersson,B., Wentland,M.A., Ricafrente,J.Y., Liu,W. and Gibbs,R.A.
  TITLE     A 'double adaptor' method for improved shotgun library construction
  JOURNAL   Anal. Biochem. 236 (1), 107-113 (1996)
  MEDLINE   96207227
   PUBMED   8619474
REFERENCE   9  (residues 1 to 300)
  AUTHORS   Yu,W., Andersson,B., Worley,K.C., Muzny,D.M., Ding,Y., Liu,W.,
            Ricafrente,J.Y., Wentland,M.A., Lennon,G. and Gibbs,R.A.
  TITLE     Large-scale concatenation cDNA sequencing
  JOURNAL   Genome Res. 7 (4), 353-358 (1997)
  MEDLINE   97264341
   PUBMED   9110174
REFERENCE   10 (residues 1 to 300)
  AUTHORS   Helluin,O., Chan,C., Vilaire,G., Mousa,S., DeGrado,W.F. and
            Bennett,J.S.
  TITLE     The activation state of alphavbeta 3 regulates platelet and
            lymphocyte adhesion to intact and thrombin-cleaved osteopontin
  JOURNAL   J. Biol. Chem. 275 (24), 18337-18343 (2000)
  MEDLINE   20309787
   PUBMED   10751402
REFERENCE   11 (residues 1 to 300)
  AUTHORS   Jono,S., Peinado,C. and Giachelli,C.M.
  TITLE     Phosphorylation of osteopontin is required for inhibition of
            vascular smooth muscle cell calcification
  JOURNAL   J. Biol. Chem. 275 (26), 20197-20203 (2000)
  MEDLINE   20347938
   PUBMED   10766759
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF052124.1.
FEATURES             Location/Qualifiers
     source          1..300
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q21-q25"
                     /clone="I.M.A.G.E. Consortium clone ID 23810"
                     /sex="female"
                     /tissue_type="brain"
                     /clone_lib="1NIB"
                     /dev_stage="infant"
     Protein         1..300
                     /product="secreted phosphoprotein 1 (osteopontin, bone
                     sialoprotein I, early T-lymphocyte activation 1)"
                     /note="Secreted phosphoprotein-1 (osteopontin, bone
                     sialoprotein)"
     Region          1..300
                     /region_name="pfam00865, Osteopontin, Osteopontin"
     Region          17..300
                     /region_name="smart00017, OSTEO, Osteopontin; Osteopontin
                     is an acidic phosphorylated glycoprotein of about 40 Kd
                     which is abundant in the mineral matrix of bones and which
                     binds tightly to hydroxyapatite. It is suggested that
                     osteopontin might function as a cell attachment factor and
                     could play a key role in the adhesion of osteoclasts to
                     the mineral matrix of bone"
     variation       287
                     /allele="H"
                     /allele="R"
                     /db_xref="dbSNP:4660"
     CDS             1..300
                     /gene="SPP1"
                     /coded_by="NM_000582.1:88..990"
                     /note="similar to Homo sapiens osteopontin encoded by
                     GenBank Accession Number J04765"
                     /db_xref="LocusID:6696"
                     /db_xref="MIM:166490"
ORIGIN      
        1 mriavicfcl lgitcaipvk qadsgsseek qlynkypdav atwlnpdpsq kqnllapqtl
       61 psksneshdh mddmddeddd dhvdsqdsid sndsddvddt ddshqsdesh hsdesdelvt
      121 dfptdlpate vftpvvptvd tydgrgdsvv yglrskskkf rrpdiqypda tdeditshme
      181 seelngayka ipvaqdlnap sdwdsrgkds yetsqlddqs aethshkqsr lykrkandes
      241 nehsdvidsq elskvsrefh shefhshedm lvvdpkskee dkhlkfrish eldsassevn
//



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1: NP_000346. transcobalamin II...[gi:21071010] Links  


LOCUS       TCN2                     427 aa            linear   PRI 27-AUG-2002
DEFINITION  transcobalamin II precursor [Homo sapiens].
ACCESSION   NP_000346
VERSION     NP_000346.2  GI:21071010
DBSOURCE    REFSEQ: aaccession NM_000355.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 427)
  AUTHORS   Quadros,E.V., Rothenberg,S.P., Pan,Y.C. and Stein,S.
  TITLE     Purification and molecular characterization of human transcobalamin
            II
  JOURNAL   J. Biol. Chem. 261 (33), 15455-15460 (1986)
  MEDLINE   87057168
   PUBMED   3782074
REFERENCE   2  (residues 1 to 427)
  AUTHORS   Platica,O., Janeczko,R., Quadros,E.V., Regec,A., Romain,R. and
            Rothenberg,S.P.
  TITLE     The cDNA sequence and the deduced amino acid sequence of human
            transcobalamin II show homology with rat intrinsic factor and human
            transcobalamin I
  JOURNAL   J. Biol. Chem. 266 (12), 7860-7863 (1991)
  MEDLINE   91210312
   PUBMED   1708393
REFERENCE   3  (residues 1 to 427)
  AUTHORS   Li,N., Seetharam,S., Lindemans,J., Alpers,D.H., Arwert,F. and
            Seetharam,B.
  TITLE     Isolation and sequence analysis of variant forms of human
            transcobalamin II
  JOURNAL   Biochim. Biophys. Acta 1172 (1-2), 21-30 (1993)
  MEDLINE   93176815
   PUBMED   8439564
REFERENCE   4  (residues 1 to 427)
  AUTHORS   Quadros,E.V., Sai,P. and Rothenberg,S.P.
  TITLE     Functional human transcobalamin II isoproteins are secreted by
            insect cells using the baculovirus expression system
  JOURNAL   Blood 81 (5), 1239-1245 (1993)
  MEDLINE   93184316
   PUBMED   8443384
REFERENCE   5  (residues 1 to 427)
  AUTHORS   Li,N., Seetharam,S. and Seetharam,B.
  TITLE     Genomic structure of human transcobalamin II: comparison to human
            intrinsic factor and transcobalamin I
  JOURNAL   Biochem. Biophys. Res. Commun. 208 (2), 756-764 (1995)
  MEDLINE   95209692
   PUBMED   7695633
REFERENCE   6  (residues 1 to 427)
  AUTHORS   Regec,A., Quadros,E.V., Platica,O. and Rothenberg,S.P.
  TITLE     The cloning and characterization of the human transcobalamin II
            gene
  JOURNAL   Blood 85 (10), 2711-2719 (1995)
  MEDLINE   95261033
   PUBMED   7742531
REFERENCE   7  (residues 1 to 427)
  AUTHORS   Namour,F., Olivier,J., Abdelmouttaleb,I., Adjalla,C., Debard,R.,
            Salvat,C. and Gueant,J.
  TITLE     Transcobalamin codon 259 polymorphism in HT-29 and Caco-2 cells and
            in Caucasians: relation to transcobalamin and homocysteine
            concentration in blood
  JOURNAL   Blood 97 (4), 1092-1098 (2001)
  MEDLINE   21093851
   PUBMED   11159542
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M60396.1 and AF047576.1.
            On May 22, 2002 this sequence version replaced gi:4507409.
            Summary: This gene encodes a member of the vitamin B12-binding
            protein family. This family of proteins, alternatively referred to
            as R binders, is expressed in various tissues and secretions. This
            plasma protein binds cobalamin and mediates the transport of
            cobalamin into cells. This protein and other mammalian
            cobalamin-binding proteins, such as transcobalamin I and gastric
            intrisic factor, may have evolved by duplication of a common
            ancestral gene.
FEATURES             Location/Qualifiers
     source          1..427
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q12.2"
     Protein         1..427
                     /product="transcobalamin II precursor"
     sig_peptide     1..18
     Region          18..427
                     /region_name="pfam01122, Cobalamin_bind, Eukaryotic
                     cobalamin-binding protein"
     mat_peptide     19..427
                     /product="transcobalamin II"
     variation       259
                     /allele="P"
                     /allele="R"
                     /db_xref="dbSNP:1801198"
     variation       376
                     /allele="S"
                     /allele="L"
                     /db_xref="dbSNP:3178000"
     CDS             1..427
                     /gene="TCN2"
                     /coded_by="NM_000355.2:159..1442"
                     /db_xref="LocusID:6948"
                     /db_xref="MIM:275350"
ORIGIN      
        1 mrhlgaflfl lgvlgaltem ceipemdshl veklgqhllp wmdrlslehl npsiyvglrl
       61 sslqagtked lylhslklgy qqcllgsafs eddgdcqgkp smgqlalyll alrancefvr
      121 ghkgdrlvsq lkwfledekr aighdhkghp htsyyqyglg ilalclhqkr vhdsvvdkll
      181 yavepfhqgh hsvdtaamag laftclkrsn fnpgrrqrit mairtvreei lkaqtpeghf
      241 gnvystplal qflmtspmrg aelgtaclka rvallaslqd gafqnalmis qllpvlnhkt
      301 yidlifpdcl aprvmlepaa etipqtqeii svtlqvlsll ppyrqsisvl agstvedvlk
      361 kahelggfty etqaslsgpy ltsvmgkaag erefwqllrd pntpllqgia dyrpkdgeti
      421 elrlvsw
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_000595. fibroblast growth...[gi:11276087] Links  


LOCUS       FGFR1                    822 aa            linear   PRI 27-AUG-2002
DEFINITION  fibroblast growth factor receptor 1 isoform 1 precursor;
            fms-related tyrosine kinase-2; heparin-binding growth factor
            receptor; FMS-like tyrosine kinase 2; basic fibroblast growth
            factor receptor 1; N-sam tyrosine kinase; FLG protein;
            protein-tyrosine kinase; tyrosylprotein kinase; hydroxyaryl-protein
            kinase [Homo sapiens].
ACCESSION   NP_000595
VERSION     NP_000595.1  GI:11276087
DBSOURCE    REFSEQ: aaccession NM_000604.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Ruta,M., Burgess,W., Givol,D., Epstein,J., Neiger,N., Kaplow,J.,
            Crumley,G., Dionne,C., Jaye,M. and Schlessinger,J.
  TITLE     Receptor for acidic fibroblast growth factor is related to the
            tyrosine kinase encoded by the fms-like gene (FLG)
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 86 (22), 8722-8726 (1989)
  MEDLINE   90046865
   PUBMED   2554327
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Isacchi,A., Bergonzoni,L. and Sarmientos,P.
  TITLE     Complete sequence of a human receptor for acidic and basic
            fibroblast growth factors
  JOURNAL   Nucleic Acids Res. 18 (7), 1906 (1990)
  MEDLINE   90245600
   PUBMED   2159626
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Itoh,N., Terachi,T., Ohta,M. and Seo,M.K.
  TITLE     The complete amino acid sequence of the shorter form of human basic
            fibroblast growth factor receptor deduced from its cDNA
  JOURNAL   Biochem. Biophys. Res. Commun. 169 (2), 680-685 (1990)
  MEDLINE   90290512
   PUBMED   2162671
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Dionne,C.A., Crumley,G., Bellot,F., Kaplow,J.M., Searfoss,G.,
            Ruta,M., Burgess,W.H., Jaye,M. and Schlessinger,J.
  TITLE     Cloning and expression of two distinct high-affinity receptors
            cross-reacting with acidic and basic fibroblast growth factors
  JOURNAL   EMBO J. 9 (9), 2685-2692 (1990)
  MEDLINE   90360977
   PUBMED   1697263
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Johnson,D.E., Lee,P.L., Lu,J. and Williams,L.T.
  TITLE     Diverse forms of a receptor for acidic and basic fibroblast growth
            factors
  JOURNAL   Mol. Cell. Biol. 10 (9), 4728-4736 (1990)
  MEDLINE   90355989
   PUBMED   2167437
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Hou,J.Z., Kan,M.K., McKeehan,K., McBride,G., Adams,P. and
            McKeehan,W.L.
  TITLE     Fibroblast growth factor receptors from liver vary in three
            structural domains
  JOURNAL   Science 251 (4994), 665-668 (1991)
  MEDLINE   91126480
   PUBMED   1846977
REFERENCE   7  (residues 1 to 822)
  AUTHORS   Eisemann,A., Ahn,J.A., Graziani,G., Tronick,S.R. and Ron,D.
  TITLE     Alternative splicing generates at least five different isoforms of
            the human basic-FGF receptor
  JOURNAL   Oncogene 6 (7), 1195-1202 (1991)
  MEDLINE   91319400
   PUBMED   1650441
REFERENCE   8  (residues 1 to 822)
  AUTHORS   Johnson,D.E., Lu,J., Chen,H., Werner,S. and Williams,L.T.
  TITLE     The human fibroblast growth factor receptor genes: a common
            structural arrangement underlies the mechanisms for generating
            receptor forms that differ in their third immunoglobulin domain
  JOURNAL   Mol. Cell. Biol. 11 (9), 4627-4634 (1991)
  MEDLINE   91342665
   PUBMED   1652059
REFERENCE   9  (residues 1 to 822)
  AUTHORS   Crumley,G., Bellot,F., Kaplow,J.M., Schlessinger,J., Jaye,M. and
            Dionne,C.A.
  TITLE     High-affinity binding and activation of a truncated FGF receptor by
            both aFGF and bFGF
  JOURNAL   Oncogene 6 (12), 2255-2262 (1991)
  MEDLINE   92115326
   PUBMED   1722570
REFERENCE   10 (residues 1 to 822)
  AUTHORS   Wennstrom,S., Sandstrom,C. and Claesson-Welsh,L.
  TITLE     cDNA cloning and expression of a human FGF receptor which binds
            acidic and basic FGF
  JOURNAL   Growth Factors 4 (3), 197-208 (1991)
  MEDLINE   92118394
   PUBMED   1722683
REFERENCE   11 (residues 1 to 822)
  AUTHORS   Hattori,Y., Odagiri,H., Katoh,O., Sakamoto,H., Morita,T.,
            Shimotohno,K., Tobinai,K., Sugimura,T. and Terada,M.
  TITLE     K-sam-related gene, N-sam, encodes fibroblast growth factor
            receptor and is expressed in T-lymphocytic tumors
  JOURNAL   Cancer Res. 52 (12), 3367-3371 (1992)
  MEDLINE   92282615
   PUBMED   1317750
REFERENCE   12 (residues 1 to 822)
  AUTHORS   Johnson,D.E. and Williams,L.T.
  TITLE     Structural and functional diversity in the FGF receptor multigene
            family
  JOURNAL   Adv. Cancer Res. 60, 1-41 (1993)
  MEDLINE   93111178
   PUBMED   8417497
REFERENCE   13 (residues 1 to 822)
  AUTHORS   Muenke,M., Schell,U., Hehr,A., Robin,N.H., Losken,H.W.,
            Schinzel,A., Pulleyn,L.J., Rutland,P., Reardon,W., Malcolm,S. et
            al.
  TITLE     A common mutation in the fibroblast growth factor receptor 1 gene
            in Pfeiffer syndrome
  JOURNAL   Nat. Genet. 8 (3), 269-274 (1994)
  MEDLINE   95179173
   PUBMED   7874169
REFERENCE   14 (residues 1 to 822)
  AUTHORS   Wood,S., Schertzer,M. and Yaremko,M.L.
  TITLE     Sequence identity locates CEBPD and FGFR1 to mapped human loci
            within proximal 8p
  JOURNAL   Cytogenet. Cell Genet. 70 (3-4), 188-191 (1995)
  MEDLINE   95309017
   PUBMED   7789168
REFERENCE   15 (residues 1 to 822)
  AUTHORS   Wang,L.Y., Edenson,S.P., Yu,Y.L., Senderowicz,L. and Turck,C.W.
  TITLE     A natural kinase-deficient variant of fibroblast growth factor
            receptor 1
  JOURNAL   Biochemistry (N.Y.) 35 (31), 10134-10142 (1996)
  MEDLINE   96322333
   PUBMED   8756477
REFERENCE   16 (residues 1 to 822)
  AUTHORS   Lopez,M.E. and Korc,M.
  TITLE     A novel type I fibroblast growth factor receptor activates
            mitogenic signaling in the absence of detectable tyrosine
            phosphorylation of FRS2
  JOURNAL   J. Biol. Chem. 275 (21), 15933-15939 (2000)
  MEDLINE   20283622
   PUBMED   10748122
REFERENCE   17 (residues 1 to 822)
  AUTHORS   Hart,K.C., Robertson,S.C., Kanemitsu,M.Y., Meyer,A.N., Tynan,J.A.
            and Donoghue,D.J.
  TITLE     Transformation and Stat activation by derivatives of FGFR1, FGFR3,
            and FGFR4
  JOURNAL   Oncogene 19 (29), 3309-3320 (2000)
  MEDLINE   20374012
   PUBMED   10918587
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X66945.1 and M34641.1.
            Summary: The protein encoded by this gene is a member of the
            fibroblast growth factor receptor family, where amino acid sequence
            is highly conserved between members and throughout evolution. FGFR
            family members differ from one another in their ligand affinities
            and tissue distribution. A full-length representative protein
            consists of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member binds both acidic and basic fibroblast growth factors and is
            involved in limb induction. Mutations in this gene can lead to
            Pfeiffer syndrome and Jackson-Weiss syndrome. The genomic
            organization of this gene is very similar to family members 2-4,
            encompassing 19 exons that are subject to complex alternative
            splicing, which allows for structural, tissue expression and ligand
            affinity variations among the isoforms.
            Transcript Variant: This variant (1) uses alternatively spliced
            exon 9 to encode the IIIc-type carboxyl terminus for the third Ig
            domain, resulting in the longest isoform (1).
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.2-p11.1"
     Protein         1..822
                     /product="fibroblast growth factor receptor 1 isoform 1
                     precursor"
                     /EC_number="2.7.1.112"
                     /note="fms-related tyrosine kinase-2; heparin-binding
                     growth factor receptor; FMS-like tyrosine kinase 2; basic
                     fibroblast growth factor receptor 1; N-sam tyrosine
                     kinase; FLG protein; protein-tyrosine kinase;
                     tyrosylprotein kinase; hydroxyaryl-protein kinase"
     sig_peptide     1..21
     mat_peptide     22..822
                     /product="fibroblast growth factor receptor 1, isoform 1"
     Region          61..108
                     /region_name="smart00408, IGc2, Immunoglobulin C-2 Type"
     Region          168..247
                     /region_name="smart00409, IG, Immunoglobulin"
     Region          172..232
                     /region_name="pfam00047, ig, Immunoglobulin domain.
                     Members of the immunoglobulin superfamily are found in
                     hundreds of proteins of different functions. Examples
                     include antibodies, the giant muscle kinase titin and
                     receptor tyrosine kinases. Immunoglobulin-like domains may
                     be involved in protein-protein and protein-ligand
                     interactions. The Pfam alignments do not include the first
                     and last strand of the immunoglobulin-like domain"
     Region          173..237
                     /region_name="smart00408, IGc2, Immunoglobulin C-2 Type"
     Region          262..359
                     /region_name="smart00409, IG, Immunoglobulin"
     Region          270..348
                     /region_name="smart00408, IGc2, Immunoglobulin C-2 Type"
     Region          270..343
                     /region_name="pfam00047, ig, Immunoglobulin domain.
                     Members of the immunoglobulin superfamily are found in
                     hundreds of proteins of different functions. Examples
                     include antibodies, the giant muscle kinase titin and
                     receptor tyrosine kinases. Immunoglobulin-like domains may
                     be involved in protein-protein and protein-ligand
                     interactions. The Pfam alignments do not include the first
                     and last strand of the immunoglobulin-like domain"
     Region          478..754
                     /region_name="pfam00069, pkinase, Protein kinase domain"
     Region          478..754
                     /region_name="smart00219, TyrKc, Tyrosine kinase,
                     catalytic domain; Phosphotransferases. Tyrosine-specific
                     kinase subfamily"
     Region          480..753
                     /region_name="smart00220, S_TKc, erine/Threonine protein
                     kinases, catalytic domain; Phosphotransferases. Serine or
                     threonine-specific kinase subfamily"
     CDS             1..822
                     /gene="FGFR1"
                     /coded_by="NM_000604.2:727..3195"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="LocusID:2260"
                     /db_xref="MIM:136350"
ORIGIN      
        1 mwswkcllfw avlvtatlct arpsptlpeq aqpwgapvev esflvhpgdl lqlrcrlrdd
       61 vqsinwlrdg vqlaesnrtr itgeevevqd svpadsglya cvtsspsgsd ttyfsvnvsd
      121 alpssedddd dddssseeke tdntkpnrmp vapywtspek mekklhavpa aktvkfkcps
      181 sgtpnptlrw lkngkefkpd hriggykvry atwsiimdsv vpsdkgnytc iveneygsin
      241 htyqldvver sphrpilqag lpanktvalg snvefmckvy sdpqphiqwl khievngski
      301 gpdnlpyvqi lktagvnttd kemevlhlrn vsfedageyt clagnsigls hhsawltvle
      361 aleerpavmt splyleiiiy ctgafliscm vgsvivykmk sgtkksdfhs qmavhklaks
      421 iplrrqvtvs adssasmnsg vllvrpsrls ssgtpmlagv seyelpedpr welprdrlvl
      481 gkplgegcfg qvvlaeaigl dkdkpnrvtk vavkmlksda tekdlsdlis ememmkmigk
      541 hkniinllga ctqdgplyvi veyaskgnlr eylqarrppg leycynpshn peeqlsskdl
      601 vscayqvarg meylaskkci hrdlaarnvl vtednvmkia dfglardihh idyykkttng
      661 rlpvkwmape alfdriythq sdvwsfgvll weiftlggsp ypgvpveelf kllkeghrmd
      721 kpsnctnely mmmrdcwhav psqrptfkql vedldrival tsnqeyldls mpldqyspsf
      781 pdtrsstcss gedsvfshep lpeepclprh paqlangglk rr
//



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1: NP_000595. fibroblast growth...[gi:11276087] Links  


LOCUS       FGFR1                    822 aa            linear   PRI 27-AUG-2002
DEFINITION  fibroblast growth factor receptor 1 isoform 1 precursor;
            fms-related tyrosine kinase-2; heparin-binding growth factor
            receptor; FMS-like tyrosine kinase 2; basic fibroblast growth
            factor receptor 1; N-sam tyrosine kinase; FLG protein;
            protein-tyrosine kinase; tyrosylprotein kinase; hydroxyaryl-protein
            kinase [Homo sapiens].
ACCESSION   NP_000595
VERSION     NP_000595.1  GI:11276087
DBSOURCE    REFSEQ: aaccession NM_000604.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 822)
  AUTHORS   Ruta,M., Burgess,W., Givol,D., Epstein,J., Neiger,N., Kaplow,J.,
            Crumley,G., Dionne,C., Jaye,M. and Schlessinger,J.
  TITLE     Receptor for acidic fibroblast growth factor is related to the
            tyrosine kinase encoded by the fms-like gene (FLG)
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 86 (22), 8722-8726 (1989)
  MEDLINE   90046865
   PUBMED   2554327
REFERENCE   2  (residues 1 to 822)
  AUTHORS   Isacchi,A., Bergonzoni,L. and Sarmientos,P.
  TITLE     Complete sequence of a human receptor for acidic and basic
            fibroblast growth factors
  JOURNAL   Nucleic Acids Res. 18 (7), 1906 (1990)
  MEDLINE   90245600
   PUBMED   2159626
REFERENCE   3  (residues 1 to 822)
  AUTHORS   Itoh,N., Terachi,T., Ohta,M. and Seo,M.K.
  TITLE     The complete amino acid sequence of the shorter form of human basic
            fibroblast growth factor receptor deduced from its cDNA
  JOURNAL   Biochem. Biophys. Res. Commun. 169 (2), 680-685 (1990)
  MEDLINE   90290512
   PUBMED   2162671
REFERENCE   4  (residues 1 to 822)
  AUTHORS   Dionne,C.A., Crumley,G., Bellot,F., Kaplow,J.M., Searfoss,G.,
            Ruta,M., Burgess,W.H., Jaye,M. and Schlessinger,J.
  TITLE     Cloning and expression of two distinct high-affinity receptors
            cross-reacting with acidic and basic fibroblast growth factors
  JOURNAL   EMBO J. 9 (9), 2685-2692 (1990)
  MEDLINE   90360977
   PUBMED   1697263
REFERENCE   5  (residues 1 to 822)
  AUTHORS   Johnson,D.E., Lee,P.L., Lu,J. and Williams,L.T.
  TITLE     Diverse forms of a receptor for acidic and basic fibroblast growth
            factors
  JOURNAL   Mol. Cell. Biol. 10 (9), 4728-4736 (1990)
  MEDLINE   90355989
   PUBMED   2167437
REFERENCE   6  (residues 1 to 822)
  AUTHORS   Hou,J.Z., Kan,M.K., McKeehan,K., McBride,G., Adams,P. and
            McKeehan,W.L.
  TITLE     Fibroblast growth factor receptors from liver vary in three
            structural domains
  JOURNAL   Science 251 (4994), 665-668 (1991)
  MEDLINE   91126480
   PUBMED   1846977
REFERENCE   7  (residues 1 to 822)
  AUTHORS   Eisemann,A., Ahn,J.A., Graziani,G., Tronick,S.R. and Ron,D.
  TITLE     Alternative splicing generates at least five different isoforms of
            the human basic-FGF receptor
  JOURNAL   Oncogene 6 (7), 1195-1202 (1991)
  MEDLINE   91319400
   PUBMED   1650441
REFERENCE   8  (residues 1 to 822)
  AUTHORS   Johnson,D.E., Lu,J., Chen,H., Werner,S. and Williams,L.T.
  TITLE     The human fibroblast growth factor receptor genes: a common
            structural arrangement underlies the mechanisms for generating
            receptor forms that differ in their third immunoglobulin domain
  JOURNAL   Mol. Cell. Biol. 11 (9), 4627-4634 (1991)
  MEDLINE   91342665
   PUBMED   1652059
REFERENCE   9  (residues 1 to 822)
  AUTHORS   Crumley,G., Bellot,F., Kaplow,J.M., Schlessinger,J., Jaye,M. and
            Dionne,C.A.
  TITLE     High-affinity binding and activation of a truncated FGF receptor by
            both aFGF and bFGF
  JOURNAL   Oncogene 6 (12), 2255-2262 (1991)
  MEDLINE   92115326
   PUBMED   1722570
REFERENCE   10 (residues 1 to 822)
  AUTHORS   Wennstrom,S., Sandstrom,C. and Claesson-Welsh,L.
  TITLE     cDNA cloning and expression of a human FGF receptor which binds
            acidic and basic FGF
  JOURNAL   Growth Factors 4 (3), 197-208 (1991)
  MEDLINE   92118394
   PUBMED   1722683
REFERENCE   11 (residues 1 to 822)
  AUTHORS   Hattori,Y., Odagiri,H., Katoh,O., Sakamoto,H., Morita,T.,
            Shimotohno,K., Tobinai,K., Sugimura,T. and Terada,M.
  TITLE     K-sam-related gene, N-sam, encodes fibroblast growth factor
            receptor and is expressed in T-lymphocytic tumors
  JOURNAL   Cancer Res. 52 (12), 3367-3371 (1992)
  MEDLINE   92282615
   PUBMED   1317750
REFERENCE   12 (residues 1 to 822)
  AUTHORS   Johnson,D.E. and Williams,L.T.
  TITLE     Structural and functional diversity in the FGF receptor multigene
            family
  JOURNAL   Adv. Cancer Res. 60, 1-41 (1993)
  MEDLINE   93111178
   PUBMED   8417497
REFERENCE   13 (residues 1 to 822)
  AUTHORS   Muenke,M., Schell,U., Hehr,A., Robin,N.H., Losken,H.W.,
            Schinzel,A., Pulleyn,L.J., Rutland,P., Reardon,W., Malcolm,S. et
            al.
  TITLE     A common mutation in the fibroblast growth factor receptor 1 gene
            in Pfeiffer syndrome
  JOURNAL   Nat. Genet. 8 (3), 269-274 (1994)
  MEDLINE   95179173
   PUBMED   7874169
REFERENCE   14 (residues 1 to 822)
  AUTHORS   Wood,S., Schertzer,M. and Yaremko,M.L.
  TITLE     Sequence identity locates CEBPD and FGFR1 to mapped human loci
            within proximal 8p
  JOURNAL   Cytogenet. Cell Genet. 70 (3-4), 188-191 (1995)
  MEDLINE   95309017
   PUBMED   7789168
REFERENCE   15 (residues 1 to 822)
  AUTHORS   Wang,L.Y., Edenson,S.P., Yu,Y.L., Senderowicz,L. and Turck,C.W.
  TITLE     A natural kinase-deficient variant of fibroblast growth factor
            receptor 1
  JOURNAL   Biochemistry (N.Y.) 35 (31), 10134-10142 (1996)
  MEDLINE   96322333
   PUBMED   8756477
REFERENCE   16 (residues 1 to 822)
  AUTHORS   Lopez,M.E. and Korc,M.
  TITLE     A novel type I fibroblast growth factor receptor activates
            mitogenic signaling in the absence of detectable tyrosine
            phosphorylation of FRS2
  JOURNAL   J. Biol. Chem. 275 (21), 15933-15939 (2000)
  MEDLINE   20283622
   PUBMED   10748122
REFERENCE   17 (residues 1 to 822)
  AUTHORS   Hart,K.C., Robertson,S.C., Kanemitsu,M.Y., Meyer,A.N., Tynan,J.A.
            and Donoghue,D.J.
  TITLE     Transformation and Stat activation by derivatives of FGFR1, FGFR3,
            and FGFR4
  JOURNAL   Oncogene 19 (29), 3309-3320 (2000)
  MEDLINE   20374012
   PUBMED   10918587
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X66945.1 and M34641.1.
            Summary: The protein encoded by this gene is a member of the
            fibroblast growth factor receptor family, where amino acid sequence
            is highly conserved between members and throughout evolution. FGFR
            family members differ from one another in their ligand affinities
            and tissue distribution. A full-length representative protein
            consists of an extracellular region, composed of three
            immunoglobulin-like domains, a single hydrophobic membrane-spanning
            segment and a cytoplasmic tyrosine kinase domain. The extracellular
            portion of the protein interacts with fibroblast growth factors,
            setting in motion a cascade of downstream signals, ultimately
            influencing mitogenesis and differentiation. This particular family
            member binds both acidic and basic fibroblast growth factors and is
            involved in limb induction. Mutations in this gene can lead to
            Pfeiffer syndrome and Jackson-Weiss syndrome. The genomic
            organization of this gene is very similar to family members 2-4,
            encompassing 19 exons that are subject to complex alternative
            splicing, which allows for structural, tissue expression and ligand
            affinity variations among the isoforms.
            Transcript Variant: This variant (1) uses alternatively spliced
            exon 9 to encode the IIIc-type carboxyl terminus for the third Ig
            domain, resulting in the longest isoform (1).
FEATURES             Location/Qualifiers
     source          1..822
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="8"
                     /map="8p11.2-p11.1"
     Protein         1..822
                     /product="fibroblast growth factor receptor 1 isoform 1
                     precursor"
                     /EC_number="2.7.1.112"
                     /note="fms-related tyrosine kinase-2; heparin-binding
                     growth factor receptor; FMS-like tyrosine kinase 2; basic
                     fibroblast growth factor receptor 1; N-sam tyrosine
                     kinase; FLG protein; protein-tyrosine kinase;
                     tyrosylprotein kinase; hydroxyaryl-protein kinase"
     sig_peptide     1..21
     mat_peptide     22..822
                     /product="fibroblast growth factor receptor 1, isoform 1"
     Region          61..108
                     /region_name="smart00408, IGc2, Immunoglobulin C-2 Type"
     Region          168..247
                     /region_name="smart00409, IG, Immunoglobulin"
     Region          172..232
                     /region_name="pfam00047, ig, Immunoglobulin domain.
                     Members of the immunoglobulin superfamily are found in
                     hundreds of proteins of different functions. Examples
                     include antibodies, the giant muscle kinase titin and
                     receptor tyrosine kinases. Immunoglobulin-like domains may
                     be involved in protein-protein and protein-ligand
                     interactions. The Pfam alignments do not include the first
                     and last strand of the immunoglobulin-like domain"
     Region          173..237
                     /region_name="smart00408, IGc2, Immunoglobulin C-2 Type"
     Region          262..359
                     /region_name="smart00409, IG, Immunoglobulin"
     Region          270..348
                     /region_name="smart00408, IGc2, Immunoglobulin C-2 Type"
     Region          270..343
                     /region_name="pfam00047, ig, Immunoglobulin domain.
                     Members of the immunoglobulin superfamily are found in
                     hundreds of proteins of different functions. Examples
                     include antibodies, the giant muscle kinase titin and
                     receptor tyrosine kinases. Immunoglobulin-like domains may
                     be involved in protein-protein and protein-ligand
                     interactions. The Pfam alignments do not include the first
                     and last strand of the immunoglobulin-like domain"
     Region          478..754
                     /region_name="pfam00069, pkinase, Protein kinase domain"
     Region          478..754
                     /region_name="smart00219, TyrKc, Tyrosine kinase,
                     catalytic domain; Phosphotransferases. Tyrosine-specific
                     kinase subfamily"
     Region          480..753
                     /region_name="smart00220, S_TKc, erine/Threonine protein
                     kinases, catalytic domain; Phosphotransferases. Serine or
                     threonine-specific kinase subfamily"
     CDS             1..822
                     /gene="FGFR1"
                     /coded_by="NM_000604.2:727..3195"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="LocusID:2260"
                     /db_xref="MIM:136350"
ORIGIN      
        1 mwswkcllfw avlvtatlct arpsptlpeq aqpwgapvev esflvhpgdl lqlrcrlrdd
       61 vqsinwlrdg vqlaesnrtr itgeevevqd svpadsglya cvtsspsgsd ttyfsvnvsd
      121 alpssedddd dddssseeke tdntkpnrmp vapywtspek mekklhavpa aktvkfkcps
      181 sgtpnptlrw lkngkefkpd hriggykvry atwsiimdsv vpsdkgnytc iveneygsin
      241 htyqldvver sphrpilqag lpanktvalg snvefmckvy sdpqphiqwl khievngski
      301 gpdnlpyvqi lktagvnttd kemevlhlrn vsfedageyt clagnsigls hhsawltvle
      361 aleerpavmt splyleiiiy ctgafliscm vgsvivykmk sgtkksdfhs qmavhklaks
      421 iplrrqvtvs adssasmnsg vllvrpsrls ssgtpmlagv seyelpedpr welprdrlvl
      481 gkplgegcfg qvvlaeaigl dkdkpnrvtk vavkmlksda tekdlsdlis ememmkmigk
      541 hkniinllga ctqdgplyvi veyaskgnlr eylqarrppg leycynpshn peeqlsskdl
      601 vscayqvarg meylaskkci hrdlaarnvl vtednvmkia dfglardihh idyykkttng
      661 rlpvkwmape alfdriythq sdvwsfgvll weiftlggsp ypgvpveelf kllkeghrmd
      721 kpsnctnely mmmrdcwhav psqrptfkql vedldrival tsnqeyldls mpldqyspsf
      781 pdtrsstcss gedsvfshep lpeepclprh paqlangglk rr
//



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1: NP_000995. ribosomal protein...[gi:4506671] Links  


LOCUS       RPLP2                    115 aa            linear   PRI 27-AUG-2002
DEFINITION  ribosomal protein P2; 60S acidic ribosomal protein P2; acidic
            ribosomal phosphoprotein P2 [Homo sapiens].
ACCESSION   NP_000995
VERSION     NP_000995.1  GI:4506671
DBSOURCE    REFSEQ: aaccession NM_001004.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 115)
  AUTHORS   Rich,B.E. and Steitz,J.A.
  TITLE     Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
            cDNA clones, in vitro synthesis, and assembly
  JOURNAL   Mol. Cell. Biol. 7 (11), 4065-4074 (1987)
  MEDLINE   88122131
   PUBMED   3323886
REFERENCE   2  (residues 1 to 115)
  AUTHORS   Sharp,M.G., Adams,S.M., Elvin,P., Walker,R.A., Brammar,W.J. and
            Varley,J.M.
  TITLE     A sequence previously identified as metastasis-related encodes an
            acidic ribosomal phosphoprotein, P2
  JOURNAL   Br. J. Cancer 61 (1), 83-88 (1990)
  MEDLINE   90122586
   PUBMED   2153399
REFERENCE   3  (residues 1 to 115)
  AUTHORS   Hochstrasser,D.F., Frutiger,S., Paquet,N., Bairoch,A., Ravier,F.,
            Pasquali,C., Sanchez,J.C., Tissot,J.D., Bjellqvist,B., Vargas,R.,
            Appel,R.D. and Hughes,G.J.
  TITLE     Human liver protein map: a reference database established by
            microsequencing and gel comparison
  JOURNAL   Electrophoresis 13 (12), 992-1001 (1992)
  MEDLINE   93162045
   PUBMED   1286669
REFERENCE   4  (residues 1 to 115)
  AUTHORS   Matoba,R., Okubo,K., Hori,N., Fukushima,A. and Matsubara,K.
  TITLE     The addition of 5'-coding information to a 3'-directed cDNA library
            improves analysis of gene expression
  JOURNAL   Gene 146 (2), 199-207 (1994)
  MEDLINE   94357437
   PUBMED   8076819
REFERENCE   5  (residues 1 to 115)
  AUTHORS   Wool,I.G., Chan,Y.L. and Gluck,A.
  TITLE     Structure and evolution of mammalian ribosomal proteins
  JOURNAL   Biochem. Cell Biol. 73 (11-12), 933-947 (1995)
  MEDLINE   96282697
   PUBMED   8722009
  REMARK    This review focuses primarily on rat ribosomal proteins, but it
            compares them to human ribosomal proteins.
REFERENCE   6  (residues 1 to 115)
  AUTHORS   Uechi,T., Tanaka,T. and Kenmochi,N.
  TITLE     A complete map of the human ribosomal protein genes: assignment of
            80 genes to the cytogenetic map and implications for human
            disorders
  JOURNAL   Genomics 72 (3), 223-230 (2001)
  MEDLINE   21295043
   PUBMED   11401437
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC005354.1, BC005920.1 and
            BC007573.1.
            Summary: Ribosomes, the organelles that catalyze protein synthesis,
            consist of a small 40S subunit and a large 60S subunit. Together
            these subunits are composed of 4 RNA species and approximately 80
            structurally distinct proteins. This gene encodes a ribosomal
            phosphoprotein that is a component of the 60S subunit. The protein,
            which is a functional equivalent of the E. coli L7/L12 ribosomal
            protein, belongs to the L12P family of ribosomal proteins. It plays
            an important role in the elongation step of protein synthesis.
            Unlike most ribosomal proteins, which are basic, the encoded
            protein is acidic. Its C-terminal end is nearly identical to the
            C-terminal ends of the ribosomal phosphoproteins P0 and P1. The P2
            protein can interact with P0 and P1 to form a pentameric complex
            consisting of P1 and P2 dimers, and a P0 monomer. The protein is
            located in the cytoplasm. As is typical for genes encoding
            ribosomal proteins, there are multiple processed pseudogenes of
            this gene dispersed through the genome.
FEATURES             Location/Qualifiers
     source          1..115
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15.5-p15.4"
                     /clone="MGC:12453 IMAGE:4052568"
     Protein         1..115
                     /product="ribosomal protein P2"
                     /note="60S acidic ribosomal protein P2; acidic ribosomal
                     phosphoprotein P2"
     Region          1..62
                     /region_name="pfam00428, 60s_ribosomal, 60s Acidic
                     ribosomal protein. This family includes archaebacterial
                     L12, eukaryotic P0, P1 and P2"
     CDS             1..115
                     /gene="RPLP2"
                     /coded_by="NM_001004.2:77..424"
                     /db_xref="LocusID:6181"
                     /db_xref="MIM:180530"
ORIGIN      
        1 mryvasylla alggnsspsa kdikkildsv gieadddrln kviselngkn iedviaqgig
       61 klasvpagga vavsaapgsa apaagsapaa aeekkdekke eseesdddmg fglfd
//



Revised: July 5, 2002.
 
 


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1: NP_004336. cathelicidin anti...[gi:4757904] Links  


LOCUS       CAMP                     170 aa            linear   PRI 01-NOV-2000
DEFINITION  cathelicidin antimicrobial peptide [Homo sapiens].
ACCESSION   NP_004336
VERSION     NP_004336.1  GI:4757904
DBSOURCE    REFSEQ: aaccession NM_004345.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 170)
  AUTHORS   Agerberth,B., Gunne,H., Odeberg,J., Kogner,P., Boman,H.G. and
            Gudmundsson,G.H.
  TITLE     FALL-39, a putative human peptide antibiotic, is cysteine-free and
            expressed in bone marrow and testis
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 92 (1), 195-199 (1995)
  MEDLINE   95116523
   PUBMED   7529412
REFERENCE   2  (residues 1 to 170)
  AUTHORS   Larrick JW, Hirata M, Balint RF, Lee J, Zhong J and Wright SC.
  TITLE     Human CAP18: a novel antimicrobial lipopolysaccharide-binding
            protein
  JOURNAL   Infect. Immun. 63 (4), 1291-1297 (1995)
  MEDLINE   95197251
   PUBMED   7890387
REFERENCE   3  (residues 1 to 170)
  AUTHORS   Cowland JB, Johnsen AH and Borregaard N.
  TITLE     hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil
            specific granules
  JOURNAL   FEBS Lett. 368 (1), 173-176 (1995)
  MEDLINE   95339969
   PUBMED   7615076
REFERENCE   4  (residues 1 to 170)
  AUTHORS   Gudmundsson GH, Magnusson KP, Chowdhary BP, Johansson M, Andersson
            L and Boman HG.
  TITLE     Structure of the gene for porcine peptide antibiotic PR-39, a
            cathelin gene family member: comparative mapping of the locus for
            the human peptide antibiotic FALL-39
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 92 (15), 7085-7089 (1995)
  MEDLINE   95350216
   PUBMED   7624374
REFERENCE   5  (residues 1 to 170)
  AUTHORS   Gudmundsson GH, Agerberth B, Odeberg J, Bergman T, Olsson B and
            Salcedo R.
  TITLE     The human gene FALL39 and processing of the cathelin precursor to
            the antibacterial peptide LL-37 in granulocytes
  JOURNAL   Eur. J. Biochem. 238 (2), 325-332 (1996)
  MEDLINE   96283824
   PUBMED   8681941
REFERENCE   6  (residues 1 to 170)
  AUTHORS   Larrick JW, Lee J, Ma S, Li X, Francke U, Wright SC and Balint RF.
  TITLE     Structural, functional analysis and localization of the human CAP18
            gene
  JOURNAL   FEBS Lett. 398 (1), 74-80 (1996)
  MEDLINE   97102716
   PUBMED   8946956
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from Z38026.1.
FEATURES             Location/Qualifiers
     source          1..170
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21.3"
                     /clone="Hu7"
                     /tissue_type="Bone marrow"
                     /clone_lib="human bone marrow lambdagt11"
     Protein         1..170
                     /product="cathelicidin antimicrobial peptide"
     Region          32..98
                     /region_name="Cathelicidins"
                     /note="Cathelicidins"
                     /db_xref="CDD:pfam00666"
     mat_peptide     132..170
                     /product="cathelicidin antimicrobial peptide"
     CDS             1..170
                     /gene="CAMP"
                     /coded_by="NM_004345.1:12..524"
                     /db_xref="LocusID:820"
                     /db_xref="MIM:600474"
ORIGIN      
        1 mktqrnghsl grwslvllll glvmplaiia qvlsykeavl raidginqrs sdanlyrlld
       61 ldprptmdgd pdtpkpvsft vketvcprtt qqspedcdfk kdglvkrcmg tvtlnqargs
      121 fdiscdkdnk rfallgdffr kskekigkef krivqrikdf lrnlvprtes
//



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1: NP_002347. myristoylated ala...[gi:11125772] Links  


LOCUS       MARCKS                   332 aa            linear   PRI 27-AUG-2002
DEFINITION  myristoylated alanine-rich protein kinase C substrate; 80K-L;
            phosphomyristin; myristoylated alanine-rich protein kinase C
            substrate (MARCKS, 80K-L) [Homo sapiens].
ACCESSION   NP_002347
VERSION     NP_002347.4  GI:11125772
DBSOURCE    REFSEQ: aaccession NM_002356.4
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 332)
  AUTHORS   Harlan,D.M., Graff,J.M., Stumpo,D.J., Eddy,R.L. Jr., Shows,T.B.,
            Boyle,J.M. and Blackshear,P.J.
  TITLE     The human myristoylated alanine-rich C kinase substrate (MARCKS)
            gene (MACS). Analysis of its gene product, promoter, and
            chromosomal localization
  JOURNAL   J. Biol. Chem. 266 (22), 14399-14405 (1991)
  MEDLINE   91317795
   PUBMED   1860846
REFERENCE   2  (residues 1 to 332)
  AUTHORS   Hartwig,J.H., Thelen,M., Rosen,A., Janmey,P.A., Nairn,A.C. and
            Aderem,A.
  TITLE     MARCKS is an actin filament crosslinking protein regulated by
            protein kinase C and calcium-calmodulin
  JOURNAL   Nature 356 (6370), 618-622 (1992)
  MEDLINE   92220195
   PUBMED   1560845
REFERENCE   3  (sites)
  AUTHORS   Sakai,K., Hirai,M., Kudoh,J., Minoshima,S. and Shimizu,N.
  TITLE     Molecular cloning and chromosomal mapping of a cDNA encoding human
            80K-L protein: major substrate for protein kinase C
  JOURNAL   Genomics 14 (1), 175-178 (1992)
  MEDLINE   93052291
   PUBMED   1427823
REFERENCE   4  (residues 1 to 332)
  AUTHORS   Blackshear,P.J.
  TITLE     The MARCKS family of cellular protein kinase C substrates
  JOURNAL   J. Biol. Chem. 268 (3), 1501-1504 (1993)
  MEDLINE   93131879
   PUBMED   8420923
REFERENCE   5  (residues 1 to 332)
  AUTHORS   Taniguchi,H. and Manenti,S.
  TITLE     Interaction of myristoylated alanine-rich protein kinase C
            substrate (MARCKS) with membrane phospholipids
  JOURNAL   J. Biol. Chem. 268 (14), 9960-9963 (1993)
  MEDLINE   93252971
   PUBMED   8486722
REFERENCE   6  (residues 1 to 332)
  AUTHORS   Rao,P.H., Murty,V.V., Gaidano,G., Hauptschein,R., Dalla-Favera,R.
            and Chaganti,R.S.
  TITLE     Subregional mapping of 8 single copy loci to chromosome 6 by
            fluorescence in situ hybridization
  JOURNAL   Cytogenet. Cell Genet. 66 (4), 272-273 (1994)
  MEDLINE   94215320
   PUBMED   8162705
REFERENCE   7  (residues 1 to 332)
  AUTHORS   Aderem,A.
  TITLE     The MARCKS family of protein kinase-C substrates
  JOURNAL   Biochem. Soc. Trans. 23 (3), 587-591 (1995)
  MEDLINE   96077232
   PUBMED   8566422
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from D10522.1.
            On Nov 8, 2000 this sequence version replaced gi:11064247.
            Summary: The protein encoded by this gene is a substrate for
            protein kinase C. It is localized to the plasma membrane and is an
            actin filament crosslinking protein. Phosphorylation by protein
            kinase C or binding to calcium-calmodulin inhibits its association
            with actin and with the plasma membrane, leading to its presence in
            the cytoplasm. The protein is thought to be involved in cell
            motility, phagocytosis, membrane trafficking and mitogenesis.
FEATURES             Location/Qualifiers
     source          1..332
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6q22.2"
     Protein         1..332
                     /product="myristoylated alanine-rich protein kinase C
                     substrate"
                     /note="80K-L; phosphomyristin; myristoylated alanine-rich
                     protein kinase C substrate (MARCKS, 80K-L)"
     misc_feature    1..7
                     /note="myristoylation domain"
     misc_feature    152..176
                     /note="phosphorylation site domain"
     CDS             1..332
                     /gene="MARCKS"
                     /coded_by="NM_002356.4:370..1368"
                     /db_xref="LocusID:4082"
                     /db_xref="MIM:177061"
ORIGIN      
        1 mgaqfsktaa kgeaaaerpg eaavasspsk angqenghvk vngdaspaaa esgakeelqa
       61 ngsapaadke epaaagsgaa spssaekgep aaaaapeaga spvekeapae geaaepgsat
      121 aaegeaasaa sstsspkaed gatpspsnet pkkkkkrfsf kksfklsgfs fkknkkeage
      181 ggeaeapaae ggkdeaagga aaaaaeagaa sgeqaaapge eaaageegaa ggdpqeakpq
      241 eaavapekpp asdetkaaee pskveekkae eagasaaace apsaagpgap peqeaapaee
      301 paaaaassac aapsqeaqpe cspeappaea ae
//



Revised: July 5, 2002.
 
 


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1: NP_036515. osteoclast stimul...[gi:21361409] Links  


LOCUS       OSTF1                    217 aa            linear   PRI 10-JUN-2002
DEFINITION  osteoclast stimulating factor 1 [Homo sapiens].
ACCESSION   NP_036515
VERSION     NP_036515.2  GI:21361409
DBSOURCE    REFSEQ: aaccession NM_012383.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 217)
  AUTHORS   Strausberg,R.
  TITLE     Homo sapiens osteoclast stimulating factor 1 (OSTF1), mRNA
  JOURNAL   Unpublished (2001)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC007459.1.
            On Jun 10, 2002 this sequence version replaced gi:6912564.
FEATURES             Location/Qualifiers
     source          1..217
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q24.1-24.2"
                     /clone="MGC:12230 IMAGE:4052054"
                     /tissue_type="Kidney, hypernephroma"
                     /clone_lib="NIH_MGC_58"
                     /lab_host="DH10B"
                     /note="Vector: pDNR-LIB"
     Protein         1..217
                     /product="osteoclast stimulating factor 1"
     Region          20..71
                     /region_name="SH3 domain"
                     /note="SH3"
                     /db_xref="CDD:pfam00018"
     Region          20..71
                     /region_name="Src homology 3 domains"
                     /note="SH3"
                     /db_xref="CDD:smart00326"
     Region          109..141
                     /region_name="Ank repeat"
                     /note="ank"
                     /db_xref="CDD:pfam00023"
     Region          143..173
                     /region_name="Ank repeat"
                     /note="ank"
                     /db_xref="CDD:pfam00023"
     Region          143..167
                     /region_name="ankyrin repeats"
                     /note="ANK"
                     /db_xref="CDD:smart00248"
     CDS             1..217
                     /gene="OSTF1"
                     /coded_by="NM_012383.2:109..762"
                     /db_xref="LocusID:26578"
ORIGIN      
        1 mskpppkpvk pgeggqvkvf ralytfeprt pdelyfeegd iiyitdmsdt nwwkgtskgr
       61 tglipsnyva eqaesidnpl heaakrgnls wlrecldnrv gvngldkags talywachgg
      121 hkdivemlft qpnielnqqn klgdtalhaa awkgyadivq lflakgartd lrniekklaf
      181 dmatnaacas llkkkqgtda vrtlsnaedy lddedsd
//



Revised: July 5, 2002.
 
 


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1: NP_001701. complement factor...[gi:4502397] Links  


LOCUS       BF                       764 aa            linear   PRI 25-JUN-2001
DEFINITION  complement factor B preproprotein; B-factor, properdin; C3
            proactivator; C3 proaccelerator; glycine-rich beta-glycoprotein;
            C3/C5 convertase [Homo sapiens].
ACCESSION   NP_001701
VERSION     NP_001701.1  GI:4502397
DBSOURCE    REFSEQ: aaccession NM_001710.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 764)
  AUTHORS   Woods,D.E., Markham,A.F., Ricker,A.T., Goldberger,G. and
            Colten,H.R.
  TITLE     Isolation of cDNA clones for the human complement protein factor B,
            a class III major histocompatibility complex gene product
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 79 (18), 5661-5665 (1982)
  MEDLINE   83039428
   PUBMED   6957884
REFERENCE   2  (residues 1 to 764)
  AUTHORS   Campbell,R.D. and Porter,R.R.
  TITLE     Molecular cloning and characterization of the gene coding for human
            complement protein factor B
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 80 (14), 4464-4468 (1983)
  MEDLINE   83273641
   PUBMED   6308626
REFERENCE   3  (residues 1 to 764)
  AUTHORS   Morley,B.J. and Campbell,R.D.
  TITLE     Internal homologies of the Ba fragment from human complement
            component Factor B, a class III MHC antigen
  JOURNAL   EMBO J. 3 (1), 153-157 (1984)
  MEDLINE   84158524
   PUBMED   6323161
REFERENCE   4  (residues 1 to 764)
  AUTHORS   Mole,J.E., Anderson,J.K., Davison,E.A. and Woods,D.E.
  TITLE     Complete primary structure for the zymogen of human complement
            factor B
  JOURNAL   J. Biol. Chem. 259 (6), 3407-3412 (1984)
  MEDLINE   84161997
   PUBMED   6546754
REFERENCE   5  (residues 1 to 764)
  AUTHORS   Campbell RD, Bentley DR and Morley BJ.
  TITLE     The factor B and C2 genes
  JOURNAL   Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306 (1129), 367-378
            (1984)
  MEDLINE   85038857
   PUBMED   6149579
REFERENCE   6  (residues 1 to 764)
  AUTHORS   Campbell,R.D.
  TITLE     The molecular genetics and polymorphism of C2 and factor B
  JOURNAL   Br. Med. Bull. 43 (1), 37-49 (1987)
  MEDLINE   88051634
   PUBMED   3315100
REFERENCE   7  (residues 1 to 764)
  AUTHORS   Wu,L.C., Morley,B.J. and Campbell,R.D.
  TITLE     Cell-specific expression of the human complement protein factor B
            gene: evidence for the role of two distinct 5'-flanking elements
  JOURNAL   Cell 48 (2), 331-342 (1987)
  MEDLINE   87102880
   PUBMED   3643061
REFERENCE   8  (residues 1 to 764)
  AUTHORS   Davrinche,C., Abbal,M. and Clerc,A.
  TITLE     Molecular characterization of human complement factor B subtypes
  JOURNAL   Immunogenetics 32 (5), 309-312 (1990)
  MEDLINE   91065702
   PUBMED   2249879
REFERENCE   9  (residues 1 to 764)
  AUTHORS   Schwaeble,W., Luttig,B., Sokolowski,T., Estaller,C., Weiss,E.H.,
            Meyer zum Buschenfelde,K.H., Whaley,K. and Dippold,W.
  TITLE     Human complement factor B: functional properties of a recombinant
            zymogen of the alternative activation pathway convertase
  JOURNAL   Immunobiology 188 (3), 221-232 (1993)
  MEDLINE   94041399
   PUBMED   8225386
REFERENCE   10 (residues 1 to 764)
  AUTHORS   Horiuchi,T., Kim,S., Matsumoto,M., Watanabe,I., Fujita,S. and
            Volanakis,J.E.
  TITLE     Human complement factor B: cDNA cloning, nucleotide sequencing,
            phenotypic conversion by site-directed mutagenesis and expression
  JOURNAL   Mol. Immunol. 30 (17), 1587-1592 (1993)
  MEDLINE   94067177
   PUBMED   8247029
REFERENCE   11 (residues 1 to 764)
  AUTHORS   Mejia,J.E., Jahn,I., de la Salle,H. and Hauptmann,G.
  TITLE     Human factor B. Complete cDNA sequence of the BF*S allele
  JOURNAL   Hum. Immunol. 39 (1), 49-53 (1994)
  MEDLINE   94237735
   PUBMED   8181962
REFERENCE   12 (residues 1 to 764)
  AUTHORS   Yu CY.
  TITLE     Molecular genetics of the human MHC complement gene cluster
  JOURNAL   Exp. Clin. Immunogenet. 15 (4), 213-230 (1998)
  MEDLINE   99171993
   PUBMED   10072631
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L15702.1 and BC004143.1.
            Summary: This gene encodes complement factor B, a component of the
            alternative pathway of complement activation. Factor B circulates
            in the blood as a single chain polypeptide. Upon activation of the
            alternative pathway, it is cleaved by complement factor D yielding
            the noncatalytic chain Ba and the catalytic subunit Bb. The active
            subunit Bb is a serine protease which associates with C3b to form
            the alternative pathway C3 convertase. Bb is involved in the
            proliferation of preactivated B lymphocytes, while Ba inhibits
            their proliferation. This gene localizes to the major
            histocompatibility complex (MHC) class III region on chromosome 6.
            This cluster includes several genes involved in regulation of the
            immune reaction. The polyadenylation site of this gene is 421 bp
            from the 5' end of the gene for complement component 2.
FEATURES             Location/Qualifiers
     source          1..764
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.3"
     Protein         1..764
                     /product="complement factor B preproprotein"
                     /EC_number="3.4.21.47"
                     /note="B-factor, properdin; C3 proactivator; C3
                     proaccelerator; glycine-rich beta-glycoprotein; C3/C5
                     convertase"
     sig_peptide     1..25
     Proprotein      26..764
     mat_peptide     26..259
                     /product="Ba"
     variation       32
                     /allele="Q"
                     /allele="R"
                     /db_xref="dbSNP:641153"
     Region          55..83
                     /region_name="Domain abundant in complement control
                     proteins"
                     /note="CCP"
                     /db_xref="CDD:smart00032"
     Region          103..158
                     /region_name="Domain abundant in complement control
                     proteins"
                     /note="CCP"
                     /db_xref="CDD:smart00032"
     Region          103..158
                     /region_name="Sushi domain (SCR repeat)"
                     /note="sushi"
                     /db_xref="CDD:pfam00084"
     Region          165..218
                     /region_name="Domain abundant in complement control
                     proteins"
                     /note="CCP"
                     /db_xref="CDD:smart00032"
     Region          168..218
                     /region_name="Sushi domain (SCR repeat)"
                     /note="sushi"
                     /db_xref="CDD:pfam00084"
     mat_peptide     260..764
                     /product="Bb"
     Region          269..470
                     /region_name="von Willebrand factor (vWF) type A domain"
                     /note="VWA"
                     /db_xref="CDD:smart00327"
     Region          270..468
                     /region_name="von Willebrand factor type A domain"
                     /note="vwa"
                     /db_xref="CDD:pfam00092"
     variation       365
                     /allele="I"
                     /allele="M"
                     /db_xref="dbSNP:1803306"
     Region          488..751
                     /region_name="Trypsin-like serine protease"
                     /note="Tryp_SPc"
                     /db_xref="CDD:smart00020"
     Region          491..752
                     /region_name="Trypsin"
                     /note="trypsin"
                     /db_xref="CDD:pfam00089"
     CDS             1..764
                     /gene="BF"
                     /coded_by="NM_001710.2:130..2424"
                     /db_xref="LocusID:629"
                     /db_xref="MIM:138470"
                     /db_xref="LocusID:629"
                     /db_xref="MIM:138470"
ORIGIN      
        1 mgsnlspqlc lmpfilglls ggvtttpwsl aqpqgscsle gveikggsfr llqegqaley
       61 vcpsgfypyp vqtrtcrstg swstlktqdq ktvrkaecra ihcprphdfe ngeywprspy
      121 ynvsdeisfh cydgytlrgs anrtcqvngr wsgqtaicdn gagycsnpgi pigtrkvgsq
      181 yrledsvtyh csrgltlrgs qrrtcqeggs wsgtepscqd sfmydtpqev aeaflsslte
      241 tiegvdaedg hgpgeqqkrk ivldpsgsmn iylvldgsds igasnftgak kclvnliekv
      301 asygvkpryg lvtyatypki wvkvseadss nadwvtkqln einyedhklk sgtntkkalq
      361 avysmmswpd dvppegwnrt rhviilmtdg lhnmggdpit videirdlly igkdrknpre
      421 dyldvyvfgv gplvnqvnin alaskkdneq hvfkvkdmen ledvfyqmid esqslslcgm
      481 vwehrkgtdy hkqpwqakis virpskghes cmgavvseyf vltaahcftv ddkehsikvs
      541 vggekrdlei evvlfhpnyn ingkkeagip efydydvali klknklkygq tirpiclpct
      601 egttralrlp ptttcqqqke ellpaqdika lfvseeekkl trkevyikng dkkgscerda
      661 qyapgydkvk disevvtprf lctggvspya dpntcrgdsg gplivhkrsr fiqvgviswg
      721 vvdvcknqkr qkqvpahard fhinlfqvlp wlkeklqded lgfl
//



Revised: July 5, 2002.
 
 


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1: NP_001782. cell division cyc...[gi:4757952] Links  


LOCUS       CDC42                    191 aa            linear   PRI 07-SEP-2002
DEFINITION  cell division cycle 42 isoform 1; cell division cycle 42
            (GTP-binding protein, 25kD); GTP-binding protein, 25kD; cell
            division cycle 42 (GTP binding protein, 25kD) [Homo sapiens].
ACCESSION   NP_001782
VERSION     NP_001782.1  GI:4757952
DBSOURCE    REFSEQ: aaccession NM_001791.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 191)
  AUTHORS   Munemitsu,S., Innis,M.A., Clark,R., McCormick,F., Ullrich,A. and
            Polakis,P.
  TITLE     Molecular cloning and expression of a G25K cDNA, the human homolog
            of the yeast cell cycle gene CDC42
  JOURNAL   Mol. Cell. Biol. 10 (11), 5977-5982 (1990)
  MEDLINE   91042529
   PUBMED   2122236
REFERENCE   2  (residues 1 to 191)
  AUTHORS   Shinjo,K., Koland,J.G., Hart,M.J., Narasimhan,V., Johnson,D.I.,
            Evans,T. and Cerione,R.A.
  TITLE     Molecular cloning of the gene for the human placental GTP-binding
            protein Gp (G25K): identification of this GTP-binding protein as
            the human homolog of the yeast cell-division-cycle protein CDC42
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (24), 9853-9857 (1990)
  MEDLINE   91088610
   PUBMED   2124704
REFERENCE   3  (residues 1 to 191)
  AUTHORS   Hart,M.J., Eva,A., Evans,T., Aaronson,S.A. and Cerione,R.A.
  TITLE     Catalysis of guanine nucleotide exchange on the CDC42Hs protein by
            the dbl oncogene product
  JOURNAL   Nature 354 (6351), 311-314 (1991)
  MEDLINE   92065957
   PUBMED   1956381
REFERENCE   4  (residues 1 to 191)
  AUTHORS   Barron-Casella,E.A., Torres,M.A., Scherer,S.W., Heng,H.H.,
            Tsui,L.C. and Casella,J.F.
  TITLE     Sequence analysis and chromosomal localization of human Cap Z.
            Conserved residues within the actin-binding domain may link Cap Z
            to gelsolin/severin and profilin protein families
  JOURNAL   J. Biol. Chem. 270 (37), 21472-21479 (1995)
  MEDLINE   95394897
   PUBMED   7665558
REFERENCE   5  (residues 1 to 191)
  AUTHORS   Kim,A.S., Kakalis,L.T., Abdul-Manan,N., Liu,G.A. and Rosen,M.K.
  TITLE     Autoinhibition and activation mechanisms of the Wiskott-Aldrich
            syndrome protein
  JOURNAL   Nature 404 (6774), 151-158 (2000)
  MEDLINE   20186755
   PUBMED   10724160
REFERENCE   6  (residues 1 to 191)
  AUTHORS   Garrett,W.S., Chen,L.M., Kroschewski,R., Ebersold,M., Turley,S.,
            Trombetta,S., Galan,J.E. and Mellman,I.
  TITLE     Developmental control of endocytosis in dendritic cells by Cdc42
  JOURNAL   Cell 102 (3), 325-334 (2000)
  MEDLINE   20427263
   PUBMED   10975523
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M57298.1, AL121735.1 and
            BC003682.1.
            Summary: The protein encoded by this gene is a small GTPase of the
            Rho-subfamily, which regulates signaling pathways that control
            diverse cellular functions including cell morphology, migration,
            endocytosis and cell cycle progression. This protein is highly
            similar to Saccharomyces cerevisiae Cdc 42, and is able to
            complement the yeast cdc42-1 mutant. The product of oncogene Dbl
            was reported to specifically catalyze the dissociation of GDP from
            this protein. This protein could regulate actin polymerization
            through its direct binding to Neural Wiskott-Aldrich syndrome
            protein (N-WASP), which subsequently activates Arp2/3 complex.
            Alternative splicing of this gene results in at least two
            transcript variants.
            Transcript Variant: This variant (1) differs from variant 2 at the
            3' region including a small part of the coding region and the
            entire 3' UTR. This variant encodes isoform 1 which has the same aa
            length but different C-terminus from isoform 2.
FEATURES             Location/Qualifiers
     source          1..191
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.1"
     Protein         1..191
                     /product="cell division cycle 42 isoform 1"
                     /note="cell division cycle 42 (GTP-binding protein, 25kD);
                     cell division cycle 42 (GTP binding protein, 25kD)"
     Region          2..170
                     /region_name="pfam00025, arf, ADP-ribosylation factor
                     family"
     Region          3..181
                     /region_name="pfam00009, GTP_EFTU, Elongation factor Tu
                     GTP binding domain. This domain contains a P-loop motif,
                     also found in several other families such as pfam00071,
                     pfam00025 and pfam00063. Elongation factor Tu consists of
                     three structural domains, this plus two C-terminal beta
                     barrel domains"
     Region          4..171
                     /region_name="smart00175, RAB, Rab subfamily of small
                     GTPases; Rab GTPases are implicated in vesicle
                     trafficking"
     Region          5..187
                     /region_name="pfam00071, ras, Ras family. Includes
                     sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more.
                     Shares P-loop motif with GTP_EFTU, arf and myosin_head.
                     See pfam00009 pfam00025, pfam00063. The high cutoff is so
                     high to avoid overlaps with related families"
     Region          5..169
                     /region_name="smart00173, RAS, Ras subfamily of RAS small
                     GTPases; Similar in fold and function to the bacterial
                     EF-Tu GTPase. p21Ras couples receptor Tyr kinases and G
                     protein receptors to protein kinase cascades"
     Region          6..179
                     /region_name="smart00174, RHO, Rho (Ras homology)
                     subfamily of Ras-like small GTPases; Members of this
                     subfamily of Ras-like small GTPases include Cdc42 and Rac,
                     as well as Rho isoforms"
     Region          9..135
                     /region_name="smart00176, RAN, Ran (Ras-related nuclear
                     proteins) /TC4 subfamily of small GTPases; Ran is involved
                     in the active transport of proteins through nuclear pores"
     CDS             1..191
                     /gene="CDC42"
                     /coded_by="NM_001791.2:105..680"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="LocusID:998"
                     /db_xref="MIM:116952"
ORIGIN      
        1 mqtikcvvvg dgavgktcll isyttnkfps eyvptvfdny avtvmiggep ytlglfdtag
       61 qedydrlrpl sypqtdvflv cfsvvspssf envkekwvpe ithhcpktpf llvgtqidlr
      121 ddpstiekla knkqkpitpe taeklardlk avkyvecsal tqkglknvfd eailaalepp
      181 epkksrrcvl l
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_004906. ATP-binding casse...[gi:8051575] Links  


LOCUS       ABCG1                    674 aa            linear   PRI 03-FEB-2001
DEFINITION  ATP-binding cassette sub-family G member 1 isoform a; ATP-binding
            cassette 8 (homolog of Drosophila white); ABC transporter 8; white
            protein homolog (ATP-binding cassette transporter 8) [Homo
            sapiens].
ACCESSION   NP_004906
VERSION     NP_004906.2  GI:8051575
DBSOURCE    REFSEQ: aaccession NM_004915.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 674)
  AUTHORS   Andersson,B., Wentland,M.A., Ricafrente,J.Y., Liu,W. and Gibbs,R.A.
  TITLE     A 'double adaptor' method for improved shotgun library construction
  JOURNAL   Anal. Biochem. 236 (1), 107-113 (1996)
  MEDLINE   96207227
   PUBMED   8619474
REFERENCE   2  (residues 1 to 674)
  AUTHORS   Chen,H., Rossier,C., Lalioti,M.D., Lynn,A., Chakravarti,A.,
            Perrin,G. and Antonarakis,S.E.
  TITLE     Cloning of the cDNA for a human homologue of the Drosophila white
            gene and mapping to chromosome 21q22.3
  JOURNAL   Am. J. Hum. Genet. 59 (1), 66-75 (1996)
  MEDLINE   96256850
   PUBMED   8659545
REFERENCE   3  (residues 1 to 674)
  AUTHORS   Savary,S., Denizot,F., Luciani,M., Mattei,M. and Chimini,G.
  TITLE     Molecular cloning of a mammalian ABC transporter homologous to
            Drosophila white gene
  JOURNAL   Mamm. Genome 7 (9), 673-676 (1996)
  MEDLINE   96359154
   PUBMED   8703120
REFERENCE   4  (residues 1 to 674)
  AUTHORS   Croop,J.M., Tiller,G.E., Fletcher,J.A., Lux,M.L., Raab,E.,
            Goldenson,D., Son,D., Arciniegas,S. and Wu,R.L.
  TITLE     Isolation and characterization of a mammalian homolog of the
            Drosophila white gene
  JOURNAL   Gene 185 (1), 77-85 (1997)
  MEDLINE   97186700
   PUBMED   9034316
REFERENCE   5  (residues 1 to 674)
  AUTHORS   Yu,W., Andersson,B., Worley,K.C., Muzny,D.M., Ding,Y., Liu,W.,
            Ricafrente,J.Y., Wentland,M.A., Lennon,G. and Gibbs,R.A.
  TITLE     Large-scale concatenation cDNA sequencing
  JOURNAL   Genome Res. 7 (4), 353-358 (1997)
  MEDLINE   97264341
   PUBMED   9110174
REFERENCE   6  (residues 1 to 674)
  AUTHORS   Klucken,J., Buchler,C., Orso,E., Kaminski,W.E.,
            Porsch-Ozcurumez,M., Liebisch,G., Kapinsky,M., Diederich,W.,
            Drobnik,W., Dean,M., Allikmets,R. and Schmitz,G.
  TITLE     ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a
            regulator of macrophage cholesterol and phospholipid transport
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 97 (2), 817-822 (2000)
  MEDLINE   20105556
   PUBMED   10639163
REFERENCE   7  (residues 1 to 674)
  AUTHORS   Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS,
            Toyoda A, Ishii K, Totoki Y, Choi DK, Soeda E, Ohki M, Takagi T,
            Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J,
            Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M
            and Schudy A.
  TITLE     The DNA sequence of human chromosome 21
  JOURNAL   Nature 405 (6784), 311-319 (2000)
  MEDLINE   20289799
   PUBMED   10830953
REFERENCE   8  (residues 1 to 674)
  AUTHORS   Langmann T, Porsch-Ozcurumez M, Unkelbach U, Klucken J and Schmitz
            G.
  TITLE     Genomic organization and characterization of the promoter of the
            human ATP-binding cassette transporter-G1 (ABCG1) gene(1)
  JOURNAL   Biochim. Biophys. Acta 1494 (1-2), 175-180 (2000)
  MEDLINE   20525454
   PUBMED   11072082
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X91249.1.
            On May 24, 2000 this sequence version replaced gi:4759318.
            Summary: The protein encoded by this gene is a member of the
            superfamily of ATP-binding cassette (ABC) transporters. ABC
            proteins transport various molecules across extra- and
            intra-cellular membranes. ABC genes are divided into seven distinct
            subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This
            protein is a member of the White subfamily. It is involved in
            macrophage cholesterol efflux and may regulate cellular lipid
            homeostasis in other cell types. Several alternative splice
            variants have been identified.
            Transcript Variant: This splice variant (1) includes the
            dodecapeptide sequence absent in splice variant 2.
FEATURES             Location/Qualifiers
     source          1..674
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="21"
                     /map="21q22.3"
     Protein         1..674
                     /product="ATP-binding cassette sub-family G member 1
                     isoform a"
                     /note="isoform a is encoded by transcript variant 1;
                     ATP-binding cassette 8 (homolog of Drosophila white); ABC
                     transporter 8; white protein homolog (ATP-binding cassette
                     transporter 8)"
     Region          106..204
                     /region_name="ATPases associated with a variety of
                     cellular activities"
                     /note="AAA"
                     /db_xref="CDD:AAA"
     Region          107..199
                     /region_name="ABC transporter"
                     /note="ABC_tran"
                     /db_xref="CDD:pfam00005"
     Region          151..261
                     /region_name="ATPases associated with a variety of
                     cellular activities"
                     /note="AAA"
                     /db_xref="CDD:AAA"
     Region          169..289
                     /region_name="ABC transporter"
                     /note="ABC_tran"
                     /db_xref="CDD:pfam00005"
     Region          371..382
                     /region_name="dodecapeptide"
                     /note="deleted in transcript variant 2"
     CDS             1..674
                     /gene="ABCG1"
                     /coded_by="NM_004915.2:31..2055"
                     /db_xref="LocusID:9619"
                     /db_xref="MIM:603076"
ORIGIN      
        1 maafsvgtam nassysaemt epksvcvsvd evvssnmeat etdllnghlk kvdnnlteaq
       61 rfsslprraa vniefrdlsy svpegpwwrk kgyktllkgi sgkfnsgelv aimgpsgagk
      121 stlmnilagy retgmkgavl inglprdlrc frkvscyimq ddmllphltv qeammvsahl
      181 klqekdegrr emvkeiltal gllscantrt gslsggqrkr laialelvnn ppvmffdept
      241 sgldsascfq vvslmkglaq ggrsiictih qpsaklfelf dqlyvlsqgq cvyrgkvcnl
      301 vpylrdlgln cptyhnpadf vmevasgeyg dqnsrlvrav regmcdsdhk rdlggdaevn
      361 pflwhrpsee vkqtkrlkgl rkdsssmegc hsfsascltq fcilfkrtfl simrdsvlth
      421 lritshigig lligllylgi gnetkkvlsn sgflffsmlf lmfaalmptv ltfplemgvf
      481 lrehlnywys lkayylaktm advpfqimfp vaycsivywm tsqpsdavrf vlfaalgtmt
      541 slvaqslgll igaastslqv atfvgpvtai pvllfsgffv sfdtiptylq wmsyisyvry
      601 gfegvilsiy gldredlhcd idetchfqks eailreldve naklyldfiv lgiffislrl
      661 iaylvlryki raer
//



Revised: July 5, 2002.
 
 


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1: NP_004338. caspase 5, precur...[gi:4757914] Links  


LOCUS       CASP5                    418 aa            linear   PRI 22-OCT-2001
DEFINITION  caspase 5, precursor; TY protease; apoptosis-related cysteine
            protease; ICH-3 protease [Homo sapiens].
ACCESSION   NP_004338
VERSION     NP_004338.1  GI:4757914
DBSOURCE    REFSEQ: aaccession NM_004347.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Munday,N.A., Vaillancourt,J.P., Ali,A., Casano,F.J., Miller,D.K.,
            Molineaux,S.M., Yamin,T.T., Yu,V.L. and Nicholson,D.W.
  TITLE     Molecular cloning and pro-apoptotic activity of ICErelII and
            ICErelIII, members of the ICE/CED-3 family of cysteine proteases
  JOURNAL   J. Biol. Chem. 270 (26), 15870-15876 (1995)
  MEDLINE   95318183
   PUBMED   7797592
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Nasir,J., Theilmann,J.L., Vaillancourt,J.P., Munday,N.A., Ali,A.,
            Scherer,S., Beatty,B., Nicholson,D.W. and Hayden,M.R.
  TITLE     Interleukin-1beta-converting enzyme (ICE) and related cell death
            genes ICErel-II and ICErel-III map to the same PAC clone at band
            11q22.2-22.3
  JOURNAL   Mamm. Genome 8 (8), 611-613 (1997)
  MEDLINE   97398501
   PUBMED   9250871
REFERENCE   3  (residues 1 to 418)
  AUTHORS   Lin,X.Y., Choi,M.S. and Porter,A.G.
  TITLE     Expression analysis of the human caspase-1 subfamily reveals
            specific regulation of the CASP5 gene by lipopolysaccharide and
            interferon-gamma
  JOURNAL   J. Biol. Chem. 275 (51), 39920-39926 (2000)
  MEDLINE   20568240
   PUBMED   10986288
REFERENCE   4  (residues 1 to 418)
  AUTHORS   Krippner-Heidenreich,A., Talanian,R.V., Sekul,R., Kraft,R.,
            Thole,H., Ottleben,H. and Luscher,B.
  TITLE     Targeting of the transcription factor Max during apoptosis:
            phosphorylation-regulated cleavage by caspase-5 at an unusual
            glutamic acid residue in position P1
  JOURNAL   Biochem. J. 358 (Pt 3), 705-715 (2001)
  MEDLINE   21426411
   PUBMED   11535131
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U28015.1.
            Summary: This gene encodes a member of the cysteine-aspartic acid
            protease (caspase) family. Sequential activation of caspases plays
            a central role in the execution-phase of cell apoptosis. Caspases
            exist as inactive proenzymes which undergo proteolytic processing
            at conserved aspartic residues to produce 2 subunits, large and
            small, that dimerize to form the active enzyme. Overexpression of
            the active form of this enzyme has been shown to induce apoptosis
            in fibroblasts. Max, a central component of the Myc/Max/Mad
            transcription regulation network important for cell growth,
            differentiation, and apoptosis, was reported to be cleaved by this
            protein, which required Fas-mediated dephosphorylation of Max. The
            expression of this gene was found to be regulated by
            interferon-gamma and lipopolysaccharide.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11q22.2-q22.3"
     Protein         1..418
                     /product="caspase 5, precursor"
                     /note="TY protease; apoptosis-related cysteine protease;
                     ICH-3 protease"
     Region          55..130
                     /region_name="Caspase recruitment domain"
                     /note="CARD"
                     /db_xref="CDD:smart00114"
     Region          55..130
                     /region_name="Caspase recruitment domain. Motif contained
                     in proteins involved in apoptotic signaling. Predicted to
                     possess a DEATH (pfam00531) domain-like fold"
                     /note="CARD"
                     /db_xref="CDD:pfam00619"
     mat_peptide     122..311
                     /product="CASP5, large subunit"
     Region          166..416
                     /region_name="Caspase, interleukin-1 beta converting
                     enzyme (ICE) homologues"
                     /note="CASc"
                     /db_xref="CDD:smart00115"
     Region          175..306
                     /region_name="ICE-like protease (caspase) p20 domain"
                     /note="ICE_p20"
                     /db_xref="CDD:pfam00656"
     mat_peptide     331..418
                     /product="CASP5, small subunit"
     Region          334..416
                     /region_name="ICE-like protease (caspase) p10 domain"
                     /note="ICE_p10"
                     /db_xref="CDD:pfam00655"
     CDS             1..418
                     /gene="CASP5"
                     /coded_by="NM_004347.1:35..1291"
                     /db_xref="LocusID:838"
                     /db_xref="MIM:602665"
                     /db_xref="LocusID:838"
                     /db_xref="MIM:602665"
ORIGIN      
        1 mfkgilqsgl dnfvinhmlk nnvagqtsiq tlvpntdqks tsvkkdnhkk ktvkmleylg
       61 kdvlhgvfny lakhdvltlk eeekkkyyda kiedkalilv dslrknrvah qmftqtllnm
      121 dqkitsvkpl lqieagppes aestnilklc preeflrlck knhdeiypik kredrrrlal
      181 iicntkfdhl parngahydi vgmkrllqgl gytvvdeknl tardmesvlr afaarpehks
      241 sdstflvlms hgilegicgt ahkkkkpdvl lydtifqifn nrnclslkdk pkviivqacr
      301 gekhgelwvr dspaslavis sqssenlead svckiheekd fiafcsstph nvswrdrtrg
      361 sifitelitc fqkysccchl meifrkvqks fevpqakaqm ptieratltr dfylfpgn
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_055104. calpain 6; calpai...[gi:13186316] Links  


LOCUS       CAPN6                    641 aa            linear   PRI 27-AUG-2002
DEFINITION  calpain 6; calpain-like protease; calpamodulin [Homo sapiens].
ACCESSION   NP_055104
VERSION     NP_055104.2  GI:13186316
DBSOURCE    REFSEQ: aaccession NM_014289.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 641)
  AUTHORS   Sorimachi,H., Saido,T.C. and Suzuki,K.
  TITLE     New era of calpain research. Discovery of tissue-specific calpains
  JOURNAL   FEBS Lett. 343 (1), 1-5 (1994)
  MEDLINE   94215696
   PUBMED   8163008
REFERENCE   2  (residues 1 to 641)
  AUTHORS   Dear,N., Matena,K., Vingron,M. and Boehm,T.
  TITLE     A new subfamily of vertebrate calpains lacking a calmodulin-like
            domain: implications for calpain regulation and evolution
  JOURNAL   Genomics 45 (1), 175-184 (1997)
  MEDLINE   97480729
   PUBMED   9339374
REFERENCE   3  (residues 1 to 641)
  AUTHORS   Matena,K., Boehm,T. and Dear,N.
  TITLE     Genomic organization of mouse Capn5 and Capn6 genes confirms that
            they are a distinct calpain subfamily
  JOURNAL   Genomics 48 (1), 117-120 (1998)
  MEDLINE   98163754
   PUBMED   9503024
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AL031117.1.
            On Mar 2, 2001 this sequence version replaced gi:7656957.
            Summary: Calpains are ubiquitous, well-conserved family of
            calcium-dependent, cysteine proteases. The calpain proteins are
            heterodimers consisting of an invariant small subunit and variable
            large subunits. The large subunit possesses a cysteine protease
            domain, and both subunits possess calcium-binding domains. Calpains
            have been implicated in neurodegenerative processes, as their
            activation can be triggered by calcium influx and oxidative stress.
            The protein encoded by this gene is highly expressed in the
            placenta. Its C-terminal region lacks any homology to the
            calmodulin-like domain of other calpains. It also lacks critical
            active site residues and thus is suggested to be proteolytically
            inactive.
FEATURES             Location/Qualifiers
     source          1..641
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq23"
     Protein         1..641
                     /product="calpain 6"
                     /EC_number="3.4.22.17"
                     /note="calpain-like protease; calpamodulin"
     Region          8..350
                     /region_name="smart00230, CysPc, Calpain-like thiol
                     protease family; Calpain-like thiol protease family
                     (peptidase family C2). Calcium activated neutral protease
                     (large subunit)"
     Region          26..340
                     /region_name="pfam00648, Peptidase_C2, Calpain family
                     cysteine protease"
     Region          350..495
                     /region_name="pfam01067, Calpain_III, Calpain large
                     subunit, domain III. The function of the domain III and I
                     are currently unknown. Domain II is a cysteine protease
                     and domain IV is a calcium binding domain. Calpains are
                     believed to participate in intracellular signaling
                     pathways mediated by calcium ions"
     Region          350..493
                     /region_name="smart00720, calpain_III, calpain_III domain"
     Region          520..599
                     /region_name="smart00239, C2, Protein kinase C conserved
                     region 2 (CalB); Ca2+-binding motif present in
                     phospholipases, protein kinases C, and synaptotamins
                     (among others). Some do not appear to contain Ca2+-binding
                     sites. Particular C2s appear to bind phospholipids,
                     inositol polyphosphates, and intracellular proteins.
                     Unusual occurrence in perforin. Synaptotagmin and PLC C2s
                     are permuted in sequence with respect to N- and C-terminal
                     beta strands. SMART detects C2 domains using one or both
                     of two profiles"
     Region          520..597
                     /region_name="pfam00168, C2, C2 domain"
     CDS             1..641
                     /gene="CAPN6"
                     /coded_by="NM_014289.2:169..2094"
                     /db_xref="LocusID:827"
                     /db_xref="MIM:300146"
ORIGIN      
        1 mgpplklfkn qkyqelkqec ikdsrlfcdp tflpendslf ynrllpgkvv wkrpqdicdd
       61 phlivgnisn hqltqgrlgh kpmvsafscl avqeshwtkt ipnhkeqewd pqktekyagi
      121 fhfrfwhfge wtevviddll ptingdlvfs fstsmnefwn allekayakl lgcyealdgl
      181 titdiivdft gtlaetvdmq kgrytelvee kyklfgelyk tftkgglicc siespnqeeq
      241 evetdwgllk ghtytmtdir kirlgerlve vfsaekvymv rlrnplgrqe wsgpwseise
      301 ewqqltasdr knlglvmsdd gefwmsledf crnfhklnvc rnvnnpifgr kelesvlgcw
      361 tvdddplmnr sggcynnrdt flqnpqyift vpedghkvim slqqkdlrty rrmgrpdnyi
      421 igfelfkvem nrkfrlhhly iqeragtsty idtrtvflsk ylkkgnyvlv ptmfqhgrts
      481 efllrifsev pvqlreltld mpkmscwnla rgypkvvtqi tvhsaedlek kyanetvnpy
      541 lvikcgkeev rspvqkntvh aifdtqaify rrttdipiiv qvwnsrkfcd qflgqvtlda
      601 dpsdcrdlks lylrkkggpt akvkqghisf kvissddlte l
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_054883. FXYD domain-conta...[gi:21618361] Links  


LOCUS       FXYD5                    178 aa            linear   PRI 27-AUG-2002
DEFINITION  FXYD domain-containing ion transport regulator 5; dysadherin [Homo
            sapiens].
ACCESSION   NP_054883
VERSION     NP_054883.3  GI:21618361
DBSOURCE    REFSEQ: aaccession NM_014164.3
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Adams,M.D., Kerlavage,A.R., Fleischmann,R.D., Fuldner,R.A.,
            Bult,C.J., Lee,N.H., Kirkness,E.F., Weinstock,K.G., Gocayne,J.D.,
            White,O. et al.
  TITLE     Initial assessment of human gene diversity and expression patterns
            based upon 83 million nucleotides of cDNA sequence
  JOURNAL   Nature 377 (6547 Suppl), 3-174 (1995)
  MEDLINE   96026280
   PUBMED   7566098
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Sweadner,K.J. and Rael,E.
  TITLE     The FXYD gene family of small ion transport regulators or channels:
            cDNA sequence, protein signature sequence, and expression
  JOURNAL   Genomics 68 (1), 41-56 (2000)
  MEDLINE   20408885
   PUBMED   10950925
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Zhang,Q.H., Ye,M., Wu,X.Y., Ren,S.X., Zhao,M., Zhao,C.J., Fu,G.,
            Shen,Y., Fan,H.Y., Lu,G., Zhong,M., Xu,X.R., Han,Z.G., Zhang,J.W.,
            Tao,J., Huang,Q.H., Zhou,J., Hu,G.X., Gu,J., Chen,S.J. and Chen,Z.
  TITLE     Cloning and functional analysis of cDNAs with open reading frames
            for 300 previously undefined genes expressed in CD34+ hematopoietic
            stem/progenitor cells
  JOURNAL   Genome Res. 10 (10), 1546-1560 (2000)
  MEDLINE   20499367
   PUBMED   11042152
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Omasa,T., Chen,Y.G., Mantalaris,A. and Wu,J.H.
  TITLE     A cDNA from human bone marrow encoding a protein exhibiting
            homology to the ATP1gamma1/PLM/MAT8 family of transmembrane
            proteins
  JOURNAL   Biochim. Biophys. Acta 1517 (2), 307-310 (2001)
  MEDLINE   21240216
   PUBMED   11342114
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF161462.1, AA044211.1,
            AA296696.1 and BG025158.1.
            On Jun 27, 2002 this sequence version replaced gi:11612665.
            Summary: This reference sequence was derived from AF161462.1 and
            ESTs; validated by multiple replicate ESTs and human genomic
            sequence. This gene encodes a member of a family of small membrane
            proteins that share a 35-amino acid signature sequence domain,
            beginning with the sequence PFXYD and containing 7 invariant and 6
            highly conserved amino acids. The approved human gene nomenclature
            for the family is FXYD-domain containing ion transport regulator.
            Mouse FXYD5 has been termed RIC (Related to Ion Channel). FXYD2,
            also known as the gamma subunit of the Na,K-ATPase, regulates the
            properties of that enzyme. FXYD1 (phospholemman), FXYD2 (gamma),
            FXYD3 (MAT-8), FXYD4 (CHIF), and FXYD5 (RIC) have been shown to
            induce channel activity in experimental expression systems.
            Transmembrane topology has been established for two family members
            (FXYD1 and FXYD2), with the N-terminus extracellular and the
            C-terminus on the cytoplasmic side of the membrane. This gene
            product, FXYD5, has not been characterized as a protein. [RefSeq
            curation by Kathleen J. Sweadner, Ph.D.,
            sweadner@helix.mgh.harvard.edu.].
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q12-q13.1"
     Protein         1..178
                     /product="FXYD domain-containing ion transport regulator
                     5"
                     /note="dysadherin"
     variation       35
                     /allele="A"
                     /allele="S"
                     /db_xref="dbSNP:1688005"
     Region          131..176
                     /region_name="pfam02038, ATP1G1_PLM_MAT8, ATP1G1/PLM/MAT8
                     family"
     Region          135..168
                     /region_name="FXYD domain"
     variation       176
                     /allele="H"
                     /allele="R"
                     /db_xref="dbSNP:12110"
     CDS             1..178
                     /gene="FXYD5"
                     /coded_by="NM_014164.3:143..679"
                     /db_xref="LocusID:53827"
                     /db_xref="MIM:606669"
ORIGIN      
        1 mspsgrlcll tivglilptr gqtlkdttss ssadstimdi qvptrapdav ytelqptspt
       61 ptwpadetpq pqtqtqqleg tdgplvtdpe thkstkaahp tddtttlser pspstdvqtd
      121 pqtlkpsgfh eddpffydeh tlrkrgllva avlfitgiii ltsgkcrqls rlcrnrcr
//



Revised: July 5, 2002.
 
 


Disclaimer | Write to the Help Desk
NCBI | NLM | NIH 

 

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   Search PubMed Protein Nucleotide PopSet Taxonomy Genome OMIM Structure Domains GEO Books Books2 MapViewDr TestDb UniSTS CDD SNP Journals UniGene  for        
 
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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_000600. stromal cell-deri...[gi:10834988] Links  


LOCUS       SDF1                      93 aa            linear   PRI 28-AUG-2002
DEFINITION  stromal cell-derived factor 1 [Homo sapiens].
ACCESSION   NP_000600
VERSION     NP_000600.1  GI:10834988
DBSOURCE    REFSEQ: aaccession NM_000609.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 93)
  AUTHORS   Shirozu,M., Nakano,T., Inazawa,J., Tashiro,K., Tada,H.,
            Shinohara,T. and Honjo,T.
  TITLE     Structure and chromosomal localization of the human stromal
            cell-derived factor 1 (SDF1) gene
  JOURNAL   Genomics 28 (3), 495-500 (1995)
  MEDLINE   96039262
   PUBMED   7490086
REFERENCE   2  (residues 1 to 93)
  AUTHORS   Bleul,C.C., Farzan,M., Choe,H., Parolin,C., Clark-Lewis,I.,
            Sodroski,J. and Springer,T.A.
  TITLE     The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin
            and blocks HIV-1 entry
  JOURNAL   Nature 382 (6594), 829-833 (1996)
  MEDLINE   96351077
   PUBMED   8752280
REFERENCE   3  (residues 1 to 93)
  AUTHORS   Rubbert,A., Combadiere,C., Ostrowski,M., Arthos,J., Dybul,M.,
            Machado,E., Cohn,M.A., Hoxie,J.A., Murphy,P.M., Fauci,A.S. and
            Weissman,D.
  TITLE     Dendritic cells express multiple chemokine receptors used as
            coreceptors for HIV entry
  JOURNAL   J. Immunol. 160 (8), 3933-3941 (1998)
  MEDLINE   98217183
   PUBMED   9558100
REFERENCE   4  (residues 1 to 93)
  AUTHORS   Zaitseva,M.B., Lee,S., Rabin,R.L., Tiffany,H.L., Farber,J.M.,
            Peden,K.W., Murphy,P.M. and Golding,H.
  TITLE     CXCR4 and CCR5 on human thymocytes: biological function and role in
            HIV-1 infection
  JOURNAL   J. Immunol. 161 (6), 3103-3113 (1998)
  MEDLINE   98414309
   PUBMED   9743377
REFERENCE   5  (residues 1 to 93)
  AUTHORS   Weber,K.S., Klickstein,L.B. and Weber,C.
  TITLE     Specific activation of leukocyte beta2 integrins lymphocyte
            function-associated antigen-1 and Mac-1 by chemokines mediated by
            distinct pathways via the alpha subunit cytoplasmic domains
  JOURNAL   Mol. Biol. Cell 10 (4), 861-873 (1999)
  MEDLINE   99213982
   PUBMED   10198043
REFERENCE   6  (residues 1 to 93)
  AUTHORS   Su,S.B., Gong,W., Grimm,M., Utsunomiya,I., Sargeant,R.,
            Oppenheim,J.J. and Ming Wang,J.
  TITLE     Inhibition of tyrosine kinase activation blocks the down-regulation
            of CXC chemokine receptor 4 by HIV-1 gp120 in CD4+ T cells
  JOURNAL   J. Immunol. 162 (12), 7128-7132 (1999)
  MEDLINE   99288069
   PUBMED   10358157
REFERENCE   7  (residues 1 to 93)
  AUTHORS   Kozak,S.L., Kuhmann,S.E., Platt,E.J. and Kabat,D.
  TITLE     Roles of CD4 and coreceptors in binding, endocytosis, and
            proteolysis of gp120 envelope glycoproteins derived from human
            immunodeficiency virus type 1
  JOURNAL   J. Biol. Chem. 274 (33), 23499-23507 (1999)
  MEDLINE   99367483
   PUBMED   10438529
REFERENCE   8  (residues 1 to 93)
  AUTHORS   Vicente-Manzanares,M., Rey,M., Jones,D.R., Sancho,D., Mellado,M.,
            Rodriguez-Frade,J.M., del Pozo,M.A., Yanez-Mo,M., de Ana,A.M.,
            Martinez-A,C., Merida,I. and Sanchez-Madrid,F.
  TITLE     Involvement of phosphatidylinositol 3-kinase in stromal
            cell-derived factor-1 alpha-induced lymphocyte polarization and
            chemotaxis
  JOURNAL   J. Immunol. 163 (7), 4001-4012 (1999)
  MEDLINE   99421856
   PUBMED   10491003
REFERENCE   9  (residues 1 to 93)
  AUTHORS   Sotsios,Y., Whittaker,G.C., Westwick,J. and Ward,S.G.
  TITLE     The CXC chemokine stromal cell-derived factor activates a
            Gi-coupled phosphoinositide 3-kinase in T lymphocytes
  JOURNAL   J. Immunol. 163 (11), 5954-5963 (1999)
  MEDLINE   20040387
   PUBMED   10570282
REFERENCE   10 (residues 1 to 93)
  AUTHORS   Lalani,A.S., Masters,J., Zeng,W., Barrett,J., Pannu,R., Everett,H.,
            Arendt,C.W. and McFadden,G.
  TITLE     Use of chemokine receptors by poxviruses
  JOURNAL   Science 286 (5446), 1968-1971 (1999)
  MEDLINE   20050961
   PUBMED   10583963
REFERENCE   11 (residues 1 to 93)
  AUTHORS   Luttichau,H.R., Stine,J., Boesen,T.P., Johnsen,A.H., Chantry,D.,
            Gerstoft,J. and Schwartz,T.W.
  TITLE     A highly selective CC chemokine receptor (CCR)8 antagonist encoded
            by the poxvirus molluscum contagiosum
  JOURNAL   J. Exp. Med. 191 (1), 171-180 (2000)
  MEDLINE   20088902
   PUBMED   10620615
REFERENCE   12 (residues 1 to 93)
  AUTHORS   Cheng,Z.J., Zhao,J., Sun,Y., Hu,W., Wu,Y.L., Cen,B., Wu,G.X. and
            Pei,G.
  TITLE     beta-arrestin differentially regulates the chemokine receptor
            CXCR4-mediated signaling and receptor internalization, and this
            implicates multiple interaction sites between beta-arrestin and
            CXCR4
  JOURNAL   J. Biol. Chem. 275 (4), 2479-2485 (2000)
  MEDLINE   20112807
   PUBMED   10644702
REFERENCE   13 (residues 1 to 93)
  AUTHORS   Ghezzi,S., Noonan,D.M., Aluigi,M.G., Vallanti,G., Cota,M.,
            Benelli,R., Morini,M., Reeves,J.D., Vicenzi,E., Poli,G. and
            Albini,A.
  TITLE     Inhibition of CXCR4-dependent HIV-1 infection by extracellular
            HIV-1 Tat
  JOURNAL   Biochem. Biophys. Res. Commun. 270 (3), 992-996 (2000)
  MEDLINE   20237116
   PUBMED   10772939
REFERENCE   14 (residues 1 to 93)
  AUTHORS   Poznansky,M.C., Olszak,I.T., Foxall,R., Evans,R.H., Luster,A.D. and
            Scadden,D.T.
  TITLE     Active movement of T cells away from a chemokine
  JOURNAL   Nat. Med. 6 (5), 543-548 (2000)
  MEDLINE   20264563
   PUBMED   10802710
REFERENCE   15 (residues 1 to 93)
  AUTHORS   Bajetto,A., Barbero,S., Bonavia,R., Piccioli,P., Pirani,P.,
            Florio,T. and Schettini,G.
  TITLE     Stromal cell-derived factor-1alpha induces astrocyte proliferation
            through the activation of extracellular signal-regulated kinases
            1/2 pathway
  JOURNAL   J. Neurochem. 77 (5), 1226-1236 (2001)
  MEDLINE   21283069
   PUBMED   11389173
REFERENCE   16 (residues 1 to 93)
  AUTHORS   Spotila,L.D.
  TITLE     Novel sequences expressed by mineralizing human osteoblasts in
            culture
  JOURNAL   Unpublished
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U16752.1.
            Summary: For background information on chemokines, see CXCL11
            (SCYB11; MIM 604852). Stromal cell-derived factors 1-alpha and
            1-beta are small cytokines that belong to the intercrine family,
            members of which activate leukocytes and are often induced by
            proinflammatory stimuli such as lipopolysaccharide, TNF (see MIM
            191160), or IL1 (see MIM 147760). The intercrines are characterized
            by the presence of 4 conserved cysteines which form 2 disulfide
            bonds. They can be classified into 2 subfamilies. In the CC
            subfamily, which includes beta chemokine, the cysteine residues are
            adjacent to each other. In the CXC subfamily, which includes alpha
            chemokine, they are separated by an intervening amino acid. The
            SDF1 proteins belong to the latter group.[supplied by OMIM].
FEATURES             Location/Qualifiers
     source          1..93
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="10"
                     /map="10q11.1"
                     /clone="sdf5-8.7"
                     /cell_type="fibroblast"
                     /clone_lib="lambda ZAP human fibroblast cDNA library"
                     /note="a shorter clone with an identical sequence was
                     purified from a human osteoblast cDNA library"
     Protein         1..93
                     /product="stromal cell-derived factor 1"
     Region          24..85
                     /region_name="pfam00048, IL8, Small cytokines
                     (intecrine/chemokine), interleukin-8 like. Includes a
                     number of secreted growth factors and interferons involved
                     in mitogenic, chemotactic, and inflammatory activity.
                     Structure contains two highly conserved disulfide bonds"
     Region          27..85
                     /region_name="smart00199, SCY, Intercrine alpha family
                     (small cytokine C-X-C) (chemokine CXC); Family of
                     cytokines involved in cell-specific chemotaxis, mediation
                     of cell growth, and the inflammatory response"
     CDS             1..93
                     /gene="SDF1"
                     /coded_by="NM_000609.1:81..362"
                     /db_xref="LocusID:6387"
                     /db_xref="MIM:600835"
ORIGIN      
        1 mnakvvvvlv lvltalclsd gkpvslsyrc pcrffeshva ranvkhlkil ntpncalqiv
       61 arlknnnrqv cidpklkwiq eylekalnkr fkm
//



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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_004039. beta-2-microglobu...[gi:4757826] Links  


LOCUS       B2M                      119 aa            linear   PRI 25-JUL-2002
DEFINITION  beta-2-microglobulin [Homo sapiens].
ACCESSION   NP_004039
VERSION     NP_004039.1  GI:4757826
DBSOURCE    REFSEQ: aaccession NM_004048.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 119)
  AUTHORS   Connors,L.H., Shirahama,T., Skinner,M., Fenves,A. and Cohen,A.S.
  TITLE     In vitro formation of amyloid fibrils from intact beta
            2-microglobulin
  JOURNAL   Biochem. Biophys. Res. Commun. 131 (3), 1063-1068 (1985)
  MEDLINE   86025565
   PUBMED   2413854
REFERENCE   2  (residues 1 to 119)
  AUTHORS   Wang,Z., Cao,Y., Albino,A.P., Zeff,R.A., Houghton,A. and Ferrone,S.
  TITLE     Lack of HLA class I antigen expression by melanoma cells SK-MEL-33
            caused by a reading frameshift in beta 2-microglobulin messenger
            RNA
  JOURNAL   J. Clin. Invest. 91 (2), 684-692 (1993)
  MEDLINE   93163363
   PUBMED   8432869
REFERENCE   3  (residues 1 to 119)
  AUTHORS   Kad,N.M., Thomson,N.H., Smith,D.P., Smith,D.A. and Radford,S.E.
  TITLE     Beta(2)-microglobulin and its deamidated variant, N17D form amyloid
            fibrils with a range of morphologies in vitro
  JOURNAL   J. Mol. Biol. 313 (3), 559-571 (2001)
  MEDLINE   21534733
   PUBMED   11676539
REFERENCE   4  (residues 1 to 119)
  AUTHORS   Matsumoto,K. and Minamitani,T.
  TITLE     Human mRNA for beta 2-microglobulin
  JOURNAL   Published Only in DataBase (1998)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB021288.1.
FEATURES             Location/Qualifiers
     source          1..119
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="15"
                     /map="15q21-q22.2"
                     /cell_line="HeLa"
                     /clone_lib="HeLa cDNA library"
     Protein         1..119
                     /product="beta-2-microglobulin"
     Region          38..102
                     /region_name="pfam00047, ig, Immunoglobulin domain.
                     Members of the immunoglobulin superfamily are found in
                     hundreds of proteins of different functions. Examples
                     include antibodies, the giant muscle kinase titin and
                     receptor tyrosine kinases. Immunoglobulin-like domains may
                     be involved in protein-protein and protein-ligand
                     interactions. The Pfam alignments do not include the first
                     and last strand of the immunoglobulin-like domain"
     Region          40..110
                     /region_name="smart00407, IGc1, Immunoglobulin C-Type"
     CDS             1..119
                     /gene="B2M"
                     /coded_by="NM_004048.1:14..373"
                     /db_xref="LocusID:567"
                     /db_xref="MIM:109700"
ORIGIN      
        1 msrsvalavl allslsglea iqrtpkiqvy srhpaengks nflncyvsgf hpsdievdll
       61 kngeriekve hsdlsfskdw sfyllyytef tptekdeyac rvnhvtlsqp kivkwdrdm
//



Revised: July 5, 2002.
 
 


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1: NP_003055. secretory leukocy...[gi:4507065] Links  


LOCUS       SLPI                     132 aa            linear   PRI 27-AUG-2002
DEFINITION  secretory leukocyte protease inhibitor precursor;
            antileukoproteinase; seminal proteinase inhibitor; mucus proteinase
            inhibitor [Homo sapiens].
ACCESSION   NP_003055
VERSION     NP_003055.1  GI:4507065
DBSOURCE    REFSEQ: aaccession NM_003064.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 132)
  AUTHORS   Seemuller,U., Arnhold,M., Fritz,H., Wiedenmann,K., Machleidt,W.,
            Heinzel,R., Appelhans,H., Gassen,H.G. and Lottspeich,F.
  TITLE     The acid-stable proteinase inhibitor of human mucous secretions
            (HUSI-I, antileukoprotease). Complete amino acid sequence as
            revealed by protein and cDNA sequencing and structural homology to
            whey proteins and Red Sea turtle proteinase inhibitor
  JOURNAL   FEBS Lett. 199 (1), 43-48 (1986)
  MEDLINE   86164996
   PUBMED   3485543
REFERENCE   2  (residues 1 to 132)
  AUTHORS   Thompson,R.C. and Ohlsson,K.
  TITLE     Isolation, properties, and complete amino acid sequence of human
            secretory leukocyte protease inhibitor, a potent inhibitor of
            leukocyte elastase
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 83 (18), 6692-6696 (1986)
  MEDLINE   86313644
   PUBMED   3462719
REFERENCE   3  (residues 1 to 132)
  AUTHORS   Heinzel,R., Appelhans,H., Gassen,G., Seemuller,U., Machleidt,W.,
            Fritz,H. and Steffens,G.
  TITLE     Molecular cloning and expression of cDNA for human
            antileukoprotease from cervix uterus
  JOURNAL   Eur. J. Biochem. 160 (1), 61-67 (1986)
  MEDLINE   87030258
   PUBMED   3533531
REFERENCE   4  (residues 1 to 132)
  AUTHORS   Stetler,G., Brewer,M.T. and Thompson,R.C.
  TITLE     Isolation and sequence of a human gene encoding a potent inhibitor
            of leukocyte proteases
  JOURNAL   Nucleic Acids Res. 14 (20), 7883-7896 (1986)
  MEDLINE   87040761
   PUBMED   3640338
REFERENCE   5  (residues 1 to 132)
  AUTHORS   Grutter,M.G., Fendrich,G., Huber,R. and Bode,W.
  TITLE     The 2.5 A X-ray crystal structure of the acid-stable proteinase
            inhibitor from human mucous secretions analysed in its complex with
            bovine alpha-chymotrypsin
  JOURNAL   EMBO J. 7 (2), 345-351 (1988)
  MEDLINE   88211544
   PUBMED   3366116
REFERENCE   6  (residues 1 to 132)
  AUTHORS   Fritz,H.
  TITLE     Human mucus proteinase inhibitor (human MPI). Human seminal
            inhibitor I (HUSI-I), antileukoprotease (ALP), secretory leukocyte
            protease inhibitor (SLPI)
  JOURNAL   Biol. Chem. Hoppe-Seyler 369 Suppl, 79-82 (1988)
  MEDLINE   89076538
   PUBMED   3060147
REFERENCE   7  (residues 1 to 132)
  AUTHORS   Eisenberg,S.P., Hale,K.K., Heimdal,P. and Thompson,R.C.
  TITLE     Location of the protease-inhibitory region of secretory leukocyte
            protease inhibitor
  JOURNAL   J. Biol. Chem. 265 (14), 7976-7981 (1990)
  MEDLINE   90243669
   PUBMED   2110563
REFERENCE   8  (residues 1 to 132)
  AUTHORS   Abe,T., Kobayashi,N., Yoshimura,K., Trapnell,B.C., Kim,H.,
            Hubbard,R.C., Brewer,M.T., Thompson,R.C. and Crystal,R.G.
  TITLE     Expression of the secretory leukoprotease inhibitor gene in
            epithelial cells
  JOURNAL   J. Clin. Invest. 87 (6), 2207-2215 (1991)
  MEDLINE   91250579
   PUBMED   1674946
REFERENCE   9  (residues 1 to 132)
  AUTHORS   Kikuchi,T., Abe,T., Hoshi,S., Matsubara,N., Tominaga,Y., Satoh,K.
            and Nukiwa,T.
  TITLE     Structure of the murine secretory leukoprotease inhibitor (Slpi)
            gene and chromosomal localization of the human and murine SLPI
            genes
  JOURNAL   Am. J. Respir. Cell Mol. Biol. 19 (6), 875-880 (1998)
  MEDLINE   99061820
   PUBMED   9843921
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X04470.1 and M74444.1.
            Summary:  This gene encodes a secreted inhibitor which protects
            epithelial tissues from serine proteases.  It is found in various
            secretions including seminal plasma, cervical mucus, and bronchial
            secretions, and has affinity for trypsin, leukocyte elastase, and
            cathepsin G.  Its inhibitory effect contributes to the immune
            response by protecting epithelial surfaces from attack by
            endogenous proteolytic enzymes; the protein is also thought to have
            broad-spectrum anti-biotic activity.
FEATURES             Location/Qualifiers
     source          1..132
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q12"
     Protein         1..132
                     /product="secretory leukocyte protease inhibitor
                     precursor"
                     /note="antileukoproteinase; seminal proteinase inhibitor;
                     mucus proteinase inhibitor"
     sig_peptide     1..25
     mat_peptide     26..132
                     /product="secretory leukocyte protease inhibitor"
     Region          31..76
                     /region_name="smart00217, WAP, WAP domain"
     Region          31..75
                     /region_name="pfam00095, wap, WAP-type (Whey Acidic
                     Protein) 'four-disulfide core'"
     Region          85..130
                     /region_name="smart00217, WAP, WAP domain"
     Region          85..129
                     /region_name="pfam00095, wap, WAP-type (Whey Acidic
                     Protein) 'four-disulfide core'"
     CDS             1..132
                     /gene="SLPI"
                     /coded_by="NM_003064.2:23..421"
                     /db_xref="LocusID:6590"
                     /db_xref="MIM:107285"
ORIGIN      
        1 mkssglfpfl vllalgtlap wavegsgksf kagvcppkks aqclrykkpe cqsdwqcpgk
       61 krccpdtcgi kcldpvdtpn ptrrkpgkcp vtygqclmln ppnfcemdgq ckrdlkccmg
      121 mcgkscvspv ka
//



Revised: July 5, 2002.
 
 


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1: NP_003608. regulator of G-pr...[gi:4506519] Links  


LOCUS       RGS5                     181 aa            linear   PRI 01-NOV-2000
DEFINITION  regulator of G-protein signalling 5; Regulator of G protein
            signaling-5 [Homo sapiens].
ACCESSION   NP_003608
VERSION     NP_003608.1  GI:4506519
DBSOURCE    REFSEQ: aaccession NM_003617.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (sites)
  AUTHORS   Seki,N., Sugano,S., Suzuki,Y., Nakagawara,A., Ohira,M.,
            Muramatsu,M., Saito,T. and Hori,T.
  TITLE     Isolation, tissue expression, and chromosomal assignment of human
            RGS5, a novel G-protein signaling regulator gene
  JOURNAL   J. Hum. Genet. 43 (3), 202-205 (1998)
  MEDLINE   98419174
   PUBMED   9747037
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AB008109.1.
FEATURES             Location/Qualifiers
     source          1..181
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q23"
                     /clone="nb-20"
                     /tissue_type="neuroblastoma"
     Protein         1..181
                     /product="regulator of G-protein signalling 5"
                     /function="G protein signaling regulator"
                     /note="Regulator of G protein signaling-5"
     Region          64..180
                     /region_name="Regulator of G protein signaling domain"
                     /note="RGS"
                     /db_xref="CDD:pfam00615"
     Region          64..179
                     /region_name="Regulator of G protein signalling domain"
                     /note="RGS"
                     /db_xref="CDD:RGS"
     CDS             1..181
                     /gene="RGS5"
                     /coded_by="NM_003617.1:82..627"
                     /db_xref="LocusID:8490"
                     /db_xref="MIM:603276"
ORIGIN      
        1 mckglaalph sclerakeik iklgillqkp dsvgdlvipy nekpekpakt qktsldealq
       61 wrdsldkllq nnyglasfks flksefseen lefwiacedy kkikspakma ekakqiyeef
      121 iqteapkevn idhftkditm knlvepslss fdmaqkriha lmekdslprf vrsefyqeli
      181 k
//



Revised: July 5, 2002.
 
 


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1: NP_000349. transforming grow...[gi:4507467] Links  


LOCUS       TGFBI                    683 aa            linear   PRI 05-SEP-2002
DEFINITION  transforming growth factor, beta-induced, 68kDa; corneal dystrophy;
            kerato-epithelin; transforming growth factor, beta-induced, 68kD
            [Homo sapiens].
ACCESSION   NP_000349
VERSION     NP_000349.1  GI:4507467
DBSOURCE    REFSEQ: aaccession NM_000358.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 683)
  AUTHORS   Skonier,J., Neubauer,M., Madisen,L., Bennett,K., Plowman,G.D. and
            Purchio,A.F.
  TITLE     cDNA cloning and sequence analysis of beta ig-h3, a novel gene
            induced in a human adenocarcinoma cell line after treatment with
            transforming growth factor-beta
  JOURNAL   DNA Cell Biol. 11 (7), 511-522 (1992)
  MEDLINE   93000472
   PUBMED   1388724
REFERENCE   2  (residues 1 to 683)
  AUTHORS   Stone,E.M., Mathers,W.D., Rosenwasser,G.O., Holland,E.J.,
            Folberg,R., Krachmer,J.H., Nichols,B.E., Gorevic,P.D., Taylor,C.M.,
            Streb,L.M. et al.
  TITLE     Three autosomal dominant corneal dystrophies map to chromosome 5q
  JOURNAL   Nat. Genet. 6 (1), 47-51 (1994)
  MEDLINE   94184364
   PUBMED   8136834
REFERENCE   3  (residues 1 to 683)
  AUTHORS   Skonier,J., Bennett,K., Rothwell,V., Kosowski,S., Plowman,G.,
            Wallace,P., Edelhoff,S., Disteche,C., Neubauer,M., Marquardt,H. et
            al.
  TITLE     beta ig-h3: a transforming growth factor-beta-responsive gene
            encoding a secreted protein that inhibits cell attachment in vitro
            and suppresses the growth of CHO cells in nude mice
  JOURNAL   DNA Cell Biol. 13 (6), 571-584 (1994)
  MEDLINE   94296561
   PUBMED   8024701
REFERENCE   4  (residues 1 to 683)
  AUTHORS   Munier,F.L., Korvatska,E., Djemai,A., Le Paslier,D., Zografos,L.,
            Pescia,G. and Schorderet,D.F.
  TITLE     Kerato-epithelin mutations in four 5q31-linked corneal dystrophies
  JOURNAL   Nat. Genet. 15 (3), 247-251 (1997)
  MEDLINE   97207642
   PUBMED   9054935
REFERENCE   5  (residues 1 to 683)
  AUTHORS   Korvatska,E., Munier,F.L., Djemai,A., Wang,M.X., Frueh,B.,
            Chiou,A.G., Uffer,S., Ballestrazzi,E., Braunstein,R.E.,
            Forster,R.K., Culbertson,W.W., Boman,H., Zografos,L. and
            Schorderet,D.F.
  TITLE     Mutation hot spots in 5q31-linked corneal dystrophies
  JOURNAL   Am. J. Hum. Genet. 62 (2), 320-324 (1998)
  MEDLINE   98130534
   PUBMED   9463327
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M77349.1.
FEATURES             Location/Qualifiers
     source          1..683
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q31"
                     /cell_line="A549"
                     /cell_type="adenocarcinoma"
     Protein         1..683
                     /product="transforming growth factor, beta-induced, 68kDa"
                     /note="corneal dystrophy; kerato-epithelin; transforming
                     growth factor, beta-induced, 68kD"
     sig_peptide     1..15
                     /gene="BIGH3"
                     /note="putative"
     mat_peptide     16..683
                     /gene="BIGH3"
                     /product="transforming growth factor-beta induced protein"
     Region          134..236
                     /region_name="pfam02469, Fasciclin, Fasciclin domain. This
                     extracellular domain is found repeated four times in
                     grasshopper fasciclin I as well as in proteins from
                     mammals, sea urchins, plants, yeast and bacteria"
     Region          139..236
                     /region_name="smart00554, FAS1, Four repeated domains in
                     the Fasciclin I family of proteins, present in many other
                     contexts"
     Region          252..373
                     /region_name="pfam02469, Fasciclin, Fasciclin domain. This
                     extracellular domain is found repeated four times in
                     grasshopper fasciclin I as well as in proteins from
                     mammals, sea urchins, plants, yeast and bacteria"
     Region          276..373
                     /region_name="smart00554, FAS1, Four repeated domains in
                     the Fasciclin I family of proteins, present in many other
                     contexts"
     Region          389..500
                     /region_name="pfam02469, Fasciclin, Fasciclin domain. This
                     extracellular domain is found repeated four times in
                     grasshopper fasciclin I as well as in proteins from
                     mammals, sea urchins, plants, yeast and bacteria"
     Region          411..501
                     /region_name="smart00554, FAS1, Four repeated domains in
                     the Fasciclin I family of proteins, present in many other
                     contexts"
     Region          502..634
                     /region_name="pfam02469, Fasciclin, Fasciclin domain. This
                     extracellular domain is found repeated four times in
                     grasshopper fasciclin I as well as in proteins from
                     mammals, sea urchins, plants, yeast and bacteria"
     Region          538..635
                     /region_name="smart00554, FAS1, Four repeated domains in
                     the Fasciclin I family of proteins, present in many other
                     contexts"
     CDS             1..683
                     /gene="TGFBI"
                     /coded_by="NM_000358.1:48..2099"
                     /note="putative"
                     /db_xref="LocusID:7045"
                     /db_xref="MIM:601692"
ORIGIN      
        1 malfvrllal alalalgpaa tlagpakspy qlvlqhsrlr grqhgpnvca vqkvigtnrk
       61 yftnckqwyq rkicgkstvi syeccpgyek vpgekgcpaa lplsnlyetl gvvgstttql
      121 ytdrteklrp emegpgsfti fapsneawas lpaevldslv snvniellna lryhmvgrrv
      181 ltdelkhgmt ltsmyqnsni qihhypngiv tvncarllka dhhatngvvh lidkvistit
      241 nniqqiieie dtfetlraav aasglntmle gngqytllap tneafekips etlnrilgdp
      301 ealrdllnnh ilksamcaea ivaglsvetl egttlevgcs gdmltingka iisnkdilat
      361 ngvihyidel lipdsaktlf elaaesdvst aidlfrqagl gnhlsgserl tllaplnsvf
      421 kdgtppidah trnllrnhii kdqlaskyly hgqtletlgg kklrvfvyrn slcienscia
      481 ahdkrgrygt lftmdrvltp pmgtvmdvlk gdnrfsmlva aiqsagltet lnregvytvf
      541 aptneafral pprersrllg dakelanilk yhigdeilvs ggigalvrlk slqgdklevs
      601 lknnvvsvnk epvaepdima tngvvhvitn vlqppanrpq ergdeladsa leifkqasaf
      661 srasqrsvrl apvyqkller mkh
//



Revised: July 5, 2002.
 
 


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1: NP_002113. major histocompat...[gi:18426975] Links  


LOCUS       HLA-DQA1                 255 aa            linear   PRI 30-JAN-2002
DEFINITION  major histocompatibility complex, class II, DQ alpha 1 precursor
            [Homo sapiens].
ACCESSION   NP_002113
VERSION     NP_002113.2  GI:18426975
DBSOURCE    REFSEQ: aaccession NM_002122.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 255)
  AUTHORS   Schenning,L., Larhammar,D., Bill,P., Wiman,K., Jonsson,A.K.,
            Rask,L. and Peterson,P.A.
  TITLE     Both alpha and beta chains of HLA-DC class II histocompatibility
            antigens display extensive polymorphism in their amino-terminal
            domains
  JOURNAL   EMBO J. 3 (2), 447-452 (1984)
  MEDLINE   84182509
   PUBMED   6585297
REFERENCE   2  (residues 1 to 255)
  AUTHORS   Turco,E., Care,A., Compagnone-Post,P., Robinson,C., Cascino,I. and
            Trucco,M.
  TITLE     Allelic forms of the alpha- and beta-chain genes encoding
            DQw1-positive heterodimers
  JOURNAL   Immunogenetics 26 (4-5), 282-290 (1987)
  MEDLINE   88006310
   PUBMED   2888727
REFERENCE   3  (residues 1 to 255)
  AUTHORS   Jonsson,A.K., Andersson,L. and Rask,L.
  TITLE     Complete sequences of DQA1 and DQB1 cDNA clones corresponding to
            the DQw4 specificity
  JOURNAL   Immunogenetics 30 (3), 232-234 (1989)
  MEDLINE   89379293
   PUBMED   2777341
REFERENCE   4  (residues 1 to 255)
  AUTHORS   Todd,J.A., Fukui,Y., Kitagawa,T. and Sasazuki,T.
  TITLE     The A3 allele of the HLA-DQA1 locus is associated with
            susceptibility to type 1 diabetes in Japanese
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 87 (3), 1094-1098 (1990)
  MEDLINE   90138944
   PUBMED   2300572
REFERENCE   5  (residues 1 to 255)
  AUTHORS   Yasunaga,S., Kimura,A., Hamaguchi,K., Ronningen,K.S. and
            Sasazuki,T.
  TITLE     Different contribution of HLA-DR and -DQ genes in susceptibility
            and resistance to insulin-dependent diabetes mellitus (IDDM)
  JOURNAL   Tissue Antigens 47 (1), 37-48 (1996)
  MEDLINE   97083137
   PUBMED   8929711
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from L34083.1, L46875.1 and
            M20431.1.
            On Jan 30, 2002 this sequence version replaced gi:4504407.
            Summary: HLA-DQA1 belongs to the HLA class II alpha chain
            paralogues. The class II molecule is a heterodimer consisting of an
            alpha (DQA) and a beta chain (DQB), both anchored in the membrane.
            It plays a central role in the immune system by presenting peptides
            derived from extracellular proteins. Class II molecules are
            expressed in antigen presenting cells (APC: B Lymphocytes,
            dendritic cells, macrophages). The alpha chain is approximately
            33-35 kDa. It is encoded by 5 exons, exon one encodes the leader
            peptide, exons 2 and 3 encode the two extracellular domains, exon 4
            encodes the transmembrane domain and the cytoplasmic tail. Within
            the DQ molecule both the alpha chain and the beta chain contain the
            polymorphisms specifying the peptide binding specificities,
            resulting in up to 4 different molecules. Typing for these
            polymorphisms is routinely done for bone marrow transplantation.
FEATURES             Location/Qualifiers
     source          1..255
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.3"
     Protein         1..255
                     /product="major histocompatibility complex, class II, DQ
                     alpha 1 precursor"
     sig_peptide     1..23
     mat_peptide     24..255
                     /product="major histocompatibility complex, class II, DQ
                     alpha 1"
     Region          29..110
                     /region_name="Class II histocompatibility antigen, alpha
                     domain"
                     /note="MHC_II_alpha"
                     /db_xref="CDD:pfam00993"
     variation       57
                     /allele="Q"
                     /allele="E"
                     /db_xref="dbSNP:1130036"
     variation       63
                     /allele="E"
                     /allele="G"
                     /db_xref="dbSNP:1142323"
     variation       68
                     /allele="A"
                     /allele="V"
                     /db_xref="dbSNP:1142324"
     variation       70
                     /allele="R"
                     /allele="W"
                     /db_xref="dbSNP:1142326"
     variation       71
                     /allele="L"
                     /allele="W"
                     /db_xref="dbSNP:1142328"
     variation       73
                     /allele="E"
                     /allele="V"
                     /db_xref="dbSNP:3208105"
     variation       78
                     /allele="R"
                     /allele="G"
                     /db_xref="dbSNP:1142330"
     variation       84
                     /allele="C"
                     /allele="G"
                     /db_xref="dbSNP:1142331"
     variation       84
                     /allele="V"
                     /allele="G"
                     /db_xref="dbSNP:1142332"
     variation       87
                     /allele="R"
                     /allele="T"
                     /db_xref="dbSNP:1142333"
     variation       89
                     /allele="I"
                     /allele="M"
                     /db_xref="dbSNP:1142334"
     variation       92
                     /allele="A"
                     /allele="T"
                     /db_xref="dbSNP:1142335"
     Region          126..191
                     /region_name="Immunoglobulin domain"
                     /note="ig"
                     /db_xref="CDD:pfam00047"
     Region          128..199
                     /region_name="Immunoglobulin C-Type"
                     /note="IGc1"
                     /db_xref="CDD:smart00407"
     CDS             1..255
                     /gene="HLA-DQA1"
                     /coded_by="NM_002122.2:1..768"
                     /db_xref="LocusID:3117"
                     /db_xref="MIM:146880"
                     /db_xref="LocusID:3117"
                     /db_xref="MIM:146880"
ORIGIN      
        1 milnkalllg alalttvmsp cggedivadh vascgvnlyq fygpsgqyth efdgdeqfyv
       61 dlerketawr wpefskfggf dpqgalrnma vakhnlnimi krynstaatn evpevtvfsk
      121 spvtlgqpnt liclvdnifp pvvnitwlsn gqsvtegvse tsflsksdhs ffkisyltfl
      181 psadeiydck vehwgldqpl lkhwepeipa pmseltetvv calglsvglm givvgtvfii
      241 qglrsvgasr hqgpl
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_001895. catenin (cadherin...[gi:4503131] Links  


LOCUS       CTNNB1                   781 aa            linear   PRI 25-SEP-2002
DEFINITION  catenin (cadherin-associated protein), beta 1, 88kDa; catenin
            (cadherin-associated protein), beta 1 (88kD); catenin
            (cadherin-associated protein), beta 1 (88kDa [Homo sapiens].
ACCESSION   NP_001895
VERSION     NP_001895.1  GI:4503131
DBSOURCE    REFSEQ: aaccession NM_001904.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 781)
  AUTHORS   Kraus,C., Liehr,T., Hulsken,J., Behrens,J., Birchmeier,W.,
            Grzeschik,K.H. and Ballhausen,W.G.
  TITLE     Localization of the human beta-catenin gene (CTNNB1) to 3p21: a
            region implicated in tumor development
  JOURNAL   Genomics 23 (1), 272-274 (1994)
  MEDLINE   95130097
   PUBMED   7829088
REFERENCE   2  (residues 1 to 781)
  AUTHORS   Hulsken,J., Birchmeier,W. and Behrens,J.
  TITLE     E-cadherin and APC compete for the interaction with beta-catenin
            and the cytoskeleton
  JOURNAL   J. Cell Biol. 127 (6 Pt 2), 2061-2069 (1994)
  MEDLINE   95105247
   PUBMED   7806582
REFERENCE   3  (residues 1 to 781)
  AUTHORS   Nollet,F., Berx,G., Molemans,F. and van Roy,F.
  TITLE     Genomic organization of the human beta-catenin gene (CTNNB1)
  JOURNAL   Genomics 32 (3), 413-424 (1996)
  MEDLINE   96435919
   PUBMED   8838805
REFERENCE   4  (residues 1 to 781)
  AUTHORS   Korinek,V., Barker,N., Morin,P.J., van Wichen,D., de Weger,R.,
            Kinzler,K.W., Vogelstein,B. and Clevers,H.
  TITLE     Constitutive transcriptional activation by a beta-catenin-Tcf
            complex in APC-/- colon carcinoma
  JOURNAL   Science 275 (5307), 1784-1787 (1997)
  MEDLINE   97218301
   PUBMED   9065401
REFERENCE   5  (residues 1 to 781)
  AUTHORS   Morin,P.J., Sparks,A.B., Korinek,V., Barker,N., Clevers,H.,
            Vogelstein,B. and Kinzler,K.W.
  TITLE     Activation of beta-catenin-Tcf signaling in colon cancer by
            mutations in beta-catenin or APC
  JOURNAL   Science 275 (5307), 1787-1790 (1997)
  MEDLINE   97218302
   PUBMED   9065402
REFERENCE   6  (residues 1 to 781)
  AUTHORS   Chan,E.F., Gat,U., McNiff,J.M. and Fuchs,E.
  TITLE     A common human skin tumour is caused by activating mutations in
            beta-catenin
  JOURNAL   Nat. Genet. 21 (4), 410-413 (1999)
  MEDLINE   99206611
   PUBMED   10192393
REFERENCE   7  (residues 1 to 781)
  AUTHORS   Kolligs,F.T., Kolligs,B., Hajra,K.M., Hu,G., Tani,M., Cho,K.R. and
            Fearon,E.R.
  TITLE     gamma-catenin is regulated by the APC tumor suppressor and its
            oncogenic activity is distinct from that of beta-catenin
  JOURNAL   Genes Dev. 14 (11), 1319-1331 (2000)
  MEDLINE   20296720
   PUBMED   10837025
REFERENCE   8  (residues 1 to 781)
  AUTHORS   Ilan,N., Cheung,L., Pinter,E. and Madri,J.A.
  TITLE     Platelet-endothelial cell adhesion molecule-1 (CD31), a scaffolding
            molecule for selected catenin family members whose binding is
            mediated by different tyrosine and serine/threonine phosphorylation
  JOURNAL   J. Biol. Chem. 275 (28), 21435-21443 (2000)
  MEDLINE   20347262
   PUBMED   10801826
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X87838.1.
FEATURES             Location/Qualifiers
     source          1..781
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3p21"
                     /cell_line="5637"
     Protein         1..781
                     /product="catenin (cadherin-associated protein), beta 1,
                     88kDa"
                     /note="catenin (cadherin-associated protein), beta 1
                     (88kD); catenin (cadherin-associated protein), beta 1
                     (88kDa"
     Region          230..262
                     /region_name="Armadillo/beta-catenin-like repeat. Approx.
                     40 amino acid repeat. Tandem repeats form super-helix of
                     helices that is proposed to mediate interaction of
                     beta-catenin with its ligands. CAUTION: This family does
                     not contain all known armadillo repeats"
                     /note="Armadillo_seg"
                     /db_xref="CDD:pfam00514"
     Region          230..262
                     /region_name="Armadillo/beta-catenin-like repeats"
                     /note="ARM"
                     /db_xref="CDD:smart00185"
     Region          350..390
                     /region_name="Armadillo/beta-catenin-like repeat. Approx.
                     40 amino acid repeat. Tandem repeats form super-helix of
                     helices that is proposed to mediate interaction of
                     beta-catenin with its ligands. CAUTION: This family does
                     not contain all known armadillo repeats"
                     /note="Armadillo_seg"
                     /db_xref="CDD:pfam00514"
     Region          350..390
                     /region_name="Armadillo/beta-catenin-like repeats"
                     /note="ARM"
                     /db_xref="CDD:smart00185"
     Region          583..623
                     /region_name="Armadillo/beta-catenin-like repeats"
                     /note="ARM"
                     /db_xref="CDD:smart00185"
     Region          583..622
                     /region_name="Armadillo/beta-catenin-like repeat. Approx.
                     40 amino acid repeat. Tandem repeats form super-helix of
                     helices that is proposed to mediate interaction of
                     beta-catenin with its ligands. CAUTION: This family does
                     not contain all known armadillo repeats"
                     /note="Armadillo_seg"
                     /db_xref="CDD:pfam00514"
     CDS             1..781
                     /gene="CTNNB1"
                     /coded_by="NM_001904.1:215..2560"
                     /db_xref="LocusID:1499"
                     /db_xref="MIM:116806"
ORIGIN      
        1 matqadlmel dmamepdrka avshwqqqsy ldsgihsgat ttapslsgkg npeeedvdts
       61 qvlyeweqgf sqsftqeqva didgqyamtr aqrvraamfp etldegmqip stqfdaahpt
      121 nvqrlaepsq mlkhavvnli nyqddaelat raipeltkll ndedqvvvnk aavmvhqlsk
      181 keasrhaimr spqmvsaivr tmqntndvet arctagtlhn lshhreglla ifksggipal
      241 vkmlgspvds vlfyaittlh nlllhqegak mavrlagglq kmvallnktn vkflaittdc
      301 lqilaygnqe skliilasgg pqalvnimrt ytyekllwtt srvlkvlsvc ssnkpaivea
      361 ggmqalglhl tdpsqrlvqn clwtlrnlsd aatkqegmeg llgtlvqllg sddinvvtca
      421 agilsnltcn nyknkmmvcq vggiealvrt vlragdredi tepaicalrh ltsrhqeaem
      481 aqnavrlhyg lpvvvkllhp pshwplikat vglirnlalc panhaplreq gaiprlvqll
      541 vrahqdtqrr tsmggtqqqf vegvrmeeiv egctgalhil ardvhnrivi rglntiplfv
      601 qllyspieni qrvaagvlce laqdkeaaea ieaegatapl tellhsrneg vatyaaavlf
      661 rmsedkpqdy kkrlsvelts slfrtepmaw netadlgldi gaqgeplgyr qddpsyrsfh
      721 sggygqdalg mdpmmehemg ghhpgadypv dglpdlghaq dlmdglppgd snqlawfdtd
      781 l
//



Revised: July 5, 2002.
 
 


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  Summary ASN.1 FASTA TinySeq XML GI List GenPept GBSeq XML Graphics XML default             
 
 

1: NP_059973. surfeit 2; surfei...[gi:19557687] Links  


LOCUS       SURF2                    256 aa            linear   PRI 27-AUG-2002
DEFINITION  surfeit 2; surfeit locus protein 2 [Homo sapiens].
ACCESSION   NP_059973
VERSION     NP_059973.2  GI:19557687
DBSOURCE    REFSEQ: aaccession NM_017503.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 256)
  AUTHORS   Yon,J., Jones,T., Garson,K., Sheer,D. and Fried,M.
  TITLE     The organization and conservation of the human Surfeit gene cluster
            and its localization telomeric to the c-abl and can proto-oncogenes
            at chromosome band 9q34.1
  JOURNAL   Hum. Mol. Genet. 2 (3), 237-240 (1993)
  MEDLINE   93271979
   PUBMED   8499913
REFERENCE   2  (residues 1 to 256)
  AUTHORS   Lennard,A., Gaston,K. and Fried,M.
  TITLE     The Surf-1 and Surf-2 genes and their essential bidirectional
            promoter elements are conserved between mouse and human
  JOURNAL   DNA Cell Biol. 13 (11), 1117-1126 (1994)
  MEDLINE   95217332
   PUBMED   7702754
REFERENCE   3  (residues 1 to 256)
  AUTHORS   Duhig,T., Ruhrberg,C., Mor,O. and Fried,M.
  TITLE     The human Surfeit locus
  JOURNAL   Genomics 52 (1), 72-78 (1998)
  MEDLINE   98414511
   PUBMED   9740673
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC014411.1 and BM789997.1.
            On Mar 20, 2002 this sequence version replaced gi:8924250.
            Summary: This gene is located in the surfeit gene cluster, a group
            of very tightly linked genes that do not share sequence similarity.
            The gene shares a bidirectional promoter with SURF1, which is
            located on the opposite strand. The function of the encoded protein
            from this housekeeping gene has not yet been determined.
FEATURES             Location/Qualifiers
     source          1..256
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q34.2"
                     /clone="MGC:19914 IMAGE:4548425"
                     /clone_lib="NIH_MGC_18"
     Protein         1..256
                     /product="surfeit 2"
                     /note="surfeit locus protein 2"
     CDS             1..256
                     /gene="SURF2"
                     /coded_by="NM_017503.2:42..812"
                     /db_xref="LocusID:6835"
                     /db_xref="MIM:185630"
ORIGIN      
        1 mselpgdvra flrehpslrl qtdarkvrci ltghelpcrl pelqvytrgk kyqrlvrasp
       61 afdyaefeph ivpstknphq lfckltlrhi nkcpehvlrh tqgrryqral ckyeecqkqg
      121 veyvpaclvh rrrrredqmd gdgprpreaf weptssdegg aasddsmtdl yppelftrkd
      181 lgstedgdgt ddfltdkede kakpprekat degrrettvy rglvqkrgkk qlgslkkkfk
      241 shhrkpksfs sckqpg
//



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&&&&&&&



Table 1 Protein Sequences (part 2)    



    
 
PubMed Nucleotide Protein Genome Structure PopSet Taxonomy OMIM Books 
 
   Search PubMed Protein Nucleotide PopSet Taxonomy Genome OMIM Structure Domains GEO Books Books2 MapViewDr TestDb UniSTS CDD SNP Journals UniGene  for        
 
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1: NP_004604. transglutaminase ...[gi:4759228] Links  


LOCUS       TGM2                     687 aa            linear   PRI 01-NOV-2000
DEFINITION  transglutaminase 2 (C polypeptide,
            protein-glutamine-gamma-glutamyltransferase) [Homo sapiens].
ACCESSION   NP_004604
VERSION     NP_004604.1  GI:4759228
DBSOURCE    REFSEQ: aaccession NM_004613.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 687)
  AUTHORS   Gentile,V., Saydak,M., Chiocca,E.A., Akande,O., Birckbichler,P.J.,
            Lee,K.N., Stein,J.P. and Davies,P.J.
  TITLE     Isolation and characterization of cDNA clones to mouse macrophage
            and human endothelial cell tissue transglutaminases
  JOURNAL   J. Biol. Chem. 266 (1), 478-483 (1991)
  MEDLINE   91093168
   PUBMED   1670766
REFERENCE   2  (residues 1 to 687)
  AUTHORS   Gentile V, Davies PJ and Baldini A.
  TITLE     The human tissue transglutaminase gene maps on chromosome 20q12 by
            in situ fluorescence hybridization
  JOURNAL   Genomics 20 (2), 295-297 (1994)
  MEDLINE   94292215
   PUBMED   7912692
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from M55153.1.
FEATURES             Location/Qualifiers
     source          1..687
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="20"
                     /map="20q12"
                     /clone="1"
                     /cell_type="endothelial cell"
                     /tissue_type="umbilical vein"
                     /tissue_lib="lambda-ZAP"
     Protein         1..687
                     /product="transglutaminase 2 (C polypeptide,
                     protein-glutamine-gamma-glutamyltransferase)"
                     /EC_number="2.3.2.13"
     Region          2..124
                     /region_name="Transglutaminase family"
                     /note="Transglutamin_N"
                     /db_xref="CDD:pfam00868"
     Region          272..360
                     /region_name="Transglutaminase-like superfamily"
                     /note="Transglut_core"
                     /db_xref="CDD:pfam01841"
     Region          273..360
                     /region_name="Transglutaminase/protease-like homologues"
                     /note="TGc"
                     /db_xref="CDD:TGc"
     Region          458..686
                     /region_name="Transglutaminase family"
                     /note="Transglutamin_C"
                     /db_xref="CDD:pfam00927"
     CDS             1..687
                     /gene="TGM2"
                     /coded_by="NM_004613.1:136..2199"
                     /db_xref="LocusID:7052"
                     /db_xref="MIM:190196"
ORIGIN      
        1 maeelvlerc dleletngrd hhtadlcrek lvvrrgqpfw ltlhfegrny qasvdsltfs
       61 vvtgpapsqe agtkarfplr daveegdwta tvvdqqdctl slqlttpana piglyrlsle
      121 astgyqgssf vlghfillfn awcpadavyl dseeerqeyv ltqqgfiyqg sakfiknipw
      181 nfgqfqdgil diclilldvn pkflknagrd csrrsspvyv grvgsgmvnc nddqgvllgr
      241 wdnnygdgvs pmswigsvdi lrrwknhgcq rvkygqcwvf aavactvlrc lgiptrvvtn
      301 ynsahdqnsn llieyfrnef geiqgdksem iwnfhcwves wmtrpdlqpg yegwqaldpt
      361 pqeksegtyc cgpvpvraik egdlstkyda pfvfaevnad vvdwiqqddg svhksinrsl
      421 ivglkistks vgrderedit htykypegss eereaftran hlnklaekee tgmamrirvg
      481 qsmnmgsdfd vfahitnnta eeyvcrlllc artvsyngil gpecgtkyll nltlepfsek
      541 svplcilyek yrdcltesnl ikvrallvep vinsyllaer dlylenpeik irilgepkqk
      601 rklvaevslq nplpvalegc tftvegaglt eeqktveipd pveageevkv rmdlvplhmg
      661 lhklvvnfes dklkavkgfr nviigpa
//



Revised: July 5, 2002.
 
 


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1: NP_055579. DAZ associated pr...[gi:7661886] Links  


LOCUS       DAZAP2                   168 aa            linear   PRI 27-AUG-2002
DEFINITION  DAZ associated protein 2; KIAA0058 gene product [Homo sapiens].
ACCESSION   NP_055579
VERSION     NP_055579.1  GI:7661886
DBSOURCE    REFSEQ: aaccession NM_014764.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1
  AUTHORS   Nomura,N., Nagase,T., Miyajima,N., Sazuka,T., Tanaka,A., Sato,S.,
            Seki,N., Kawarabayasi,Y., Ishikawa,K. and Tabata,S.
  TITLE     Prediction of the coding sequences of unidentified human genes. II.
            The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
            analysis of cDNA clones from human cell line KG-1
  JOURNAL   DNA Res. 1 (5), 223-229 (1994)
  MEDLINE   96051398
REFERENCE   2  (residues 1 to 168)
  AUTHORS   Tsui,S., Dai,T., Roettger,S., Schempp,W., Salido,E.C. and Yen,P.H.
  TITLE     Identification of two novel proteins that interact with
            germ-cell-specific RNA-binding proteins DAZ and DAZL1
  JOURNAL   Genomics 65 (3), 266-273 (2000)
  MEDLINE   20313893
   PUBMED   10857750
COMMENT     PREDICTED REFSEQ: The mRNA record is supported by experimental
            evidence; however, the coding sequence is predicted. The reference
            sequence was derived from D31767.1.
FEATURES             Location/Qualifiers
     source          1..168
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q33-q34"
                     /sex="male"
                     /cell_line="KG-1"
                     /cell_type="myeloblast"
     Protein         1..168
                     /product="DAZ associated protein 2"
                     /note="KIAA0058 gene product"
     CDS             1..168
                     /gene="DAZAP2"
                     /coded_by="NM_014764.1:70..576"
                     /db_xref="LocusID:9802"
ORIGIN      
        1 mnskgqyptq ptypvqppgn pvypqtlhlp qappytdapp ayselyrpsf vhpgaatvpt
       61 msaafpgasl ylpmaqsvav gplgstipma yypvgpiypp gstvlveggy dagarfgaga
      121 tagnippppp gcppnaaqla vmqganvlvt qrkgnffmgg sdggytiw
//



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1: NP_006466. osteoblast specif...[gi:5453834] Links  


LOCUS       OSF-2                    836 aa            linear   PRI 14-MAY-2002
DEFINITION  osteoblast specific factor 2 (fasciclin I-like) [Homo sapiens].
ACCESSION   NP_006466
VERSION     NP_006466.1  GI:5453834
DBSOURCE    REFSEQ: aaccession NM_006475.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 836)
  AUTHORS   Kikuno,R.
  TITLE     Homo sapiens osteoblast specific factor 2 (fasciclin I-like)
            (OSF-2), mRNA
  JOURNAL   Unpublished (1992)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from D13666.1.
FEATURES             Location/Qualifiers
     source          1..836
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q13.2"
                     /clone="pKOT158"
                     /cell_type="osteoblast"
                     /tissue_type="osteosarcoma"
     Protein         1..836
                     /product="osteoblast specific factor 2 (fasciclin I-like)"
     Region          111..230
                     /region_name="Fasciclin domain"
                     /note="Fasciclin"
                     /db_xref="CDD:pfam02469"
     Region          133..230
                     /region_name="Four repeated domains in the Fasciclin I
                     family of proteins, present in many other contexts"
                     /note="FAS1"
                     /db_xref="CDD:smart00554"
     Region          235..367
                     /region_name="Fasciclin domain"
                     /note="Fasciclin"
                     /db_xref="CDD:pfam02469"
     Region          270..367
                     /region_name="Four repeated domains in the Fasciclin I
                     family of proteins, present in many other contexts"
                     /note="FAS1"
                     /db_xref="CDD:smart00554"
     Region          379..494
                     /region_name="Fasciclin domain"
                     /note="Fasciclin"
                     /db_xref="CDD:pfam02469"
     Region          404..494
                     /region_name="Four repeated domains in the Fasciclin I
                     family of proteins, present in many other contexts"
                     /note="FAS1"
                     /db_xref="CDD:smart00554"
     Region          497..630
                     /region_name="Fasciclin domain"
                     /note="Fasciclin"
                     /db_xref="CDD:pfam02469"
     Region          532..630
                     /region_name="Four repeated domains in the Fasciclin I
                     family of proteins, present in many other contexts"
                     /note="FAS1"
                     /db_xref="CDD:smart00554"
     CDS             1..836
                     /gene="OSF-2"
                     /coded_by="NM_006475.1:12..2522"
                     /note="OSF-2os"
                     /db_xref="LocusID:10631"
ORIGIN      
        1 mipflpmfsl llllivnpin annhydkila hsrirgrdqg pnvcalqqil gtkkkyfstc
       61 knwykksicg qkttvlyecc pgymrmegmk gcpavlpidh vygtlgivga tttqrysdas
      121 klreeiegkg sftyfapsne awdnldsdir rglesnvnve llnalhshmi nkrmltkdlk
      181 ngmiipsmyn nlglfinhyp ngvvtvncar iihgnqiatn gvvhvidrvl tqigtsiqdf
      241 ieaeddlssf raaaitsdil ealgrdghft lfaptneafe klprgvlerf mgdkvaseal
      301 mkyhilntlq csesimggav fetlegntie igcdgdsitv ngikmvnkkd ivtnngvihl
      361 idqvlipdsa kqvielagkq qttftdlvaq lglasalrpd geytllapvn nafsddtlsm
      421 vqrllklilq nhilkvkvgl nelyngqile tiggkqlrvf vyrtavcien scmekgskqg
      481 rngaihifre iikpaekslh eklkqdkrfs tflslleaad lkelltqpgd wtlfvptnda
      541 fkgmtseeke ilirdknalq niilyhltpg vfigkgfepg vtnilkttqg skiflkevnd
      601 tllvnelksk esdimttngv ihvvdkllyp adtpvgndql leilnkliky iqikfvrgst
      661 fkeipvtvyt tkiitkvvep kikviegslq piiktegptl tkvkiegepe frlikegeti
      721 tevihgepii kkytkiidgv pveiteketr eeriitgpei kytristggg eteetlkkll
      781 qeevtkvtkf ieggdghlfe deeikrllqg dtpvrklqan kkvqgsrrrl regrsq
//



Revised: July 5, 2002.
 
 


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1: NP_005552. lysosomal-associa...[gi:7669501] Links  


LOCUS       LAMP1                    416 aa            linear   PRI 01-NOV-2000
DEFINITION  lysosomal-associated membrane protein 1 [Homo sapiens].
ACCESSION   NP_005552
VERSION     NP_005552.2  GI:7669501
DBSOURCE    REFSEQ: aaccession NM_005561.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 416)
  AUTHORS   Viitala,J., Carlsson,S.R., Siebert,P.D. and Fukuda,M.
  TITLE     Molecular cloning of cDNAs encoding lamp A, a human lysosomal
            membrane glycoprotein with apparent Mr approximately equal to
            120,000
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 85 (11), 3743-3747 (1988)
  MEDLINE   88234502
   PUBMED   3131762
REFERENCE   2  (residues 1 to 416)
  AUTHORS   Fukuda,M., Viitala,J., Matteson,J. and Carlsson,S.R.
  TITLE     Cloning of cDNAs encoding human lysosomal membrane glycoproteins,
            h-lamp-1 and h-lamp-2. Comparison of their deduced amino acid
            sequences
  JOURNAL   J. Biol. Chem. 263 (35), 18920-18928 (1988)
  MEDLINE   89066687
   PUBMED   3198605
REFERENCE   3  (residues 1 to 416)
  AUTHORS   Mane,S.M., Marzella,L., Bainton,D.F., Holt,V.K., Cha,Y.,
            Hildreth,J.E. and August,J.T.
  TITLE     Purification and characterization of human lysosomal membrane
            glycoproteins
  JOURNAL   Arch. Biochem. Biophys. 268 (1), 360-378 (1989)
  MEDLINE   89104438
   PUBMED   2912382
REFERENCE   4  (residues 1 to 416)
  AUTHORS   Carlsson,S.R. and Fukuda,M.
  TITLE     Structure of human lysosomal membrane glycoprotein 1. Assignment of
            disulfide bonds and visualization of its domain arrangement
  JOURNAL   J. Biol. Chem. 264 (34), 20526-20531 (1989)
  MEDLINE   90062189
   PUBMED   2584229
REFERENCE   5  (residues 1 to 416)
  AUTHORS   Mattei,M.G., Matterson,J., Chen,J.W., Williams,M.A. and Fukuda,M.
  TITLE     Two human lysosomal membrane glycoproteins, h-lamp-1 and h-lamp-2,
            are encoded by genes localized to chromosome 13q34 and chromosome
            Xq24-25, respectively
  JOURNAL   J. Biol. Chem. 265 (13), 7548-7551 (1990)
  MEDLINE   90237058
   PUBMED   2332441
REFERENCE   6  (residues 1 to 416)
  AUTHORS   Carlsson,S.R. and Fukuda,M.
  TITLE     The polylactosaminoglycans of human lysosomal membrane
            glycoproteins lamp-1 and lamp-2. Localization on the peptide
            backbones
  JOURNAL   J. Biol. Chem. 265 (33), 20488-20495 (1990)
  MEDLINE   91056099
   PUBMED   2243102
REFERENCE   7  (residues 1 to 416)
  AUTHORS   Schleutker,J., Haataja,L., Renlund,M., Puhakka,L., Viitala,J.,
            Peltonen,L. and Aula,P.
  TITLE     Confirmation of the chromosomal localization of human lamp genes
            and their exclusion as candidate genes for Salla disease
  JOURNAL   Hum. Genet. 88 (1), 95-97 (1991)
  MEDLINE   92070952
   PUBMED   1959930
REFERENCE   8  (residues 1 to 416)
  AUTHORS   Sawada,R., Jardine,K.A. and Fukuda,M.
  TITLE     The genes of major lysosomal membrane glycoproteins, lamp-1 and
            lamp-2. 5'-flanking sequence of lamp-2 gene and comparison of exon
            organization in two genes
  JOURNAL   J. Biol. Chem. 268 (12), 9014-9022 (1993)
  MEDLINE   93232065
   PUBMED   8517882
REFERENCE   9  (residues 1 to 416)
  AUTHORS   Carlsson,S.R., Lycksell,P.O. and Fukuda,M.
  TITLE     Assignment of O-glycan attachment sites to the hinge-like regions
            of human lysosomal membrane glycoproteins lamp-1 and lamp-2
  JOURNAL   Arch. Biochem. Biophys. 304 (1), 65-73 (1993)
  MEDLINE   93312023
   PUBMED   8323299
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from J04182.1.
            On Apr 28, 2000 this sequence version replaced gi:5031849.
            Summary: The protein encoded by this gene is a member of a family
            of membrane glycoproteins.  This glycoprotein provides selectins
            with carbohydrate ligands.  It may also play a role in tumor cell
            metastasis.
FEATURES             Location/Qualifiers
     source          1..416
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="13"
                     /map="13q34"
     Protein         1..416
                     /product="lysosomal-associated membrane protein 1"
     sig_peptide     1..27
     mat_peptide     28..416
                     /product="lysosomal-associated membrane protein 1"
     Region          43..416
                     /region_name="Lysosome-associated membrane glycoprotein
                     (Lamp)"
                     /note="Lamp"
                     /db_xref="CDD:pfam01299"
     CDS             1..416
                     /gene="LAMP1"
                     /coded_by="NM_005561.2:191..1441"
                     /db_xref="LocusID:3916"
                     /db_xref="MIM:153330"
ORIGIN      
        1 maprsarrpl llllpvaaar phalssaamf mvkngngtac imanfsaafs vnydtksgpk
       61 nmtfdlpsda tvvlnrsscg kentsdpslv iafgrghtlt lnftrnatry svqlmsfvyn
      121 lsdthlfpna sskeiktves itdiradidk kyrcvsgtqv hmnnvtvtlh datiqaylsn
      181 ssfsrgetrc eqdrpsptta ppappspsps pvpkspsvdk ynvsgtngtc llasmglqln
      241 ltyerkdntt vtrllninpn ktsasgscga hlvtlelhse gttvllfqfg mnasssrffl
      301 qgiqlntilp dardpafkaa ngslralqat vgnsykcnae ehvrvtkafs vnifkvwvqa
      361 fkveggqfgs veeclldens tlipiavgga laglvlivli aylvgrkrsh agyqti
//



Revised: July 5, 2002.
 
 


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1: NP_000705. peripheral benzod...[gi:4502481] Links  


LOCUS       BZRP                     169 aa            linear   PRI 27-AUG-2002
DEFINITION  peripheral benzodiazapine receptor; Benzodiazepine receptor,
            peripheral type (benzodiazepine peripheral binding site);
            benzodiazepine receptor (peripheral); PBR-S; PBR [Homo sapiens].
ACCESSION   NP_000705
VERSION     NP_000705.1  GI:4502481
DBSOURCE    REFSEQ: aaccession NM_000714.3
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 169)
  AUTHORS   Riond,J., Mattei,M.G., Kaghad,M., Dumont,X., Guillemot,J.C., Le
            Fur,G., Caput,D. and Ferrara,P.
  TITLE     Molecular cloning and chromosomal localization of a human
            peripheral-type benzodiazepine receptor
  JOURNAL   Eur. J. Biochem. 195 (2), 305-311 (1991)
  MEDLINE   91146565
   PUBMED   1847678
REFERENCE   2  (residues 1 to 169)
  AUTHORS   Chang,Y.J., McCabe,R.T., Rennert,H., Budarf,M.L., Sayegh,R.,
            Emanuel,B.S., Skolnick,P. and Strauss,J.F. III.
  TITLE     The human 'peripheral-type' benzodiazepine receptor: regional
            mapping of the gene and characterization of the receptor expressed
            from cDNA
  JOURNAL   DNA Cell Biol. 11 (6), 471-480 (1992)
  MEDLINE   92398778
   PUBMED   1326278
REFERENCE   3  (residues 1 to 169)
  AUTHORS   Lin,D., Chang,Y.J., Strauss,J.F. III and Miller,W.L.
  TITLE     The human peripheral benzodiazepine receptor gene: cloning and
            characterization of alternative splicing in normal tissues and in a
            patient with congenital lipoid adrenal hyperplasia
  JOURNAL   Genomics 18 (3), 643-650 (1993)
  MEDLINE   94140364
   PUBMED   8307574
REFERENCE   4  (residues 1 to 169)
  AUTHORS   Yakovlev,A.G., Ruffo,M., Jurka,J. and Krueger,K.E.
  TITLE     Comparison of repetitive elements in the third intron of human and
            rodent mitochondrial benzodiazepine receptor-encoding genes
  JOURNAL   Gene 155 (2), 201-205 (1995)
  MEDLINE   95237610
   PUBMED   7721091
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M36035.1, L21951.1 and
            U12421.1.
            Summary: Present mainly in the mitochondrial compartment of
            peripheral tissues, PBR interacts with some benzodiazepines and has
            different affinities than its endogenous counterpart. PBR appears
            to be a key factor in the flow of cholesterol into mitochondria to
            permit the initiation of steroid hormone synthesis.  It is
            speculated that patients with congenital lipoid adrenal
            hyperplasia, who cannot make any steroids, might have a genetic
            lesion in BZRP.  A short form, PBR-S is also expressed in the same
            tissues, but at a level about ten times that of PBR.
            Transcript Variant: This splice variant, PBR, includes all four
            exons of the BZRP gene.
FEATURES             Location/Qualifiers
     source          1..169
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="22"
                     /map="22q13.31"
     Protein         1..169
                     /product="peripheral benzodiazapine receptor"
                     /note="Benzodiazepine receptor, peripheral type
                     (benzodiazepine peripheral binding site); benzodiazepine
                     receptor (peripheral); PBR-S"
     Region          5..156
                     /region_name="pfam03073, TspO_MBR, TspO/MBR family.
                     Tryptophan-rich sensory protein (TspO) is an integral
                     membrane protein that acts as a negative regulator of the
                     expression of specific photosynthesis genes in response to
                     oxygen/light. It is involved in the efflux of porphyrin
                     intermediates from the cell. This reduces the activity of
                     coproporphyrinogen III oxidase, which is thought to lead
                     to the accumulation of a putative repressor molecule that
                     inhibits the expression of specific photosynthesis genes.
                     Several conserved aromatic residues are necessary for TspO
                     function: they are thought to be involved in binding
                     porphyrin intermediates. In, the rat mitochondrial
                     peripheral benzodiazepine receptor (MBR) was shown to not
                     only retain its structure within a bacterial outer
                     membrane, but also to be able to functionally substitute
                     for TspO in TspO- mutants, and to act in a similar manner
                     to TspO in its in situ location: the outer mitochondrial
                     membrane. The biological significance of MBR remains
                     unclear, however. It is thought to be involved in a
                     variety of cellular functions, including cholesterol
                     transport in steroidogenic tissues"
     CDS             1..169
                     /gene="BZRP"
                     /coded_by="NM_000714.3:88..597"
                     /db_xref="LocusID:706"
                     /db_xref="MIM:109610"
ORIGIN      
        1 mappwvpamg ftlapslgcf vgsrfvhgeg lrwyaglqkp swhpphwvlg pvwgtlysam
       61 gygsylvwke lggftekavv plglytgqla lnwawppiff garqmgwalv dlllvsgaaa
      121 attvawyqvs plaarllypy lawlafattl nycvwrdnhg whggrrlpe
//



Revised: July 5, 2002.
 
 


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1: NP_000382. ceroid-lipofuscin...[gi:5729770] Links  


LOCUS       CLN2                     563 aa            linear   PRI 23-JUL-2002
DEFINITION  ceroid-lipofuscinosis, neuronal 2, late infantile
            (Jansky-Bielschowsky disease) [Homo sapiens].
ACCESSION   NP_000382
VERSION     NP_000382.3  GI:5729770
DBSOURCE    REFSEQ: aaccession NM_000391.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 563)
  AUTHORS   Sleat,D.E., Donnelly,R.J., Lackland,H., Liu,C.G., Sohar,I.,
            Pullarkat,R.K. and Lobel,P.
  TITLE     Association of mutations in a lysosomal protein with classical
            late-infantile neuronal ceroid lipofuscinosis
  JOURNAL   Science 277 (5333), 1802-1805 (1997)
  MEDLINE   97442529
   PUBMED   9295267
REFERENCE   2  (residues 1 to 563)
  AUTHORS   Liu,C.G., Sleat,D.E., Donnelly,R.J. and Lobel,P.
  TITLE     Structural organization and sequence of CLN2, the defective gene in
            classical late infantile neuronal ceroid lipofuscinosis
  JOURNAL   Genomics 50 (2), 206-212 (1998)
  MEDLINE   98317534
   PUBMED   9653647
REFERENCE   3  (residues 1 to 563)
  AUTHORS   Rawlings,N.D. and Barrett,A.J.
  TITLE     Tripeptidyl-peptidase I is apparently the CLN2 protein absent in
            classical late-infantile neuronal ceroid lipofuscinosis
  JOURNAL   Biochim. Biophys. Acta 1429 (2), 496-500 (1999)
  MEDLINE   99143780
   PUBMED   9989235
REFERENCE   4  (residues 1 to 563)
  AUTHORS   Vines,D.J. and Warburton,M.J.
  TITLE     Classical late infantile neuronal ceroid lipofuscinosis fibroblasts
            are deficient in lysosomal tripeptidyl peptidase I
  JOURNAL   FEBS Lett. 443 (2), 131-135 (1999)
  MEDLINE   99142696
   PUBMED   9989590
REFERENCE   5  (residues 1 to 563)
  AUTHORS   Lin,L. and Lobel,P.
  TITLE     Expression and analysis of CLN2 variants in CHO cells: Q100R
            represents a polymorphism, and G389E and R447H represent
            loss-of-function mutations
  JOURNAL   Hum. Mutat. 18 (2), 165 (2001)
  MEDLINE   21354493
   PUBMED   11462245
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF039704.1.
            On Aug 11, 1999 this sequence version replaced gi:5597013.
FEATURES             Location/Qualifiers
     source          1..563
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p15"
                     /tissue_type="placenta"
                     /clone_lib="Clontech genomic library, Cat number HL1067j"
     Protein         1..563
                     /product="ceroid-lipofuscinosis, neuronal 2, late
                     infantile (Jansky-Bielschowsky disease)"
     variation       62
                     /allele="S"
                     /allele="L"
                     /db_xref="dbSNP:2734715"
     variation       100
                     /allele="Q"
                     /allele="R"
                     /db_xref="dbSNP:1800746"
     CDS             1..563
                     /gene="CLN2"
                     /coded_by="NM_000391.2:30..1721"
                     /note="deficient in late-infantile neuronal ceroid
                     lipofuscinosis"
                     /db_xref="LocusID:1200"
                     /db_xref="MIM:204500"
ORIGIN      
        1 mglqacllgl falilsgkcs yspepdqrrt lppgwvslgr adpeeelslt falrqqnver
       61 lselvqavsd psspqygkyl tlenvadlvr pspltlhtvq kwllaagaqk chsvitqdfl
      121 tcwlsirqae lllpgaefhh yvggptethv vrsphpyqlp qalaphvdfv gglhrfppts
      181 slrqrpepqv tgtvglhlgv tpsvirkryn ltsqdvgsgt snnsqacaqf leqyfhdsdl
      241 aqfmrlfggn fahqasvarv vgqqgrgrag ieasldvqyl msaganistw vysspgrheg
      301 qepflqwlml lsnesalphv htvsygdded slssayiqrv ntelmkaaar gltllfasgd
      361 sgagcwsvsg rhqfrptfpa sspyvttvgg tsfqepflit neivdyisgg gfsnvfprps
      421 yqeeavtkfl sssphlppss yfnasgrayp dvaalsdgyw vvsnrvpipw vsgtsastpv
      481 fggilsline hrilsgrppl gflnprlyqq hgaglfdvtr gchescldee vegqgfcsgp
      541 gwdpvtgwgt pnfpallktl lnp
//



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1: NP_056107. KIAA0747 protein ...[gi:14149680] Links  


LOCUS       MBC2                    1104 aa            linear   PRI 08-OCT-2002
DEFINITION  KIAA0747 protein [Homo sapiens].
ACCESSION   NP_056107
VERSION     NP_056107.1  GI:14149680
DBSOURCE    REFSEQ: aaccession NM_015292.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1104)
  AUTHORS   Nagase,T., Ishikawa,K., Suyama,M., Kikuno,R., Miyajima,N.,
            Tanaka,A., Kotani,H., Nomura,N. and Ohara,O.
  TITLE     Prediction of the coding sequences of unidentified human genes. XI.
            The complete sequences of 100 new cDNA clones from brain which code
            for large proteins in vitro
  JOURNAL   DNA Res. 5 (5), 277-286 (1998)
  MEDLINE   99087487
   PUBMED   9872452
REFERENCE   2  (residues 1 to 1104)
  AUTHORS   Morris,N.J., Ross,S.A., Neveu,J.M., Lane,W.S. and Lienhard,G.E.
  TITLE     Cloning and preliminary characterization of a 121 kDa protein with
            multiple predicted C2 domains
  JOURNAL   Biochim. Biophys. Acta 1431 (2), 525-530 (1999)
  MEDLINE   99280327
   PUBMED   10350628
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC004998.1.
FEATURES             Location/Qualifiers
     source          1..1104
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q12"
                     /clone="MGC:4422 IMAGE:2958094"
                     /tissue_type="Kidney, renal cell adenocarcinoma"
                     /clone_lib="NIH_MGC_14"
                     /lab_host="DH10B-R"
                     /note="Vector: pOTB7"
     Protein         1..1104
                     /product="KIAA0747 protein"
     Region          330..432
                     /region_name="Protein kinase C conserved region 2 (CalB)"
                     /note="C2"
                     /db_xref="CDD:smart00239"
     Region          331..417
                     /region_name="C2 domain"
                     /note="C2"
                     /db_xref="CDD:pfam00168"
     Region          479..548
                     /region_name="Protein kinase C conserved region 2 (CalB)"
                     /note="C2"
                     /db_xref="CDD:smart00239"
     Region          480..548
                     /region_name="C2 domain"
                     /note="C2"
                     /db_xref="CDD:pfam00168"
     Region          648..750
                     /region_name="Protein kinase C conserved region 2 (CalB)"
                     /note="C2"
                     /db_xref="CDD:smart00239"
     Region          649..716
                     /region_name="C2 domain"
                     /note="C2"
                     /db_xref="CDD:pfam00168"
     Region          799..865
                     /region_name="Protein kinase C conserved region 2 (CalB)"
                     /note="C2"
                     /db_xref="CDD:smart00239"
     Region          800..865
                     /region_name="C2 domain"
                     /note="C2"
                     /db_xref="CDD:pfam00168"
     Region          989..1092
                     /region_name="Protein kinase C conserved region 2 (CalB)"
                     /note="C2"
                     /db_xref="CDD:smart00239"
     Region          992..1077
                     /region_name="C2 domain"
                     /note="C2"
                     /db_xref="CDD:pfam00168"
     CDS             1..1104
                     /gene="MBC2"
                     /coded_by="NM_015292.1:51..3365"
                     /db_xref="LocusID:23344"
ORIGIN      
        1 merspgegps pspmdqpsap sdptdqppaa hakpdpgsgg qpagpgaage alavltsfgr
       61 rllvlipvyl agavglsvgf vlfglalylg wrrvrdeker slraarqlld deeqltaktl
      121 ymshrelpaw vsfpdvekae wlnkivaqvw pflgqymekl laetvapavr gsnphlqtft
      181 ftrvelgekp lriigvkvhp gqrkeqilld lnisyvgdvq idvevkkyfc kagvkgmqlh
      241 gvlrvilepl igdlpfvgav smffirrptl dinwtgmtnl ldipglssls dtmimdsiaa
      301 flvlpnrllv plvpdlqdva qlrsplprgi irihllaarg lsskdkyvkg liegksdpya
      361 lvrlgtqtfc srvideelnp qwgetyevmv hevpgqeiev evfdkdpdkd dflgrmkldv
      421 gkvlqasvld dwfplqggqg qvhlrlewls llsdaekleq vlqwnwgvss rpdppsaail
      481 vvyldraqdl plkkgnkepn pmvqlsiqdv tqeskavyst ncpvweeafr fflqdpqsqe
      541 ldvqvkddsr altlgaltlp larlltapel ildqwfqlss sgpnsrlymk lvmrilylds
      601 seicfptvpg cpgawdvdse npqrgssvda pprpchttpd sqfgtehvlr ihvleaqdli
      661 akdrflgglv kgksdpyvkl klagrsfrsh vvredlnprw nevfevivts vpgqelevev
      721 fdkdldkddf lgrckvrltt vlnsgfldew ltledvpsgr lhlrlerltp rptaaeleev
      781 lqvnsliqtq ksaelaaall siymeraedl plrkgtkhls pyatltvgds shktktisqt
      841 sapvwdesas flirkphtes lelqvrgegt gvlgslslpl sellvadqlc ldrwftlssg
      901 qgqvllraql gilvsqhsgv eahshsyshs ssslseepel sggpphitss apelrqrlth
      961 vdspleapag plgqvkltlw yyseerklvs ivhgcrslrq ngrdppdpyv sllllpdknr
     1021 gtkrrtsqkk rtlspefner fewelpldea qrrkldvsvk snssfmsrer ellgkvqldl
     1081 aetdlsqgva rwydlmdnkd kgss
//



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1: NP_000261. purine nucleoside...[gi:4557801] Links  


LOCUS       NP                       289 aa            linear   PRI 27-AUG-2002
DEFINITION  purine nucleoside phosphorylase [Homo sapiens].
ACCESSION   NP_000261
VERSION     NP_000261.1  GI:4557801
DBSOURCE    REFSEQ: aaccession NM_000270.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 289)
  AUTHORS   Williams,S.R., Goddard,J.M. and Martin,D.W. Jr.
  TITLE     Human purine nucleoside phosphorylase cDNA sequence and genomic
            clone characterization
  JOURNAL   Nucleic Acids Res. 12 (14), 5779-5787 (1984)
  MEDLINE   84272252
   PUBMED   6087295
REFERENCE   2  (residues 1 to 289)
  AUTHORS   Williams,S.R., Gekeler,V., McIvor,R.S. and Martin,D.W. Jr.
  TITLE     A human purine nucleoside phosphorylase deficiency caused by a
            single base change
  JOURNAL   J. Biol. Chem. 262 (5), 2332-2338 (1987)
  MEDLINE   87137463
   PUBMED   3029074
REFERENCE   3  (residues 1 to 289)
  AUTHORS   Markert,M.L.
  TITLE     Purine nucleoside phosphorylase deficiency
  JOURNAL   Immunodefic Rev 3 (1), 45-81 (1991)
  MEDLINE   92030090
   PUBMED   1931007
REFERENCE   4  (residues 1 to 289)
  AUTHORS   Andrews,L.G. and Markert,M.L.
  TITLE     Exon skipping in purine nucleoside phosphorylase mRNA processing
            leading to severe immunodeficiency
  JOURNAL   J. Biol. Chem. 267 (11), 7834-7838 (1992)
  MEDLINE   92218449
   PUBMED   1560016
REFERENCE   5  (residues 1 to 289)
  AUTHORS   Erion,M.D., Takabayashi,K., Smith,H.B., Kessi,J., Wagner,S.,
            Honger,S., Shames,S.L. and Ealick,S.E.
  TITLE     Purine nucleoside phosphorylase. 1. Structure-function studies
  JOURNAL   Biochemistry 36 (39), 11725-11734 (1997)
  MEDLINE   97452591
   PUBMED   9305962
REFERENCE   6  (residues 1 to 289)
  AUTHORS   Erion,M.D., Stoeckler,J.D., Guida,W.C., Walter,R.L. and Ealick,S.E.
  TITLE     Purine nucleoside phosphorylase. 2. Catalytic mechanism
  JOURNAL   Biochemistry 36 (39), 11735-11748 (1997)
  MEDLINE   97452592
   PUBMED   9305963
REFERENCE   7  (residues 1 to 289)
  AUTHORS   Stoeckler,J.D., Poirot,A.F., Smith,R.M., Parks,R.E. Jr.,
            Ealick,S.E., Takabayashi,K. and Erion,M.D.
  TITLE     Purine nucleoside phosphorylase. 3. Reversal of purine base
            specificity by site-directed mutagenesis
  JOURNAL   Biochemistry 36 (39), 11749-11756 (1997)
  MEDLINE   97452593
   PUBMED   9305964
REFERENCE   8  (residues 1 to 289)
  AUTHORS   Sheppard,T.L., Ordoukhanian,P. and Joyce,G.F.
  TITLE     A DNA enzyme with N-glycosylase activity
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 97 (14), 7802-7807 (2000)
  MEDLINE   20345067
   PUBMED   10884411
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X00737.1.
            Summary: NP encodes the enzyme purine nucleoside phosphorylase that
            together with adenosine deaminase (ADA) serves a key role in purine
            catabolism, referred to as the salvage pathway. Mutations in either
            enzyme result in a severe combined immunodeficiency (SCID).
FEATURES             Location/Qualifiers
     source          1..289
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q13.1"
     Protein         1..289
                     /product="purine nucleoside phosphorylase"
                     /EC_number="2.4.2.1"
     Region          24..284
                     /region_name="pfam00896, Mtap_PNP, Phosphorylase family 2"
     CDS             1..289
                     /gene="NP"
                     /coded_by="NM_000270.1:110..979"
                     /db_xref="LocusID:4860"
                     /db_xref="MIM:164050"
ORIGIN      
        1 mengytyedy kntaewllsh tkhrpqvaii cgsglggltd kltqaqifdy seipnfprst
       61 vpghagrlvf gflngracvm mqgrfhmyeg yplwkvtfpv rvfhllgvdt lvvtnaaggl
      121 npkfevgdim lirdhinlpg fsgqnplrgp nderfgdrfp amsdaydrtm rqralstwkq
      181 mgeqrelqeg tyvmvagpsf etvaecrvlq klgadavgms tvpevivarh cglrvfgfsl
      241 itnkvimdye slekanheev laagkqaaqk leqfvsilma siplpdkas
//



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1: NP_002154. interferon consen...[gi:4504567] Links  


LOCUS       ICSBP1                   426 aa            linear   PRI 10-FEB-2002
DEFINITION  interferon consensus sequence binding protein 1; H-ICSBP [Homo
            sapiens].
ACCESSION   NP_002154
VERSION     NP_002154.1  GI:4504567
DBSOURCE    REFSEQ: aaccession NM_002163.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 426)
  AUTHORS   Weisz,A., Marx,P., Sharf,R., Appella,E., Driggers,P.H., Ozato,K.
            and Levi,B.Z.
  TITLE     Human interferon consensus sequence binding protein is a negative
            regulator of enhancer elements common to interferon-inducible genes
  JOURNAL   J. Biol. Chem. 267 (35), 25589-25596 (1992)
  MEDLINE   93094284
   PUBMED   1460054
REFERENCE   2  (residues 1 to 426)
  AUTHORS   Holtschke,T., Lohler,J., Kanno,Y., Fehr,T., Giese,N.,
            Rosenbauer,F., Lou,J., Knobeloch,K.P., Gabriele,L., Waring,J.F.,
            Bachmann,M.F., Zinkernagel,R.M., Morse,H.C. III, Ozato,K. and
            Horak,I.
  TITLE     Immunodeficiency and chronic myelogenous leukemia-like syndrome in
            mice with a targeted mutation of the ICSBP gene
  JOURNAL   Cell 87 (2), 307-317 (1996)
  MEDLINE   97015086
   PUBMED   8861914
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M91196.1.
            Summary: Interferon consensus sequence-binding protein (ICSBP) is a
            transcription factor of the interferon (IFN) regulatory factor
            (IRF) family. Proteins of this family are composed of a conserved
            DNA-binding domain in the N-terminal region and a divergent
            C-terminal region that serves as the regulatory domain.  The IRF
            family proteins bind to the IFN-stimulated response element (ISRE)
            and regulate expression of genes stimulated by type I IFNs, namely
            IFN-alpha and IFN-beta.  IRF family proteins also control
            expression of IFN-alpha and IFN-beta-regulated genes that are
            induced by viral infection.
FEATURES             Location/Qualifiers
     source          1..426
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16q24.1"
     Protein         1..426
                     /product="interferon consensus sequence binding protein 1"
                     /function="involved in the transcription regulation of
                     interferon-inducible genes"
                     /note="H-ICSBP"
     Region          3..114
                     /region_name="Interferon regulatory factor transcription
                     factor"
                     /note="IRF"
                     /db_xref="CDD:pfam00605"
     Region          5..114
                     /region_name="interferon regulatory factor"
                     /note="IRF"
                     /db_xref="CDD:smart00348"
     CDS             1..426
                     /gene="ICSBP1"
                     /coded_by="NM_002163.1:48..1328"
                     /db_xref="LocusID:3394"
                     /db_xref="MIM:601565"
ORIGIN      
        1 mcdrnggrrl rqwlieqids smypgliwen eeksmfripw khagkqdynq evdasifkaw
       61 avfkgkfkeg dkaepatwkt rlrcalnksp dfeevtdrsq ldisepykvy rivpeeeqkc
      121 klgvatagcv nevtemecgr seidelikep svddymgmik rspsppeacr sqllpdwwaq
      181 qpstgvplvt gyttydahhs afsqmvisfy yggklvgqat ttcpegcrls lsqpglpgtk
      241 lygpeglelv rfppadaips erqrqvtrkl fghlergvll hssrqgvfvk rlcqgrvfcs
      301 gnavvckgrp nklerdevvq vfdtsqffre lqqfynsqgr lpdgrvvlcf geefpdmapl
      361 rsklilvqie qlyvrqlaee agkscgagsv mqapeepppd qvfrmfpdic ashqrsffre
      421 nqqitv
//



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1: NP_001469. UDP-N-acetyl-alph...[gi:4503893] Links  


LOCUS       GALGT                    533 aa            linear   PRI 03-FEB-2001
DEFINITION  UDP-N-acetyl-alpha-D-galactosamine:(N-acetylneuraminyl)-
            galactosylglucosylceramide N-acetylgalactosaminyltransferase;
            UDP-N-acetyl-alpha-D-galactosamine:(N-acetylneuraminyl)-;
            beta1,4GalNAc-T; GalNAc-T [Homo sapiens].
ACCESSION   NP_001469
VERSION     NP_001469.1  GI:4503893
DBSOURCE    REFSEQ: aaccession NM_001478.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 533)
  AUTHORS   Nagata,Y., Yamashiro,S., Yodoi,J., Lloyd,K.O., Shiku,H. and
            Furukawa,K.
  TITLE     Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase
            cDNAs that determine the expression of GM2 and GD2 gangliosides
  JOURNAL   J. Biol. Chem. 267 (17), 12082-12089 (1992)
  MEDLINE   92291088
   PUBMED   1601877
REFERENCE   2  (residues 1 to 533)
  AUTHORS   Nagata,Y., Yamashiro,S., Yodoi,J., Lloyd,K.O., Shiku,H. and
            Furukawa,K.
  TITLE     Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase
            cDNAs that determine the expression of GM2 and GD2 gangliosides
  JOURNAL   J. Biol. Chem. 269 (9), 7045 (1994)
  MEDLINE   94165113
   PUBMED   8120069
REFERENCE   3  (residues 1 to 533)
  AUTHORS   Furukawa,K., Soejima,H., Niikawa,N. and Shiku,H.
  TITLE     Genomic organization and chromosomal assignment of the human beta1,
            4-N-acetylgalactosaminyltransferase gene. Identification of
            multiple transcription units
  JOURNAL   J. Biol. Chem. 271 (34), 20836-20844 (1996)
  MEDLINE   96355429
   PUBMED   8702839
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M83651.1 and L76079.1.
            Summary: GM2 and GD2 gangliosides are sialic acid-containing
            glycosphingolipids. GalNAc-T is the enzyme involved in the
            biosynthesis of G(M2) and G(D2) glycosphingolipids. GalNAc-T
            catalyzes the transfer of GalNAc into G(M3) and G(D3) by a beta-1,4
            linkage, resulting in the synthesis of G(M2) and G(D2),
            respectively.
            Transcript Variant: This entry contains mRNA sequence for
            alternative untranslated exon 1a which overlaps with that of
            alternative untranslated exon 1b. An alternative untranslated exon
            1c that does not overlap with this sequence has also been
            described.
FEATURES             Location/Qualifiers
     source          1..533
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q13.3"
     Protein         1..533
                     /product="UDP-N-acetyl-alpha-D-galactosamine:(N-
                     acetylneuraminyl)-galactosylglucosylceramide
                     N-acetylgalactosaminyltransferase"
                     /EC_number="2.4.1.92"
                     /note="beta-1,4 N-acetylgalactosaminyltransferase;
                     G(M2)/G(D2) synthase;
                     UDP-N-acetyl-alpha-D-galactosamine:(N-acetylneuraminyl)-;
                     beta1,4GalNAc-T; GalNAc-T"
     Site            8..25
                     /site_type="transmembrane-region"
                     /note="signal-anchor"
     variation       35
                     /allele="L"
                     /allele="V"
                     /db_xref="dbSNP:774896"
     variation       172
                     /allele="R"
                     /allele="G"
                     /db_xref="dbSNP:810205"
     Region          280..439
                     /region_name="Glycosyl transferases"
                     /note="Glycos_transf_2"
                     /db_xref="CDD:pfam00535"
     CDS             1..533
                     /gene="GALGT"
                     /coded_by="NM_001478.2:434..2035"
                     /db_xref="LocusID:2583"
                     /db_xref="MIM:601873"
ORIGIN      
        1 mwlgrralca lvlllacasl gllyastrda pglrlplapw appqsprrpe lpdlapepry
       61 ahipvrikeq vvgllawnnc scessggglp lpfqkqvrai dltkafdpae lraasatreq
      121 efqaflsrsq spadqlliap ansplqyplq gvevqplrsi lvpglslqaa sgqevyqvnl
      181 taslgtwdva gevtgvtltg egqadltlvs pgldqlnrql qlvtyssrsy qtntadtvrf
      241 stegheaaft irirhppnpr lyppgslpqg aqynisalvt iatktflryd rlralitsir
      301 rfyptvtvvi addsdkperv sgpyvehylm pfgkgwfagr nlavsqvttk yvlwvdddfv
      361 ftartrlerl vdvlertpld lvggavreis gfattyrqll svepgapglg nclrqrrgfh
      421 helvgfpgcv vtdgvvnffl artdkvrevg fdprlsrvah leffldglgs lrvgscsdvv
      481 vdhasklklp wtsrdagaet yaryrypgsl desqmakhrl lffkhrlqcm tsq
//



Revised: July 5, 2002.
 
 


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1: NP_004116. guanine nucleotid...[gi:21361097] Links  


LOCUS       GNG10                    153 aa            linear   PRI 10-JUN-2002
DEFINITION  guanine nucleotide binding protein 10 [Homo sapiens].
ACCESSION   NP_004116
VERSION     NP_004116.2  GI:21361097
DBSOURCE    REFSEQ: aaccession NM_004125.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 153)
  AUTHORS   Strausberg,R.
  TITLE     Homo sapiens guanine nucleotide binding protein 10 (GNG10), mRNA
  JOURNAL   Unpublished (2001)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC015391.1.
            On Jun 10, 2002 this sequence version replaced gi:4758446.
FEATURES             Location/Qualifiers
     source          1..153
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
                     /clone="MGC:21698 IMAGE:4425229"
                     /tissue_type="Kidney, hypernephroma"
                     /clone_lib="NIH_MGC_89"
                     /lab_host="DH10B"
                     /note="Vector: pCMV-SPORT6"
     Protein         1..153
                     /product="guanine nucleotide binding protein 10"
     Region          48..112
                     /region_name="DnaJ molecular chaperone homology domain"
                     /note="DnaJ"
                     /db_xref="CDD:smart00271"
     Region          49..123
                     /region_name="DnaJ domain"
                     /note="DnaJ"
                     /db_xref="CDD:pfam00226"
     Region          109..153
                     /region_name="G protein gamma subunit-like motifs"
                     /note="GGL"
                     /db_xref="CDD:smart00224"
     Region          109..146
                     /region_name="GGL domain"
                     /note="G-gamma"
                     /db_xref="CDD:pfam00631"
     CDS             1..153
                     /gene="GNG10"
                     /coded_by="NM_004125.2:23..484"
                     /db_xref="LocusID:2790"
                     /db_xref="MIM:604389"
ORIGIN      
        1 mgapllspgw gagaagrrww mllapllpal llvrpagalv eglycgtrdc yevlgvsrsa
       61 gkaeiarayr qlarryhpdr yrpqpgdegp grtpqsaeea fllvatayet lkvsqaaael
      121 qqycmqnack dallvgvpag snpfreprsc all
//



Revised: July 5, 2002.
 
 


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1: NP_057212. coatomer protein ...[gi:11559929] Links  


LOCUS       COPG                     874 aa            linear   PRI 09-OCT-2002
DEFINITION  coatomer protein complex, subunit gamma 1; coat protein gamma-cop
            [Homo sapiens].
ACCESSION   NP_057212
VERSION     NP_057212.1  GI:11559929
DBSOURCE    REFSEQ: aaccession NM_016128.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 874)
  AUTHORS   Hahn,Y., Lee,Y.J., Yun,J.H., Yang,S.K., Park,C.W., Mita,K.,
            Huh,T.L., Rhee,M. and Chung,J.H.
  TITLE     Duplication of genes encoding non-clathrin coat protein gamma-COP
            in vertebrate, insect and plant evolution
  JOURNAL   FEBS Lett. 482 (1-2), 31-36 (2000)
  MEDLINE   20472554
   PUBMED   11018518
REFERENCE   2  (residues 1 to 874)
  AUTHORS   Futatsumori,M., Kasai,K., Takatsu,H., Shin,H.W. and Nakayama,K.
  TITLE     Identification and characterization of novel isoforms of COP I
            subunits
  JOURNAL   J. Biochem. 128 (5), 793-801 (2000)
  MEDLINE   20512057
   PUBMED   11056392
REFERENCE   3  (residues 1 to 874)
  AUTHORS   Bermak,J.C., Li,M., Bullock,C., Weingarten,P. and Zhou,Q.Y.
  TITLE     Interaction of gamma-COP with a transport motif in the D1 receptor
            C-terminus
  JOURNAL   Eur. J. Cell Biol. 81 (2), 77-85 (2002)
  MEDLINE   21889771
   PUBMED   11893085
REFERENCE   4  (residues 1 to 874)
  AUTHORS   Peng,Y., Song,H., Dai,M., Huang,Q., Mao,Y., Zhang,Q., Mao,M.,
            Fu,G., Luo,M., Chen,J. and Hu,R.
  TITLE     Human coat protein gamma-cop gene
  JOURNAL   Unpublished
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AF100756.1.
FEATURES             Location/Qualifiers
     source          1..874
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="3"
                     /map="3"
                     /tissue_type="pituitary"
     Protein         1..874
                     /product="coatomer protein complex, subunit gamma 1"
                     /note="coat protein gamma-cop"
     Region          23..537
                     /region_name="Adaptin N terminal region. This family
                     consists of the N terminal region of various alpha, beta
                     and gamma subunits of the AP-1, AP-2 and AP-3 adaptor
                     protein complexes. The adaptor protein (AP) complexes are
                     involved in the formation of clathrin-coated pits and
                     vesicles. The N-terminal region of the various adaptor
                     proteins (APs) is constant by comparison to the C-terminal
                     which is variable within members of the AP-2 family"
                     /note="Adaptin_N"
                     /db_xref="CDD:pfam01602"
     CDS             1..874
                     /gene="COPG"
                     /coded_by="NM_016128.2:76..2700"
                     /db_xref="LocusID:22820"
ORIGIN      
        1 mlkkfdkkde esgggsnpfq hleksavlqe arvfnetpin prkcahiltk ilylinqgeh
       61 lgtteateaf famtklfqsn dptlrrmcyl tikemsciae dviivtsslt kdmtgkedny
      121 rgpavralcq itdstmlqai erymkqaivd kvpsvsssal vsslhllkcs fdvvkrwvne
      181 aqeaassdni mvqyhalgll yhvrkndrla vnkmiskvtr hglkspfayc mmirvaskql
      241 eeedgsrdsp lfdfiesclr nkhemvvyea asaivnlpgc sakelapavs vlqlfcsspk
      301 aalryaavrt lnkvamkhps avtacnldle nlvtdsnrsi atlaittllk tgsessidrl
      361 mkqissfmse isdefkvvvv qaisalcqky prkhavlmnf lftmlreegg feykraivdc
      421 iisiieense sketglshlc efiedceftv latrilhllg qegpkttnps kyirfiynrv
      481 vleheevrag avsalakfga qneemlpsil vllkrcvmdd dnevrdratf ylnvleqkqk
      541 alnagyilng ltvsipgler alqqytleps ekpfdlksvp latapmaeqr testpitavk
      601 qpekvaatrq eifqeqlaav pefrglgplf ksspepvalt eseteyvirc tkhtftnhmv
      661 fqfdctntln dqtlenvtvq mepteayevl cyvparslpy nqpgtcytlv alpkedptav
      721 actfscmmkf tvkdcdpttg etddegyede yvledlevtv adhiqkvmkl nfeaawdevg
      781 defekeetft lstiktleea vgnivkflgm hpcersdkvp dnknthtlll agvfrgghdi
      841 lvrsrlllld tvtmqvtars leelpvdiil asvg
//



Revised: July 5, 2002.
 
 


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1: NP_006111. major histocompat...[gi:18765715] Links  


LOCUS       HLA-DMA                  261 aa            linear   PRI 19-FEB-2002
DEFINITION  major histocompatibility complex, class II, DM alpha precursor; HLA
            class II alpha chain-like; class II histocompatibility antigen, M
            alpha chain [Homo sapiens].
ACCESSION   NP_006111
VERSION     NP_006111.2  GI:18765715
DBSOURCE    REFSEQ: aaccession NM_006120.2
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 261)
  AUTHORS   Kelly,A.P., Monaco,J.J., Cho,S.G. and Trowsdale,J.
  TITLE     A new human HLA class II-related locus, DM
  JOURNAL   Nature 353 (6344), 571-573 (1991)
  MEDLINE   92018223
   PUBMED   1922365
REFERENCE   2  (residues 1 to 261)
  AUTHORS   Kelly,A., Powis,S.H., Glynne,R., Radley,E., Beck,S. and
            Trowsdale,J.
  TITLE     Second proteasome-related gene in the human MHC class II region
  JOURNAL   Nature 353 (6345), 667-668 (1991)
  MEDLINE   92018253
   PUBMED   1922385
REFERENCE   3  (residues 1 to 261)
  AUTHORS   Radley,E., Alderton,R.P., Kelly,A., Trowsdale,J. and Beck,S.
  TITLE     Genomic organization of HLA-DMA and HLA-DMB. Comparison of the gene
            organization of all six class II families in the human major
            histocompatibility complex
  JOURNAL   J. Biol. Chem. 269 (29), 18834-18838 (1994)
  MEDLINE   94308138
   PUBMED   8034636
REFERENCE   4  (residues 1 to 261)
  AUTHORS   Weber,D.A., Evavold,B.D. and Jensen,P.E.
  TITLE     Enhanced dissociation of HLA-DR-bound peptides in the presence of
            HLA-DM
  JOURNAL   Science 274 (5287), 618-620 (1996)
  MEDLINE   97002457
   PUBMED   8849454
REFERENCE   5  (residues 1 to 261)
  AUTHORS   Kropshofer,H., Hammerling,G.J. and Vogt,A.B.
  TITLE     The impact of the non-classical MHC proteins HLA-DM and HLA-DO on
            loading of MHC class II molecules
  JOURNAL   Immunol. Rev. 172, 267-278 (1999)
  MEDLINE   20097570
   PUBMED   10631952
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from X62744.1.
            On Feb 19, 2002 this sequence version replaced gi:5174459.
            Summary: HLA-DMA belongs to the HLA class II alpha chain
            paralogues. This class II molecule is a heterodimer consisting of
            an alpha (DMA) and a beta chain (DMB), both anchored in the
            membrane. It is located in intracellular vesicles. DM plays a
            central role in the peptide loading of MHC class II molecules by
            helping to release the CLIP molecule from the peptide binding site.
            Class II molecules are expressed in antigen presenting cells (APC:
            B lymphocytes, dendritic cells, macrophages). The alpha chain is
            approximately 33-35 kDa and its gene contains 5 exons. Exon one
            encodes the leader peptide, exons 2 and 3 encode the two
            extracellular domains, exon 4 encodes the transmembrane domain and
            the cytoplasmic tail.
FEATURES             Location/Qualifiers
     source          1..261
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p21.3"
     Protein         1..261
                     /product="major histocompatibility complex, class II, DM
                     alpha precursor"
                     /note="HLA class II alpha chain-like; class II
                     histocompatibility antigen, M alpha chain"
     sig_peptide     1..26
     mat_peptide     27..261
                     /product="major histocompatibility complex, class II, DM
                     alpha"
     Region          41..124
                     /region_name="Class II histocompatibility antigen, alpha
                     domain"
                     /note="MHC_II_alpha"
                     /db_xref="CDD:pfam00993"
     Region          140..204
                     /region_name="Immunoglobulin domain"
                     /note="ig"
                     /db_xref="CDD:pfam00047"
     Region          142..207
                     /region_name="Immunoglobulin C-Type"
                     /note="IGc1"
                     /db_xref="CDD:smart00407"
     variation       166
                     /allele="I"
                     /allele="V"
                     /allele="I"
                     /allele="V"
                     /allele="I"
                     /allele="V"
                     /db_xref="dbSNP:1063478"
     CDS             1..261
                     /gene="HLA-DMA"
                     /coded_by="NM_006120.2:46..831"
                     /db_xref="LocusID:3108"
                     /db_xref="MIM:142855"
                     /db_xref="LocusID:3108"
                     /db_xref="MIM:142855"
ORIGIN      
        1 mgheqnqgaa llqmlpllwl lphswavpea ptpmwpddlq nhtflhtvyc qdgspsvgls
       61 eaydedqlff fdfsqntrvp rlpefadwaq eqgdapailf dkefcewmiq qigpkldgki
      121 pvsrgfpiae vftlkplefg kpntlvcfvs nlfppmltvn wqhhsvpveg fgptfvsavd
      181 glsfqafsyl nftpepsdif scivtheidr ytaiaywvpr nalpsdllen vlcgvafglg
      241 vlgiivgivl iiyfrkpcsg d
//



Revised: July 5, 2002.
 
 


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1: NP_003235. TGFB-induced fact...[gi:4507473] Links  


LOCUS       TGIF                     272 aa            linear   PRI 24-JUL-2001
DEFINITION  TGFB-induced factor (TALE family homeobox); TG-interacting factor
            [Homo sapiens].
ACCESSION   NP_003235
VERSION     NP_003235.1  GI:4507473
DBSOURCE    REFSEQ: aaccession NM_003244.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 272)
  AUTHORS   Munke M, Page DC, Brown LG, Armson BA, Zackai EH, Mennuti MT and
            Emanuel BS.
  TITLE     Molecular detection of a Yp/18 translocation in a 45,X
            holoprosencephalic male
  JOURNAL   Hum. Genet. 80 (3), 219-223 (1988)
  MEDLINE   89053303
   PUBMED   3192211
REFERENCE   2  (residues 1 to 272)
  AUTHORS   Overhauser J, Mitchell HF, Zackai EH, Tick DB, Rojas K and Muenke
            M.
  TITLE     Physical mapping of the holoprosencephaly critical region in
            18p11.3
  JOURNAL   Am. J. Hum. Genet. 57 (5), 1080-1085 (1995)
  MEDLINE   96026102
   PUBMED   7485158
REFERENCE   3  (residues 1 to 272)
  AUTHORS   Bertolino,E., Reimund,B., Wildt-Perinic,D. and Clerc,R.G.
  TITLE     A novel homeobox protein which recognizes a TGT core and
            functionally interferes with a retinoid-responsive motif
  JOURNAL   J. Biol. Chem. 270 (52), 31178-31188 (1995)
  MEDLINE   96125101
   PUBMED   8537382
REFERENCE   4  (residues 1 to 272)
  AUTHORS   Gripp KW, Wotton D, Edwards MC, Roessler E, Ades L, Meinecke P,
            Richieri-Costa A, Zackai EH, Massague J, Muenke M and Elledge SJ.
  TITLE     Mutations in TGIF cause holoprosencephaly and link NODAL signalling
            to human neural axis determination
  JOURNAL   Nat. Genet. 25 (2), 205-208 (2000)
  MEDLINE   20296626
   PUBMED   10835638
REFERENCE   5  (residues 1 to 272)
  AUTHORS   Yang Y, Hwang CK, D'Souza UM, Lee SH, Junn E and Mouradian MM.
  TITLE     Three-amino acid extension loop homeodomain proteins Meis2 and TGIF
            differentially regulate transcription
  JOURNAL   J. Biol. Chem. 275 (27), 20734-20741 (2000)
  MEDLINE   20347166
   PUBMED   10764806
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from X89750.1.
FEATURES             Location/Qualifiers
     source          1..272
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18p11.3"
                     /tissue_type="liver"
                     /clone_lib="Clontech"
     Protein         1..272
                     /product="TGFB-induced factor (TALE family homeobox)"
                     /note="TG-interacting factor"
     Region          41..92
                     /region_name="Homeodomain"
                     /note="HOX"
                     /db_xref="CDD:smart00389"
     variation       163
                     /allele="P"
                     /allele="L"
                     /db_xref="dbSNP:2229333"
     CDS             1..272
                     /gene="TGIF"
                     /coded_by="NM_003244.1:312..1130"
                     /db_xref="LocusID:7050"
                     /db_xref="MIM:602630"
ORIGIN      
        1 mkgkkgivaa sgsetededs mdipldlsss agsgkrrrrg nlpkesvqil rdwlyehryn
       61 aypseqekal lsqqthlstl qvcnwfinar rrllpdmlrk dgkdpnqfti srrgakiset
      121 ssvesvmgik nfmpaleetp fhsctagpnp tlgrplspkp sspgsvlarp svichttvta
      181 lkdvpfslcq svgvgqntdi qqiaaknftd tslmypedtc ksgpstntqs glfntppptp
      241 pdlnqdfsgf qllvdvalkr aaemelqakl ta
//



Revised: July 5, 2002.
 
 


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1: NP_009017. AND-1 protein [Ho...[gi:5901892] Links  


LOCUS       AND-1                   1129 aa            linear   PRI 15-JUL-2001
DEFINITION  AND-1 protein [Homo sapiens].
ACCESSION   NP_009017
VERSION     NP_009017.1  GI:5901892
DBSOURCE    REFSEQ: aaccession NM_007086.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1129)
  AUTHORS   Kohler,A., Schmidt-Zachmann,M.S. and Franke,W.W.
  TITLE     AND-1, a natural chimeric DNA-binding protein, combines an HMG-box
            with regulatory WD-repeats
  JOURNAL   J. Cell. Sci. 110 (Pt 9), 1051-1062 (1997)
  MEDLINE   97318764
   PUBMED   9175701
COMMENT     PREDICTED REFSEQ: The mRNA record is supported by experimental
            evidence; however, the coding sequence is predicted. The reference
            sequence was derived from AJ006266.1.
FEATURES             Location/Qualifiers
     source          1..1129
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="14"
                     /map="14q22.1"
                     /tissue_type="fetal brain"
                     /tissue_type="colon carcinoma"
                     /clone_lib="Stratagene Human fetal brain lambda Uni-ZAP
                     library"
     Protein         1..1129
                     /product="AND-1 protein"
                     /function="DNA-binding protein"
     Region          10..40
                     /region_name="WD domain"
                     /note="WD40"
                     /db_xref="CDD:pfam00400"
     Region          11..41
                     /region_name="WD40 repeats"
                     /note="WD40"
                     /db_xref="CDD:smart00320"
     Region          125..163
                     /region_name="WD40 repeats"
                     /note="WD40"
                     /db_xref="CDD:smart00320"
     Region          127..163
                     /region_name="WD domain"
                     /note="WD40"
                     /db_xref="CDD:pfam00400"
     Region          1017..1072
                     /region_name="HMG (high mobility group) box"
                     /note="HMG_box"
                     /db_xref="CDD:pfam00505"
     Region          1017..1072
                     /region_name="high mobility group"
                     /note="HMG"
                     /db_xref="CDD:smart00398"
     CDS             1..1129
                     /gene="AND-1"
                     /coded_by="NM_007086.1:40..3429"
                     /db_xref="LocusID:11169"
ORIGIN      
        1 mpatrkpmry ghteghtevc fddsgsfivt cgsdgdvriw edlddddpkf invgekaysc
       61 alksgklvta vsnntiqvht fpegvpdgil trfttnanhv vfngdgtkia agssdflvki
      121 vdvmdssqqk tfrghdapvl slsfdpkdif lasascdgsv rvwqisdqtc aiswpllqkc
      181 ndvinaksic rlawqpksgk llaipveksv klyrreswsh qfdlsdnfis qtlnivtwsp
      241 cgqylaagsi ngliivwnve tkdcmervkh ekgyaicgla whptcgrisy tdaegnlgll
      301 envcdpsgkt ssskvssrve kdyndlfdgd dmsnagdfln dnaveipsfs kgiinddedd
      361 edlmmasgrp rqrshiledd ensvdismlk tgssllkeee edgqegsihn lplvtsqrpf
      421 ydgpmptprq kpfqsgstpl hlthrfmvwn sigiircynd eqdnaidvef hdtsihhath
      481 lsntlnytia dlsheailla cestdelask lhclhfsswd sskewiidlp qnedieaicl
      541 gqgwaaaats alllrlftig gvqkevfsla gpvvsmaghg eqlfivyhrg tgfdgdqclg
      601 vqllelgkkk kqilhgdplp ltrksylawi gfsaegtpcy vdsegivrml nrglgntwtp
      661 icntrehckg ksdhywvvgi henpqqlrci pckgsrfppt lprpavails fklpycqiat
      721 ekgqmeeqfw rsvifhnhld ylakngyeye estknqatke qqellmkmla lscklerefr
      781 cveladlmtq navnlaikya srsrklilaq klselaveka aeltatqvee eeeeedfrkk
      841 lnagysntat ewsqprfrnq veedaedsge addeekpeih kpgqnsfsks tnssdvsaks
      901 gavtfssqgr vnpfkvsass kepamsmnsa rstnildnmg ksskkstals rttnnekspi
      961 ikplipkpkp kqasaasyfq krnsqtnkte evkeenlknv lsetpaicpp qntenqrpkt
     1021 gfqmwleenr snilsdnpdf sdeadiikeg mirfrvlste erkvwankak getasegtea
     1081 kkrkrvvdes detenqeeka kenlnlskkq kpldfstnqk lsafafkqe
//



Revised: July 5, 2002.
 
 


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1: NP_000601. CD44 antigen (hom...[gi:21361193] Links  


LOCUS       CD44                     742 aa            linear   PRI 10-JUN-2002
DEFINITION  CD44 antigen (homing function and Indian blood group system); CD44
            antigen (homing function) [Homo sapiens].
ACCESSION   NP_000601
VERSION     NP_000601.2  GI:21361193
DBSOURCE    REFSEQ: aaccession NM_000610.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AJ251595.1.
            On Jun 10, 2002 this sequence version replaced gi:10835163.
FEATURES             Location/Qualifiers
     source          1..742
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="11"
                     /map="11p13"
     Protein         1..742
                     /product="CD44 antigen (homing function and Indian blood
                     group system)"
                     /function="hyaluronate receptor"
                     /note="CD44 antigen (homing function)"
     sig_peptide     1..24
     mat_peptide     24..742
                     /product="CD44 antigen (homing function and Indian blood
                     group system)"
     Region          32..120
                     /region_name="Link (Hyaluronan-binding)"
                     /note="LINK"
                     /db_xref="CDD:smart00445"
     Region          32..119
                     /region_name="Extracellular link domain"
                     /note="Xlink"
                     /db_xref="CDD:pfam00193"
     CDS             1..742
                     /gene="CD44"
                     /coded_by="NM_000610.2:179..2407"
                     /db_xref="LocusID:960"
                     /db_xref="MIM:107269"
ORIGIN      
        1 mdkfwwhaaw glclvplsla qidlnitcrf agvfhvekng rysisrteaa dlckafnstl
       61 ptmaqmekal sigfetcryg fieghvvipr ihpnsicaan ntgvyiltyn tsqydtycfn
      121 asappeedct svtdlpnafd gpititivnr dgtryvqkge yrtnpediyp snptdddvss
      181 gssserssts ggyifytfst vhpipdedsp witdstdrip attlmstsat atetatkrqe
      241 awdwfswlfl psesknhlht ttqmagtssn tisagwepne enederdrhl sfsgsgiddd
      301 edfisstist tprafdhtkq nqdwtqwnps hsnpevllqt ttrmtdvdrn gttayegnwn
      361 peahpplihh ehheeeetph ststiqatps stteetatqk eqwfgnrwhe gyrqtpreds
      421 hsttgtaaas ahtshpmqgr ttpspedssw tdffnpishp mgrghqagrr mdmdsshstt
      481 lqptanpntg lvenldrtgp lsmttqqsns qsfstshegl eedkdhptts tltssnrndv
      541 tggrrdpnhs egsttllegy tshyphtkes rtfipvtsak tgsfgvtavt vgdsnsnvnr
      601 slsgdqdtfh psggshtthg sesdghshgs qegganttsg pirtpqipew liilasllal
      661 alilavciav nsrrrcgqkk klvinsgnga vedrkpsgln geasksqemv hlvnkesset
      721 pdqfmtadet rnlqnvdmki gv
//



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1: NP_003795. receptor (TNFRSF)...[gi:4506539] Links  


LOCUS       RIPK1                    671 aa            linear   PRI 14-MAY-2002
DEFINITION  receptor (TNFRSF)-interacting serine-threonine kinase 1; receptor
            interacting protein [Homo sapiens].
ACCESSION   NP_003795
VERSION     NP_003795.1  GI:4506539
DBSOURCE    REFSEQ: aaccession NM_003804.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 671)
  AUTHORS   Hsu,H., Huang,J., Shu,H.B., Baichwal,V. and Goeddel,D.V.
  TITLE     TNF-dependent recruitment of the protein kinase RIP to the TNF
            receptor-1 signaling complex
  JOURNAL   Immunity 4 (4), 387-396 (1996)
  MEDLINE   96200892
   PUBMED   8612133
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U50062.1.
FEATURES             Location/Qualifiers
     source          1..671
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="6"
                     /map="6p24.3"
                     /tissue_type="umbilical vein endothelium"
     Protein         1..671
                     /product="receptor (TNFRSF)-interacting serine-threonine
                     kinase 1"
                     /note="receptor interacting protein"
     Region          22..285
                     /region_name="Tyrosine kinase, catalytic domain"
                     /note="TyrKc"
                     /db_xref="CDD:smart00219"
     Region          22..281
                     /region_name="Serine/Threonine protein kinases, catalytic
                     domain"
                     /note="S_TKc"
                     /db_xref="CDD:smart00220"
     Region          22..279
                     /region_name="Protein kinase domain"
                     /note="pkinase"
                     /db_xref="CDD:pfam00069"
     Region          573..667
                     /region_name="DEATH domain, found in proteins involved in
                     cell death (apoptosis)."
                     /note="DEATH"
                     /db_xref="CDD:smart00005"
     Region          584..665
                     /region_name="Death domain"
                     /note="death"
                     /db_xref="CDD:pfam00531"
     CDS             1..671
                     /gene="RIPK1"
                     /coded_by="NM_003804.1:1..2016"
                     /note="Ser/Thr protein kinase; protein has death domain
                     sequence at the carboxyl terminus"
                     /db_xref="LocusID:8737"
                     /db_xref="MIM:603453"
ORIGIN      
        1 mqpdmslnvi kmkssdfles aeldsggfgk vslcfhrtqg lmimktvykg pnciehneal
       61 leeakmmnrl rhsrvvkllg viieegkysl vmeymekgnl mhvlkaemst plsvkgriil
      121 eiiegmcylh gkgvihkdlk penilvdndf hikiadlgla sfkmwsklnn eehnelrevd
      181 gtakknggtl yymapehlnd vnakpteksd vysfavvlwa ifankepyen aiceqqlimc
      241 iksgnrpdvd diteycprei islmklcwea npearptfpg ieekfrpfyl sqleesveed
      301 vkslkkeysn enavvkrmqs lqldcvavps srsnsateqp gslhssqglg mgpveeswfa
      361 pslehpqeen epslqsklqd eanyhlygsr mdrqtkqqpr qnvaynreee rrrrvshdpf
      421 aqqrpyenfq ntegkgtvys saashgnavh qpsgltsqpq vlyqnnglys shgfgtrpld
      481 pgtagprvwy rpipshmpsl hnipvpetny lgntptmpfs slpptdesik ytiynstgiq
      541 igaynymeig gtssslldst ntnfkeepaa kyqaifdntt sltdkhldpi renlgkhwkn
      601 carklgftqs qideidhdye rdglkekvyq mlqkwvmreg ikgatvgkla qalhqcsrid
      661 llssliyvsq n
//



Revised: July 5, 2002.
 
 


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1: NP_001685. ATPase, H+ transp...[gi:4502313] Links  


LOCUS       ATP6V0C                  155 aa            linear   PRI 07-SEP-2002
DEFINITION  ATPase, H+ transporting, lysosomal, V0 subunit c; ATPase, H+
            transporting, lysosomal 16kD, V0 subunit c; vacuolar proton pump,
            16 kDa subunit; ATPase, H+ transporting, lysosomal, 16-KD; vacuolar
            ATP synthase 16 kDa proteolipid subunit; H(+)-transporting
            two-sector ATPase, 16 kDa subunit; vacuolar H+ ATPase proton
            channel subunit; ATPase, H+ transporting, lysosomal (vacuolar
            proton pump) 16kD [Homo sapiens].
ACCESSION   NP_001685
VERSION     NP_001685.1  GI:4502313
DBSOURCE    REFSEQ: aaccession NM_001694.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 155)
  AUTHORS   Gillespie,G.A., Somlo,S., Germino,G.G., Weinstat-Saslow,D. and
            Reeders,S.T.
  TITLE     CpG island in the region of an autosomal dominant polycystic kidney
            disease locus defines the 5' end of a gene encoding a putative
            proton channel
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 88 (10), 4289-4293 (1991)
  MEDLINE   91239553
   PUBMED   1709739
REFERENCE   2  (residues 1 to 155)
  AUTHORS   Finbow,M.E. and Harrison,M.A.
  TITLE     The vacuolar H+-ATPase: a universal proton pump of eukaryotes
  JOURNAL   Biochem. J. 324 (Pt 3), 697-712 (1997)
  MEDLINE   97327715
   PUBMED   9210392
REFERENCE   3  (residues 1 to 155)
  AUTHORS   Stevens,T.H. and Forgac,M.
  TITLE     Structure, function and regulation of the vacuolar (H+)-ATPase
  JOURNAL   Annu Rev Cell Dev Biol 13, 779-808 (1997)
  MEDLINE   98105098
   PUBMED   9442887
REFERENCE   4  (residues 1 to 155)
  AUTHORS   Kane,P.M.
  TITLE     Introduction: V-ATPases 1992-1998
  JOURNAL   J. Bioenerg. Biomembr. 31 (1), 3-5 (1999)
  MEDLINE   99270691
   PUBMED   10340843
REFERENCE   5  (residues 1 to 155)
  AUTHORS   Nelson,N. and Harvey,W.R.
  TITLE     Vacuolar and plasma membrane proton-adenosinetriphosphatases
  JOURNAL   Physiol. Rev. 79 (2), 361-385 (1999)
  MEDLINE   99238916
   PUBMED   10221984
REFERENCE   6  (residues 1 to 155)
  AUTHORS   Forgac,M.
  TITLE     Structure and properties of the vacuolar (H+)-ATPases
  JOURNAL   J. Biol. Chem. 274 (19), 12951-12954 (1999)
  MEDLINE   99240666
   PUBMED   10224039
REFERENCE   7  (residues 1 to 155)
  AUTHORS   Wieczorek,H., Brown,D., Grinstein,S., Ehrenfeld,J. and Harvey,W.R.
  TITLE     Animal plasma membrane energization by proton-motive V-ATPases
  JOURNAL   Bioessays 21 (8), 637-648 (1999)
  MEDLINE   99369629
   PUBMED   10440860
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC009290.1 and BI548787.1.
            Summary: This gene encodes a component of vacuolar ATPase
            (V-ATPase), a multisubunit enzyme that mediates acidification of
            eukaryotic intracellular organelles. V-ATPase dependent organelle
            acidification is necessary for such intracellular processes as
            protein sorting, zymogen activation, and receptor-mediated
            endocytosis. V-ATPase is comprised of a cytosolic V1 domain and a
            transmembrane V0 domain. The V1 domain consists of a hexamer of
            three A and three B subunits plus the C, D, and E subunits. It
            contains the ATP catalytic site. The encoded protein is part of the
            transmembrane V0 domain. This gene had the previous symbols of
            ATP6C and ATP6L.
FEATURES             Location/Qualifiers
     source          1..155
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="16"
                     /map="16p13.3"
                     /clone="MGC:16615 IMAGE:4111426"
     Protein         1..155
                     /product="ATPase, H+ transporting, lysosomal, V0 subunit
                     c"
                     /EC_number="3.6.3.14"
                     /note="ATPase, H+ transporting, lysosomal 16kD, V0 subunit
                     c; vacuolar proton pump, 16 kDa subunit; ATPase, H+
                     transporting, lysosomal, 16-KD; vacuolar ATP synthase 16
                     kDa proteolipid subunit; H(+)-transporting two-sector
                     ATPase, 16 kDa subunit; vacuolar H+ ATPase proton channel
                     subunit; ATPase, H+ transporting, lysosomal (vacuolar
                     proton pump) 16kD"
     Region          14..76
                     /region_name="pfam00137, ATP-synt_C, ATP synthase subunit
                     C"
     CDS             1..155
                     /gene="ATP6V0C"
                     /coded_by="NM_001694.2:153..620"
                     /db_xref="LocusID:527"
                     /db_xref="MIM:108745"
ORIGIN      
        1 msesksgpey asffavmgas aamvfsalga aygtaksgtg iaamsvmrpe qimksiipvv
       61 magiiaiygl vvavliansl nddislyksf lqlgaglsvg lsglaagfai givgdagvrg
      121 taqqprlfvg mililifaev lglyglival ilstk
//



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1: NP_055555. KIAA0111 gene pro...[gi:7661920] Links  


LOCUS       KIAA0111                 411 aa            linear   PRI 10-DEC-2001
DEFINITION  KIAA0111 gene product [Homo sapiens].
ACCESSION   NP_055555
VERSION     NP_055555.1  GI:7661920
DBSOURCE    REFSEQ: aaccession NM_014740.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 411)
  AUTHORS   Nagase,T., Miyajima,N., Tanaka,A., Sazuka,T., Seki,N., Sato,S.,
            Tabata,S., Ishikawa,K.-i., Kawarabayasi,Y., Kotani,H. and Nomura,N.
  TITLE     Prediction of the coding sequences of unidentified human genes.
            III. The coding sequences of 40 new genes (KIAA0081-KIAA0120)
            deduced by analysis of cDNA clones from human cell line KG-1
  JOURNAL   DNA Res. 2 (1), 37-43 (1995)
  MEDLINE   95308325
   PUBMED   7788527
COMMENT     PREDICTED REFSEQ: The mRNA record is supported by experimental
            evidence; however, the coding sequence is predicted. The reference
            sequence was derived from D21853.1.
FEATURES             Location/Qualifiers
     source          1..411
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
                     /clone="HA0659"
                     /sex="male"
                     /cell_line="KG-1"
                     /cell_type="myeloblast"
     Protein         1..411
                     /product="KIAA0111 gene product"
     Region          51..254
                     /region_name="DEAD/DEAH box helicase. Members of this
                     family include the DEAD and DEAH box helicases. Helicases
                     are involved in unwinding nucleic acids. The DEAD box
                     helicases are involved in various aspects of RNA
                     metabolism"
                     /note="DEAD"
                     /db_xref="CDD:pfam00270"
     Region          75..254
                     /region_name="DEAD-like helicases superfamily"
                     /note="DEXDc"
                     /db_xref="CDD:smart00487"
     Region          291..372
                     /region_name="Helicase conserved C-terminal domain. The
                     Prosite family is restricted to DEAD/H helicases"
                     /note="helicase_C"
                     /db_xref="CDD:pfam00271"
     Region          291..372
                     /region_name="helicase superfamily c-terminal domain"
                     /note="HELICc"
                     /db_xref="CDD:smart00490"
     CDS             1..411
                     /gene="KIAA0111"
                     /coded_by="NM_014740.1:215..1450"
                     /db_xref="LocusID:9775"
ORIGIN      
        1 mattatmats gsarkrllke edmtkvefet seevdvtptf dtmglredll rgiyaygfek
       61 psaiqqraik qiikgrdvia qsqsgtgkta tfsisvlqcl diqvretqal ilaptrelav
      121 qiqkgllalg dymnvqchac iggtnvgedi rkldygqhvv agtpgrvfdm irrrslrtra
      181 ikmlvldead emlnkgfkeq iydvyrylpp atqvvlisat lpheilemtn kfmtdpiril
      241 vkrdeltleg ikqffvaver eewkfdtlcd lydtltitqa vifcntkrkv dwltekmrea
      301 nftvssmhgd mpqkeresim kefrsgasrv listdvwarg ldvpqvslii nydlpnnrel
      361 yihrigrsgr ygrkgvainf vknddirilr dieqyystqi dempmnvadl i
//



Revised: July 5, 2002.
 
 


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1: NP_055205. EBNA-2 co-activat...[gi:7657431] Links  


LOCUS       p100                     885 aa            linear   PRI 02-NOV-2000
DEFINITION  EBNA-2 co-activator (100kD) [Homo sapiens].
ACCESSION   NP_055205
VERSION     NP_055205.1  GI:7657431
DBSOURCE    REFSEQ: aaccession NM_014390.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 885)
  AUTHORS   Tong,X., Drapkin,R., Yalamanchili,R., Mosialos,G. and Kieff,E.
  TITLE     The Epstein-Barr virus nuclear protein 2 acidic domain forms a
            complex with a novel cellular coactivator that can interact with
            TFIIE
  JOURNAL   Mol. Cell. Biol. 15 (9), 4735-4744 (1995)
  MEDLINE   95379816
   PUBMED   7651391
REFERENCE   2  (residues 1 to 885)
  AUTHORS   Callebaut I and Mornon JP.
  TITLE     The human EBNA-2 coactivator p100: multidomain organization and
            relationship to the staphylococcal nuclease fold and to the tudor
            protein involved in Drosophila melanogaster development
  JOURNAL   Biochem. J. 321 (Pt 1), 125-132 (1997)
  MEDLINE   97157029
   PUBMED   9003410
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U22055.1.
FEATURES             Location/Qualifiers
     source          1..885
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31"
                     /cell_type="EBV transformed B cells (IB4 cells)"
     Protein         1..885
                     /product="EBNA-2 co-activator (100kD)"
                     /function="associates with the EBV nuclear protein 2
                     acidic domain"
     Region          1..141
                     /region_name="Staphylococcal nuclease homologues"
                     /note="SNc"
                     /db_xref="CDD:SNc"
     Region          48..141
                     /region_name="Staphylococcal nuclease homologues"
                     /note="SNase"
                     /db_xref="CDD:pfam00565"
     Region          168..303
                     /region_name="Staphylococcal nuclease homologues"
                     /note="SNc"
                     /db_xref="CDD:SNc"
     Region          179..301
                     /region_name="Staphylococcal nuclease homologues"
                     /note="SNase"
                     /db_xref="CDD:pfam00565"
     Region          316..470
                     /region_name="Staphylococcal nuclease homologues"
                     /note="SNc"
                     /db_xref="CDD:SNc"
     Region          316..470
                     /region_name="Staphylococcal nuclease homologues"
                     /note="SNase"
                     /db_xref="CDD:pfam00565"
     Region          503..635
                     /region_name="Staphylococcal nuclease homologues"
                     /note="SNc"
                     /db_xref="CDD:SNc"
     Region          503..634
                     /region_name="Staphylococcal nuclease homologues"
                     /note="SNase"
                     /db_xref="CDD:pfam00565"
     Region          703..759
                     /region_name="Tudor domain"
                     /note="TUDOR"
                     /db_xref="CDD:TUDOR"
     Region          708..758
                     /region_name="Tudor domain"
                     /note="TUDOR"
                     /db_xref="CDD:pfam00567"
     Region          823..870
                     /region_name="Staphylococcal nuclease homologues"
                     /note="SNc"
                     /db_xref="CDD:SNc"
     Region          825..868
                     /region_name="Staphylococcal nuclease homologues"
                     /note="SNase"
                     /db_xref="CDD:pfam00565"
     CDS             1..885
                     /gene="p100"
                     /coded_by="NM_014390.1:268..2925"
                     /db_xref="LocusID:27044"
                     /db_xref="MIM:602181"
ORIGIN      
        1 mvlsgcaiiv rgqprggppp erqinlsnir agnlarraaa tqpdakdtpd epwafparef
       61 lrkkligkev cftienktpq greygmiylg kdtngeniae slvaeglatr regmrannpe
      121 qnrlseceeq akaakkgmws egngshtird lkytienprh fvdshhqkpv naiiehvrdg
      181 svvralllpd yylvtvmlsg ikcptfrrea dgsetpepfa aeakfftesr llqrdvqiil
      241 eschnqnivg tilhpngnit elllkegfar cvdwsiavyt rgaeklraae rfakerrlri
      301 wrdyvaptan ldqkdkqfva kvmqvlnada ivvklnsgdy ktihlssirp prlegentqd
      361 knkklrplyd ipymfearef lrkkligkkv nvtvdyirpa spatetvpaf sertcatvti
      421 gginiaealv skglatviry rqdddqrssh ydellaaear aikngkglhs kkevpihrva
      481 disgdtqkak qflpflqrag rseavveyvf sgsrlklylp ketclitfll agiecprgar
      541 nlpglvqege pfseeatlft kelvlqreve vevesmdkag nfigwlhidg anlsvllveh
      601 alskvhftae rssyykslls aeeaakqkke kvwahyeeqp veevmpvlee kersasykpv
      661 fvteitddlh fyvqdvetgt qfqklmenmr ndiashppve gsyaprrgef ciakfvdgew
      721 yrarvekves pakihvfyid ygnrevlpst rlgtlspafs trvlpaqate yafafiqvpq
      781 dddartdavd svvrdiqntq cllnvehlsa gcphvtlqfa dskgdvglgl vkeglvmvev
      841 rkekqfqkvi teylnaqesa ksarlnlwry gdfraddade fgysr
//



Revised: July 5, 2002.
 
 


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1: NP_005132. fibrinogen, beta ...[gi:11761631] Links  


LOCUS       FGB                      491 aa            linear   PRI 03-FEB-2001
DEFINITION  fibrinogen, beta chain preproprotein; fibrinogen, B beta
            polypeptide [Homo sapiens].
ACCESSION   NP_005132
VERSION     NP_005132.1  GI:11761631
DBSOURCE    REFSEQ: aaccession NM_005141.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 491)
  AUTHORS   Chung,D.W., Que,B.G., Rixon,M.W., Mace,M. Jr. and Davie,E.W.
  TITLE     Characterization of complementary deoxyribonucleic acid and genomic
            deoxyribonucleic acid for the beta chain of human fibrinogen
  JOURNAL   Biochemistry 22 (13), 3244-3250 (1983)
  MEDLINE   83283433
   PUBMED   6688356
REFERENCE   2  (residues 1 to 491)
  AUTHORS   Chung,D.W., Rixon,M.W., Que,B.G. and Davie,E.W.
  TITLE     Cloning of fibrinogen genes and their cDNA
  JOURNAL   Ann. N. Y. Acad. Sci. 408, 449-456 (1983)
  MEDLINE   83254384
   PUBMED   6575700
REFERENCE   3  (residues 1 to 491)
  AUTHORS   Doolittle,R.F.
  TITLE     Fibrinogen and fibrin
  JOURNAL   Annu. Rev. Biochem. 53, 195-229 (1984)
  MEDLINE   84305751
   PUBMED   6383194
REFERENCE   4  (residues 1 to 491)
  AUTHORS   Huber,P., Dalmon,J., Courtois,G., Laurent,M., Assouline,Z. and
            Marguerie,G.
  TITLE     Characterization of the 5'-flanking region for the human fibrinogen
            beta gene
  JOURNAL   Nucleic Acids Res. 15 (4), 1615-1625 (1987)
  MEDLINE   87146483
   PUBMED   3029722
REFERENCE   5  (residues 1 to 491)
  AUTHORS   Herrick,S., Blanc-Brude,O., Gray,A. and Laurent,G.
  TITLE     Fibrinogen
  JOURNAL   Int. J. Biochem. Cell Biol. 31 (7), 741-746 (1999)
  MEDLINE   99397060
   PUBMED   10467729
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from J00129.1 and M64983.1.
            Summary: The protein encoded by this gene is the beta component of
            fibrinogen, a blood-borne glycoprotein comprised of three pairs of
            nonidentical polypeptide chains. Following vascular injury,
            fibrinogen is cleaved by thrombin to form fibrin which is the most
            abundant component of blood clots. In addition, various cleavage
            products of fibrinogen and fibrin regulate cell adhesion and
            spreading, display vasoconstrictor and chemotactic activities, and
            are mitogens for several cell types. Mutations in this gene lead to
            several disorders, including afibrinogenemia, dysfibrinogenemia,
            hypodysfibrinogenemia and thrombotic tendency. S1 mapping studies
            on the 5'-flanking region of this gene revealed three transcription
            initiation points. Transcript variants utilizing alternative polyA
            signals have been described in the literature.
FEATURES             Location/Qualifiers
     source          1..491
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q28"
     Protein         1..491
                     /product="fibrinogen, beta chain preproprotein"
                     /note="fibrinogen, B beta polypeptide"
     sig_peptide     1..30
     Proprotein      31..491
     mat_peptide     31..44
                     /product="fibrinopeptide B"
                     /note="processed active peptide"
     mat_peptide     45..491
                     /product="fibrinogen, beta chain"
                     /note="thrombin cleavage product"
     Region          114..222
                     /region_name="Syntaxin N-terminal domain"
                     /note="SynN"
                     /db_xref="CDD:SynN"
     Region          236..487
                     /region_name="Fibrinogen-related domains (FReDs)"
                     /note="FBG"
                     /db_xref="CDD:FBG"
     Region          237..487
                     /region_name="Fibrinogen beta and gamma chains"
                     /note="fibrinogen_C"
                     /db_xref="CDD:pfam00147"
     CDS             1..491
                     /gene="FGB"
                     /coded_by="NM_005141.1:9..1484"
                     /db_xref="LocusID:2244"
                     /db_xref="MIM:134830"
ORIGIN      
        1 mkrmvswsfh klktmkhlll lllcvflvks qgvndneegf fsarghrpld kkreeapslr
       61 papppisggg yrarpakaaa tqkkverkap daggclhadp dlgvlcptgc qlqeallqqe
      121 rpirnsvdel nnnveavsqt ssssfqymyl lkdlwqkrqk qvkdnenvvn eysselekhq
      181 lyidetvnsn iatnlrvlrs ilenlrskiq klesdvsaqm eycrtpctvs cnipvvsgke
      241 ceeiirkgge tsemyliqpd ssvkpyrvyc dmntenggwt viqnrqdgsv dfgrkwdpyk
      301 qgfgnvatnt dgknycglpg eywlgndkis qltrmgptel liemedwkgd kvkahyggft
      361 vqneankyqi svnkyrgtag nalmdgasql mgenrtmtih ngmffstydr dndgwltsdp
      421 rkqcskedgg gwwynrchaa npngryywgg qytwdmakhg tddgvvwmnw kgswysmrkm
      481 smkirpffpq q
//



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1: NP_062831. CTP synthase II; ...[gi:21361829] Links  


LOCUS       CTPS2                    586 aa            linear   PRI 10-JUN-2002
DEFINITION  CTP synthase II; CTP synthetase type 2 [Homo sapiens].
ACCESSION   NP_062831
VERSION     NP_062831.2  GI:21361829
DBSOURCE    REFSEQ: aaccession NM_019857.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 586)
  AUTHORS   Isogai,T. and Otsuki,T.
  TITLE     Homo sapiens CTP synthase II (CTPS2), mRNA
  JOURNAL   Unpublished (2000)
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from AK024070.1.
            On Jun 10, 2002 this sequence version replaced gi:9789919.
FEATURES             Location/Qualifiers
     source          1..586
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp22"
                     /clone="Y79AA1002416"
                     /cell_line="Y79"
                     /cell_type="retinoblastoma"
                     /clone_lib="Y79AA1"
                     /note="cloning vector: pME18SFL3"
     Protein         1..586
                     /product="CTP synthase II"
                     /note="CTP synthetase type 2"
     Region          310..538
                     /region_name="Glutamine amidotransferase class-I"
                     /note="GATase"
                     /db_xref="CDD:pfam00117"
     CDS             1..586
                     /gene="CTPS2"
                     /coded_by="NM_019857.2:239..1999"
                     /db_xref="LocusID:56474"
                     /db_xref="MIM:300380"
ORIGIN      
        1 mkyilvtggv isgigkgiia ssigtilksc glrvtaikid pyinidagtf spyehgevfv
       61 lndggevdld lgnyerfldi nlykdnnitt gkiyqhvink errgdylgkt vqvvphitda
      121 vqewvmnqak vpvdgnkeep qicvielggt igdiegmpfv eafrqfqfka krenfcnihv
      181 slvpqlsatg eqktkptqns vralrglgls pdlivcrsss piemavkeki smfchvnpeq
      241 vicihdvsst yrvpvlleeq sivkyfkerl hlpigdsasn llfkwrnmad ryerlqkics
      301 ialvgkytkl rdcyasvfka lehsalainh klnlmyidsi dlekiteted pvkfheawqk
      361 lckadgilvp ggfgirgtlg klqaiswart kkipflgvcl gmqlaviefa rnclnlkdad
      421 stefrpnapv plvidmpehn pgnlggtmrl girrtvfkte nsilrklygd vpfieerhrh
      481 rfevnpnlik qfeqndlsfv gqdvdgdrme iielanhpyf vgvqfhpefs srpmkpsppy
      541 lglllaatgn lnaylqqgck lsssdrysda sddsfsepri aeleis
//



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1: NP_004036. ATX1 antioxidant ...[gi:4757804] Links  


LOCUS       ATOX1                     68 aa            linear   PRI 27-AUG-2002
DEFINITION  ATX1 antioxidant protein 1 homolog [Homo sapiens].
ACCESSION   NP_004036
VERSION     NP_004036.1  GI:4757804
DBSOURCE    REFSEQ: aaccession NM_004045.1
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 68)
  AUTHORS   Klomp,L.W., Lin,S.J., Yuan,D.S., Klausner,R.D., Culotta,V.C. and
            Gitlin,J.D.
  TITLE     Identification and functional expression of HAH1, a novel human
            gene involved in copper homeostasis
  JOURNAL   J. Biol. Chem. 272 (14), 9221-9226 (1997)
  MEDLINE   97238857
   PUBMED   9083055
REFERENCE   2  (residues 1 to 68)
  AUTHORS   Hung,I.H., Casareno,R.L., Labesse,G., Mathews,F.S. and Gitlin,J.D.
  TITLE     HAH1 is a copper-binding protein with distinct amino acid residues
            mediating copper homeostasis and antioxidant defense
  JOURNAL   J. Biol. Chem. 273 (3), 1749-1754 (1998)
  MEDLINE   98104166
   PUBMED   9430722
REFERENCE   3  (residues 1 to 68)
  AUTHORS   Hamza,I., Schaefer,M., Klomp,L.W. and Gitlin,J.D.
  TITLE     Interaction of the copper chaperone HAH1 with the Wilson disease
            protein is essential for copper homeostasis
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 96 (23), 13363-13368 (1999)
  MEDLINE   20027553
   PUBMED   10557326
REFERENCE   4  (residues 1 to 68)
  AUTHORS   Boultwood,J., Strickson,A.J., Jabs,E.W., Cheng,J.F., Fidler,C. and
            Wainscoat,J.S.
  TITLE     Physical mapping of the human ATX1 homologue (HAH1) to the critical
            region of the 5q- syndrome within 5q32, and immediately adjacent to
            the SPARC gene
  JOURNAL   Hum. Genet. 106 (1), 127-129 (2000)
  MEDLINE   20435072
   PUBMED   10982193
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U70660.1.
            Summary: The protein encoded by this gene plays a role in copper
            homeostasis by binding and transporting cytosolic copper to ATPase
            proteins in the trans-Golgi network for later incorporation to the
            ceruloplasmin.  This protein also functions as an antioxidant
            against superoxide and hydrogen peroxide, and therefore, may play a
            significant role in cancer carcinogenesis.  Because of its
            cytogenetic location, this gene represents a candidate gene for
            5q-syndrome.
FEATURES             Location/Qualifiers
     source          1..68
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q32"
     Protein         1..68
                     /product="ATX1 antioxidant protein 1 homolog"
     Region          5..43
                     /region_name="pfam00403, HMA, Heavy-metal-associated
                     domain"
     CDS             1..68
                     /gene="ATOX1"
                     /coded_by="NM_004045.1:114..320"
                     /note="human ATX1 homolog"
                     /db_xref="LocusID:475"
                     /db_xref="MIM:602270"
ORIGIN      
        1 mpkhefsvdm tcggcaeavs rvlnklggvk ydidlpnkkv ciesehsmdt llatlkktgk
       61 tvsylgle
//



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1: NP_001151. apoptotic proteas...[gi:4502123] Links  


LOCUS       APAF1                   1194 aa            linear   PRI 03-FEB-2001
DEFINITION  apoptotic protease activating factor isoform b; apoptotic protease
            activating factor 1 [Homo sapiens].
ACCESSION   NP_001151
VERSION     NP_001151.1  GI:4502123
DBSOURCE    REFSEQ: aaccession NM_001160.1
KEYWORDS    .
SOURCE      Homo sapiens
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1194)
  AUTHORS   Zou,H., Henzel,W.J., Liu,X., Lutschg,A. and Wang,X.
  TITLE     Apaf-1, a human protein homologous to C. elegans CED-4,
            participates in cytochrome c-dependent activation of caspase-3
  JOURNAL   Cell 90 (3), 405-413 (1997)
  MEDLINE   97410306
   PUBMED   9267021
REFERENCE   2  (residues 1 to 1194)
  AUTHORS   Ishikawa,K., Nagase,T., Nakajima,D., Seki,N., Ohira,M.,
            Miyajima,N., Tanaka,A., Kotani,H., Nomura,N. and Ohara,O.
  TITLE     Prediction of the coding sequences of unidentified human genes.
            VIII. 78 new cDNA clones from brain which code for large proteins
            in vitro
  JOURNAL   DNA Res. 4 (5), 307-313 (1997)
  MEDLINE   98116655
   PUBMED   9455477
REFERENCE   3  (residues 1 to 1194)
  AUTHORS   Smith,T.F., Gaitatzes,C., Saxena,K. and Neer,E.J.
  TITLE     The WD repeat: a common architecture for diverse functions
  JOURNAL   Trends Biochem. Sci. 24 (5), 181-185 (1999)
  MEDLINE   99257314
   PUBMED   10322433
REFERENCE   4  (residues 1 to 1194)
  AUTHORS   Saleh,A., Srinivasula,S.M., Acharya,S., Fishel,R. and Alnemri,E.S.
  TITLE     Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a
            prerequisite for procaspase-9 activation
  JOURNAL   J. Biol. Chem. 274 (25), 17941-17945 (1999)
  MEDLINE   99292765
   PUBMED   10364241
REFERENCE   5  (residues 1 to 1194)
  AUTHORS   Hahn,C., Hirsch,B., Jahnke,D., Durkop,H. and Stein,H.
  TITLE     Three new types of Apaf-1 in mammalian cells
  JOURNAL   Biochem. Biophys. Res. Commun. 261 (3), 746-749 (1999)
  MEDLINE   99373149
   PUBMED   10441496
REFERENCE   6  (residues 1 to 1194)
  AUTHORS   Kim,H., Jung,Y.K., Kwon,Y.K. and Park,S.H.
  TITLE     Assignment of apoptotic protease activating factor-1 gene (APAF1)
            to human chromosome band 12q23 by fluorescence in situ
            hybridization
  JOURNAL   Cytogenet. Cell Genet. 87 (3-4), 252-253 (1999)
  MEDLINE   20169199
   PUBMED   10702682
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AF013263.1.
            Summary: Caspases are a highly conserved family of cysteine
            proteases that cleave their substrates after an aspartate residue.
            They play fundamental roles in the initiation and execution of
            apoptosis. The gene described here encodes a WD-repeat containing
            protein. WD-repeat-containing proteins are those that contain 4 or
            more copies of the WD-repeat (tryptophan-aspartate repeat), a
            sequence motif approximately 31 amino acids long, that encodes a
            structural repeat. Activation of procaspase-9 by the APAF1 gene in
            the cytochrome c/dATP-dependent pathway requires proteolytic
            cleavage to generate the mature caspase molecule. It was shown that
            a truncated APAF1 variant lacking the WD-repeat domain makes APAF1
            constitutively active and capable of processing procaspase-9
            independent of cytochrome c and dATP. Moreover the truncated
            protein was unable to release the mature caspase-9 from the complex
            raising the possibility that the WD-40 repeats play a role in the
            release of mature caspase-9.
            Transcript Variant: Exon 17A is not included in this isoform. It
            lacks one WD-repeat domain and is the constitutively active shorter
            isoform.
FEATURES             Location/Qualifiers
     source          1..1194
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="12"
                     /map="12q23"
     Protein         1..1194
                     /product="apoptotic protease activating factor isoform b"
                     /function="cytochrome c-dependent activation of caspase-3"
                     /note="isoform b is encoded by transcript variant 2;
                     apoptotic protease activating factor 1"
     Region          2..89
                     /region_name="Caspase recruitment domain"
                     /note="CARD"
                     /db_xref="CDD:pfam00619"
     Region          93..403
                     /region_name="NB-ARC domain"
                     /note="NB-ARC"
                     /db_xref="CDD:pfam00931"
     Region          119..168
                     /region_name="RNA helicase"
                     /note="RNA_helicase"
                     /db_xref="CDD:pfam00910"
     CDS             1..1194
                     /gene="APAF1"
                     /coded_by="NM_001160.1:578..4162"
                     /db_xref="LocusID:317"
                     /db_xref="MIM:602233"
ORIGIN      
        1 mdakarncll qhrealekdi ktsyimdhmi sdgfltisee ekvrneptqq qraamlikmi
       61 lkkdndsyvs fynallhegy kdlaallhdg ipvvssssvr tvlceggvpq rpvvfvtrkk
      121 lvnaiqqkls klkgepgwvt ihgmagcgks vlaaeavrdh sllegcfpgg vhwvsvgkqd
      181 ksgllmklqn lctrldqdes fsqrlplnie eakdrlrilm lrkhprslli lddvwdswvl
      241 kafdsqcqil lttrdksvtd svmgpkyvvp vesslgkekg leilslfvnm kkadlpeqah
      301 siikeckgsp lvvsligall rdfpnrweyy lkqlqnkqfk rirksssydy ealdeamsis
      361 vemlredikd yytdlsilqk dvkvptkvlc ilwdmeteev edilqefvnk sllfcdrngk
      421 sfryylhdlq vdfltekncs qlqdlhkkii tqfqryhqph tlspdqedcm ywynflayhm
      481 asakmhkelc almfsldwik aktelvgpah lihefveyrh ildekdcavs enfqeflsln
      541 ghllgrqpfp nivqlglcep etsevyqqak lqakqevdng mlylewinkk nitnlsrlvv
      601 rphtdavyha cfsedgqria scgadktlqv fkaetgekll eikahedevl ccafstddrf
      661 iatcsvdkkv kiwnsmtgel vhtydehseq vncchftnss hhlllatgss dcflklwdln
      721 qkecrntmfg htnsvnhcrf spddkllasc sadgtlklwd atsanerksi nvkqfflnle
      781 dpqedmeviv kccswsadga rimvaaknki flwntdsrsk vadcrghlsw vhgvmfspdg
      841 ssfltssddq tirlwetkkv cknsavmlkq evdvvfqene vmvlavdhir rlqlingrtg
      901 qidylteaqv sccclsphlq yiafgdenga ieilelvnnr ifqsrfqhkk tvwhiqftad
      961 ektlisssdd aeiqvwnwql dkciflrghq etvkdfrllk nsrllswsfd gtvkvwniit
     1021 gnkekdfvch qgtvlscdis hdatkfssts adktakiwsf dlllplhelr ghngcvrcsa
     1081 fsvdstllat gddngeiriw nvsngellhl caplseegaa thggwvtdlc fspdgkmlis
     1141 aggyikwwnv vtgessqtfy tngtnlkkih vspdfktyvt vdnlgilyil qtle
//



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1: NP_065207. polypeptide N-ace...[gi:13124891] Links  


LOCUS       GALNT1                   559 aa            linear   PRI 31-JUL-2002
DEFINITION  polypeptide N-acetylgalactosaminyltransferase 1;
            UDP-N-acetyl-alpha-D-galactosamine:polypeptide
            N-acetylgalactosaminyltransferase 1; GalNAc-T1; GalNAc transferase
            1; protein-UDP acetylgalactosaminyltransferase 1;
            UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 [Homo
            sapiens].
ACCESSION   NP_065207
VERSION     NP_065207.2  GI:13124891
DBSOURCE    REFSEQ: aaccession NM_020474.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Meurer,J.A., Naylor,J.M., Baker,C.A., Thomsen,D.R., Homa,F.L. and
            Elhammer,A.P.
  TITLE     cDNA cloning, expression, and chromosomal localization of a human
            UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase
  JOURNAL   J. Biochem. 118 (3), 568-574 (1995)
  MEDLINE   96115928
   PUBMED   8690719
REFERENCE   2  (residues 1 to 559)
  AUTHORS   White,T., Bennett,E.P., Takio,K., Sorensen,T., Bonding,N. and
            Clausen,H.
  TITLE     Purification and cDNA cloning of a human
            UDP-N-acetyl-alpha-D-galactosamine:polypeptide
            N-acetylgalactosaminyltransferase
  JOURNAL   J. Biol. Chem. 270 (41), 24156-24165 (1995)
  MEDLINE   96025800
   PUBMED   7592619
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Meurer,J.A., Drong,R.F., Homa,F.L., Slightom,J.L. and Elhammer,A.P.
  TITLE     Organization of a human UDP-GalNAc:polypeptide,
            N-acetylgalactosaminyltransferase gene and a related processed
            pseudogene
  JOURNAL   Glycobiology 6 (2), 231-241 (1996)
  MEDLINE   96285863
   PUBMED   8727794
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Takai,S., Hinoda,Y., Adachi,T., Imai,K. and Oshima,M.
  TITLE     A human UDP-GalNAc: polypeptide, N-acetylgalactosaminyltransferase
            type 1 gene is located at the chromosomal region 18q12.1
  JOURNAL   Hum. Genet. 99 (3), 293-294 (1997)
  MEDLINE   97203192
   PUBMED   9050910
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Bennett,E.P., Weghuis,D.O., Merkx,G., van Kessel,A.G., Eiberg,H.
            and Clausen,H.
  TITLE     Genomic organization and chromosomal localization of three members
            of the UDP-N-acetylgalactosamine: polypeptide
            N-acetylgalactosaminyltransferase family
  JOURNAL   Glycobiology 8 (6), 547-555 (1998)
  MEDLINE   98256183
   PUBMED   9592121
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from U41514.1 and Y10343.1.
            On Feb 26, 2001 this sequence version replaced gi:9994173.
            Summary: This gene encodes a member of the
            UDP-N-acetyl-alpha-D-galactosamine:polypeptide
            N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes.
            GalNAc-Ts initiate mucin-type O-linked glycosylation in the Golgi
            apparatus by catalyzing the transfer of GalNAc to serine and
            threonine residues on target proteins. They are characterized by an
            N-terminal transmembrane domain, a stem region, a lumenal catalytic
            domain containing a GT1 motif and Gal/GalNAc transferase motif, and
            a C-terminal ricin/lectin-like domain. GalNAc-Ts have different,
            but overlapping, substrate specificities and patterns of
            expression. Transcript variants derived from this gene that utilize
            alternative polyA signals have been described in the literature.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="18"
                     /map="18q12.1"
     Protein         1..559
                     /product="polypeptide N-acetylgalactosaminyltransferase 1"
                     /EC_number="2.4.1.41"
                     /note="UDP-N-acetyl-alpha-D-galactosamine:polypeptide
                     N-acetylgalactosaminyltransferase 1; GalNAc-T1; GalNAc
                     transferase 1; protein-UDP acetylgalactosaminyltransferase
                     1; UDP-GalNAc:polypeptide
                     N-acetylgalactosaminyltransferase 1"
     Region          9..28
                     /region_name="transmembrane domain"
     Region          119..303
                     /region_name="pfam00535, Glycos_transf_2, Glycosyl
                     transferase. Diverse family, transferring sugar from
                     UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or
                     CDP-abequose, to a range of substrates including
                     cellulose, dolichol phosphate and teichoic acids"
     Region          432..473
                     /region_name="pfam00652, Ricin_B_lectin, QXW lectin
                     repeat"
     Region          434..551
                     /region_name="smart00458, RICIN, Ricin-type beta-trefoil;
                     Carbohydrate-binding domain formed from presumed gene
                     triplication"
     Region          514..552
                     /region_name="pfam00652, Ricin_B_lectin, QXW lectin
                     repeat"
     CDS             1..559
                     /gene="GALNT1"
                     /coded_by="NM_020474.2:32..1711"
                     /db_xref="LocusID:2589"
                     /db_xref="MIM:602273"
ORIGIN      
        1 mrkfayckvv latsliwvll dmflllyfse cnkcdekker glpagdvlep vqkphegpge
       61 mgkpvvipke dqekmkemfk inqfnlmase mialnrslpd vrlegcktkv ypdnlpttsv
      121 vivfhneaws tllrtvhsvi nrsprhmiee ivlvddaser dflkrplesy vkklkvpvhv
      181 irmeqrsgli rarlkgaavs kgqvitflda hcectvgwle pllarikhdr rtvvcpiidv
      241 isddtfeyma gsdmtyggfn wklnfrwypv pqremdrrkg drtlpvrtpt magglfsidr
      301 dyfqeigtyd agmdiwggen leisfriwqc ggtleivtcs hvghvfrkat pytfpggtgq
      361 iinknnrrla evwmdefknf fyiispgvtk vdygdissrv glrhklqckp fswyleniyp
      421 dsqiprhyfs lgeirnvetn qcldnmarke nekvgifnch gmggnqvfsy tankeirtdd
      481 lcldvsklng pvtmlkchhl kgnqlweydp vkltlqhvns nqcldkatee dsqvpsirdc
      541 ngsrsqqwll rnvtlpeif
//



Revised: July 5, 2002.
 
 


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&&&&&&&




ADDITIONAL PROTEIN SEQUENCES FOR TABLE 1 




    
 
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  SUMMARY ASN.1 FASTA TINYSEQ XML GI LIST GENPEPT GBSEQ XML GRAPHICS XML DEFAULT             
 
 

1: NP_001045. SULFOTRANSFERASE ...[GI:4507303] LINKS  


LOCUS       SULT1A2                  295 AA            LINEAR   PRI 31-OCT-2000
DEFINITION  SULFOTRANSFERASE FAMILY, CYTOSOLIC, 1A, PHENOL-PREFERRING, MEMBER
            2; SULFOTRANSFERASE FAMILY 1A, PHENOL-PREFERRING, MEMBER 2 [HOMO
            SAPIENS].
ACCESSION   NP_001045
VERSION     NP_001045.1  GI:4507303
DBSOURCE    REFSEQ: AACCESSION NM_001054.1
KEYWORDS    .
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 295)
  AUTHORS   HER,C., RAFTOGIANIS,R. AND WEINSHILBOUM,R.M.
  TITLE     HUMAN PHENOL SULFOTRANSFERASE STP2 GENE: MOLECULAR CLONING,
            STRUCTURAL CHARACTERIZATION, AND CHROMOSOMAL LOCALIZATION
  JOURNAL   GENOMICS 33 (3), 409-420 (1996)
  MEDLINE   96299636
   PUBMED   8661000
REFERENCE   2  (RESIDUES 1 TO 295)
  AUTHORS   ZHU,X., VERONESE,M.E., IOCCO,P. AND MCMANUS,M.E.
  TITLE     CDNA CLONING AND EXPRESSION OF A NEW FORM OF HUMAN ARYL
            SULFOTRANSFERASE
  JOURNAL   INT. J. BIOCHEM. CELL BIOL. 28 (5), 565-571 (1996)
  MEDLINE   96252882
   PUBMED   8697101
REFERENCE   3  (RESIDUES 1 TO 295)
  AUTHORS   DOOLEY,T.P. AND HUANG,Z.
  TITLE     GENOMIC ORGANIZATION AND DNA SEQUENCES OF TWO HUMAN PHENOL
            SULFOTRANSFERASE GENES (STP1 AND STP2) ON THE SHORT ARM OF
            CHROMOSOME 16
  JOURNAL   BIOCHEM. BIOPHYS. RES. COMMUN. 228 (1), 134-140 (1996)
  MEDLINE   97069665
   PUBMED   8912648
REFERENCE   4  (RESIDUES 1 TO 295)
  AUTHORS   GAEDIGK,A., BEATTY,B.G. AND GRANT,D.M.
  TITLE     CLONING, STRUCTURAL ORGANIZATION, AND CHROMOSOMAL MAPPING OF THE
            HUMAN PHENOL SULFOTRANSFERASE STP2 GENE
  JOURNAL   GENOMICS 40 (2), 242-246 (1997)
  MEDLINE   97237042
   PUBMED   9119390
COMMENT     PROVISIONAL REFSEQ: THIS RECORD HAS NOT YET BEEN SUBJECT TO FINAL
            NCBI REVIEW. THE REFERENCE SEQUENCE WAS DERIVED FROM U34804.1.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..295
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="16"
                     /MAP="16P12.1-P11.2"
     PROTEIN         1..295
                     /PRODUCT="SULFOTRANSFERASE FAMILY, CYTOSOLIC, 1A,
                     PHENOL-PREFERRING, MEMBER 2"
                     /NOTE="SULFOTRANSFERASE FAMILY 1A, PHENOL-PREFERRING,
                     MEMBER 2"
     REGION          16..283
                     /REGION_NAME="SULFOTRANSFERASE PROTEINS"
                     /NOTE="SULFOTRANSFER"
                     /DB_XREF="CDD:PFAM00685"
     CDS             1..295
                     /GENE="SULT1A2"
                     /CODED_BY="NM_001054.1:426..1313"
                     /DB_XREF="LOCUSID:6799"
                     /DB_XREF="MIM:601292"
ORIGIN      
        1 MELIQDISRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLISTYPKSG TTWVSQILDM
       61 IYQGGDLEKC HRAPIFMRVP FLEFKVPGIP SGMETLKNTP APRLLKTHLP LALLPQTLLD
      121 QKVKVVYVAR NAKDVAVSYY HFYHMAKVYP HPGTWESFLE KFMAGEVSYG SWYQHVQEWW
      181 ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETV DLMVEHTSFK EMKKNPMTNY
      241 TTVRREFMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL
//



REVISED: JULY 5, 2002.
 
 


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  SUMMARY ASN.1 FASTA TINYSEQ XML GI LIST GENPEPT GBSEQ XML GRAPHICS XML DEFAULT             
 
 

1: XP_031238. SIMILAR TO PANCRE...[GI:14726804] LINKS  


LOCUS       C1QG                     245 AA            LINEAR   PRI 01-AUG-2002
DEFINITION  SIMILAR TO PANCREATIC ELASTASE (EC 3.4.21.36) IIIA PRECURSOR -
            HUMAN [HOMO SAPIENS].
ACCESSION   XP_031238
VERSION     XP_031238.1  GI:14726804
DBSOURCE    REFSEQ: AACCESSION XM_031238.7
KEYWORDS    .
SOURCE      HOMO SAPIENS (HUMAN)
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 245)
  AUTHORS   NCBI ANNOTATION PROJECT.
  TITLE     DIRECT SUBMISSION
  JOURNAL   SUBMITTED (31-JUL-2002) NATIONAL CENTER FOR BIOTECHNOLOGY
            INFORMATION, NIH, BETHESDA, MD 20894, USA
COMMENT     GENOME ANNOTATION REFSEQ:  THIS MODEL REFERENCE SEQUENCE WAS
            PREDICTED FROM NCBI CONTIG NT_004610 BY AUTOMATED COMPUTATIONAL
            ANALYSIS USING GENE PREDICTION METHOD: BLAST, SUPPORTED BY MRNA AND
            EST EVIDENCE.
            ALSO SEE:
                DOCUMENTATION OF NCBI'S ANNOTATION PROCESS
             
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..245
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="1"
     PROTEIN         1..245
                     /PRODUCT="SIMILAR TO PANCREATIC ELASTASE (EC 3.4.21.36)
                     IIIA PRECURSOR - HUMAN"
     REGION          113..245
                     /REGION_NAME="SMART00110, C1Q, COMPLEMENT COMPONENT C1Q
                     DOMAIN; GLOBULAR DOMAIN FOUND IN MANY COLLAGENS AND
                     EPONYMOUSLY IN COMPLEMENT C1Q. WHEN PART OF FULL LENGTH
                     PROTEINS THESE DOMAINS FORM A 'BOUQUET' DUE TO THE
                     MULTIMERIZATION OF HETEROTRIMERS. THE C1Q FOLD IS SIMILAR
                     TO THAT OF TUMOUR NECROSIS FACTOR"
     REGION          121..242
                     /REGION_NAME="PFAM00386, C1Q, C1Q DOMAIN. C1Q IS A SUBUNIT
                     OF THE C1 ENZYME COMPLEX THAT ACTIVATES THE SERUM
                     COMPLEMENT SYSTEM"
     VARIATION       149
                     /ALLELE="R"
                     /ALLELE="G"
                     /DB_XREF="DBSNP:1052042"
     CDS             1..245
                     /GENE="C1QG"
                     /CODED_BY="XM_031238.7:119..856"
                     /DB_XREF="LOCUSID:714"
                     /DB_XREF="MIM:120575"
ORIGIN      
        1 MDVGPSSLPH LGLKLLLLLL LLPLRGQANT GCYGIPGMPG LPGAPGKDGY DGLPGPKGEP
       61 GIPAIPGIRG PKGQKGEPGL PGHPGKNGPM GPPGMPGVPG PMGIPGEPGE EGRYKQKFQS
      121 VFTVTRQTHQ PPAPNSLIRF NAVLTNPQGD YDTSTGKFTC KVPGLYYFVY HASHTANLCV
      181 LLYRSGVKVV TFCGHTSKTN QVNSGGVLLR LQVGEEVWLA VNDYYDMVGI QGSDSVFSGF
      241 LLFPD
//



REVISED: JULY 5, 2002.
 
 


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  SUMMARY ASN.1 FASTA TINYSEQ XML GI LIST GENPEPT GBSEQ XML GRAPHICS XML DEFAULT             
 
 

1: NP_006417. DIHYDROPYRIMIDINA...[GI:11321617] LINKS  


LOCUS       DPYSL4                   572 AA            LINEAR   PRI 27-AUG-2002
DEFINITION  DIHYDROPYRIMIDINASE-LIKE 4 [HOMO SAPIENS].
ACCESSION   NP_006417
VERSION     NP_006417.1  GI:11321617
DBSOURCE    REFSEQ: AACCESSION NM_006426.1
KEYWORDS    .
SOURCE      HOMO SAPIENS (HUMAN)
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (SITES)
  AUTHORS   HAMAJIMA,N., MATSUDA,K., SAKATA,S., TAMAKI,N., SASAKI,M. AND
            NONAKA,M.
  TITLE     A NOVEL GENE FAMILY DEFINED BY HUMAN DIHYDROPYRIMIDINASE AND THREE
            RELATED PROTEINS WITH DIFFERENTIAL TISSUE DISTRIBUTION
  JOURNAL   GENE 180 (1-2), 157-163 (1996)
  MEDLINE   97128821
REFERENCE   2  (RESIDUES 1 TO 572)
  AUTHORS   BYK,T., OZON,S. AND SOBEL,A.
  TITLE     THE ULIP FAMILY PHOSPHOPROTEINS--COMMON AND SPECIFIC PROPERTIES
  JOURNAL   EUR. J. BIOCHEM. 254 (1), 14-24 (1998)
  MEDLINE   98314496
   PUBMED   9652388
REFERENCE   3  (RESIDUES 1 TO 572)
  AUTHORS   HONNORAT,J., BYK,T., KUSTERS,I., AGUERA,M., RICARD,D., ROGEMOND,V.,
            QUACH,T., AUNIS,D., SOBEL,A., MATTEI,M.G., KOLATTUKUDY,P.,
            BELIN,M.F. AND ANTOINE,J.C.
  TITLE     ULIP/CRMP PROTEINS ARE RECOGNIZED BY AUTOANTIBODIES IN
            PARANEOPLASTIC NEUROLOGICAL SYNDROMES
  JOURNAL   EUR. J. NEUROSCI. 11 (12), 4226-4232 (1999)
  MEDLINE   20062489
   PUBMED   10594648
REFERENCE   4  (SITES)
  AUTHORS   HAMAJIMA,N., KATO,Y., KOUWAKI,M., WADA,Y., SASASKI,M. AND NONAKA,M.
  TITLE     NOVEL MEMBERS OF DIHYDROPYRIMIDINASE RELATED PROTEIN FAMILY
  JOURNAL   UNPUBLISHED
COMMENT     PROVISIONAL REFSEQ: THIS RECORD HAS NOT YET BEEN SUBJECT TO FINAL
            NCBI REVIEW. THE REFERENCE SEQUENCE WAS DERIVED FROM AB006713.1.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..572
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="10"
                     /MAP="10Q26"
                     /TISSUE_TYPE="BRAIN"
                     /DEV_STAGE="FETUS"
     PROTEIN         1..572
                     /PRODUCT="DIHYDROPYRIMIDINASE-LIKE 4"
     REGION          19..102
                     /REGION_NAME="PFAM01979, ADENINE_DEAM, ADENINE DEAMINASE.
                     ADENINE DEAMINASE EC:3.5.4.2 HYDROLYSES ADENINE TO FORM
                     HYPOXANTHINE AND AMMONIA. THE ENZYME IS PART OF A LARGE
                     METAL DEPENDENT HYDROLASE SUPERFAMILY. ADENINE DEAMINASES
                     REACTION IS IMPORTANT FOR ADENINE UTILIZATION AS A PURINE
                     AND ALSO AS A NITROGEN SOURCE"
     REGION          56..453
                     /REGION_NAME="PFAM00744, DIHYDROOROTASE,
                     DIHYDROOROTASE-LIKE. THIS FAMILY ARE PREDICTED TO ADOPT A
                     TIM BARREL FOLD"
     CDS             1..572
                     /GENE="DPYSL4"
                     /CODED_BY="NM_006426.1:149..1867"
                     /DB_XREF="LOCUSID:10570"
ORIGIN      
        1 MSFQGKKSIP RITSDRLLIR GGRIVNDDQS FYADVHVEDG LIKQIGENLI VPGGIKTIDA
       61 HGLMVLPGGV DVHTRLQMPV LGMTPADDFC QGTKAALAGG TTMILDHVFP DTGVSLLAAY
      121 ERWRERADSA ACCDYSLHVD ITRWHESIKE ELEALVKEKG VNSFLVFMAY KDRCQCSDSQ
      181 MYEIFSIIRD LGALAQVHAE NGDIVEEEQK RLLELGITGP EGHVLSHPEE VEAEAVYRAV
      241 TIAKQANCPL YVTKVMSKGA ADAIAQAKRR GVVVFGEPIT ASLGTDGSHY WSKNWAKAAA
      301 FVTSPPVNPD PTTADHLTCL LSSGDLQVTG SAHCTFTTAQ KAVGKDNFAL IPEGTNGIEE
      361 RMSMVWEKCV ASGKMDENEF VAVTSTNAAK IFNFYPRKGR VAVGSDADLV IWNPKATKII
      421 SAKTHNLNVE YNIFEGVECR GAPAVVISQG RVALEDGKMF VTPGAGRFVP RKTFPDFVYK
      481 RIKARNRLAE IHGVPRGLYD GPVHEVMVPA KPGSGAPARA SCPGKISVPP VRNLHQSGFS
      541 LSGSQADDHI ARRTAQKIMA PPGGRSNITS LS
//



REVISED: JULY 5, 2002.
 
 


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  SUMMARY ASN.1 FASTA TINYSEQ XML GI LIST GENPEPT GBSEQ XML GRAPHICS XML DEFAULT             
 
 

1: NP_037361. APOPTOTIC PROTEAS...[GI:7108333] LINKS  


LOCUS       APAF1                   1237 AA            LINEAR   PRI 03-FEB-2001
DEFINITION  APOPTOTIC PROTEASE ACTIVATING FACTOR ISOFORM A; APOPTOTIC PROTEASE
            ACTIVATING FACTOR 1 [HOMO SAPIENS].
ACCESSION   NP_037361
VERSION     NP_037361.1  GI:7108333
DBSOURCE    REFSEQ: AACCESSION NM_013229.1
KEYWORDS    .
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 1237)
  AUTHORS   ZOU,H., HENZEL,W.J., LIU,X., LUTSCHG,A. AND WANG,X.
  TITLE     APAF-1, A HUMAN PROTEIN HOMOLOGOUS TO C. ELEGANS CED-4,
            PARTICIPATES IN CYTOCHROME C-DEPENDENT ACTIVATION OF CASPASE-3
  JOURNAL   CELL 90 (3), 405-413 (1997)
  MEDLINE   97410306
   PUBMED   9267021
REFERENCE   2  (RESIDUES 1 TO 1237)
  AUTHORS   ISHIKAWA,K., NAGASE,T., NAKAJIMA,D., SEKI,N., OHIRA,M.,
            MIYAJIMA,N., TANAKA,A., KOTANI,H., NOMURA,N. AND OHARA,O.
  TITLE     PREDICTION OF THE CODING SEQUENCES OF UNIDENTIFIED HUMAN GENES.
            VIII. 78 NEW CDNA CLONES FROM BRAIN WHICH CODE FOR LARGE PROTEINS
            IN VITRO
  JOURNAL   DNA RES. 4 (5), 307-313 (1997)
  MEDLINE   98116655
   PUBMED   9455477
REFERENCE   3  (RESIDUES 1 TO 1237)
  AUTHORS   SMITH,T.F., GAITATZES,C., SAXENA,K. AND NEER,E.J.
  TITLE     THE WD REPEAT: A COMMON ARCHITECTURE FOR DIVERSE FUNCTIONS
  JOURNAL   TRENDS BIOCHEM. SCI. 24 (5), 181-185 (1999)
  MEDLINE   99257314
   PUBMED   10322433
REFERENCE   4  (RESIDUES 1 TO 1237)
  AUTHORS   SALEH,A., SRINIVASULA,S.M., ACHARYA,S., FISHEL,R. AND ALNEMRI,E.S.
  TITLE     CYTOCHROME C AND DATP-MEDIATED OLIGOMERIZATION OF APAF-1 IS A
            PREREQUISITE FOR PROCASPASE-9 ACTIVATION
  JOURNAL   J. BIOL. CHEM. 274 (25), 17941-17945 (1999)
  MEDLINE   99292765
   PUBMED   10364241
REFERENCE   5  (RESIDUES 1 TO 1237)
  AUTHORS   HAHN,C., HIRSCH,B., JAHNKE,D., DURKOP,H. AND STEIN,H.
  TITLE     THREE NEW TYPES OF APAF-1 IN MAMMALIAN CELLS
  JOURNAL   BIOCHEM. BIOPHYS. RES. COMMUN. 261 (3), 746-749 (1999)
  MEDLINE   99373149
   PUBMED   10441496
REFERENCE   6  (RESIDUES 1 TO 1237)
  AUTHORS   KIM,H., JUNG,Y.K., KWON,Y.K. AND PARK,S.H.
  TITLE     ASSIGNMENT OF APOPTOTIC PROTEASE ACTIVATING FACTOR-1 GENE (APAF1)
            TO HUMAN CHROMOSOME BAND 12Q23 BY FLUORESCENCE IN SITU
            HYBRIDIZATION
  JOURNAL   CYTOGENET. CELL GENET. 87 (3-4), 252-253 (1999)
  MEDLINE   20169199
   PUBMED   10702682
COMMENT     REVIEWED REFSEQ: THIS RECORD HAS BEEN CURATED BY NCBI STAFF. THE
            REFERENCE SEQUENCE WAS DERIVED FROM AF134397.1 AND AF013263.1.
            SUMMARY: CASPASES ARE A HIGHLY CONSERVED FAMILY OF CYSTEINE
            PROTEASES THAT CLEAVE THEIR SUBSTRATES AFTER AN ASPARTATE RESIDUE.
            THEY PLAY FUNDAMENTAL ROLES IN THE INITIATION AND EXECUTION OF
            APOPTOSIS. THE GENE DESCRIBED HERE ENCODES A WD-REPEAT CONTAINING
            PROTEIN. WD-REPEAT-CONTAINING PROTEINS ARE THOSE THAT CONTAIN 4 OR
            MORE COPIES OF THE WD-REPEAT (TRYPTOPHAN-ASPARTATE REPEAT), A
            SEQUENCE MOTIF APPROXIMATELY 31 AMINO ACIDS LONG, THAT ENCODES A
            STRUCTURAL REPEAT. ACTIVATION OF PROCASPASE-9 BY THE APAF1 GENE IN
            THE CYTOCHROME C/DATP-DEPENDENT PATHWAY REQUIRES PROTEOLYTIC
            CLEAVAGE TO GENERATE THE MATURE CASPASE MOLECULE. IT WAS SHOWN THAT
            A TRUNCATED APAF1 VARIANT LACKING THE WD-REPEAT DOMAIN MAKES APAF1
            CONSTITUTIVELY ACTIVE AND CAPABLE OF PROCESSING PROCASPASE-9
            INDEPENDENT OF CYTOCHROME C AND DATP. MOREOVER THE TRUNCATED
            PROTEIN WAS UNABLE TO RELEASE THE MATURE CASPASE-9 FROM THE COMPLEX
            RAISING THE POSSIBILITY THAT THE WD-40 REPEATS PLAY A ROLE IN THE
            RELEASE OF MATURE CASPASE-9.
            TRANSCRIPT VARIANT:  THIS ISOFORM INCLUDES ONE ADDITIONAL WD-REPEAT
            DOMAIN, ENCODED BY EXON 17A, THAT IS MISSING IN VARIANT 2.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..1237
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="12"
                     /MAP="12Q23"
     PROTEIN         1..1237
                     /PRODUCT="APOPTOTIC PROTEASE ACTIVATING FACTOR ISOFORM A"
                     /FUNCTION="MEDIATES AUTOCATALYTIC ACTIVATION OF
                     PROCASPASE-9"
                     /NOTE="ISOFORM A IS ENCODED BY TRANSCRIPT VARIANT 1;
                     APOPTOTIC PROTEASE ACTIVATING FACTOR 1"
     REGION          2..89
                     /REGION_NAME="CASPASE RECRUITMENT DOMAIN"
                     /NOTE="CARD"
                     /DB_XREF="CDD:PFAM00619"
     REGION          93..403
                     /REGION_NAME="NB-ARC DOMAIN"
                     /NOTE="NB-ARC"
                     /DB_XREF="CDD:PFAM00931"
     REGION          119..168
                     /REGION_NAME="RNA HELICASE"
                     /NOTE="RNA_HELICASE"
                     /DB_XREF="CDD:PFAM00910"
     CDS             1..1237
                     /GENE="APAF1"
                     /CODED_BY="NM_013229.1:578..4291"
                     /DB_XREF="LOCUSID:317"
                     /DB_XREF="MIM:602233"
ORIGIN      
        1 MDAKARNCLL QHREALEKDI KTSYIMDHMI SDGFLTISEE EKVRNEPTQQ QRAAMLIKMI
       61 LKKDNDSYVS FYNALLHEGY KDLAALLHDG IPVVSSSSVR TVLCEGGVPQ RPVVFVTRKK
      121 LVNAIQQKLS KLKGEPGWVT IHGMAGCGKS VLAAEAVRDH SLLEGCFPGG VHWVSVGKQD
      181 KSGLLMKLQN LCTRLDQDES FSQRLPLNIE EAKDRLRILM LRKHPRSLLI LDDVWDSWVL
      241 KAFDSQCQIL LTTRDKSVTD SVMGPKYVVP VESSLGKEKG LEILSLFVNM KKADLPEQAH
      301 SIIKECKGSP LVVSLIGALL RDFPNRWEYY LKQLQNKQFK RIRKSSSYDY EALDEAMSIS
      361 VEMLREDIKD YYTDLSILQK DVKVPTKVLC ILWDMETEEV EDILQEFVNK SLLFCDRNGK
      421 SFRYYLHDLQ VDFLTEKNCS QLQDLHKKII TQFQRYHQPH TLSPDQEDCM YWYNFLAYHM
      481 ASAKMHKELC ALMFSLDWIK AKTELVGPAH LIHEFVEYRH ILDEKDCAVS ENFQEFLSLN
      541 GHLLGRQPFP NIVQLGLCEP ETSEVYQQAK LQAKQEVDNG MLYLEWINKK NITNLSRLVV
      601 RPHTDAVYHA CFSEDGQRIA SCGADKTLQV FKAETGEKLL EIKAHEDEVL CCAFSTDDRF
      661 IATCSVDKKV KIWNSMTGEL VHTYDEHSEQ VNCCHFTNSS HHLLLATGSS DCFLKLWDLN
      721 QKECRNTMFG HTNSVNHCRF SPDDKLLASC SADGTLKLWD ATSANERKSI NVKQFFLNLE
      781 DPQEDMEVIV KCCSWSADGA RIMVAAKNKI FLFDIHTSGL LGEIHTGHHS TIQYCDFSPQ
      841 NHLAVVALSQ YCVELWNTDS RSKVADCRGH LSWVHGVMFS PDGSSFLTSS DDQTIRLWET
      901 KKVCKNSAVM LKQEVDVVFQ ENEVMVLAVD HIRRLQLING RTGQIDYLTE AQVSCCCLSP
      961 HLQYIAFGDE NGAIEILELV NNRIFQSRFQ HKKTVWHIQF TADEKTLISS SDDAEIQVWN
     1021 WQLDKCIFLR GHQETVKDFR LLKNSRLLSW SFDGTVKVWN IITGNKEKDF VCHQGTVLSC
     1081 DISHDATKFS STSADKTAKI WSFDLLLPLH ELRGHNGCVR CSAFSVDSTL LATGDDNGEI
     1141 RIWNVSNGEL LHLCAPLSEE GAATHGGWVT DLCFSPDGKM LISAGGYIKW WNVVTGESSQ
     1201 TFYTNGTNLK KIHVSPDFKT YVTVDNLGIL YILQTLE
//



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1: AAA59587. HUMAN METALLOTHIO...[GI:386865] LINKS  


LOCUS       AAA59587                  61 AA            LINEAR   PRI 07-JAN-1995
DEFINITION  HUMAN METALLOTHIONEIN-IE.
ACCESSION   AAA59587
VERSION     AAA59587.1  GI:386865
DBSOURCE    LOCUS HUMMETIE AACCESSION M10942.1
KEYWORDS    .
SOURCE      HOMO SAPIENS (HUMAN)
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 61)
  AUTHORS   SCHMIDT,C.J., JUBIER,M.F. AND HAMER,D.H.
  TITLE     STRUCTURE AND EXPRESSION OF TWO HUMAN METALLOTHIONEIN-I ISOFORM
            GENES AND A RELATED PSEUDOGENE
  JOURNAL   J. BIOL. CHEM. 260 (12), 7731-7737 (1985)
  MEDLINE   85207825
   PUBMED   2581970
COMMENT     ON AUG 28, 1993 THIS SEQUENCE VERSION REPLACED GI:187539.
            THE SIGNIFICANCE OF CONSERVED SEQUENCES IN THE HUMAN
            METALLOTHIONEIN MULTI-GENE FAMILY IS DISCUSSED; EVOLUTIONARY
            COMPARISONS AND THEIR IMPLICATIONS ARE ALSO CONSIDERED.  A
            POTENTIAL POLYADENYLATION SIGNAL CAN BE FOUND AT 1722-1727.
            METHOD: CONCEPTUAL TRANSLATION.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..61
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /MAP="16Q13"
     PROTEIN         1..61
                     /NAME="HUMAN METALLOTHIONEIN-IE"
     CDS             1..61
                     /GENE="MT1E"
                     /CODED_BY="JOIN(M10942.1:483..510,M10942.1:1098..1163,
                     M10942.1:1512..1603)"
                     /DB_XREF="GDB:G00-125-569"
ORIGIN      
        1 MDPNCSCATG GSCTCAGSCK CKECKCTSCK KSCCSCCPVG CAKCAQGCVC KGASEKCSCC
       61 A
//



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1: NP_037384. C-TYPE (CALCIUM D...[GI:10281669] LINKS  


LOCUS       CLECSF5                  188 AA            LINEAR   PRI 02-NOV-2000
DEFINITION  C-TYPE (CALCIUM DEPENDENT, CARBOHYDRATE-RECOGNITION DOMAIN) LECTIN,
            SUPERFAMILY MEMBER 5 [HOMO SAPIENS].
ACCESSION   NP_037384
VERSION     NP_037384.1  GI:10281669
DBSOURCE    REFSEQ: AACCESSION NM_013252.1
KEYWORDS    .
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 188)
  AUTHORS   BAKKER,A.B., BAKER,E., SUTHERLAND,G.R., PHILLIPS,J.H. AND
            LANIER,L.L.
  TITLE     MYELOID DAP12-ASSOCIATING LECTIN (MDL)-1 IS A CELL SURFACE RECEPTOR
            INVOLVED IN THE ACTIVATION OF MYELOID CELLS
  JOURNAL   PROC. NATL. ACAD. SCI. U.S.A. 96 (17), 9792-9796 (1999)
  MEDLINE   99380598
   PUBMED   10449773
REFERENCE   2  (RESIDUES 1 TO 188)
  AUTHORS   MUELLER,A., MERZ,H. AND FELLER,A.C.
  TITLE     EXPRESSION OF MDL-1 IN HUMAN BLOOD AND CELL LINES
  JOURNAL   UNPUBLISHED
COMMENT     PROVISIONAL REFSEQ: THIS RECORD HAS NOT YET BEEN SUBJECT TO FINAL
            NCBI REVIEW. THE REFERENCE SEQUENCE WAS DERIVED FROM AJ271684.1.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..188
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="7"
                     /MAP="7Q33"
                     /CELL_LINE="U937"
     PROTEIN         1..188
                     /PRODUCT="C-TYPE (CALCIUM DEPENDENT,
                     CARBOHYDRATE-RECOGNITION DOMAIN) LECTIN, SUPERFAMILY
                     MEMBER 5"
     REGION          71..146
                     /REGION_NAME="C-TYPE LECTIN (CTL) OR
                     CARBOHYDRATE-RECOGNITION DOMAIN (CRD)"
                     /NOTE="CLECT"
                     /DB_XREF="CDD:CLECT"
     CDS             1..188
                     /GENE="CLECSF5"
                     /CODED_BY="NM_013252.1:198..764"
                     /DB_XREF="LOCUSID:23601"
                     /DB_XREF="MIM:604987"
ORIGIN      
        1 MNWHMIISGL IVVVLKVVGM TLFLLYFPQI FNKSNDGFTT TRSYGTVSQI FGSSSPSPNG
       61 FITTRSYGTV CPKDWEFYQA RCFFLSTSES SWNESRDFCK GKGSTLAIVN TPEKLKFLQD
      121 ITDAEKYFIG LIYHREEKRW RWINNSVFNG NVTNQNQNFN CATIGLTKTF DAASCDISYR
      181 RICEKNAK
//



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1: NP_060512. HYPOTHETICAL PROT...[GI:8922318] LINKS  


LOCUS       FLJ10260                 578 AA            LINEAR   PRI 14-MAY-2002
DEFINITION  HYPOTHETICAL PROTEIN FLJ10260 [HOMO SAPIENS].
ACCESSION   NP_060512
VERSION     NP_060512.1  GI:8922318
DBSOURCE    REFSEQ: AACCESSION NM_018042.1
KEYWORDS    .
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 578)
  AUTHORS   ISOGAI,T. AND OTSUKI,T.
  TITLE     HOMO SAPIENS HYPOTHETICAL PROTEIN FLJ10260 (FLJ10260), MRNA
  JOURNAL   UNPUBLISHED (2000)
COMMENT     PREDICTED REFSEQ: THE MRNA RECORD IS SUPPORTED BY EXPERIMENTAL
            EVIDENCE; HOWEVER, THE CODING SEQUENCE IS PREDICTED. THE REFERENCE
            SEQUENCE WAS DERIVED FROM AK001122.1.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..578
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="17"
                     /MAP="17Q12"
                     /CLONE="HEMBB1000973"
                     /TISSUE_TYPE="WHOLE EMBRYO, MAINLY BODY"
                     /CLONE_LIB="HEMBB1"
                     /DEV_STAGE="EMBRYO, 10 WEEKS"
                     /NOTE="CLONING VECTOR: PME18SFL3"
     PROTEIN         1..578
                     /PRODUCT="HYPOTHETICAL PROTEIN FLJ10260"
     CDS             1..578
                     /GENE="FLJ10260"
                     /CODED_BY="NM_018042.1:354..2090"
                     /DB_XREF="LOCUSID:55106"
ORIGIN      
        1 MNISVDLETN YAELVLDVGR VTLGENSRKK MKDCKLRKKQ NESVSRAMCA LLNSGGGVIK
       61 AEIENEDYSY TKDGIGLDLE NSFSNILLFV PEYLDFMQNG NYFLIFVKSW SLNTSGLRIT
      121 TLSSNLYKRD ITSAKVMNAT AALEFLKDMK KTRGRLYLRP ELLAKRPCVD IQEENNMKAL
      181 AGVFFDRTEL DRKEKLTFTE STHVEIKNFS TEKLLQRIKE ILPQYVSAFA NTDGGYLFIG
      241 LNEDKEIIGF KAEMSDLDDL EREIEKSIRK MPVHHFCMEK KKINYSCKFL GVYDKGSLCG
      301 YVCALRVERF CCAVFAKEPD SWHVKDNRVM QLTRKEWIQF MVEAEPKFSS SYEEVISQIN
      361 ASLPAPHSWP LLEWQRQRHH CPGLSGRITY TPENLCRKLF LQHEGLKQLI CEEMDSVRKG
      421 SLIFSRSWSV DLGLQENHKV LCDALLISQD SPPVLYTFHM VQDEEFKGYS TQTALTLKQK
      481 LAKIGGYTKK VCVMTKIFYL SPEGMTSCQY DLRSQVIYPE SYYFTRRKYL LKALFKALKR
      541 LKSLRDQFSF AENLYQIIGI DCFQKNDKKM FKSCRRLT
//



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1: A37128. METALLOPROTEINASE...[GI:106989] LINKS  


LOCUS       A37128                   220 AA            LINEAR   PRI 18-JUN-1999
DEFINITION  METALLOPROTEINASE INHIBITOR 2 PRECURSOR - HUMAN.
ACCESSION   A37128
VERSION     A37128  GI:106989
DBSOURCE    PIR: LOCUS A37128;
            
            SUMMARY: #LENGTH 220 #MOLECULAR-WEIGHT 24399 #CHECKSUM 6096
            ;
            GENETIC: #GENE GDB:TIMP2 ##CROSS-REFERENCES GDB:132612; OMIM:188825
            #MAP_POSITION 17Q25-17Q25
            ;
            SUPERFAMILY: METALLOPROTEINASE INHIBITOR
            ;
            PIR DATES: 08-MAR-1991 #SEQUENCE_REVISION 12-APR-1996 #TEXT_CHANGE
            18-JUN-1999
            .
KEYWORDS    ERYTHROPOIESIS; EXTRACELLULAR MATRIX; METALLOPROTEINASE INHIBITOR;
            MITOGEN.
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 220)
  AUTHORS   STETLER-STEVENSON,W.G., KRUTZSCH,H.C. AND LIOTTA,L.A.
  TITLE     TISSUE INHIBITOR OF METALLOPROTEINASE (TIMP-2). A NEW MEMBER OF THE
            METALLOPROTEINASE INHIBITOR FAMILY
  JOURNAL   J. BIOL. CHEM. 264 (29), 17374-17378 (1989)
  MEDLINE   90008902
   PUBMED   2793861
REFERENCE   2  (RESIDUES 1 TO 220)
  AUTHORS   GOLDBERG,G.I., MARMER,B.L., GRANT,G.A., EISEN,A.Z., WILHELM,S. AND
            HE,C.S.
  TITLE     HUMAN 72-KILODALTON TYPE IV COLLAGENASE FORMS A COMPLEX WITH A
            TISSUE INHIBITOR OF METALLOPROTEASES DESIGNATED TIMP-2
  JOURNAL   PROC. NATL. ACAD. SCI. U.S.A. 86 (21), 8207-8211 (1989)
  MEDLINE   90046765
   PUBMED   2554304
REFERENCE   3  (RESIDUES 1 TO 220)
  AUTHORS   BOONE,T.C., JOHNSON,M.J., DE CLERCK,Y.A. AND LANGLEY,K.E.
  TITLE     CDNA CLONING AND EXPRESSION OF A METALLOPROTEINASE INHIBITOR
            RELATED TO TISSUE INHIBITOR OF METALLOPROTEINASES
  JOURNAL   PROC. NATL. ACAD. SCI. U.S.A. 87 (7), 2800-2804 (1990)
  MEDLINE   90207285
   PUBMED   2157214
REFERENCE   4  (RESIDUES 1 TO 220)
  AUTHORS   STETLER-STEVENSON,W.G., BROWN,P.D., ONISTO,M., LEVY,A.T. AND
            LIOTTA,L.A.
  TITLE     TISSUE INHIBITOR OF METALLOPROTEINASES-2 (TIMP-2) MRNA EXPRESSION
            IN TUMOR CELL LINES AND HUMAN TUMOR TISSUES
  JOURNAL   J. BIOL. CHEM. 265 (23), 13933-13938 (1990)
  MEDLINE   90338014
   PUBMED   2380196
REFERENCE   5  (RESIDUES 1 TO 220)
  AUTHORS   WARD,R.V., HEMBRY,R.M., REYNOLDS,J.J. AND MURPHY,G.
  TITLE     THE PURIFICATION OF TISSUE INHIBITOR OF METALLOPROTEINASES-2 FROM
            ITS 72 KDA PROGELATINASE COMPLEX. DEMONSTRATION OF THE BIOCHEMICAL
            SIMILARITIES OF TISSUE INHIBITOR OF METALLOPROTEINASES-2 AND TISSUE
            INHIBITOR OF METALLOPROTEINASES-1
  JOURNAL   BIOCHEM. J. 278 (PT 1), 179-187 (1991)
  MEDLINE   91354200
   PUBMED   1909113
REFERENCE   6  (RESIDUES 1 TO 220)
  AUTHORS   OSTHUES,A., KNAUPER,V., OBERHOFF,R., REINKE,H. AND TSCHESCHE,H.
  TITLE     ISOLATION AND CHARACTERIZATION OF TISSUE INHIBITORS OF
            METALLOPROTEINASES (TIMP-1 AND TIMP-2) FROM HUMAN RHEUMATOID
            SYNOVIAL FLUID
  JOURNAL   FEBS LETT. 296 (1), 16-20 (1992)
  MEDLINE   92111776
   PUBMED   1730286
REFERENCE   7  (RESIDUES 1 TO 220)
  AUTHORS   OHBA,Y., GOTO,Y., KIMURA,Y., SUZUKI,F., HISA,T., TAKAHASHI,K. AND
            TAKIGAWA,M.
  TITLE     PURIFICATION OF AN ANGIOGENESIS INHIBITOR FROM CULTURE MEDIUM
            CONDITIONED BY A HUMAN CHONDROSARCOMA-DERIVED CHONDROCYTIC CELL
            LINE, HCS-2/8
  JOURNAL   BIOCHIM. BIOPHYS. ACTA 1245 (1), 1-8 (1995)
  MEDLINE   95383380
   PUBMED   7544625
REFERENCE   8  (RESIDUES 1 TO 220)
  AUTHORS   MALIK,K., SEJIMA,H., AOKI,T. AND IWATA,K.
  TITLE     DIRECT SUBMISSION
  JOURNAL   SUBMITTED (~AUG-1990) TO THE EMBL DATA LIBRARY
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..220
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
     PROTEIN         1..220
                     /PRODUCT="METALLOPROTEINASE INHIBITOR 2 PRECURSOR"
                     /NOTE="CHONDROCYTE-DERIVED ANGIOGENESIS INHIBITOR; TIMP-2;
                     TISSUE INHIBITOR OF METALLOPROTEINASES 2"
     REGION          1..26
                     /REGION_NAME="DOMAIN"
                     /NOTE="SIGNAL SEQUENCE"
     REGION          27..220
                     /REGION_NAME="PRODUCT"
                     /NOTE="METALLOPROTEINASE INHIBITOR 2"
     BOND            BOND(27,98)
                     /BOND_TYPE="DISULFIDE"
     BOND            BOND(29,127)
                     /BOND_TYPE="DISULFIDE"
     BOND            BOND(39,152)
                     /BOND_TYPE="DISULFIDE"
     BOND            BOND(154,201)
                     /BOND_TYPE="DISULFIDE"
     BOND            BOND(159,164)
                     /BOND_TYPE="DISULFIDE"
     BOND            BOND(172,193)
                     /BOND_TYPE="DISULFIDE"
ORIGIN      
        1 MGAAARTLRL ALGLLLLATL LRPADACSCS PVHPQQAFCN ADVVIRAKAV SEKEVDSGND
       61 IYGNPIKRIQ YEIKQIKMFK GPEKDIEFIY TAPSSAVCGV SLDVGGKKEY LIAGKAEGDG
      121 KMHITLCDFI VPWDTLSTTQ KKSLNHRYQM GCECKITRCP MIPCYISSPD ECLWMDWVTE
      181 KNINGHQAKF FACIKRSDGS CAWYRGAAPP KQEFLDIEDP
//



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1: P01922. HEMOGLOBIN ALPHA ...[GI:122412] LINKS  


LOCUS       HBA_HUMAN                142 AA            LINEAR   PRI 15-JUN-2002
DEFINITION  HEMOGLOBIN ALPHA CHAIN.
ACCESSION   P01922
VERSION     P01922  GI:122412
DBSOURCE    SWISSPROT: LOCUS HBA_HUMAN, ACCESSION P01922;
            CLASS: STANDARD.
            CREATED: JUL 21, 1986.
            SEQUENCE UPDATED: JUL 21, 1986.
            ANNOTATION UPDATED: JUN 15, 2002.
            XREFS: GI: 183793, GI: 386764, GI: 386765, GI: 28546, GI: 28547,
            GI: 28552, GI: 1340147, GI: 28557, GI: 28558, GI: 31747, GI:
            1335076, GI: 38222, GI: 38223, GI: 38224, GI: 38225, GI: 1817575,
            GI: 1817577, GI: 1817578, GI: 7428611, GI: 7428612, GI: 319896, PDB
            ACCESSION 1COH, PDB ACCESSION 1FDH, PDB ACCESSION 1HBS, PDB
            ACCESSION 1HCO, PDB ACCESSION 2HCO, PDB ACCESSION 1HHO, PDB
            ACCESSION 2HHB, PDB ACCESSION 3HHB, PDB ACCESSION 4HHB, PDB
            ACCESSION 1THB, PDB ACCESSION 1NIH, PDB ACCESSION 1BAB, PDB
            ACCESSION 1BBB, PDB ACCESSION 1CMY, PDB ACCESSION 1DXT, PDB
            ACCESSION 1DXU, PDB ACCESSION 1DXV, PDB ACCESSION 1HBA, PDB
            ACCESSION 1HBB, PDB ACCESSION 2HBC, PDB ACCESSION 2HBD, PDB
            ACCESSION 2HBE, PDB ACCESSION 2HBF, PDB ACCESSION 2HBS, PDB
            ACCESSION 1HGA, PDB ACCESSION 1HGB, PDB ACCESSION 1HGC, PDB
            ACCESSION 2HHD, PDB ACCESSION 2HHE, PDB ACCESSION 1CLS, PDB
            ACCESSION 1GBU, PDB ACCESSION 1GBV, PDB ACCESSION 1GLI, PDB
            ACCESSION 1DSH, PDB ACCESSION 1HAB, PDB ACCESSION 1HAC, PDB
            ACCESSION 1HDB, PDB ACCESSION 1SDK, PDB ACCESSION 1SDL, PDB
            ACCESSION 1AXF, PDB ACCESSION 1ABY, PDB ACCESSION 1A00, PDB
            ACCESSION 1A01, PDB ACCESSION 1A0U, PDB ACCESSION 1A0V, PDB
            ACCESSION 1A0W, PDB ACCESSION 1A0X, PDB ACCESSION 1A0Y, PDB
            ACCESSION 1A0Z, PDB ACCESSION 1RVW, PDB ACCESSION 1VWT, PDB
            ACCESSION 1A3N, PDB ACCESSION 1A3O, PDB ACCESSION 1AJ9, PDB
            ACCESSION 1A9W, PDB ACCESSION 1ABW, PDB ACCESSION 1BUW, PDB
            ACCESSION 6HBW, PDB ACCESSION 1BZ0, PDB ACCESSION 1BZ1, PDB
            ACCESSION 1BZZ, PDB ACCESSION 1B86, PDB ACCESSION 1BIJ, PDB
            ACCESSION 1QI8, PDB ACCESSION 1QSH, PDB ACCESSION 1QSI
            XREFS (NON-SEQUENCE DATABASES): SWISS-2DPAGEP01922,
            SIENA-2DPAGEP01922, MIM 141800, MIM 141850, MIM 141860,
            INTERPROIPR002338, INTERPROIPR000971, PFAMPF00042, PRINTSPR00612,
            PROSITEPS01033
KEYWORDS    HEME; OXYGEN TRANSPORT; TRANSPORT; ERYTHROCYTE; DISEASE MUTATION;
            POLYMORPHISM; ACETYLATION; 3D-STRUCTURE.
SOURCE      HOMO SAPIENS (HUMAN)
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 142)
  AUTHORS   MICHELSON,A.M. AND ORKIN,S.H.
  TITLE     THE 3' UNTRANSLATED REGIONS OF THE DUPLICATED HUMAN ALPHA-GLOBIN
            GENES ARE UNEXPECTEDLY DIVERGENT
  JOURNAL   CELL 22 (2 PT 2), 371-377 (1980)
  MEDLINE   81088339
   PUBMED   7448866
  REMARK    SEQUENCE FROM N.A. (ALPHA-1).
REFERENCE   2  (RESIDUES 1 TO 142)
  AUTHORS   LIEBHABER,S.A., GOOSSENS,M.J. AND KAN,Y.W.
  TITLE     CLONING AND COMPLETE NUCLEOTIDE SEQUENCE OF HUMAN 5'-ALPHA-GLOBIN
            GENE
  JOURNAL   PROC. NATL. ACAD. SCI. U.S.A. 77 (12), 7054-7058 (1980)
  MEDLINE   81175088
   PUBMED   6452630
  REMARK    SEQUENCE FROM N.A. (ALPHA-2).
REFERENCE   3  (RESIDUES 1 TO 142)
  AUTHORS   WILSON,J.T., WILSON,L.B., REDDY,V.B., CAVALLESCO,C., GHOSH,P.K.,
            DERIEL,J.K., FORGET,B.G. AND WEISSMAN,S.M.
  TITLE     NUCLEOTIDE SEQUENCE OF THE CODING PORTION OF HUMAN ALPHA GLOBIN
            MESSENGER RNA
  JOURNAL   J. BIOL. CHEM. 255 (7), 2807-2815 (1980)
  MEDLINE   80137531
   PUBMED   6244294
  REMARK    SEQUENCE FROM N.A. (ALPHA-2).
REFERENCE   4  (RESIDUES 1 TO 142)
  AUTHORS   FLINT,J. AND HIGGS,D.R.
  TITLE     DIRECT SUBMISSION
  JOURNAL   SUBMITTED (~JAN-1997)
  REMARK    SEQUENCE FROM N.A. (ALPHA-1 AND ALPHA-2).
REFERENCE   5  (RESIDUES 1 TO 142)
  AUTHORS   BRAUNITZER,G., GEHRING-MULLER,R., HILSCHMANN,N., HILSE,K.,
            HOBOM,G., RUDLOFF,V. AND WITTMANN-LIEBOLD,B.
  TITLE     THE CONSTITUTION OF NORMAL ADULT HUMAN HAEMOGLOBIN
  JOURNAL   HOPPE-SEYLER'S Z. PHYSIOL. CHEM. 325, 283-286 (1961)
  REMARK    SEQUENCE.
REFERENCE   6  (RESIDUES 1 TO 142)
  AUTHORS   HILL,R.J. AND KONIGSBERG,W.
  TITLE     THE STRUCTURE OF HUMAN HEMOGLOBIN: IV. THE CHYMOTRYPTIC DIGESTION
            OF THE ALPHA CHAIN OF HUMAN HEMOGLOBIN
  JOURNAL   J. BIOL. CHEM. 237, 3151-3156 (1962)
  REMARK    SEQUENCE.
REFERENCE   7  (RESIDUES 1 TO 142)
  AUTHORS   SCHROEDER,W.A., SHELTON,J.R., SHELTON,J.B. AND CORMICK,J.
  TITLE     THE AMINO ACID SEQUENCE OF THE ALPHA CHAIN OF HUMAN FETAL
            HEMOGLOBIN
  JOURNAL   BIOCHEMISTRY 2, 1353-1357 (1963)
  REMARK    SEQUENCE.
REFERENCE   8  (RESIDUES 1 TO 142)
  AUTHORS   FERMI,G.
  TITLE     THREE-DIMENSIONAL FOURIER SYNTHESIS OF HUMAN DEOXYHAEMOGLOBIN AT
            2-5 A RESOLUTION: REFINEMENT OF THE ATOMIC MODEL
  JOURNAL   J. MOL. BIOL. 97 (2), 237-256 (1975)
  MEDLINE   76027820
   PUBMED   1177322
  REMARK    X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
REFERENCE   9  (RESIDUES 1 TO 142)
  AUTHORS   SILVA,M.M., ROGERS,P.H. AND ARNONE,A.
  TITLE     A THIRD QUATERNARY STRUCTURE OF HUMAN HEMOGLOBIN A AT 1.7-A
            RESOLUTION
  JOURNAL   J. BIOL. CHEM. 267 (24), 17248-17256 (1992)
  MEDLINE   92381041
   PUBMED   1512262
  REMARK    X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF LIGANDED R2 STATE.
REFERENCE   10 (RESIDUES 1 TO 142)
  AUTHORS   SUTHERLAND-SMITH,A.J., BAKER,H.M., HOFMANN,O.M., BRITTAIN,T. AND
            BAKER,E.N.
  TITLE     CRYSTAL STRUCTURE OF A HUMAN EMBRYONIC HAEMOGLOBIN: THE
            CARBONMONOXY FORM OF GOWER II (ALPHA2 EPSILON2) HAEMOGLOBIN AT 2.9
            A RESOLUTION
  JOURNAL   J. MOL. BIOL. 280 (3), 475-484 (1998)
  MEDLINE   98332748
   PUBMED   9665850
  REMARK    X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER 2.
REFERENCE   11 (RESIDUES 1 TO 142)
  AUTHORS   KAVANAUGH,J.S., MOO-PENN,W.F. AND ARNONE,A.
  TITLE     ACCOMMODATION OF INSERTIONS IN HELICES: THE MUTATION IN HEMOGLOBIN
            CATONSVILLE (PRO 37 ALPHA-GLU-THR 38 ALPHA) GENERATES A
            3(10)-->ALPHA BULGE
  JOURNAL   BIOCHEMISTRY 32 (10), 2509-2513 (1993)
  MEDLINE   93192190
   PUBMED   8448109
  REMARK    X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF HB CATONSVILLE.
REFERENCE   12 (RESIDUES 1 TO 142)
  AUTHORS   RIFKIN,D. AND KONIGSBERG,W.
  TITLE     THE CHARACTERIZATION OF THE TRYPTIC PEPTIDES FROM THE HEMOGLOBIN OF
            THE CHIMPANZEE (PAN TROGLODYTES)
  JOURNAL   BIOCHIM. BIOPHYS. ACTA 104 (2), 457-461 (1965)
  MEDLINE   66071496
   PUBMED   5855051
  REMARK    SEQUENCE.
            SPECIES=P.TROGLODYTES
REFERENCE   13 (RESIDUES 1 TO 142)
  AUTHORS   LIEBHABER,S.A. AND BEGLEY,K.A.
  TITLE     STRUCTURAL AND EVOLUTIONARY ANALYSIS OF THE TWO CHIMPANZEE
            ALPHA-GLOBIN MRNAS
  JOURNAL   NUCLEIC ACIDS RES. 11 (24), 8915-8929 (1983)
  MEDLINE   84169526
   PUBMED   6689503
  REMARK    SEQUENCE FROM N.A.
            SPECIES=P.TROGLODYTES
REFERENCE   14 (RESIDUES 1 TO 142)
  AUTHORS   GOODMAN,M., BRAUNITZER,G., STANGL,A. AND SCHRANK,B.
  TITLE     EVIDENCE ON HUMAN ORIGINS FROM HAEMOGLOBINS OF AFRICAN APES
  JOURNAL   NATURE 303 (5917), 546-548 (1983)
  MEDLINE   83219265
   PUBMED   6406908
  REMARK    SEQUENCE.
            SPECIES=P.PANISCUS
REFERENCE   15 (RESIDUES 1 TO 142)
  AUTHORS   ABBES,S., M'RAD,A., FITZGERALD,P.A., DORMER,P., BLOUQUIT,Y.,
            KISTER,J., GALACTEROS,F. AND WAJCMAN,H.
  TITLE     HB AL-AIN ABU DHABI [ALPHA 18(A16)GLY----ASP]: A NEW HEMOGLOBIN
            VARIANT DISCOVERED IN AN EMIRATEE FAMILY
  JOURNAL   HEMOGLOBIN 16 (5), 355-362 (1992)
  MEDLINE   93053723
   PUBMED   1428941
  REMARK    VARIANT AL-AIN ABU DHABI.
REFERENCE   16 (RESIDUES 1 TO 142)
  AUTHORS   FUJIWARA,N., MAEKAWA,T. AND MATSUDA,G.
  TITLE     HEMOGLOBIN ATAGO (ALPHA2-85TYR BETA-2) A NEW ABNORMAL HUMAN
            HEMOGLOBIN FOUND IN NAGASAKI. BIOCHEMICAL STUDIES ON HEMOGLOBINS
            AND MYOGLOBINS. VI
  JOURNAL   INT. J. PROTEIN RES. 3 (1), 35-39 (1971)
  MEDLINE   72030550
   PUBMED   5115619
  REMARK    VARIANT ATAGO.
REFERENCE   17 (RESIDUES 1 TO 142)
  AUTHORS   BRENNAN,S.O. AND MATTHEWS,J.R.
  TITLE     HB AUCKLAND [ALPHA 87(F8) HIS-->ASN]: A NEW MUTATION OF THE
            PROXIMAL HISTIDINE IDENTIFIED BY ELECTROSPRAY MASS SPECTROMETRY
  JOURNAL   HEMOGLOBIN 21 (5), 393-403 (1997)
  MEDLINE   97463291
   PUBMED   9322075
  REMARK    VARIANT AUCKLAND.
REFERENCE   18 (RESIDUES 1 TO 142)
  AUTHORS   BRIMHALL,B.J., DUERST,M., HOLLAN,S.R., STENZEL,P., SZELENYI,J. AND
            JONES,R.T.
  TITLE     STRUCTURAL CHARACTERIZATIONS OF HEMOGLOBINS J-BUDA (ALPHA 61 (E10)
            LYS-TO-ASN) AND G-PEST (ALPHA 74 (EF3) ASP-TO-ASN)
  JOURNAL   BIOCHIM. BIOPHYS. ACTA 336, 344-360 (1974)
  REMARK    VARIANTS J-BUDA AND G-PEST.
REFERENCE   19 (RESIDUES 1 TO 142)
  AUTHORS   ZENG,Y.-T., HUANG,S.-Z., QIU,X.-K., CHENG,G.-C., REN,Z.-R.,
            JIN,Q.-C., CHEN,C.-Y., JIAO,C.-T., TANG,Z.-G., LIU,R.-H.,
            BAO,X.-H., ZENG,L.-Z., DUAN,Y.-Q. AND ZHANG,G.-Y.
  TITLE     HEMOGLOBIN CHONGQING [ALPHA 2(NA2)LEU----ARG] AND HEMOGLOBIN HARBIN
            [ALPHA 16(A14)LYS----MET] FOUND IN CHINA
  JOURNAL   HEMOGLOBIN 8 (6), 569-581 (1984)
  MEDLINE   85130255
   PUBMED   6526652
  REMARK    VARIANTS CHONGQING AND HARBIN.
REFERENCE   20 (RESIDUES 1 TO 142)
  AUTHORS   AYALA,S., COLOMER,D., GELPI,J.L. AND CORRONS,J.L.
  TITLE     ALPHA-THALASSAEMIA DUE TO A SINGLE CODON DELETION IN THE
            ALPHA1-GLOBIN GENE. COMPUTATIONAL STRUCTURAL ANALYSIS OF THE NEW
            ALPHA-CHAIN VARIANT. MUTATIONS IN BRIEF NO. 132. ONLINE
  JOURNAL   HUM. MUTAT. 11 (5), 412 (1998)
  MEDLINE   99220879
   PUBMED   10206681
  REMARK    VARIANT CLINIC.
REFERENCE   21 (RESIDUES 1 TO 142)
  AUTHORS   WILSON,J.B., WEBBER,B.B., PLASESKA,D., DE ALARCON,P.A.,
            MCMILLAN,S.K. AND HUISMAN,T.H.
  TITLE     HB DAVENPORT OR ALPHA 2(78)(EF7)ASN----HIS BETA 2
  JOURNAL   HEMOGLOBIN 14 (6), 599-605 (1990)
  MEDLINE   91331854
   PUBMED   2101836
  REMARK    VARIANT DAVENPORT.
REFERENCE   22 (RESIDUES 1 TO 142)
  AUTHORS   WILSON,J.B., WEBBER,B.B., KUTLAR,A., REESE,A.L., MCKIE,V.C.,
            LUTCHER,C.L., FELICE,A.E. AND HUISMAN,T.H.
  TITLE     HB EVANS OR ALPHA 262(E11)VAL----MET BETA 2; AN UNSTABLE HEMOGLOBIN
            CAUSING A MILD HEMOLYTIC ANEMIA
  JOURNAL   HEMOGLOBIN 13 (6), 557-566 (1989)
  MEDLINE   90109650
   PUBMED   2606724
  REMARK    VARIANT EVANS.
REFERENCE   23 (RESIDUES 1 TO 142)
  AUTHORS   CASH,F.E., MONPLAISIR,N., GOOSSENS,M. AND LIEBHABER,S.A.
  TITLE     LOCUS ASSIGNMENT OF TWO ALPHA-GLOBIN STRUCTURAL MUTANTS FROM THE
            CARIBBEAN BASIN: ALPHA FORT DE FRANCE (ALPHA 45 ARG) AND ALPHA
            SPANISH TOWN (ALPHA 27 VAL)
  JOURNAL   BLOOD 74 (2), 833-835 (1989)
  MEDLINE   89323437
   PUBMED   2752146
  REMARK    VARIANTS FORT DE FRANCE AND SPANISH TOWN.
REFERENCE   24 (RESIDUES 1 TO 142)
  AUTHORS   WAJCMAN,H., KISTER,J., RIOU,J., GALACTEROS,F., GIROT,R.,
            MAIER-REDELSPERGER,M., NAYUDU,N.V. AND GIORDANO,P.C.
  TITLE     HB GODAVARI [ALPHA 95(G2)PRO-->THR]: A NEUTRAL AMINO ACID
            SUBSTITUTION IN THE ALPHA 1 BETA 2 INTERFACE THAT MODIFIES THE
            ELECTROPHORETIC MOBILITY OF HEMOGLOBIN
  JOURNAL   HEMOGLOBIN 22 (1), 11-22 (1998)
  MEDLINE   98153063
   PUBMED   9494044
  REMARK    VARIANT GODAVARY.
REFERENCE   25 (RESIDUES 1 TO 142)
  AUTHORS   HUISMAN,T.H., WILSON,J.B., GRAVELY,M. AND HUBBARD,M.
  TITLE     HEMOGLOBIN GRADY: THE FIRST EXAMPLE OF A VARIANT WITH ELONGATED
            CHAINS DUE TO AN INSERTION OF RESIDUES
  JOURNAL   PROC. NATL. ACAD. SCI. U.S.A. 71 (8), 3270-3273 (1974)
  MEDLINE   75010592
   PUBMED   4528583
  REMARK    VARIANT GRADY.
REFERENCE   26 (RESIDUES 1 TO 142)
  AUTHORS   ORISAKA,M., TAJIMA,T., HARANO,T., HARANO,K., KUSHIDA,Y. AND IMAI,K.
  TITLE     A NEW ALPHA CHAIN VARIANT, HB HANAMAKI OR ALPHA
            2(139)(HC1)LYS----GLU BETA 2, FOUND IN A JAPANESE FAMILY
  JOURNAL   HEMOGLOBIN 16 (1-2), 67-71 (1992)
  MEDLINE   92340291
   PUBMED   1634363
  REMARK    VARIANT HANAMAKI.
REFERENCE   27 (RESIDUES 1 TO 142)
  AUTHORS   HARANO,T., HARANO,K., SHIBATA,S., UEDA,S., IMAI,K. AND SEKI,M.
  TITLE     HB HANDA [ALPHA 90 (FG 2) LYS REPLACED BY MET]: STRUCTURE AND
            BIOSYNTHESIS OF A NEW SLIGHTLY HIGHER OXYGEN AFFINITY VARIANT
  JOURNAL   HEMOGLOBIN 6 (4), 379-389 (1982)
  MEDLINE   83056269
   PUBMED   6815131
  REMARK    VARIANT HANDA.
REFERENCE   28 (RESIDUES 1 TO 142)
  AUTHORS   CHARACHE,S., MONDZAC,A.M. AND GESSNER,U.
  TITLE     HEMOGLOBIN HASHARON (ALPHA-2-47 HIS(CD5)BETA-2): A HEMOGLOBIN FOUND
            IN LOW CONCENTRATION
  JOURNAL   J. CLIN. INVEST. 48 (5), 834-847 (1969)
  MEDLINE   69165810
   PUBMED   5780195
  REMARK    VARIANT HASHARON.
REFERENCE   29 (RESIDUES 1 TO 142)
  AUTHORS   FLEMING,P.J., SUMNER,D.R., WYATT,K., HUGHES,W.G., MELROSE,W.D.,
            JUPE,D.M. AND BAIKIE,M.J.
  TITLE     HEMOGLOBIN HOBART OR ALPHA 20(BL)HIS----ARG: A NEW ALPHA CHAIN
            HEMOGLOBIN VARIANT
  JOURNAL   HEMOGLOBIN 11 (3), 211-220 (1987)
  MEDLINE   88006902
   PUBMED   3654264
  REMARK    VARIANT HOBART.
REFERENCE   30 (RESIDUES 1 TO 142)
  AUTHORS   REED,R.E., WINTER,W.P. AND RUCKNAGEL,D.L.
  TITLE     HAEMOGLOBIN INKSTER (ALPHA2 85ASPARTIC ACID LEADS TO VALINE BETA2)
            COEXISTING WITH BETA-THALASSAEMIA IN A CAUCASIAN FAMILY
  JOURNAL   BR. J. HAEMATOL. 26 (3), 475-484 (1974)
  MEDLINE   74302151
   PUBMED   4212045
  REMARK    VARIANT INKSTER.
REFERENCE   31 (RESIDUES 1 TO 142)
  AUTHORS   MIYASHITA,H., HASHIMOTO,K., MOHRI,H., OHOKUBO,T., HARANO,T.,
            HARANO,K. AND IMAI,K.
  TITLE     HB KANAGAWA [ALPHA 40(C5)LYS----MET]: A NEW ALPHA CHAIN VARIANT
            WITH AN INCREASED OXYGEN AFFINITY
  JOURNAL   HEMOGLOBIN 16 (1-2), 1-10 (1992)
  MEDLINE   92340282
   PUBMED   1634355
  REMARK    VARIANT KANAGAWA.
REFERENCE   32 (RESIDUES 1 TO 142)
  AUTHORS   GIORDANO,P.C., HARTEVELD,C.L., STRENG,H., OOSTERWIJK,J.C.,
            HEISTER,J.G., AMONS,R. AND BERNINI,L.F.
  TITLE     HB KURDISTAN [ALPHA 47(CE5)ASP-->TYR], A NEW ALPHA CHAIN VARIANT IN
            COMBINATION WITH BETA (0)-THALASSEMIA
  JOURNAL   HEMOGLOBIN 18 (1), 11-18 (1994)
  MEDLINE   94252883
   PUBMED   8195005
  REMARK    VARIANT KURDISTAN.
REFERENCE   33 (RESIDUES 1 TO 142)
  AUTHORS   HARANO,T., HARANO,K., IMAI,K., MURAKAMI,T. AND MATSUBARA,H.
  TITLE     HB KUROSAKI [ALPHA 7(A5)LYS-->GLU]: A NEW ALPHA CHAIN VARIANT FOUND
            IN A JAPANESE WOMAN
  JOURNAL   HEMOGLOBIN 19 (3-4), 197-201 (1995)
  MEDLINE   96031515
   PUBMED   7558876
  REMARK    VARIANT KUROSAKI.
REFERENCE   34 (RESIDUES 1 TO 142)
  AUTHORS   YALCIN,A., AVCU,F., BEYAN,C., GURGEY,A. AND URAL,A.U.
  TITLE     A CASE OF HB J-MEERUT (OR HB J-BIRMINGHAM) [ALPHA 120(H3)ALA-->GLU]
  JOURNAL   HEMOGLOBIN 18 (6), 433-435 (1994)
  MEDLINE   95229430
   PUBMED   7713747
  REMARK    VARIANT J-MEERUT OR J-BIRMINGHAM.
REFERENCE   35 (RESIDUES 1 TO 142)
  AUTHORS   WAJCMAN,H., KALMES,G., GROFF,P., PROME,D., RIOU,J. AND
            GALACTEROS,F.
  TITLE     HB MELUSINE [ALPHA 114(GH2)PRO-->SER]: A NEW NEUTRAL HEMOGLOBIN
            VARIANT
  JOURNAL   HEMOGLOBIN 17 (5), 397-405 (1993)
  MEDLINE   94124250
   PUBMED   8294199
  REMARK    VARIANT MELUSINE.
REFERENCE   36 (RESIDUES 1 TO 142)
  AUTHORS   BRIMHALL,B., JONES,R.T., SCHNEIDER,R.G., HOSTY,T.S., TOMLIN,G. AND
            ATKINS,R.
  TITLE     TWO NEW HEMOGLOBINS. HEMOGLOBIN ALABAMA (BETA39(C5)GLN LEADS TO
            LYS) AND HEMOGLOBIN MONTGOMERY (ALPHA 48(CD 6) LEU LEADS TO ARG)
  JOURNAL   BIOCHIM. BIOPHYS. ACTA 379 (1), 28-32 (1975)
  MEDLINE   75109326
   PUBMED   1115799
  REMARK    VARIANT MONTGOMERY.
REFERENCE   37 (RESIDUES 1 TO 142)
  AUTHORS   HONIG,G.R., SHAMSUDDIN,M., ZAIZOV,R., STEINHERZ,M., SOLAR,I. AND
            KIRSCHMANN,C.
  TITLE     HEMOGLOBIN PETAH TIKVA (ALPHA 110 ALA REPLACED BY ASP): A NEW
            UNSTABLE VARIANT WITH ALPHA-THALASSEMIA-LIKE EXPRESSION
  JOURNAL   BLOOD 57 (4), 705-711 (1981)
  MEDLINE   81134478
   PUBMED   7470621
  REMARK    VARIANT PETAH TIKVA.
REFERENCE   38 (RESIDUES 1 TO 142)
  AUTHORS   WAJCMAN,H., PREHU,M.O., PREHU,C., BLOUQUIT,Y., PROME,D. AND
            GALACTEROS,F.
  TITLE     HEMOGLOBIN PHNOM PENH [ALPHA117PHE(H1)-ILE-ALPHA118THR(H2)];
            EVIDENCE FOR A HOTSPOT FOR INSERTION OF RESIDUES IN THE THIRD EXON
            OF THE ALPHA1-GLOBIN GENE
  JOURNAL   HUM. MUTAT. SUPPL. 1, S20-S22 (1998)
  REMARK    VARIANT PHNOM PENH.
REFERENCE   39 (RESIDUES 1 TO 142)
  AUTHORS   ZWERDLING,T., WILLIAMS,S., NASR,S.A. AND RUCKNAGEL,D.L.
  TITLE     HB PORT HURON [ALPHA 56 (E5)LYS----ARG]: A NEW ALPHA CHAIN VARIANT
  JOURNAL   HEMOGLOBIN 15 (5), 381-391 (1991)
  MEDLINE   92202056
   PUBMED   1802882
  REMARK    VARIANT PORT HURON.
REFERENCE   40 (RESIDUES 1 TO 142)
  AUTHORS   SUMIDA,I., OTA,Y., IMAMURA,T. AND YANASE,T.
  TITLE     HEMOGLOBIN SAWARA: ALPHA 6(A4) ASPARTIC ACID LEADS TO ALANINE
  JOURNAL   BIOCHIM. BIOPHYS. ACTA 322 (1), 23-26 (1973)
  MEDLINE   74008827
   PUBMED   4744335
  REMARK    VARIANT SAWARA.
REFERENCE   41 (RESIDUES 1 TO 142)
  AUTHORS   ZENG,Y.T., HUANG,S.Z., ZHOU,X.D., QIU,X.K., DONG,Q.Y., LI,M.Y. AND
            BAI,J.H.
  TITLE     HB SHENYANG (ALPHA 26 (B7) ALA REPLACED BY GLU): A NEW UNSTABLE
            VARIANT FOUND IN CHINA
  JOURNAL   HEMOGLOBIN 6 (6), 625-628 (1982)
  MEDLINE   83135048
   PUBMED   7161109
  REMARK    VARIANT SHENYANG.
REFERENCE   42 (RESIDUES 1 TO 142)
  AUTHORS   SANGUANSERMSRI,T., MATRAGOON,S., CHANGLOAH,L. AND FLATZ,G.
  TITLE     HEMOGLOBIN SUAN-DOK (ALPHA 2 109 (G16) LEU REPLACED BY ARG BETA 2):
            AN UNSTABLE VARIANT ASSOCIATED WITH ALPHA-THALASSEMIA
  JOURNAL   HEMOGLOBIN 3 (2-3), 161-174 (1979)
  MEDLINE   80006169
   PUBMED   478977
  REMARK    VARIANT SUAN-DOK.
REFERENCE   43 (RESIDUES 1 TO 142)
  AUTHORS   HARKNESS,M., HARKNESS,D.R., KUTLAR,F., KUTLAR,A., WILSON,J.B.,
            WEBBER,B.B., CODRINGTON,J.F. AND HUISMAN,T.H.
  TITLE     HB SUN PRAIRIE OR ALPHA(2)130(H13)ALA----PRO BETA 2, A NEW UNSTABLE
            VARIANT OCCURRING IN LOW QUANTITIES
  JOURNAL   HEMOGLOBIN 14 (5), 479-489 (1990)
  MEDLINE   91177710
   PUBMED   2079430
  REMARK    VARIANT SUN PRAIRIE.
REFERENCE   44 (RESIDUES 1 TO 142)
  AUTHORS   HARANO,T., HARANO,K., IMAI,K. AND TERUNUMA,S.
  TITLE     HB SWAN RIVER [ALPHA 6(A4)ASP-->GLY] OBSERVED IN A JAPANESE MAN
  JOURNAL   HEMOGLOBIN 20 (1), 75-78 (1996)
  MEDLINE   96351655
   PUBMED   8745434
  REMARK    VARIANT SWAN RIVER.
REFERENCE   45 (RESIDUES 1 TO 142)
  AUTHORS   VASSEUR,C., BLOUQUIT,Y., KISTER,J., PROME,D., KAVANAUGH,J.S.,
            ROGERS,P.H., GUILLEMIN,C., ARNONE,A., GALACTEROS,F., POYART,C.,
            ROSA,J. AND WAJCMAN,H.
  TITLE     HEMOGLOBIN THIONVILLE. AN ALPHA-CHAIN VARIANT WITH A SUBSTITUTION
            OF A GLUTAMATE FOR VALINE AT NA-1 AND HAVING AN ACETYLATED
            METHIONINE NH2 TERMINUS
  JOURNAL   J. BIOL. CHEM. 267 (18), 12682-12691 (1992)
  MEDLINE   92316953
   PUBMED   1618774
  REMARK    VARIANT THIONVILLE.
REFERENCE   46 (RESIDUES 1 TO 142)
  AUTHORS   DARBELLAY,R., MACH-PASCUAL,S., ROSE,K., GRAF,J. AND BERIS,P.
  TITLE     HAEMOGLOBIN TUNIS-BIZERTE: A NEW ALPHA 1 GLOBIN 129 LEU-->PRO
            UNSTABLE VARIANT WITH THALASSAEMIC PHENOTYPE
  JOURNAL   BR. J. HAEMATOL. 90 (1), 71-76 (1995)
  MEDLINE   95306384
   PUBMED   7786798
  REMARK    VARIANT TUNIS-BIZERTE.
REFERENCE   47 (RESIDUES 1 TO 142)
  AUTHORS   LANGDOWN,J.V., DAVIDSON,R.J. AND WILLIAMSON,D.
  TITLE     A NEW ALPHA CHAIN VARIANT, HB TURRIFF [ALPHA 99(G6)LYS----GLU]: THE
            INTERFERENCE OF ABNORMAL HEMOGLOBINS IN HB A1C DETERMINATION
  JOURNAL   HEMOGLOBIN 16 (1-2), 11-17 (1992)
  MEDLINE   92340284
   PUBMED   1634357
  REMARK    VARIANT TURRIFF.
REFERENCE   48 (RESIDUES 1 TO 142)
  AUTHORS   WAJCMAN,H., KISTER,J., M'RAD,A., MARDEN,M.C., RIOU,J. AND
            GALACTEROS,F.
  TITLE     HB VAL DE MARNE [ALPHA 133(H16)SER-->ARG]: A NEW HEMOGLOBIN VARIANT
            WITH MODERATE INCREASE IN OXYGEN AFFINITY
  JOURNAL   HEMOGLOBIN 17 (5), 407-417 (1993)
  MEDLINE   94124251
   PUBMED   8294200
  REMARK    VARIANT VAL DE MARNE.
REFERENCE   49 (RESIDUES 1 TO 142)
  AUTHORS   JIANG,N.H., LIANG,S., WEN,X.J., LIANG,R., SU,C. AND TANG,Z.
  TITLE     HB WESTMEAD: AN ALPHA 2-GLOBIN GENE MUTATION DETECTED BY POLYMERASE
            CHAIN REACTION AND STU I CLEAVAGE
  JOURNAL   HEMOGLOBIN 15 (4), 291-295 (1991)
  MEDLINE   92155975
   PUBMED   1686260
  REMARK    VARIANT WESTMEAD.
REFERENCE   50 (RESIDUES 1 TO 142)
  AUTHORS   COMO,P.F., BARBER,S., SAGE,R.E., TRENT,R.J. AND KRONENBERG,H.
  TITLE     HEMOGLOBIN WOODVILLE: ALPHA (2)6(A4) ASPARTIC ACID----TYROSINE
  JOURNAL   HEMOGLOBIN 10 (2), 135-141 (1986)
  MEDLINE   86167529
   PUBMED   3754246
  REMARK    VARIANT WOODVILLE.
REFERENCE   51 (RESIDUES 1 TO 142)
  AUTHORS   FUJISAWA,K., HATTORI,Y., OHBA,Y. AND ANDO,S.
  TITLE     HB YUDA OR ALPHA 130(H13)ALA----ASP; A NEW ALPHA CHAIN VARIANT WITH
            LOW OXYGEN AFFINITY
  JOURNAL   HEMOGLOBIN 16 (5), 435-439 (1992)
  MEDLINE   93053734
   PUBMED   1428950
  REMARK    VARIANT YUDA.
REFERENCE   52 (RESIDUES 1 TO 142)
  AUTHORS   WAJCMAN,H., BLOUQUIT,Y., VASSEUR,C., LE QUERREC,A., LANIECE,M.,
            MELEVENDI,C., RASORE,A. AND GALACTEROS,F.
  TITLE     TWO NEW HUMAN HEMOGLOBIN VARIANTS CAUSED BY UNUSUAL MUTATIONAL
            EVENTS: HB ZAIRE CONTAINS A FIVE RESIDUE REPETITION WITHIN THE
            ALPHA-CHAIN AND HB DUINO HAS TWO RESIDUES SUBSTITUTED IN THE
            BETA-CHAIN
  JOURNAL   HUM. GENET. 89 (6), 676-680 (1992)
  MEDLINE   92380658
   PUBMED   1511986
  REMARK    VARIANT ZAIRE.
COMMENT     -------------------------------------------------------------------
            THIS SWISS-PROT ENTRY IS COPYRIGHT. IT IS PRODUCED THROUGH A
            COLLABORATION BETWEEN THE SWISS INSTITUTE OF BIOINFORMATICS AND
            THE EMBL OUTSTATION - THE EUROPEAN BIOINFORMATICS INSTITUTE.
            THE ORIGINAL ENTRY IS AVAILABLE FROM HTTP://WWW.EXPASY.CH/SPROT
            AND HTTP://WWW.EBI.AC.UK/SPROT
            ------------------------------------------------------------------.
            [FUNCTION] INVOLVED IN OXYGEN TRANSPORT FROM THE LUNG TO THE
            VARIOUS PERIPHERAL TISSUES.
            [SUBUNIT] HETEROTETRAMER OF TWO ALPHA CHAINS AND TWO BETA CHAINS
            (IN ADULT HEMOGLOBIN); TWO ALPHA CHAINS AND TWO EPSILON CHAINS (IN
            EARLY EMBRYONIC HEMOGLOBIN GOWER-2); TWO ALPHA CHAINS AND TWO GAMMA
            CHAINS (IN FETAL HEMOGLOBIN F).
            [TISSUE SPECIFICITY] RED BLOOD CELLS.
            [DISEASE] SOME RARE FORMS OF ALPHA-THALASSEMIA ARE DUE TO POINT
            MUTATIONS (NON-DELETIONAL ALPHA-THALASSEMIA). THE THALASSAEMIC
            PHENOTYPE IS DUE TO UNSTABLE GLOBIN ALPHA CHAINS THAT ARE RAPIDLY
            CATABOLIZED PRIOR TO FORMATION OF THE ALPHA-BETA DIMERS.
            [MISCELLANEOUS] GIVES BLOOD ITS RED COLOR.
            [SIMILARITY] BELONGS TO THE GLOBIN FAMILY.
            [DATABASE] NAME=HB VARIANT; NOTE=HUMAN HEMOGLOBIN VARIANTS;
            WWW='HTTP://GLOBIN.CSE.PSU.EDU/GLOBIN/HTML/HUISMAN/VARIANTS/".
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..142
                     /ORGANISM="PAN TROGLODYTES"
                     /DB_XREF="TAXON:9598"
     SOURCE          1..142
                     /ORGANISM="PAN PANISCUS"
                     /DB_XREF="TAXON:9597"
     SOURCE          1..142
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
     GENE            1..142
                     /GENE="HBA1"
                     /NOTE="HBA2"
     PROTEIN         1..142
                     /GENE="HBA1"
                     /PRODUCT="HEMOGLOBIN ALPHA CHAIN"
     SITE            1
                     /GENE="HBA1"
                     /SITE_TYPE="ACETYLATION"
                     /NOTE="(IN VARIANT THIONVILLE; WHERE THE INITIATOR MET IS
                     NOT CLEAVED)."
     REGION          2
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="V -> E (IN THIONVILLE; O2 AFFINITY DOWN).
                     /FTID=VAR_002719."
     REGION          3
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> R (IN CHONGQING; O2 AFFINITY UP).
                     /FTID=VAR_002720."
     REGION          5..18
                     /GENE="HBA1"
                     /REGION_NAME="HELICAL REGION"
     REGION          6
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> D (IN J-TORONTO). /FTID=VAR_002721."
     REGION          6
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> P (IN KARACHI). /FTID=VAR_002722."
     REGION          7
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> A (IN SAWARA; O2 AFFINITY UP).
                     /FTID=VAR_002723."
     REGION          7
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> G (IN SWAN RIVER). /FTID=VAR_002724."
     REGION          7
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> N (IN DUNN; O2 AFFINITY UP).
                     /FTID=VAR_002725."
     REGION          7
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> V (IN FERNDOWN; O2 AFFINITY UP).
                     /FTID=VAR_002726."
     REGION          7
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> Y (IN WOODVILLE; O2 AFFINITY UP).
                     /FTID=VAR_002727."
     REGION          8
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> E (IN KUROSAKI). /FTID=VAR_002728."
     REGION          12
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> E (IN ANANTHARAJ). /FTID=VAR_002729."
     REGION          13
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> D (IN J-PARIS 1/J-ALJEZUR). /FTID=VAR_002730."
     REGION          15
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="W -> R (IN EVANSTON; O2 AFFINITY UP).
                     /FTID=VAR_002731."
     REGION          16
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="G -> R (IN OTTAWA/SIAM). /FTID=VAR_002732."
     REGION          17
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> M (IN HARBIN; SLIGHTLY UNSTABLE).
                     /FTID=VAR_002733."
     REGION          17
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> N (IN BEIJING). /FTID=VAR_002734."
     REGION          19..21
                     /GENE="HBA1"
                     /REGION_NAME="HELICAL REGION"
     REGION          19
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="G -> D (IN AL-AIN-ABU DHABI). /FTID=VAR_002735."
     REGION          19
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="G -> R (IN HANDSWORTH). /FTID=VAR_002736."
     REGION          20
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> D (IN J-KUROSH). /FTID=VAR_002737."
     REGION          20
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> E (IN J-TASHIKUERGAN). /FTID=VAR_002738."
     REGION          21
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> Q (IN LE LAMENTIN). /FTID=VAR_002739."
     REGION          21
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> R (IN HOBART). /FTID=VAR_002740."
     REGION          22..36
                     /GENE="HBA1"
                     /REGION_NAME="HELICAL REGION"
     REGION          22
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> D (IN J-NYANZA). /FTID=VAR_002741."
     REGION          22
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> P (IN FONTAINEBLAU). /FTID=VAR_002742."
     REGION          23
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="G -> D (IN J-MEDELLIN). /FTID=VAR_002743."
     REGION          24
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="E -> G (IN REIMS; SLIGHTLY UNSTABLE).
                     /FTID=VAR_002744."
     REGION          24
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="E -> K (IN CHAD). /FTID=VAR_002745."
     REGION          25
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="Y -> H (IN LUXEMBOURG; UNSTABLE).
                     /FTID=VAR_002746."
     REGION          27
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> E (IN SHENYANG; UNSTABLE). /FTID=VAR_002747."
     REGION          28
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="E -> D (IN HEKINAN). /FTID=VAR_002748."
     REGION          28
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="E -> G (IN FORT WORTH). /FTID=VAR_002749."
     REGION          28
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="E -> V (IN SPANISH TOWN). /FTID=VAR_002750."
     REGION          31
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="E -> K (IN O-PADOVA). /FTID=VAR_002751."
     REGION          32
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="R -> S (IN PRATO; UNSTABLE). /FTID=VAR_002752."
     REGION          35
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> R (IN QUEENS/OGI). /FTID=VAR_002753."
     REGION          38..43
                     /GENE="HBA1"
                     /REGION_NAME="HELICAL REGION"
     REGION          38
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="P -> R (IN BOURMEDES). /FTID=VAR_002754."
     REGION          38
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="P -> PE (IN CATONSVILLE). /FTID=VAR_002755."
     REGION          41
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> M (IN KANAGAWA; O2 AFFINITY UP).
                     /FTID=VAR_002756."
     REGION          42
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="T -> S (IN MIYANO; O2 AFFINITY UP).
                     /FTID=VAR_002757."
     REGION          44
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="F -> L (IN HIROSAKI; UNSTABLE). /FTID=VAR_002758."
     REGION          45..46
                     /GENE="HBA1"
                     /REGION_NAME="HYDROGEN BONDED TURN"
     REGION          45
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="P -> L (IN MILLEDGEVILLE; O2 AFFINITY UP).
                     /FTID=VAR_002759."
     REGION          45
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="P -> R (IN KAWACHI; O2 AFFINITY UP).
                     /FTID=VAR_002760."
     REGION          46
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> Q (IN BARI). /FTID=VAR_002761."
     REGION          46
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> R (IN FORT DE FRANCE; O2 AFFINITY UP).
                     /FTID=VAR_002762."
     REGION          48
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> A (IN CORDELE; UNSTABLE). /FTID=VAR_002763."
     REGION          48
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> G (IN UMI/MICHIGAN; UNSTABLE).
                     /FTID=VAR_002764."
     REGION          48
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> H (IN HASHARON/SINAI; UNSTABLE).
                     /FTID=VAR_002765."
     REGION          48
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> Y (IN KURDISTAN). /FTID=VAR_002766."
     REGION          49
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> R (IN MONTGOMERY). /FTID=VAR_002767."
     REGION          50
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="S -> R (IN SAVARIA). /FTID=VAR_002768."
     REGION          51..52
                     /GENE="HBA1"
                     /REGION_NAME="HYDROGEN BONDED TURN"
     REGION          51
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> R (IN AICHI; SLIGHTLY UNSTABLE).
                     /FTID=VAR_002769."
     REGION          52
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="G -> D (IN J-ABIDJAN). /FTID=VAR_002770."
     REGION          52
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="G -> R (IN RUSS). /FTID=VAR_002771."
     REGION          54..72
                     /GENE="HBA1"
                     /REGION_NAME="HELICAL REGION"
     REGION          54
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> D (IN J-ROVIGO; UNSTABLE). /FTID=VAR_002772."
     REGION          55
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="Q -> R (IN HIKOSHIMA/SHIMONOSEKI).
                     /FTID=VAR_002773."
     REGION          57
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> R (IN PORT HURON). /FTID=VAR_002774."
     REGION          57
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> T (IN THAILAND). /FTID=VAR_002775."
     REGION          58
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="G -> R (IN L-PERSIAN GULF). /FTID=VAR_002776."
     REGION          59
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> Y (IN M-BOSTON/M-OSAKA; O2 AFFINITY DOWN).
                     /FTID=VAR_002777."
     SITE            59
                     /GENE="HBA1"
                     /SITE_TYPE="METAL-BINDING"
                     /NOTE="IRON (HEME DISTAL LIGAND)."
     REGION          60
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="G -> D (IN ADANA; UNSTABLE; CAUSES ALPHA-
                     THALASSEMIA). /FTID=VAR_002778."
     REGION          60
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="G -> V (IN TOTTORI; UNSTABLE). /FTID=VAR_002779."
     REGION          61
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> N (IN ZAMBIA). /FTID=VAR_002780."
     REGION          61
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="MISSING (IN CLINIC; UNSTABLE; CAUSES
                     ALPHA-THALASSEMIA). /FTID=VAR_002781."
     REGION          62
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> N (IN J-BUDA). /FTID=VAR_002782."
     REGION          62
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> T (IN J-ANATOLIA). /FTID=VAR_002783."
     REGION          63
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="V -> M (IN EVANS; UNSTABLE). /FTID=VAR_002784."
     REGION          64
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> D (IN PONTOISE; UNSTABLE). /FTID=VAR_002785."
     REGION          65
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> Y (IN PERSEPOLIS). /FTID=VAR_002786."
     REGION          69
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="N -> K (IN G-PHILADELPHIA). /FTID=VAR_002787."
     REGION          72
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> E (IN J-HABANA). /FTID=VAR_002788."
     REGION          72
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> V (IN OZIERI). /FTID=VAR_002789."
     REGION          73
                     /GENE="HBA1"
                     /REGION_NAME="HYDROGEN BONDED TURN"
     REGION          73
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> R (IN DANESKGAH-TEHERAN). /FTID=VAR_002790."
     REGION          74..76
                     /GENE="HBA1"
                     /REGION_NAME="HELICAL REGION"
     REGION          75
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> A (IN LILLE). /FTID=VAR_002791."
     REGION          75
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> G (IN CHAPEL HILL). /FTID=VAR_002792."
     REGION          75
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> N (IN G-PEST). /FTID=VAR_002793."
     REGION          76
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> A (IN DUAN). /FTID=VAR_002794."
     REGION          76
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> H (IN Q-IRAN). /FTID=VAR_002795."
     REGION          77..80
                     /GENE="HBA1"
                     /REGION_NAME="HELICAL REGION"
     REGION          77
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="M -> K (IN NOKO). /FTID=VAR_002796."
     REGION          77
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="M -> T (IN AZTEC). /FTID=VAR_002797."
     REGION          78
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="P -> R (IN GUIZHOU). /FTID=VAR_002798."
     REGION          79
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="N -> H (IN DAVENPORT). /FTID=VAR_002799."
     REGION          79
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="N -> K (IN STANLEYVILLE-2). /FTID=VAR_002800."
     REGION          80
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> G (IN SINGAPORE). /FTID=VAR_012662."
     REGION          81
                     /GENE="HBA1"
                     /REGION_NAME="HYDROGEN BONDED TURN"
     REGION          81
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> R (IN ANN ARBOR; UNSTABLE). /FTID=VAR_002801."
     REGION          82..90
                     /GENE="HBA1"
                     /REGION_NAME="HELICAL REGION"
     REGION          82
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="S -> C (IN NIGERIA). /FTID=VAR_002802."
     REGION          83
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> D (IN GARDEN STATE). /FTID=VAR_002803."
     REGION          85
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="S -> R (IN ETOBICOKE; O2 AFFINITY UP).
                     /FTID=VAR_002804."
     REGION          86
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> V (IN INKSTER; O2 AFFINITY UP).
                     /FTID=VAR_002805."
     REGION          86
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> Y (IN ATAGO; O2 AFFINITY UP).
                     /FTID=VAR_002806."
     REGION          87
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> R (IN MOABIT; UNSTABLE). /FTID=VAR_002807."
     REGION          88
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> N (IN AUCKLAND; UNSTABLE). /FTID=VAR_002808."
     REGION          88
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> R (IN IWATA; UNSTABLE). /FTID=VAR_002809."
     SITE            88
                     /GENE="HBA1"
                     /SITE_TYPE="METAL-BINDING"
                     /NOTE="IRON (HEME PROXIMAL LIGAND)."
     REGION          89
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> S (IN LOIRE; O2 AFFINITY UP).
                     /FTID=VAR_002810."
     REGION          91..92
                     /GENE="HBA1"
                     /REGION_NAME="HYDROGEN BONDED TURN"
     REGION          91
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> M (IN HANDA; O2 AFFINITY UP).
                     /FTID=VAR_002811."
     REGION          92
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> P (IN PORT PHILLIP; UNSTABLE).
                     /FTID=VAR_002812."
     REGION          93
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="R -> Q (IN J-CAPE TOWN; O2 AFFINITY UP).
                     /FTID=VAR_002813."
     REGION          95
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> Y (IN SETIF; UNSTABLE). /FTID=VAR_002814."
     REGION          96
                     /GENE="HBA1"
                     /REGION_NAME="HYDROGEN BONDED TURN"
     REGION          96
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="P -> A (IN DENMARK HILL; O2 AFFINITY UP).
                     /FTID=VAR_002815."
     REGION          96
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="P -> T (IN GODAVARI; O2 AFFINITY UP).
                     /FTID=VAR_002816."
     REGION          97..113
                     /GENE="HBA1"
                     /REGION_NAME="HELICAL REGION"
     REGION          98
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="N -> K (IN DALLAS; O2 AFFINITY UP).
                     /FTID=VAR_002817."
     REGION          100
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> E (IN TURRIFF). /FTID=VAR_002818."
     REGION          103
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="S -> R (IN MANITOBA; SLIGHTLY UNSTABLE).
                     /FTID=VAR_002819."
     REGION          104
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> R (IN CONTALDO; UNSTABLE). /FTID=VAR_002820."
     REGION          110
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> R (IN SUAN-DOK; UNSTABLE; CAUSES
                     ALPHA-THALASSEMIA). /FTID=VAR_002821."
     REGION          111
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> D (IN PETAH TIKVA; UNSTABLE; CAUSES
                     ALPHA-THALASSEMIA). /FTID=VAR_002822."
     REGION          113
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> D (IN HOPKINS-II; UNSTABLE).
                     /FTID=VAR_002823."
     REGION          114
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> H (IN TWIN PEAKS). /FTID=VAR_002824."
     REGION          115..117
                     /GENE="HBA1"
                     /REGION_NAME="HYDROGEN BONDED TURN"
     REGION          115
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="P -> L (IN NOUAKCHOTT). /FTID=VAR_002825."
     REGION          115
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="P -> R (IN CHIAPAS). /FTID=VAR_002826."
     REGION          115
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="P -> S (IN MELUSINE). /FTID=VAR_002827."
     REGION          116
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> D (IN J-TONGARIKI). /FTID=VAR_002828."
     REGION          117
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="E -> A (IN UBE-4). /FTID=VAR_002829."
     REGION          117
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="E -> EHLPAE (IN ZAIRE). /FTID=VAR_002830."
     REGION          118
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="F -> FI (IN PHNOM PENH). /FTID=VAR_002831."
     REGION          119
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="T -> TEFT (IN GRADY). /FTID=VAR_002832."
     REGION          120..138
                     /GENE="HBA1"
                     /REGION_NAME="HELICAL REGION"
     REGION          121
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> E (IN J-MEERUT/J-BIRMINGHAM).
                     /FTID=VAR_002833."
     REGION          122
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="V -> M (IN OWARI). /FTID=VAR_002834."
     REGION          123
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> Q (IN WESTMEAD). /FTID=VAR_002835."
     REGION          126
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> P (IN QUONG SZE; CAUSES ALPHA-THALASSEMIA).
                     /FTID=VAR_002836."
     REGION          127
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> V (IN FUKUTOMI; O2 AFFINITY UP).
                     /FTID=VAR_002837."
     REGION          127
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="D -> Y (IN MONTERIORE; O2 AFFINITY UP).
                     /FTID=VAR_002838."
     REGION          128
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> N (IN JACKSON). /FTID=VAR_002839."
     REGION          130
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> P (IN TUNIS-BIZERTE; UNSTABLE; CAUSES
                     ALPHA-THALASSEMIA). /FTID=VAR_002840."
     REGION          131
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> P (IN SUN PRAIRIE; UNSTABLE).
                     /FTID=VAR_002841."
     REGION          131
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="A -> D (IN YUDA; O2 AFFINITY DOWN).
                     /FTID=VAR_002842."
     REGION          132
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="S -> P (IN QUESTEMBERT; HIGHLY UNSTABLE; CAUSES
                     ALPHA-THALASSEMIA). /FTID=VAR_002843."
     REGION          134
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="S -> R (IN VAL DE MARNE; O2 AFFINITY UP).
                     /FTID=VAR_002844."
     REGION          136
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="V -> E (IN PAVIE). /FTID=VAR_002845."
     REGION          137
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> M (IN CHICAGO). /FTID=VAR_002846."
     REGION          137
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="L -> P (IN BIBBA; UNSTABLE; CAUSES
                     ALPHA-THALASSEMIA). /FTID=VAR_002847."
     REGION          139..142
                     /GENE="HBA1"
                     /REGION_NAME="HYDROGEN BONDED TURN"
     REGION          139
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="S -> P (IN ATTLEBORO; O2 AFFINITY UP).
                     /FTID=VAR_002848."
     REGION          140
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> E (IN HANAKAMI; O2 AFFINITY UP).
                     /FTID=VAR_002849."
     REGION          140
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="K -> T (IN TOKONAME; O2 AFFINITY UP).
                     /FTID=VAR_002850."
     REGION          141
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="Y -> H (IN ROUEN; O2 AFFINITY UP).
                     /FTID=VAR_002851."
     REGION          142
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="R -> C (IN NUNOBIKI; O2 AFFINITY UP).
                     /FTID=VAR_002852."
     REGION          142
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="R -> L (IN LEGNANO; O2 AFFINITY UP).
                     /FTID=VAR_002853."
     REGION          142
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="R -> H (IN SURESNES; O2 AFFINITY UP).
                     /FTID=VAR_002854."
     REGION          142
                     /GENE="HBA1"
                     /REGION_NAME="VARIANT"
                     /NOTE="R -> P (IN SINGAPORE). /FTID=VAR_002855."
ORIGIN      
        1 MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
       61 KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP
      121 AVHASLDKFL ASVSTVLTSK YR
//



REVISED: JULY 5, 2002.
 
 


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NCBI | NLM | NIH 

 

OCT 21 2002 11:56:56 

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  SUMMARY ASN.1 FASTA TINYSEQ XML GI LIST GENPEPT GBSEQ XML GRAPHICS XML DEFAULT             
 
 

1: NP_060416. FK506 BINDING PRO...[GI:8923659] LINKS  


LOCUS       FKBP14                   211 AA            LINEAR   PRI 05-SEP-2002
DEFINITION  FK506 BINDING PROTEIN 14, 22 KDA; HYPOTHETICAL PROTEIN FLJ20731;
            FK506 BINDING PROTEIN 14 (22 KDA) [HOMO SAPIENS].
ACCESSION   NP_060416
VERSION     NP_060416.1  GI:8923659
DBSOURCE    REFSEQ: AACCESSION NM_017946.1
KEYWORDS    .
SOURCE      HOMO SAPIENS (HUMAN)
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 211)
  AUTHORS   PATTERSON,C.E., GAO,J., ROONEY,A.P. AND DAVIS,E.C.
  TITLE     GENOMIC ORGANIZATION OF MOUSE AND HUMAN 65 KDA FK506-BINDING
            PROTEIN GENES AND EVOLUTION OF THE FKBP MULTIGENE FAMILY
  JOURNAL   GENOMICS 79 (6), 881-889 (2002)
  MEDLINE   22032991
   PUBMED   12036304
REFERENCE   2  (SITES)
  AUTHORS   KAWAKAMI,T., NOGUCHI,S., ITOH,T., SHIGETA,K., SENBA,T.,
            MATSUMURA,K., NAKAJIMA,Y., MIZUNO,T., MORINAGA,M., OTA,T.,
            SUZUKI,Y., OBAYASHI,M., NISHI,T., SHIBAHARA,T., TANAKA,T.,
            NAKAMURA,Y., ISOGAI,T. AND SUGANO,S.
  TITLE     NEDO HUMAN CDNA SEQUENCING PROJECT
  JOURNAL   UNPUBLISHED
COMMENT     PREDICTED REFSEQ: THE MRNA RECORD IS SUPPORTED BY EXPERIMENTAL
            EVIDENCE; HOWEVER, THE CODING SEQUENCE IS PREDICTED. THE REFERENCE
            SEQUENCE WAS DERIVED FROM AK000738.1.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..211
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="7"
                     /MAP="7P15.3"
                     /CLONE="HEP10272"
                     /CELL_LINE="HEPG2"
                     /CELL_TYPE="HEPATOMA"
                     /CLONE_LIB="HEP"
                     /NOTE="CLONING VECTOR PME18SFL3"
     PROTEIN         1..211
                     /PRODUCT="FK506 BINDING PROTEIN 14, 22 KDA"
                     /NOTE="HYPOTHETICAL PROTEIN FLJ20731; FK506 BINDING
                     PROTEIN 14 (22 KDA)"
     REGION          38..132
                     /REGION_NAME="PFAM00254, FKBP, FKBP-TYPE PEPTIDYL-PROLYL
                     CIS-TRANS ISOMERASE"
     CDS             1..211
                     /GENE="FKBP14"
                     /CODED_BY="NM_017946.1:146..781"
                     /DB_XREF="LOCUSID:55033"
ORIGIN      
        1 MRLFLWNAVL TLFVTSLIGA LIPEPEVKIE VLQKPFICHR KTKGGDLMLV HYEGYLEKDG
       61 SLFHSTHKHN NGQPIWFTLG ILEALKGWDQ GLKGMCVGEK RKLIIPPALG YGKEGKGKIP
      121 PESTLIFNID LLEIRNGPRS HESFQEMDLN DDWKLSKDEV KAYLKKEFEK HGAVVNESHH
      181 DALVEDIFDK EDEDKDGFIS AREFTYKHDE L
//



REVISED: JULY 5, 2002.
 
 


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NCBI | NLM | NIH 

 

OCT 21 2002 11:56:56 

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1: P09871. COMPLEMENT C1S CO...[GI:115205] LINKS  


LOCUS       C1S_HUMAN                688 AA            LINEAR   PRI 15-JUN-2002
DEFINITION  COMPLEMENT C1S COMPONENT PRECURSOR (C1 ESTERASE).
ACCESSION   P09871
VERSION     P09871  GI:115205
DBSOURCE    SWISSPROT: LOCUS C1S_HUMAN, ACCESSION P09871;
            CLASS: STANDARD.
            EXTRA
            ACCESSIONS:Q9UM14,Q9UCU7,Q9UCU8,Q9UCU9,Q9UCV0,Q9UCV1,Q9UCV2,Q9UCV3,
            Q9UCV4,Q9UCV5,CREATED: MAR 1, 1989.
            SEQUENCE UPDATED: MAR 1, 1989.
            ANNOTATION UPDATED: JUN 15, 2002.
            XREFS: GI: 29542, GI: 763110, GI: 179645, GI: 179646, GI: 179647,
            GI: 179648, GI: 6407557, GI: 6407558, GI: 67615, GI: 87215
            XREFS (NON-SEQUENCE DATABASES): MEROPSS01.193, SWISS-2DPAGEP09871,
            MIM 120580, INTERPROIPR000152, INTERPROIPR000859,
            INTERPROIPR001314, INTERPROIPR000561, INTERPROIPR001881,
            INTERPROIPR001254, INTERPROIPR000436, PFAMPF00008, PFAMPF00084,
            PFAMPF00089, PFAMPF00431, PRINTSPR00722, SMARTSM00032,
            SMARTSM00042, SMARTSM00179, SMARTSM00020, PROSITEPS00010,
            PROSITEPS01180, PROSITEPS00022, PROSITEPS01186, PROSITEPS01187,
            PROSITEPS50240, PROSITEPS00134, PROSITEPS00135
KEYWORDS    COMPLEMENT PATHWAY; PLASMA; GLYCOPROTEIN; SERINE PROTEASE;
            HYDROLASE; HYDROXYLATION; SUSHI; REPEAT; SIGNAL; EGF-LIKE DOMAIN;
            CALCIUM-BINDING.
SOURCE      HOMO SAPIENS (HUMAN)
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 688)
  AUTHORS   KUSUMOTO,H., HIROSAWA,S., SALIER,J.P., HAGEN,F.S. AND KURACHI,K.
  TITLE     HUMAN GENES FOR COMPLEMENT COMPONENTS C1R AND C1S IN A CLOSE
            TAIL-TO-TAIL ARRANGEMENT
  JOURNAL   PROC. NATL. ACAD. SCI. U.S.A. 85 (19), 7307-7311 (1988)
  MEDLINE   89017187
  REMARK    SEQUENCE FROM N.A.
REFERENCE   2  (RESIDUES 1 TO 688)
  AUTHORS   MACKINNON,C.M., CARTER,P.E., SMYTH,S.J., DUNBAR,B. AND
            FOTHERGILL,J.E.
  TITLE     MOLECULAR CLONING OF CDNA FOR HUMAN COMPLEMENT COMPONENT C1S. THE
            COMPLETE AMINO ACID SEQUENCE
  JOURNAL   EUR. J. BIOCHEM. 169 (3), 547-553 (1987)
  MEDLINE   88082788
  REMARK    SEQUENCE FROM N.A.
            TISSUE=LIVER
REFERENCE   3  (RESIDUES 1 TO 688)
  AUTHORS   TOSI,M., DUPONCHEL,C., MEO,T. AND JULIER,C.
  TITLE     COMPLETE CDNA SEQUENCE OF HUMAN COMPLEMENT CLS AND CLOSE PHYSICAL
            LINKAGE OF THE HOMOLOGOUS GENES CLS AND CLR
  JOURNAL   BIOCHEMISTRY 26 (26), 8516-8524 (1987)
  MEDLINE   88163522
  REMARK    SEQUENCE FROM N.A.
REFERENCE   4  (RESIDUES 1 TO 688)
  AUTHORS   ENDO,Y., TAKAHASHI,M., NAKAO,M., SAIGA,H., SEKINE,H.,
            MATSUSHITA,M., NONAKA,M. AND FUJITA,T.
  TITLE     TWO LINEAGES OF MANNOSE-BINDING LECTIN-ASSOCIATED SERINE PROTEASE
            (MASP) IN VERTEBRATES
  JOURNAL   J. IMMUNOL. 161 (9), 4924-4930 (1998)
  MEDLINE   99008558
  REMARK    SEQUENCE OF 1-329 FROM N.A.
            TISSUE=PERIPHERAL BLOOD LEUKOCYTES
REFERENCE   5  (RESIDUES 1 TO 688)
  AUTHORS   TOSI,M., DUPONCHEL,C., MEO,T. AND COUTURE-TOSI,E.
  TITLE     COMPLEMENT GENES C1R AND C1S FEATURE AN INTRONLESS SERINE PROTEASE
            DOMAIN CLOSELY RELATED TO HAPTOGLOBIN
  JOURNAL   J. MOL. BIOL. 208 (4), 709-714 (1989)
  MEDLINE   90040704
  REMARK    SEQUENCE OF 291-688 FROM N.A.
REFERENCE   6  (RESIDUES 1 TO 688)
  AUTHORS   SPYCHER,S.E., NICK,H. AND RICKLI,E.E.
  TITLE     HUMAN COMPLEMENT COMPONENT C1S. PARTIAL SEQUENCE DETERMINATION OF
            THE HEAVY CHAIN AND IDENTIFICATION OF THE PEPTIDE BOND CLEAVED
            DURING ACTIVATION
  JOURNAL   EUR. J. BIOCHEM. 156 (1), 49-57 (1986)
  MEDLINE   86164350
  REMARK    SEQUENCE OF 16-61; 168-219; 287-334 AND 384-445.
REFERENCE   7  (RESIDUES 1 TO 688)
  AUTHORS   CARTER,P.E., DUNBAR,B. AND FOTHERGILL,J.E.
  TITLE     THE SERINE PROTEINASE CHAIN OF HUMAN COMPLEMENT COMPONENT C1S.
            CYANOGEN BROMIDE CLEAVAGE AND N-TERMINAL SEQUENCES OF THE FRAGMENTS
  JOURNAL   BIOCHEM. J. 215 (3), 565-571 (1983)
  MEDLINE   84104122
  REMARK    SEQUENCE OF 438-500; 503-534; 542-601; 617-623 AND 626-656.
REFERENCE   8  (RESIDUES 1 TO 688)
  AUTHORS   ILLY,C., THIELENS,N.M., GAGNON,J. AND ARLAUD,G.J.
  TITLE     EFFECT OF LACTOPEROXIDASE-CATALYZED IODINATION ON THE
            CA(2+)-DEPENDENT INTERACTIONS OF HUMAN C1S. LOCATION OF THE
            IODINATION SITES
  JOURNAL   BIOCHEMISTRY 30 (29), 7135-7141 (1991)
  MEDLINE   91308095
  REMARK    PARTIAL SEQUENCE.
            TISSUE=PLASMA
REFERENCE   9  (RESIDUES 1 TO 688)
  AUTHORS   HESS,D., SCHALLER,J. AND RICKLI,E.E.
  TITLE     IDENTIFICATION OF THE DISULFIDE BONDS OF HUMAN COMPLEMENT C1S
  JOURNAL   BIOCHEMISTRY 30 (11), 2827-2833 (1991)
  MEDLINE   91175725
  REMARK    DISULFIDE BONDS.
REFERENCE   10 (RESIDUES 1 TO 688)
  AUTHORS   ROSSI,V., GABORIAUD,C., LACROIX,M., ULRICH,J.,
            FONTECILLA-CAMPS,J.C., GAGNON,J. AND ARLAUD,G.J.
  TITLE     STRUCTURE OF THE CATALYTIC REGION OF HUMAN COMPLEMENT PROTEASE C1S:
            STUDY BY CHEMICAL CROSS-LINKING AND THREE-DIMENSIONAL HOMOLOGY
            MODELING
  JOURNAL   BIOCHEMISTRY 34 (22), 7311-7321 (1995)
  MEDLINE   95298736
  REMARK    PARTIAL SEQUENCE, AND 3D-STRUCTURE MODELING OF CATALYTIC DOMAIN.
REFERENCE   11 (RESIDUES 1 TO 688)
  AUTHORS   DRAGON-DUREY,M.A., QUARTIER,P., FREMEAUX-BACCHI,V., BLOUIN,J., DE
            BARACE,C., PRIEUR,A.M., WEISS,L. AND FRIDMAN,W.H.
  TITLE     MOLECULAR BASIS OF A SELECTIVE C1S DEFICIENCY ASSOCIATED WITH EARLY
            ONSET MULTIPLE AUTOIMMUNE DISEASES
  JOURNAL   J. IMMUNOL. 166 (12), 7612-7616 (2001)
  MEDLINE   21286517
  REMARK    DISEASE.
COMMENT     -------------------------------------------------------------------
            THIS SWISS-PROT ENTRY IS COPYRIGHT. IT IS PRODUCED THROUGH A
            COLLABORATION BETWEEN THE SWISS INSTITUTE OF BIOINFORMATICS AND
            THE EMBL OUTSTATION - THE EUROPEAN BIOINFORMATICS INSTITUTE.
            THE ORIGINAL ENTRY IS AVAILABLE FROM HTTP://WWW.EXPASY.CH/SPROT
            AND HTTP://WWW.EBI.AC.UK/SPROT
            ------------------------------------------------------------------.
            [FUNCTION] C1S B CHAIN IS A SERINE PROTEASE THAT COMBINES WITH C1Q
            AND C1S TO FORM C1, THE FIRST COMPONENT OF THE CLASSICAL PATHWAY OF
            THE COMPLEMENT SYSTEM. C1R ACTIVATES C1S SO THAT IT CAN, IN TURN,
            ACTIVATE C2 AND C4.
            [CATALYTIC ACTIVITY] CLEAVES COMPONENT C4 TO C4A AND C4B (ARG-|-ALA
            BOND), AND COMPONENT C2 TO C2A AND C2B (LYS(OR ARG)-|-LYS BOND).
            [SUBUNIT] C1 IS A CALCIUM-DEPENDENT TRIMOLECULAR COMPLEX OF C1Q, R
            AND S IN THE MOLAR RATION OF 1:2:2. ACTIVATED C1S IS AN
            DISULFIDE-LINKED HETERODIMER OF AN HEAVY CHAIN AND A LIGHT CHAIN.
            [DISEASE] DEFECTS IN C1S ARE THE CAUSE OF SELECTIVE C1S DEFICIENCY,
            THAT IS ASSOCIATED WITH EARLY ONSET MULTIPLE AUTOIMMUNE DISEASES.
            [SIMILARITY] BELONGS TO PEPTIDASE FAMILY S1.
            [SIMILARITY] CONTAINS 2 SUSHI (SCR) DOMAINS.
            [SIMILARITY] CONTAINS 2 CUB DOMAINS.
            [SIMILARITY] CONTAINS 1 EGF-LIKE DOMAIN.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..688
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
     GENE            1..688
                     /GENE="C1S"
     PROTEIN         1..688
                     /GENE="C1S"
                     /PRODUCT="COMPLEMENT C1S COMPONENT PRECURSOR"
                     /EC_NUMBER="3.4.21.42"
     REGION          1..15
                     /GENE="C1S"
                     /REGION_NAME="SIGNAL"
     REGION          16..437
                     /GENE="C1S"
                     /REGION_NAME="MATURE CHAIN"
                     /NOTE="COMPLEMENT C1S HEAVY CHAIN."
     REGION          16..130
                     /GENE="C1S"
                     /REGION_NAME="DOMAIN"
                     /NOTE="CUB 1."
     BOND            BOND(65,83)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     REGION          131..172
                     /GENE="C1S"
                     /REGION_NAME="DOMAIN"
                     /NOTE="EGF-LIKE, CALCIUM-BINDING (POTENTIAL)."
     BOND            BOND(135,147)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     BOND            BOND(143,156)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     SITE            149
                     /GENE="C1S"
                     /SITE_TYPE="HYDROXYLATION"
                     /NOTE="(PROBABLE)."
     BOND            BOND(158,171)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     SITE            174
                     /GENE="C1S"
                     /SITE_TYPE="GLYCOSYLATION"
                     /NOTE="N-LINKED (GLCNAC...)."
     REGION          175..290
                     /GENE="C1S"
                     /REGION_NAME="DOMAIN"
                     /NOTE="CUB 2."
     BOND            BOND(175,202)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     BOND            BOND(234,251)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     REGION          293..355
                     /GENE="C1S"
                     /REGION_NAME="DOMAIN"
                     /NOTE="SUSHI 1."
     BOND            BOND(294,341)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     REGION          294
                     /GENE="C1S"
                     /REGION_NAME="CONFLICT"
                     /NOTE="C -> K (IN REF. 6)."
     BOND            BOND(321,354)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     REGION          358..422
                     /GENE="C1S"
                     /REGION_NAME="DOMAIN"
                     /NOTE="SUSHI 2."
     BOND            BOND(359,403)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     BOND            BOND(386,421)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     SITE            406
                     /GENE="C1S"
                     /SITE_TYPE="GLYCOSYLATION"
                     /NOTE="N-LINKED (GLCNAC...)."
     BOND            BOND(425,549)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
                     /NOTE="INTERCHAIN."
     REGION          438..688
                     /GENE="C1S"
                     /REGION_NAME="MATURE CHAIN"
                     /NOTE="COMPLEMENT C1S LIGHT CHAIN."
     REGION          438..688
                     /GENE="C1S"
                     /REGION_NAME="DOMAIN"
                     /NOTE="SERINE PROTEASE."
     SITE            475
                     /GENE="C1S"
                     /SITE_TYPE="ACTIVE"
                     /NOTE="CHARGE RELAY SYSTEM."
     REGION          513
                     /GENE="C1S"
                     /REGION_NAME="CONFLICT"
                     /NOTE="G -> GG (IN REF. 5)."
     SITE            529
                     /GENE="C1S"
                     /SITE_TYPE="ACTIVE"
                     /NOTE="CHARGE RELAY SYSTEM."
     REGION          573
                     /GENE="C1S"
                     /REGION_NAME="CONFLICT"
                     /NOTE="T -> A (IN REF. 7)."
     BOND            BOND(595,618)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     BOND            BOND(628,659)
                     /GENE="C1S"
                     /BOND_TYPE="DISULFIDE"
     SITE            632
                     /GENE="C1S"
                     /SITE_TYPE="ACTIVE"
                     /NOTE="CHARGE RELAY SYSTEM."
     REGION          645..646
                     /GENE="C1S"
                     /REGION_NAME="CONFLICT"
                     /NOTE="TK -> GR (IN REF. 7)."
ORIGIN      
        1 MWCIVLFSLL AWVYAEPTMY GEILSPNYPQ AYPSEVEKSW DIEVPEGYGI HLYFTHLDIE
       61 LSENCAYDSV QIISGDTEEG RLCGQRSSNN PHSPIVEEFQ VPYNKLQVIF KSDFSNEERF
      121 TGFAAYYVAT DINECTDFVD VPCSHFCNNF IGGYFCSCPP EYFLHDDMKN CGVNCSGDVF
      181 TALIGEIASP NYPKPYPENS RCEYQIRLEK GFQVVVTLRR EDFDVEAADS AGNCLDSLVF
      241 VAGDRQFGPY CGHGFPGPLN IETKSNALDI IFQTDLTGQK KGWKLRYHGD PMPCPKEDTP
      301 NSVWEPAKAK YVFRDVVQIT CLDGFEVVEG RVGATSFYST CQSNGKWSNS KLKCQPVDCG
      361 IPESIENGKV EDPESTLFGS VIRYTCEEPY YYMENGGGGE YHCAGNGSWV NEVLGPELPK
      421 CVPVCGVPRE PFEEKQRIIG GSDADIKNFP WQVFFDNPWA GGALINEYWV LTAAHVVEGN
      481 REPTMYVGST SVQTSRLAKS KMLTPEHVFI HPGWKLLEVP EGRTNFDNDI ALVRLKDPVK
      541 MGPTVSPICL PGTSSDYNLM DGDLGLISGW GRTEKRDRAV RLKAARLPVA PLRKCKEVKV
      601 EKPTADAEAY VFTPNMICAG GEKGMDSCKG DSGGAFAVQD PNDKTKFYAA GLVSWGPQCG
      661 TYGLYTRVKN YVDWIMKTMQ ENSTPRED
//



REVISED: JULY 5, 2002.
 
 


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  SUMMARY ASN.1 FASTA TINYSEQ XML GI LIST GENPEPT GBSEQ XML GRAPHICS XML DEFAULT             
 
 

1: S48134. HLA-CW6 PROTEIN -...[GI:1082453] LINKS  


LOCUS       S48134                   366 AA            LINEAR   PRI 26-APR-1996
DEFINITION  HLA-CW6 PROTEIN - HUMAN.
ACCESSION   S48134
VERSION     S48134  GI:1082453
DBSOURCE    PIR: LOCUS S48134;
            
            SUMMARY: #LENGTH 366 #MOLECULAR-WEIGHT 40968 #CHECKSUM 4175
            ;
            GENETIC: #INTRONS 25/1; 115/1; 207/1; 299/1; 339/1; 350/1
            ;
            SUPERFAMILY: IMMUNOGLOBULIN HOMOLOGY
            ;
            PIR DATES: 14-JUL-1995 #SEQUENCE_REVISION 21-JUL-1995 #TEXT_CHANGE
            26-APR-1996
            .
KEYWORDS    .
SOURCE      HOMO SAPIENS (HUMAN)
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 366)
  AUTHORS   STEINLE,A., NOSSNER,E. AND SCHENDEL,D.J.
  TITLE     ISOLATION AND CHARACTERIZATION OF A GENOMIC HLA-CW6 CLONE
  JOURNAL   TISSUE ANTIGENS 39 (3), 134-137 (1992)
  MEDLINE   92285886
   PUBMED   1598685
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..366
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
     PROTEIN         1..366
                     /PRODUCT="HLA-CW6 PROTEIN"
     REGION          220..285
                     /REGION_NAME="DOMAIN"
                     /NOTE="IMMUNOGLOBULIN HOMOLOGY #LABEL IMM"
ORIGIN      
        1 MRVMAPRTLI LLLSGALALT ETWACSHSMR YFDTAVSRPG RGEPRFISVG YVDDTQFVRF
       61 DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV NLRKLRGYYN QSEDGSHTLQ
      121 WMYGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQW
      181 RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT
      241 WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP
      301 SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES
      361 LIACKA
//



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  SUMMARY ASN.1 FASTA TINYSEQ XML GI LIST GENPEPT GBSEQ XML GRAPHICS XML DEFAULT             
 
 

1: NP_006806. COATED VESICLE ME...[GI:5803149] LINKS  


LOCUS       RNP24                    201 AA            LINEAR   PRI 03-JUN-2002
DEFINITION  COATED VESICLE MEMBRANE PROTEIN [HOMO SAPIENS].
ACCESSION   NP_006806
VERSION     NP_006806.1  GI:5803149
DBSOURCE    REFSEQ: AACCESSION NM_006815.2
KEYWORDS    .
SOURCE      HOMO SAPIENS (HUMAN)
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 201)
  AUTHORS   BLUM,R., FEICK,P., PUYPE,M., VANDEKERCKHOVE,J., KLENGEL,R.,
            NASTAINCZYK,W. AND SCHULZ,I.
  TITLE     TMP21 AND P24A, TWO TYPE I PROTEINS ENRICHED IN PANCREATIC
            MICROSOMAL MEMBRANES, ARE MEMBERS OF A PROTEIN FAMILY INVOLVED IN
            VESICULAR TRAFFICKING
  JOURNAL   J. BIOL. CHEM. 271 (29), 17183-17189 (1996)
  MEDLINE   96291865
   PUBMED   8663407
COMMENT     PROVISIONAL REFSEQ: THIS RECORD HAS NOT YET BEEN SUBJECT TO FINAL
            NCBI REVIEW. THE REFERENCE SEQUENCE WAS DERIVED FROM BC025957.1.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..201
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="12"
                     /MAP="12Q24.31"
                     /CLONE="MGC:39201 IMAGE:5020405"
                     /TISSUE_TYPE="MUSCLE, RHABDOMYOSARCOMA"
                     /CLONE_LIB="NIH_MGC_17"
                     /LAB_HOST="DH10B-R"
                     /NOTE="VECTOR: POTB7"
     PROTEIN         1..201
                     /PRODUCT="COATED VESICLE MEMBRANE PROTEIN"
     REGION          19..201
                     /REGION_NAME="EMP24/GP25L/P24 FAMILY"
                     /NOTE="EMP24_GP25L"
                     /DB_XREF="CDD:PFAM01105"
     CDS             1..201
                     /GENE="RNP24"
                     /CODED_BY="NM_006815.2:24..629"
                     /DB_XREF="LOCUSID:10959"
ORIGIN      
        1 MVTLAELLVL LAALLATVSG YFVSIDAHAE ECFFERVTSG TKMGLIFEVA EGGFLDIDVE
       61 ITGPDNKGIY KGDRESSGKY TFAAHMDGTY KFCFSNRMST MTPKIVMFTI DIGEAPKGQD
      121 METEAHQNKL EEMINELAVA MTAVKHEQEY MEVRERIHRA INDNTNSRVV LWSFFEALVL
      181 VAMTLGQIYY LKRFFEVRRV V
//



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1: NP_006280. TALIN 1 [HOMO SAP...[GI:16753233] LINKS  


LOCUS       TLN1                    2541 AA            LINEAR   PRI 27-AUG-2002
DEFINITION  TALIN 1 [HOMO SAPIENS].
ACCESSION   NP_006280
VERSION     NP_006280.2  GI:16753233
DBSOURCE    REFSEQ: AACCESSION NM_006289.2
KEYWORDS    .
SOURCE      HOMO SAPIENS (HUMAN)
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 2541)
  AUTHORS   LUNA,E.J. AND HITT,A.L.
  TITLE     CYTOSKELETON--PLASMA MEMBRANE INTERACTIONS
  JOURNAL   SCIENCE 258 (5084), 955-964 (1992)
  MEDLINE   93068289
   PUBMED   1439807
REFERENCE   2  (RESIDUES 1 TO 2541)
  AUTHORS   GILMORE,A.P., OHANIAN,V., SPURR,N.K. AND CRITCHLEY,D.R.
  TITLE     LOCALISATION OF THE HUMAN GENE ENCODING THE CYTOSKELETAL PROTEIN
            TALIN TO CHROMOSOME 9P
  JOURNAL   HUM. GENET. 96 (2), 221-224 (1995)
  MEDLINE   95362253
   PUBMED   7635475
REFERENCE   3  (RESIDUES 1 TO 2541)
  AUTHORS   GENINI,M., SCHWALBE,P., SCHOLL,F.A. AND SCHAFER,B.W.
  TITLE     ISOLATION OF GENES DIFFERENTIALLY EXPRESSED IN HUMAN PRIMARY
            MYOBLASTS AND EMBRYONAL RHABDOMYOSARCOMA
  JOURNAL   INT. J. CANCER 66 (4), 571-577 (1996)
  MEDLINE   96213800
   PUBMED   8635876
REFERENCE   4  (RESIDUES 1 TO 2541)
  AUTHORS   BASS,M.D., SMITH,B.J., PRIGENT,S.A. AND CRITCHLEY,D.R.
  TITLE     TALIN CONTAINS THREE SIMILAR VINCULIN-BINDING SITES PREDICTED TO
            FORM AN AMPHIPATHIC HELIX
  JOURNAL   BIOCHEM. J. 341 (PT 2), 257-263 (1999)
  MEDLINE   99321468
   PUBMED   10393080
REFERENCE   5  (RESIDUES 1 TO 2541)
  AUTHORS   BEN-YOSEF,T. AND FRANCOMANO,C.A.
  TITLE     CHARACTERIZATION OF THE HUMAN TALIN (TLN) GENE: GENOMIC STRUCTURE,
            CHROMOSOMAL LOCALIZATION, AND EXPRESSION PATTERN
  JOURNAL   GENOMICS 62 (2), 316-319 (1999)
  MEDLINE   20079169
   PUBMED   10610730
REFERENCE   6  (RESIDUES 1 TO 2541)
  AUTHORS   YAN,B., CALDERWOOD,D.A., YASPAN,B. AND GINSBERG,M.H.
  TITLE     CALPAIN CLEAVAGE PROMOTES TALIN BINDING TO THE BETA 3 INTEGRIN
            CYTOPLASMIC DOMAIN
  JOURNAL   J. BIOL. CHEM. 276 (30), 28164-28170 (2001)
  MEDLINE   21359445
   PUBMED   11382782
COMMENT     REVIEWED REFSEQ: THIS RECORD HAS BEEN CURATED BY NCBI STAFF. THE
            REFERENCE SEQUENCE WAS DERIVED FROM AF177198.1 AND AF113217.1.
            ON NOV 6, 2001 THIS SEQUENCE VERSION REPLACED GI:5454130.
            SUMMARY: THIS GENE ENCODES A CYTOSKELETAL PROTEIN WHICH IS
            CONCENTRATED IN AREAS OF CELL-SUBSTRATUM AND CELL-CELL CONTACTS.
            THIS PROTEIN PLAYS A SIGNIFICANT ROLE IN THE ASSEMBLY OF ACTIN
            FILAMENTS AND IN SPREADING AND MIGRATION OF VARIOUS CELL TYPES,
            INCLUDING FIBROBLASTS AND OSTEOCLASTS. IT CODISTRIBUTES WITH
            INTEGRINS IN THE CELL SURFACE MEMBRANE IN ORDER TO ASSIST IN THE
            ATTACHMENT OF ADHERENT CELLS TO EXTRACELLULAR MATRICES AND OF
            LYMPHOCYTES TO OTHER CELLS. THE N-TERMINUS OF THIS PROTEIN CONTAINS
            ELEMENTS FOR LOCALIZATION TO CELL-EXTRACELLULAR MATRIX JUNCTIONS.
            THE C-TERMINUS CONTAINS BINDING SITES FOR PROTEINS SUCH AS
            BETA-1-INTEGRIN, ACTIN, AND VINCULIN.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..2541
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="9"
                     /MAP="9P13"
     PROTEIN         1..2541
                     /PRODUCT="TALIN 1"
     REGION          82..313
                     /REGION_NAME="SMART00295, B41, BAND 4.1 HOMOLOGUES; ALSO
                     KNOWN AS EZRIN/RADIXIN/MOESIN (ERM) PROTEIN DOMAINS.
                     PRESENT IN MYOSINS, EZRIN, RADIXIN, MOESIN, PROTEIN
                     TYROSINE PHOSPHATASES. PLASMA MEMBRANE-BINDING DOMAIN.
                     THESE PROTEINS PLAY STRUCTURAL AND REGULATORY ROLES IN THE
                     ASSEMBLY AND STABILIZATION OF SPECIALIZED PLASMAMEMBRANE
                     DOMAINS. SOME PDZ DOMAIN CONTAINING PROTEINS BIND ONE OR
                     MORE OF THIS FAMILY. NOW INCLUDES JAKS"
     REGION          121..313
                     /REGION_NAME="PFAM00373, BAND_41, FERM DOMAIN (BAND 4.1
                     FAMILY). THIS DOMAIN HAS BEEN RENAMED THE FERM DOMAIN,
                     WHICH STANDS FOR F FOR 4.1, E FOR EZRIN, R FOR RADIXIN AND
                     M FOR MOESIN"
     REGION          607..759
                     /REGION_NAME="SMART00307, ILWEQ, I/LWEQ DOMAIN; THOUGHT TO
                     POSSESS AN F-ACTIN BINDING FUNCTION"
     REGION          2336..2532
                     /REGION_NAME="SMART00307, ILWEQ, I/LWEQ DOMAIN; THOUGHT TO
                     POSSESS AN F-ACTIN BINDING FUNCTION"
     REGION          2341..2533
                     /REGION_NAME="PFAM01608, I_LWEQ, I/LWEQ DOMAIN. I/LWEQ
                     DOMAINS BIND TO ACTIN. IT HAS BEEN SHOWN THAT THE I/LWEQ
                     DOMAINS FROM MOUSE TALIN AND YEAST SLA2P INTERACT WITH
                     F-ACTIN. I/LWEQ DOMAINS CAN BE PLACED INTO FOUR MAJOR
                     GROUPS BASED ON SEQUENCE SIMILARITY: (1) METAZOAN TALIN;
                     (2) DICTYOSTELIUM TALA/TALB AND SLA110; (3) METAZOAN
                     HIP1P; AND (4) YEAST SLA2P. THE DOMAIN HAS FOUR CONSERVED
                     BLOCKS, THE NAME OF THE DOMAIN IS DERIVED FROM THE INITIAL
                     CONSERVED AMINO ACID OF EACH OF THE FOUR BLOCKS"
     CDS             1..2541
                     /GENE="TLN1"
                     /CODED_BY="NM_006289.2:91..7716"
                     /DB_XREF="LOCUSID:7094"
                     /DB_XREF="MIM:186745"
ORIGIN      
        1 MVALSLKISI GNVVKTMQFE PSTMVYDACR IIRERIPEAP AGPPSDFGLF LSDDDPKKGI
       61 WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI MVDDSKTVTD MLMTICARIG
      121 ITNHDEYSLV RELMEEKKEE ITGTLRKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL
      181 REQGVEEHET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG
      241 FQCQIQFGPH NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK
      301 LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WNLTNIKRWA
      361 ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML
      421 EDSVSPKKST VLQQQYNRVG KVEHGSVALP AIMRSGASGP ENFQVGSMPP AQQQITSGQM
      481 HRGHMPPLTS AQQALTGTIN SSMQAVQAAQ ATLDDFDTLP PLGQDAASKA WRKNKMDESK
      541 HEIHSQVDAI TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED
      601 EGGSGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE LLQQIGESDT
      661 DPHFQDALMQ LAKAVASAAA ALVLKAKSVA QRTEDSGLQT QVIAAATQCA LSTSQLVACT
      721 KVVAPTISSP VCQEQLVEAG RLVAKAVEGC VSASQAATED GQLLRGVGAA ATAVTQALNE
      781 LLQHVKAHAT GAGPAGRYDQ ATDTILTVTE NIFSSMGDAG EMVGQARILA QATSDLVNAI
      841 KADAEGESDL ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA
      901 TNAAAQNAIK KKLVQRLEHA AKQAAASATQ TIAAAQHAAS TPKASAGPQP LLVQSCKAVA
      961 EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM VAAAKASVPT IQDQASAMQL
     1021 SQCAKNLGTA LAELRTAAQK AQEACGPLEM DSALSVVQNL EKDLQEVKAA ARDGKLKPLP
     1081 GETMEKCTQD LGNSTKAVSS AIAQLLGEVA QGNENYAGIA ARDVAGGLRS LAQAARGVAA
     1141 LTSDPAVQAI VLDTASDVLD KASSLIEEAK KAAGHPGDPE SQQRLAQVAK AVTQALNRCV
     1201 SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN QAATELVQAS
     1261 RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ VVSNLKGISM SSSKLLLAAK
     1321 ALSTDPAAPN LKSQLAAAAR AVTDSINQLI TMCTQQAPGQ KECDNALREL ETVRELLENP
     1381 VQPINDMSYF GCLDSVMENS KVLGEAMTGI SQNAKNGNLP EFGDAISTAS KALCGFTEAA
     1441 AQAAYLVGVS DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK
     1501 HTSALCNSCR LASARTTNPT AKRQFVQSAK EVANSTANLV KTIKALDGAF TEENRAQCRA
     1561 ATAPLLEAVD NLSAFASNPE FSSIPAQISP EGRAAMEPIV ISAKTMLESA GGLIQTARAL
     1621 AVNPRDPPSW SVLAGHSRTV SDSIKKLITS MRDKAPGQLE CETAIAALNS CLRDLDQASL
     1681 AAVSQQLAPR EGISQEALHT QMLTAVQEIS HLIEPLANAA RAEASQLGHK VSQMAQYFEP
     1741 LTLAAVGAAS KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV
     1801 QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGEPEGSF VDYQTTMVRT
     1861 AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASEA KPAAVAAENE EIGSHIKHRV
     1921 QELGHGCAAL VTKAGALQCS PSDAYTKKEL IECARRVSEK VSHVLAALQA GNRGTQACIT
     1981 AASAVSGIIA DLDTTIMFAT AGTLNREGTE TFADHREGIL KTAKVLVEDT KVLVQNAAGS
     2041 QEKLAQAAQS SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA
     2101 AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT EHIRQELAVF
     2161 CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED VIATANLSRR AIADMLRACK
     2221 EAAYHPEVAP DVRLRALHYG RECANGYLEL LDHVLLTLQK PSPELKQQLT GHSKRVAGSV
     2281 TELIQAAEAM KGTEWVDPED PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN
     2341 FEEQILEAAK SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV
     2401 AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS EAMKRLQAAG
     2461 NAVKRASDNL VKAAQKAAAF EEQENETVVV KEKMVGGIAQ IIAAQEEMLR KERELEEARK
     2521 KLAQIRQQQY KFLPSELRDE H
//



REVISED: JULY 5, 2002.
 
 


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1: I37519. MHC CLASS I HISTO...[GI:2118706] LINKS  


LOCUS       I37519                   362 AA            LINEAR   PRI 23-JUL-1999
DEFINITION  MHC CLASS I HISTOCOMPATIBILITY ANTIGEN HLA-B45 ALPHA CHAIN
            PRECURSOR - HUMAN.
ACCESSION   I37519
VERSION     I37519  GI:2118706
DBSOURCE    PIR: LOCUS I37519;
            
            SUMMARY: #LENGTH 362 #MOLECULAR-WEIGHT 40414 #CHECKSUM 56
            ;
            GENETIC: #GENE GDB:HLA-B ##CROSS-REFERENCES GDB:120048; OMIM:142830
            #MAP_POSITION 6P21.3-6P21.3
            ;
            SUPERFAMILY: CLASS I HISTOCOMPATIBILITY ANTIGEN; IMMUNOGLOBULIN
            HOMOLOGY
            ;
            PIR DATES: 02-JUL-1996 #SEQUENCE_REVISION 02-JUL-1996 #TEXT_CHANGE
            23-JUL-1999
            .
KEYWORDS    GLYCOPROTEIN; HETERODIMER; TRANSMEMBRANE PROTEIN.
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 362)
  AUTHORS   MADRIGAL,J.A., BELICH,M.P., HILDEBRAND,W.H., BENJAMIN,R.J.,
            LITTLE,A.M., ZEMMOUR,J., ENNIS,P.D., WARD,F.E., PETZL-ERLER,M.L.,
            DU TOIT,E.D. AND PARHAM,P.
  TITLE     DISTINCTIVE HLA-A,B ANTIGENS OF BLACK POPULATIONS FORMED BY
            INTERALLELIC CONVERSION
  JOURNAL   J. IMMUNOL. 149 (10), 3411-3415 (1992)
  MEDLINE   93056508
   PUBMED   1431115
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..362
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
     PROTEIN         1..362
                     /PRODUCT="MHC CLASS I HISTOCOMPATIBILITY ANTIGEN HLA-B45
                     ALPHA CHAIN PRECURSOR"
     REGION          1..24
                     /REGION_NAME="DOMAIN"
                     /NOTE="SIGNAL SEQUENCE"
     SITE            110
                     /SITE_TYPE="BINDING"
                     /NOTE="CARBOHYDRATE (ASN) (COVALENT)"
     REGION          220..285
                     /REGION_NAME="DOMAIN"
                     /NOTE="IMMUNOGLOBULIN HOMOLOGY #LABEL IMM"
ORIGIN      
        1 MRVTAPRTVL LLLSAALALT ETWAGSHSMR YFHTAMSRPG RGEPRFITVG YVDDTLFVRF
       61 DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTWQ
      121 RMYGCDLGPD GRLLRGYNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQD
      181 RAYLEGLCVE SLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT
      241 WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP
      301 SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL
      361 TA
//



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1: NP_062555. METALLOCARBOXYPEP...[GI:9994201] LINKS  


LOCUS       CPX-1                    734 AA            LINEAR   PRI 02-NOV-2000
DEFINITION  METALLOCARBOXYPEPTIDASE CPX-1 [HOMO SAPIENS].
ACCESSION   NP_062555
VERSION     NP_062555.1  GI:9994201
DBSOURCE    REFSEQ: AACCESSION NM_019609.1
KEYWORDS    .
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 734)
  AUTHORS   SMITH,M.
  TITLE     HUMAN DNA SEQUENCE FROM CLONE RP5-860F19 ON CHROMOSOME 20P12.3-13.
            CONTAINS THE GENE FOR A NOVEL PROTEIN SIMILAR TO OLFACTORY NEURONAL
            TRANSCRIPTION FACTORS (COE1, COE2, COE3, EBF3, OLF1), AN RPL19 (60S
            RIBOSOMAL PROTEIN L19) PSEUDOGENE, THE GENE FOR A NOVEL PROTEIN
            (ORTHOLOG OF MOUSE METALLOCARBOXYPEPTIDASE CPX-1) AND A NOVEL GENE.
            CONTAINS ESTS, STSS, GSSS AND FOUR PUTATIVE CPG ISLANDS
  JOURNAL   UNPUBLISHED
COMMENT     PROVISIONAL REFSEQ: THIS RECORD HAS NOT YET BEEN SUBJECT TO FINAL
            NCBI REVIEW. THE REFERENCE SEQUENCE WAS DERIVED FROM AL035460.15.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..734
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="20"
                     /MAP="20P12.3-P13"
                     /CLONE="RP5-860F19"
                     /CLONE_LIB="RPCI-5"
     PROTEIN         1..734
                     /PRODUCT="METALLOCARBOXYPEPTIDASE CPX-1"
     REGION          117..271
                     /REGION_NAME="F5/8 TYPE C DOMAIN"
                     /NOTE="F5_F8_TYPE_C"
                     /DB_XREF="CDD:PFAM00754"
     REGION          299..514
                     /REGION_NAME="ZINC CARBOXYPEPTIDASE"
                     /NOTE="ZN_CARBOPEPT"
                     /DB_XREF="CDD:PFAM00246"
     REGION          460..678
                     /REGION_NAME="ZINC CARBOXYPEPTIDASE"
                     /NOTE="ZN_CARBOPEPT"
                     /DB_XREF="CDD:PFAM00246"
     CDS             1..734
                     /GENE="CPX-1"
                     /CODED_BY="NM_019609.1:1..2205"
                     /NOTE="MATCH: PROTEINS: TR:Q9Z100 TR:Q14113 TR:O54860
                     TR:O97567 TR:Q61281"
                     /DB_XREF="LOCUSID:56265"
ORIGIN      
        1 MWGLLLALAA FAPAVGPALG APRNSVLGLA QPGTTKVPGS TPALHSSPAQ PPAETANGTS
       61 EQHVRIRVIK KKKVIMKKRK KLTLTRPTPL VTAGPLVTPT PAGTLDPAEK QETGCPPLGL
      121 ESLRVSDSRL EASSSQSFGL GPHRGRLNIQ SGLEDGDLYD GAWCAEEQDA DPWFQVDAGH
      181 PTRFSGVITQ GRNSVWRYDW VTSYKVQFSN DSRTWWGSRN HSSGMDAVFP ANSDPETPVL
      241 NLLPEPQVAR FIRLLPQTWL QGGAPCLRAE ILACPVSDPN DLFLEAPASG SSDPLDFQHH
      301 NYKAMRKLMK QVQEQCPNIT RIYSIGKSYQ GLKLYVMEMS DKPGEHELGE PEVRYVAGMH
      361 GNEALGRELL LLLMQFLCHE FLRGNPRVTR LLSEMRIHLL PSMNPDGYEI AYHRGSELVG
      421 WAEGRWNNQS IDLNHNFADL NTPLWEAQDD GKVPHIVPNH HLPLPTYYTL PNATVAPETR
      481 AVIKWMKRIP FVLSANLHGG ELVVSYPFDM TRTPWAAREL TPTPDDAVFR WLSTVYAGSN
      541 LAMQDTSRRP CHSQDFSVHG NIINGADWHT VPGSMNDFSY LHTNCFEVTV ELSCDKFPHE
      601 NELPQEWENN KDALLTYLEQ VRMGIAGVVR DKDTELGIAD AVIAVDGINH DVTTAWGGDY
      661 WRLLTPGDYM VTASAEGYHS VTRNCRVTFE EGPFPCNFVL TKTPKQRLRE LLAAGAKVPP
      721 DLRRRLERLR GQKD
//



REVISED: JULY 5, 2002.
 
 


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1: NP_000590. INSULIN-LIKE GROW...[GI:10834982] LINKS  


LOCUS       IGFBP5                   272 AA            LINEAR   PRI 31-OCT-2000
DEFINITION  INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN 5 [HOMO SAPIENS].
ACCESSION   NP_000590
VERSION     NP_000590.1  GI:10834982
DBSOURCE    REFSEQ: AACCESSION NM_000599.1
KEYWORDS    .
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 272)
  AUTHORS   KIEFER,M.C., IOH,R.S., BAUER,D.M. AND ZAPF,J.
  TITLE     MOLECULAR CLONING OF A NEW HUMAN INSULIN-LIKE GROWTH FACTOR BINDING
            PROTEIN
  JOURNAL   BIOCHEM. BIOPHYS. RES. COMMUN. 176 (1), 219-225 (1991)
  MEDLINE   91207396
   PUBMED   1850258
REFERENCE   2  (RESIDUES 1 TO 272)
  AUTHORS   SHIMASAKI,S., SHIMONAKA,M., ZHANG,H.P. AND LING,N.
  TITLE     IDENTIFICATION OF FIVE DIFFERENT INSULIN-LIKE GROWTH FACTOR BINDING
            PROTEINS (IGFBPS) FROM ADULT RAT SERUM AND MOLECULAR CLONING OF A
            NOVEL IGFBP-5 IN RAT AND HUMAN
  JOURNAL   J. BIOL. CHEM. 266 (16), 10646-10653 (1991)
  MEDLINE   91244847
   PUBMED   1709938
REFERENCE   3  (RESIDUES 1 TO 272)
  AUTHORS   ALLANDER,S.V., LARSSON,C., EHRENBORG,E., SUWANICHKUL,A., WEBER,G.,
            MORRIS,S.L., BAJALICA,S., KIEFER,M.C., LUTHMAN,H. AND POWELL,D.R.
  TITLE     CHARACTERIZATION OF THE CHROMOSOMAL GENE AND PROMOTER FOR HUMAN
            INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN-5
  JOURNAL   J. BIOL. CHEM. 269 (14), 10891-10898 (1994)
  MEDLINE   94193798
   PUBMED   7511611
REFERENCE   4  (RESIDUES 1 TO 272)
  AUTHORS   ANDERSSON,B., WENTLAND,M.A., RICAFRENTE,J.Y., LIU,W. AND GIBBS,R.A.
  TITLE     A 'DOUBLE ADAPTOR' METHOD FOR IMPROVED SHOTGUN LIBRARY CONSTRUCTION
  JOURNAL   ANAL. BIOCHEM. 236 (1), 107-113 (1996)
  MEDLINE   96207227
   PUBMED   8619474
REFERENCE   5  (RESIDUES 1 TO 272)
  AUTHORS   YU,W., ANDERSSON,B., WORLEY,K.C., MUZNY,D.M., DING,Y., LIU,W.,
            RICAFRENTE,J.Y., WENTLAND,M.A., LENNON,G. AND GIBBS,R.A.
  TITLE     LARGE-SCALE CONCATENATION CDNA SEQUENCING
  JOURNAL   GENOME RES. 7 (4), 353-358 (1997)
  MEDLINE   97264341
   PUBMED   9110174
COMMENT     PROVISIONAL REFSEQ: THIS RECORD HAS NOT YET BEEN SUBJECT TO FINAL
            NCBI REVIEW. THE REFERENCE SEQUENCE WAS DERIVED FROM AF055033.1.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..272
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="2"
                     /MAP="2Q33-Q36"
                     /CLONE="IMAGE CONSORTIUM 24645"
                     /SEX="FEMALE"
                     /TISSUE_TYPE="BRAIN"
                     /CLONE_LIB="1NIB"
                     /DEV_STAGE="INFANT"
     PROTEIN         1..272
                     /PRODUCT="INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN 5"
     REGION          25..102
                     /REGION_NAME="INSULIN GROWTH FACTOR-BINDING PROTEIN
                     HOMOLOGUES"
                     /NOTE="IB"
                     /DB_XREF="CDD:IB"
     REGION          27..85
                     /REGION_NAME="INSULIN-LIKE GROWTH FACTOR BINDING PROTEINS"
                     /NOTE="IGFBP"
                     /DB_XREF="CDD:PFAM00219"
     REGION          201..263
                     /REGION_NAME="THYROGLOBULIN TYPE-1 REPEAT"
                     /NOTE="THYROGLOBULIN_1"
                     /DB_XREF="CDD:PFAM00086"
     REGION          216..266
                     /REGION_NAME="THYROGLOBULIN TYPE I REPEATS."
                     /NOTE="TY"
                     /DB_XREF="CDD:TY"
     VARIATION       264
                     /ALLELE="H"
                     /ALLELE="Q"
                     /DB_XREF="DBSNP:3193665"
     CDS             1..272
                     /GENE="IGFBP5"
                     /CODED_BY="NM_000599.1:752..1570"
                     /NOTE="SIMILAR TO HOMO SAPIENS INSULIN-LIKE GROWTH FACTOR
                     BINDING PROTEIN 5 ENCODED BY GENBANK ACCESSION NUMBER
                     L27556"
                     /DB_XREF="LOCUSID:3488"
                     /DB_XREF="MIM:146734"
ORIGIN      
        1 MVLLTAVLLL LAAYAGPAQS LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA
       61 LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE
      121 EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA
      181 PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI
      241 CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE
//



REVISED: JULY 5, 2002.
 
 


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1: NP_004030. ANNEXIN A2; ANNEX...[GI:4757756] LINKS  


LOCUS       ANXA2                    339 AA            LINEAR   PRI 01-NOV-2000
DEFINITION  ANNEXIN A2; ANNEXIN II; LIPOCORTIN II; ANNEXIN II (LIPOCORTIN I);
            CALPACTIN I, HEAVY POLYPEPTIDE (P36); ANNEXIN II (LIPOCORTIN II;
            CALPACTIN I, HEAVY POLYPEPTIDE); ANNEXIN II (LIPOCORTIN II) [HOMO
            SAPIENS].
ACCESSION   NP_004030
VERSION     NP_004030.1  GI:4757756
DBSOURCE    REFSEQ: AACCESSION NM_004039.1
KEYWORDS    .
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 339)
  AUTHORS   HUANG,K.S., WALLNER,B.P., MATTALIANO,R.J., TIZARD,R., BURNE,C.,
            FREY,A., HESSION,C., MCGRAY,P., SINCLAIR,L.K., CHOW,E.P.,
            BROWNING,J.L., RAMACHANDRAN,K.L., TANG,J., SMART,J.E. AND
            PEPINSKY,R.B.
  TITLE     TWO HUMAN 35 KD INHIBITORS OF PHOSPHOLIPASE A2 ARE RELATED TO
            SUBSTRATES OF PP60V-SRC AND OF THE EPIDERMAL GROWTH FACTOR
            RECEPTOR/KINASE
  JOURNAL   CELL 46 (2), 191-199 (1986)
  MEDLINE   86245065
   PUBMED   3013422
REFERENCE   2  (RESIDUES 1 TO 339)
  AUTHORS   HUEBNER,K., CANNIZZARO,L.A., FREY,A.Z., HECHT,B.K., HECHT,F.,
            CROCE,C.M. AND WALLNER,B.P.
  TITLE     CHROMOSOMAL LOCALIZATION OF THE HUMAN GENES FOR LIPOCORTIN I AND
            LIPOCORTIN II
  JOURNAL   ONCOGENE RES. 2 (4), 299-310 (1988)
  MEDLINE   88289023
   PUBMED   2969496
REFERENCE   3  (RESIDUES 1 TO 339)
  AUTHORS   SPANO,F., RAUGEI,G., PALLA,E., COLELLA,C. AND MELLI,M.
  TITLE     CHARACTERIZATION OF THE HUMAN LIPOCORTIN-2-ENCODING MULTIGENE
            FAMILY: ITS STRUCTURE SUGGESTS THE EXISTENCE OF A SHORT AMINO ACID
            UNIT UNDERGOING DUPLICATION
  JOURNAL   GENE 95 (2), 243-251 (1990)
  MEDLINE   91065537
   PUBMED   2174397
REFERENCE   4  (RESIDUES 1 TO 339)
  AUTHORS   RICHARD,I., BROUX,O., CHIANNILKULCHAI,N., FOUGEROUSSE,F.,
            ALLAMAND,V., BOURG,N., BRENGUIER,L., DEVAUD,C., PASTURAUD,P.,
            ROUDAUT,C. ET AL.
  TITLE     REGIONAL LOCALIZATION OF HUMAN CHROMOSOME 15 LOCI
  JOURNAL   GENOMICS 23 (3), 619-627 (1994)
  MEDLINE   95154832
   PUBMED   7851890
REFERENCE   5  (RESIDUES 1 TO 339)
  AUTHORS   TAKAHASHI,S., REDDY,S.V., CHIRGWIN,J.M., DEVLIN,R., HAIPEK,C.,
            ANDERSON,J. AND ROODMAN,G.D.
  TITLE     CLONING AND IDENTIFICATION OF ANNEXIN II AS AN AUTOCRINE/PARACRINE
            FACTOR THAT INCREASES OSTEOCLAST FORMATION AND BONE RESORPTION
  JOURNAL   J. BIOL. CHEM. 269 (46), 28696-28701 (1994)
  MEDLINE   95050673
   PUBMED   7961821
REFERENCE   6  (RESIDUES 1 TO 339)
  AUTHORS   BURGER,A., BERENDES,R., LIEMANN,S., BENZ,J., HOFMANN,A., GOTTIG,P.,
            HUBER,R., GERKE,V., THIEL,C., ROMISCH,J. AND WEBER,K.
  TITLE     THE CRYSTAL STRUCTURE AND ION CHANNEL ACTIVITY OF HUMAN ANNEXIN II,
            A PERIPHERAL MEMBRANE PROTEIN
  JOURNAL   J. MOL. BIOL. 257 (4), 839-847 (1996)
  MEDLINE   96194449
   PUBMED   8636985
COMMENT     REVIEWED REFSEQ: THIS RECORD HAS BEEN CURATED BY NCBI STAFF. THE
            REFERENCE SEQUENCE WAS DERIVED FROM D00017.1.
            SUMMARY: THIS GENE ENCODES A MEMBER OF THE ANNEXIN FAMILY.  MEMBERS
            OF THIS CALCIUM-DEPENDENT PHOSPHOLIPID-BINDING PROTEIN FAMILY PLAY
            A ROLE IN THE REGULATION OF CELLULAR GROWTH AND IN SIGNAL
            TRANSDUCTION PATHWAYS.  THIS PROTEIN FUNCTIONS AS AN AUTOCRINE
            FACTOR WHICH HEIGHTENS OSTEOCLAST FORMATION AND BONE RESORPTION.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..339
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="15"
                     /MAP="15Q21-Q22"
     PROTEIN         1..339
                     /PRODUCT="ANNEXIN A2"
                     /NOTE="ANNEXIN II; LIPOCORTIN II; ANNEXIN II (LIPOCORTIN
                     I); CALPACTIN I, HEAVY POLYPEPTIDE (P36); ANNEXIN II
                     (LIPOCORTIN II; CALPACTIN I, HEAVY POLYPEPTIDE); ANNEXIN
                     II (LIPOCORTIN II)"
     REGION          38..102
                     /REGION_NAME="ANNEXIN"
                     /NOTE="ANNEXIN"
                     /DB_XREF="CDD:PFAM00191"
     REGION          50..102
                     /REGION_NAME="ANNEXIN REPEATS"
                     /NOTE="ANX"
                     /DB_XREF="CDD:ANX"
     REGION          107..174
                     /REGION_NAME="ANNEXIN"
                     /NOTE="ANNEXIN"
                     /DB_XREF="CDD:PFAM00191"
     REGION          122..174
                     /REGION_NAME="ANNEXIN REPEATS"
                     /NOTE="ANX"
                     /DB_XREF="CDD:ANX"
     REGION          192..259
                     /REGION_NAME="ANNEXIN"
                     /NOTE="ANNEXIN"
                     /DB_XREF="CDD:PFAM00191"
     REGION          207..259
                     /REGION_NAME="ANNEXIN REPEATS"
                     /NOTE="ANX"
                     /DB_XREF="CDD:ANX"
     REGION          267..334
                     /REGION_NAME="ANNEXIN"
                     /NOTE="ANNEXIN"
                     /DB_XREF="CDD:PFAM00191"
     REGION          282..334
                     /REGION_NAME="ANNEXIN REPEATS"
                     /NOTE="ANX"
                     /DB_XREF="CDD:ANX"
     CDS             1..339
                     /GENE="ANXA2"
                     /CODED_BY="NM_004039.1:50..1069"
                     /DB_XREF="LOCUSID:302"
                     /DB_XREF="MIM:151740"
ORIGIN      
        1 MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL
       61 TNRSNAQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG
      121 LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA
      181 EDGSVIDYEL IDQDARDLYD AGVKRKGTDV PKWISIMTER SVPHLQKVFD RYKSYSPYDM
      241 LESIRKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM
      301 LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD
//



REVISED: JULY 5, 2002.
 
 


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NCBI | NLM | NIH 

 

OCT 21 2002 11:56:56 

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  SUMMARY ASN.1 FASTA TINYSEQ XML GI LIST GENPEPT GBSEQ XML GRAPHICS XML DEFAULT             
 
 

1: NP_006207. SERINE (OR CYSTEI...[GI:24307907] LINKS  


LOCUS       SERPINE2                 398 AA            LINEAR   PRI 24-OCT-2002
DEFINITION  SERINE (OR CYSTEINE) PROTEINASE INHIBITOR, CLADE E (NEXIN,
            PLASMINOGEN ACTIVATOR INHIBITOR TYPE 1), MEMBER 2; PROTEASE
            INHIBITOR 7 (PROTEASE NEXIN I); GLIA-DERIVED NEXIN [HOMO SAPIENS].
ACCESSION   NP_006207
VERSION     NP_006207.1  GI:24307907
DBSOURCE    REFSEQ: AACCESSION NM_006216.1
KEYWORDS    .
SOURCE      HOMO SAPIENS (HUMAN)
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 398)
  AUTHORS   SOMMER,J., GLOOR,S.M., ROVELLI,G.F., HOFSTEENGE,J., NICK,H.,
            MEIER,R. AND MONARD,D.
  TITLE     CDNA SEQUENCE CODING FOR A RAT GLIA-DERIVED NEXIN AND ITS HOMOLOGY
            TO MEMBERS OF THE SERPIN SUPERFAMILY
  JOURNAL   BIOCHEMISTRY 26 (20), 6407-6410 (1987)
  MEDLINE   88107544
   PUBMED   3427015
REFERENCE   2  (RESIDUES 1 TO 398)
  AUTHORS   CARTER,R.E., CEROSALETTI,K.M., BURKIN,D.J., FOURNIER,R.E.,
            JONES,C., GREENBERG,B.D., CITRON,B.A. AND FESTOFF,B.W.
  TITLE     THE GENE FOR THE SERPIN THROMBIN INHIBITOR (PI7), PROTEASE NEXIN I,
            IS LOCATED ON HUMAN CHROMOSOME 2Q33-Q35 AND ON SYNTENIC REGIONS IN
            THE MOUSE AND SHEEP GENOMES
  JOURNAL   GENOMICS 27 (1), 196-199 (1995)
  MEDLINE   95394459
   PUBMED   7665170
COMMENT     PROVISIONAL REFSEQ: THIS RECORD HAS NOT YET BEEN SUBJECT TO FINAL
            NCBI REVIEW. THE REFERENCE SEQUENCE WAS DERIVED FROM BC015663.1.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..398
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="2"
                     /MAP="2Q33-Q35"
                     /CLONE="MGC:23129 IMAGE:4578406"
                     /TISSUE_TYPE="SKIN, MELANOTIC MELANOMA."
                     /CLONE_LIB="NIH_MGC_20"
                     /LAB_HOST="DH10B-R"
                     /NOTE="VECTOR: POTB7"
     PROTEIN         1..398
                     /PRODUCT="SERINE (OR CYSTEINE) PROTEINASE INHIBITOR, CLADE
                     E (NEXIN, PLASMINOGEN ACTIVATOR INHIBITOR TYPE 1), MEMBER
                     2"
                     /NOTE="PROTEASE INHIBITOR 7 (PROTEASE NEXIN I);
                     GLIA-DERIVED NEXIN"
     REGION          20..398
                     /REGION_NAME="SERPIN (SERINE PROTEASE INHIBITOR).
                     STRUCTURE IS A MULTI-DOMAIN FOLD CONTAINING A BUNDLE OF
                     HELICES AND A BETA SANDWICH"
                     /NOTE="SERPIN"
                     /DB_XREF="CDD:PFAM00079"
     REGION          36..398
                     /REGION_NAME="SERINE PROTEINASE INHIBITORS"
                     /NOTE="SERPIN"
                     /DB_XREF="CDD:SMART00093"
     CDS             1..398
                     /GENE="SERPINE2"
                     /CODED_BY="NM_006216.1:210..1406"
                     /DB_XREF="LOCUSID:5270"
                     /DB_XREF="MIM:177010"
ORIGIN      
        1 MNWHLPLFLL ASVTLPSICS HFNPLSLEEL GSNTGIQVFN QIVKSRPHDN IVISPHGIAS
       61 VLGMLQLGAD GRTKKQLAMV MRYGVNGVGK ILKKINKAIV SKKNKDIVTV ANAVFVKNAS
      121 EIEVPFVTRN KDVFQCEVRN VNFEDPASAC DSINAWVKNE TRDMIDNLLS PDLIDGVLTR
      181 LVLVNAVYFK GLWKSRFQPE NTKKRTFVAA DGKSYQVPML AQLSVFRCGS TSAPNDLWYN
      241 FIELPYHGES ISMLIALPTE SSTPLSAIIP HISTKTIDSW MSIMVPKRVQ VILPKFTAVA
      301 QTDLKEPLKV LGITDMFDSS KANFAKITTG SENLHVSHIL QKAKIEVSED GTKASAATTA
      361 ILIARSSPPW FIVDRPFLFF IRHNPTGAVL FMGQINKP
//



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1: NP_003726. PROTOCADHERIN GAM...[GI:8850232] LINKS  


LOCUS       PCDHGA12                 932 AA            LINEAR   PRI 25-MAY-2001
DEFINITION  PROTOCADHERIN GAMMA SUBFAMILY A, 12, ISOFORM 1 PRECURSOR; CADHERIN
            21; FIBROBLAST CADHERIN FIB3 [HOMO SAPIENS].
ACCESSION   NP_003726
VERSION     NP_003726.1  GI:8850232
DBSOURCE    REFSEQ: AACCESSION NM_003735.2
KEYWORDS    .
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 932)
  AUTHORS   MATSUYOSHI,N. AND IMAMURA,S.
  TITLE     MULTIPLE CADHERINS ARE EXPRESSED IN HUMAN FIBROBLASTS
  JOURNAL   BIOCHEM. BIOPHYS. RES. COMMUN. 235 (2), 355-358 (1997)
  MEDLINE   97342499
   PUBMED   9199196
REFERENCE   2  (RESIDUES 1 TO 932)
  AUTHORS   WU,Q. AND MANIATIS,T.
  TITLE     A STRIKING ORGANIZATION OF A LARGE FAMILY OF HUMAN NEURAL
            CADHERIN-LIKE CELL ADHESION GENES
  JOURNAL   CELL 97 (6), 779-790 (1999)
  MEDLINE   99308636
   PUBMED   10380929
REFERENCE   3  (RESIDUES 1 TO 932)
  AUTHORS   WU,Q. AND MANIATIS,T.
  TITLE     LARGE EXONS ENCODING MULTIPLE ECTODOMAINS ARE A CHARACTERISTIC
            FEATURE OF PROTOCADHERIN GENES
  JOURNAL   PROC. NATL. ACAD. SCI. U.S.A. 97 (7), 3124-3129 (2000)
  MEDLINE   20202599
   PUBMED   10716726
REFERENCE   4  (RESIDUES 1 TO 932)
  AUTHORS   YAGI,T. AND TAKEICHI,M.
  TITLE     CADHERIN SUPERFAMILY GENES: FUNCTIONS, GENOMIC ORGANIZATION, AND
            NEUROLOGIC DIVERSITY
  JOURNAL   GENES DEV. 14 (10), 1169-1180 (2000)
  MEDLINE   20278059
   PUBMED   10817752
REFERENCE   5  (RESIDUES 1 TO 932)
  AUTHORS   NOLLET,F., KOOLS,P. AND VAN ROY,F.
  TITLE     PHYLOGENETIC ANALYSIS OF THE CADHERIN SUPERFAMILY ALLOWS
            IDENTIFICATION OF SIX MAJOR SUBFAMILIES BESIDES SEVERAL SOLITARY
            MEMBERS
  JOURNAL   J. MOL. BIOL. 299 (3), 551-572 (2000)
  MEDLINE   20296790
   PUBMED   10835267
REFERENCE   6  (RESIDUES 1 TO 932)
  AUTHORS   WU,Q., ZHANG,T., CHENG,J.F., KIM,Y., GRIMWOOD,J., SCHMUTZ,J.,
            DICKSON,M., NOONAN,J.P., ZHANG,M.Q., MYERS,R.M. AND MANIATIS,T.
  TITLE     COMPARATIVE DNA SEQUENCE ANALYSIS OF MOUSE AND HUMAN PROTOCADHERIN
            GENE CLUSTERS
  JOURNAL   GENOME RES. 11 (3), 389-404 (2001)
  MEDLINE   21154914
   PUBMED   11230163
COMMENT     REVIEWED REFSEQ: THIS RECORD HAS BEEN CURATED BY NCBI STAFF. THE
            REFERENCE SEQUENCE WAS DERIVED FROM AF152321.1, AL589367.1 AND
            AB011160.1.
            SUMMARY: THIS GENE IS A MEMBER OF THE PROTOCADHERIN GAMMA GENE
            CLUSTER, ONE OF THREE RELATED CLUSTERS TANDEMLY LINKED ON
            CHROMOSOME FIVE. THESE GENE CLUSTERS HAVE AN IMMUNOGLOBULIN-LIKE
            ORGANIZATION, SUGGESTING THAT A NOVEL MECHANISM MAY BE INVOLVED IN
            THEIR REGULATION AND EXPRESSION. THE GAMMA GENE CLUSTER INCLUDES 22
            GENES DIVIDED INTO 3 SUBFAMILIES. SUBFAMILY A CONTAINS 12 GENES,
            SUBFAMILY B CONTAINS 7 GENES AND 2 PSEUDOGENES, AND THE MORE
            DISTANTLY RELATED SUBFAMILY C CONTAINS 3 GENES. THE TANDEM ARRAY OF
            22 LARGE, VARIABLE REGION EXONS ARE FOLLOWED BY A CONSTANT REGION,
            CONTAINING 3 EXONS SHARED BY ALL GENES IN THE CLUSTER. EACH
            VARIABLE REGION EXON ENCODES THE EXTRACELLULAR REGION, WHICH
            INCLUDES 6 CADHERIN ECTODOMAINS AND A TRANSMEMBRANE REGION. THE
            CONSTANT REGION EXONS ENCODE THE COMMON CYTOPLASMIC REGION. THESE
            NEURAL CADHERIN-LIKE CELL ADHESION PROTEINS MOST LIKELY PLAY A
            CRITICAL ROLE IN THE ESTABLISHMENT AND FUNCTION OF SPECIFIC
            CELL-CELL CONNECTIONS IN THE BRAIN. ALTERNATIVE SPLICING HAS BEEN
            DESCRIBED FOR THE GAMMA CLUSTER GENES.
            TRANSCRIPT VARIANT: THIS VARIANT (1) INCLUDES THE CONSTANT REGION
            EXONS AND ENCODES THE LONGEST ISOFORM (1).
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..932
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /CHROMOSOME="5"
                     /MAP="5Q31"
     PROTEIN         1..932
                     /PRODUCT="PROTOCADHERIN GAMMA SUBFAMILY A, 12, ISOFORM 1
                     PRECURSOR"
                     /NOTE="CADHERIN 21; FIBROBLAST CADHERIN FIB3"
     SIG_PEPTIDE     1..29
     MAT_PEPTIDE     30..932
                     /PRODUCT="PROTOCADHERIN GAMMA SUBFAMILY A, 12, ISOFORM 1"
     REGION          65..131
                     /REGION_NAME="CADHERIN REPEATS."
                     /NOTE="CA"
                     /DB_XREF="CDD:CA"
     REGION          142..233
                     /REGION_NAME="CADHERIN DOMAIN"
                     /NOTE="CADHERIN"
                     /DB_XREF="CDD:PFAM00028"
     REGION          157..240
                     /REGION_NAME="CADHERIN REPEATS."
                     /NOTE="CA"
                     /DB_XREF="CDD:CA"
     REGION          247..338
                     /REGION_NAME="CADHERIN DOMAIN"
                     /NOTE="CADHERIN"
                     /DB_XREF="CDD:PFAM00028"
     REGION          264..345
                     /REGION_NAME="CADHERIN REPEATS."
                     /NOTE="CA"
                     /DB_XREF="CDD:CA"
     REGION          355..442
                     /REGION_NAME="CADHERIN DOMAIN"
                     /NOTE="CADHERIN"
                     /DB_XREF="CDD:PFAM00028"
     REGION          369..450
                     /REGION_NAME="CADHERIN REPEATS."
                     /NOTE="CA"
                     /DB_XREF="CDD:CA"
     REGION          457..541
                     /REGION_NAME="CADHERIN DOMAIN"
                     /NOTE="CADHERIN"
                     /DB_XREF="CDD:PFAM00028"
     REGION          474..560
                     /REGION_NAME="CADHERIN REPEATS."
                     /NOTE="CA"
                     /DB_XREF="CDD:CA"
     REGION          579..664
                     /REGION_NAME="CADHERIN DOMAIN"
                     /NOTE="CADHERIN"
                     /DB_XREF="CDD:PFAM00028"
     REGION          591..666
                     /REGION_NAME="CADHERIN REPEATS."
                     /NOTE="CA"
                     /DB_XREF="CDD:CA"
     CDS             1..932
                     /GENE="PCDHGA12"
                     /CODED_BY="NM_003735.2:170..2968"
                     /NOTE="ISOFORM 1 IS ENCODED BY TRANSCRIPT VARIANT 1"
                     /DB_XREF="LOCUSID:26025"
                     /DB_XREF="MIM:603059"
                     /DB_XREF="LOCUSID:26025"
                     /DB_XREF="MIM:603059"
ORIGIN      
        1 MIPARLHRDY KGLVLLGILL GTLWETGCTQ IRYSVPEELE KGSRVGDISR DLGLEPRELA
       61 ERGVRIIPRG RTQLFALNPR SGSLVTAGRI DREELCMGAI KCQLNLDILM EDKVKIYGVE
      121 VEVRDINDNA PYFRESELEI KISENAATEM RFPLPHAWDP DIGKNSLQSY ELSPNTHFSL
      181 IVQNGADGSK YPELVLKRAL DREEKAAHHL VLTASDGGDP VRTGTARIRV MVLDANDNAP
      241 AFAQPEYRAS VPENLALGTQ LLVVNATDPD EGVNAEVRYS FRYVDDKAAQ VFKLDCNSGT
      301 ISTIGELDHE ESGFYQMEVQ AMDNAGYSAR AKVLITVLDV NDNAPEVVLT SLASSVPENS
      361 PRGTLIALLN VNDQDSEENG QVICFIQGNL PFKLEKSYGN YYSLVTDIVL DREQVPSYNI
      421 TVTATDRGTP PLSTETHISL NVADTNDNPP VFPQASYSAY IPENNPRGVS LVSVTAHDPD
      481 CEENAQITYS LAENTIQGAS LSSYVSINSD TGVLYALSSF DYEQFRDLQV KVMARDNGHP
      541 PLSSNVSLSL FVLDQNDNAP EILYPALPTD GSTGVELAPR SAEPGYLVTK VVAVDRDSGQ
      601 NAWLSYRLLK ASEPGLFSVG LHTGEVRTAR ALLDRDALKQ SLVVAVQDHG QPPLSATVTL
      661 TVAVADSIPQ VLADLGSLES PANSETSDLT LYLVVAVAAV SCVFLAFVIL LLALRLRRWH
      721 KSRLLQASGG GLTGAPASHF VGVDGVQAFL QTYSHEVSLT TDSRKSHLIF PQPNYADMLV
      781 SQESFEKSEP LLLSGDSVFS KDSHGLIEQA PPNTDWRFSQ AQRPGTSGSQ NGDDTGTWPN
      841 NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS
      901 NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK
//



REVISED: JULY 5, 2002.
 
 


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1: NP_057325[GI:7705903]  


LOCUS       LOC51169                 261 AA            LINEAR   PRI 02-NOV-2000
DEFINITION  ENDOMUCIN-1 [HOMO SAPIENS].
ACCESSION   NP_057325
VERSION     NP_057325.1  GI:7705903
DBSOURCE    REFSEQ: AACCESSION NM_016241.1
KEYWORDS    .
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 261)
  AUTHORS   KINOSHITA,M., HONJO,T. AND NODA,M.
  TITLE     HUMAN ENDOMUCIN-1
  JOURNAL   PUBLISHED ONLY IN DATABASE (1999)
COMMENT     PROVISIONAL REFSEQ: THIS RECORD HAS NOT YET BEEN SUBJECT TO FINAL
            NCBI REVIEW. THE REFERENCE SEQUENCE WAS DERIVED FROM AB034694.1.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..261
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
                     /TISSUE_TYPE="VASCULAR ENDOTHELIUM"
                     /DEV_STAGE="NEONATE"
     PROTEIN         1..261
                     /PRODUCT="ENDOMUCIN-1"
     CDS             1..261
                     /GENE="LOC51169"
                     /CODED_BY="NM_016241.1:168..953"
                     /DB_XREF="LOCUSID:51169"
ORIGIN      
        1 MRLLQATVLF FLLSNSLCHS EDGKDVQNDS IPTPAETSTT KASVTIPGIV SVTNPNKPAD
       61 GTPPEGTTKS DVSQTSLVTT INSLTTPKHE VGTTTEGPLR NESSTMKITV PNTPTSNANS
      121 TLPGSQNKTE NQSSIRTTEI SVTTQLLDAL PKITATSSAS LTTAHTMSLL QDTEDRKIAT
      181 TPSTTPSYSS IILPVVIALV VITLLVFTLV GLYRICWKRD PGTPENGNDQ PQSDKESVKL
      241 LTVKTISHES GEHSAQGKTK N
//



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1: S48134. HLA-CW6 PROTEIN -...[GI:1082453] LINKS  


LOCUS       S48134                   366 AA            LINEAR   PRI 26-APR-1996
DEFINITION  HLA-CW6 PROTEIN - HUMAN.
ACCESSION   S48134
VERSION     S48134  GI:1082453
DBSOURCE    PIR: LOCUS S48134;
            
            SUMMARY: #LENGTH 366 #MOLECULAR-WEIGHT 40968 #CHECKSUM 4175
            ;
            GENETIC: #INTRONS 25/1; 115/1; 207/1; 299/1; 339/1; 350/1
            ;
            SUPERFAMILY: IMMUNOGLOBULIN HOMOLOGY
            ;
            PIR DATES: 14-JUL-1995 #SEQUENCE_REVISION 21-JUL-1995 #TEXT_CHANGE
            26-APR-1996
            .
KEYWORDS    .
SOURCE      HOMO SAPIENS (HUMAN)
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 366)
  AUTHORS   STEINLE,A., NOSSNER,E. AND SCHENDEL,D.J.
  TITLE     ISOLATION AND CHARACTERIZATION OF A GENOMIC HLA-CW6 CLONE
  JOURNAL   TISSUE ANTIGENS 39 (3), 134-137 (1992)
  MEDLINE   92285886
   PUBMED   1598685
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..366
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
     PROTEIN         1..366
                     /PRODUCT="HLA-CW6 PROTEIN"
     REGION          220..285
                     /REGION_NAME="DOMAIN"
                     /NOTE="IMMUNOGLOBULIN HOMOLOGY #LABEL IMM"
ORIGIN      
        1 MRVMAPRTLI LLLSGALALT ETWACSHSMR YFDTAVSRPG RGEPRFISVG YVDDTQFVRF
       61 DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV NLRKLRGYYN QSEDGSHTLQ
      121 WMYGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQW
      181 RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT
      241 WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP
      301 SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES
      361 LIACKA
//



REVISED: JULY 5, 2002.
 
 


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1: P18462. HLA CLASS I HISTO...[GI:122158] LINKS  


LOCUS       1A25_HUMAN               365 AA            LINEAR   PRI 16-OCT-2001
DEFINITION  HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-25(A-10) ALPHA CHAIN
            PRECURSOR.
ACCESSION   P18462
VERSION     P18462  GI:122158
DBSOURCE    SWISSPROT: LOCUS 1A25_HUMAN, ACCESSION P18462;
            CLASS: STANDARD.
            EXTRA ACCESSIONS:Q95362,CREATED: NOV 1, 1990.
            SEQUENCE UPDATED: NOV 1, 1990.
            ANNOTATION UPDATED: OCT 16, 2001.
            XREFS: GI: 187794, GI: 307225, GI: 1526975, GI: 1526976, GI: 107001
            XREFS (NON-SEQUENCE DATABASES): HSSPQ95352, MIM 142800,
            INTERPROIPR003006, INTERPROIPR003597, INTERPROIPR001039,
            PFAMPF00047, PFAMPF00129, PRODOMPD000050, SMARTSM00407,
            PROSITEPS00290
KEYWORDS    MHC I; TRANSMEMBRANE; GLYCOPROTEIN; SIGNAL; POLYMORPHISM.
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 365)
  AUTHORS   ENNIS,P.D., ZEMMOUR,J., SALTER,R.D. AND PARHAM,P.
  TITLE     RAPID CLONING OF HLA-A,B CDNA BY USING THE POLYMERASE CHAIN
            REACTION: FREQUENCY AND NATURE OF ERRORS PRODUCED IN AMPLIFICATION
  JOURNAL   PROC. NATL. ACAD. SCI. U.S.A. 87 (7), 2833-2837 (1990)
  MEDLINE   90207291
   PUBMED   2320591
  REMARK    SEQUENCE FROM N.A. (A*2501).
REFERENCE   2  (RESIDUES 1 TO 365)
  AUTHORS   KRAUSA,P., YOUNG,D.M. AND GOTCH,F.
  TITLE     IDENTIFICATION OF A NEW HLA-A ALLELE (A*2502) BY PCR-SSP
  JOURNAL   IMMUNOGENETICS 45 (1), 84-85 (1996)
  MEDLINE   97045042
   PUBMED   8881046
  REMARK    SEQUENCE FROM N.A. (A*2502).
            TISSUE=HEMATOPOIETIC
COMMENT     -------------------------------------------------------------------
            THIS SWISS-PROT ENTRY IS COPYRIGHT. IT IS PRODUCED THROUGH A
            COLLABORATION BETWEEN THE SWISS INSTITUTE OF BIOINFORMATICS AND
            THE EMBL OUTSTATION - THE EUROPEAN BIOINFORMATICS INSTITUTE.
            THE ORIGINAL ENTRY IS AVAILABLE FROM HTTP://WWW.EXPASY.CH/SPROT
            AND HTTP://WWW.EBI.AC.UK/SPROT
            ------------------------------------------------------------------.
            [FUNCTION] INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO THE
            IMMUNE SYSTEM.
            [SUBUNIT] DIMER OF ALPHA CHAIN AND A BETA CHAIN
            (BETA-2-MICROGLOBULIN).
            [POLYMORPHISM] THE FOLLOWING ALLELES OF A-25 ARE KNOWN: A*2501 AND
            A*2502. THE SEQUENCE SHOWN IS THAT OF A*2501.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..365
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
     GENE            1..365
                     /GENE="HLA-A"
                     /NOTE="HLAA"
     PROTEIN         1..365
                     /GENE="HLA-A"
                     /PRODUCT="HLA CLASS I HISTOCOMPATIBILITY ANTIGEN,
                     A-25(A-10) ALPHA CHAIN PRECURSOR"
     REGION          1..24
                     /GENE="HLA-A"
                     /REGION_NAME="SIGNAL"
     REGION          25..365
                     /GENE="HLA-A"
                     /REGION_NAME="MATURE CHAIN"
                     /NOTE="HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-25(A-10)
                     ALPHA CHAIN."
     REGION          25..114
                     /GENE="HLA-A"
                     /REGION_NAME="DOMAIN"
                     /NOTE="EXTRACELLULAR ALPHA-1."
     REGION          94
                     /GENE="HLA-A"
                     /REGION_NAME="VARIANT"
                     /NOTE="H -> Q (IN A*2502). /FTID=VAR_004361."
     SITE            110
                     /GENE="HLA-A"
                     /SITE_TYPE="GLYCOSYLATION"
                     /NOTE="N-LINKED (GLCNAC...) (BY SIMILARITY)."
     REGION          115..206
                     /GENE="HLA-A"
                     /REGION_NAME="DOMAIN"
                     /NOTE="EXTRACELLULAR ALPHA-2."
     BOND            BOND(125,188)
                     /GENE="HLA-A"
                     /BOND_TYPE="DISULFIDE"
                     /NOTE="BY SIMILARITY."
     REGION          207..298
                     /GENE="HLA-A"
                     /REGION_NAME="DOMAIN"
                     /NOTE="EXTRACELLULAR ALPHA-3."
     BOND            BOND(227,283)
                     /GENE="HLA-A"
                     /BOND_TYPE="DISULFIDE"
                     /NOTE="BY SIMILARITY."
     REGION          299..308
                     /GENE="HLA-A"
                     /REGION_NAME="DOMAIN"
                     /NOTE="CONNECTING PEPTIDE."
     REGION          309..332
                     /GENE="HLA-A"
                     /REGION_NAME="TRANSMEMBRANE REGION"
     REGION          333..365
                     /GENE="HLA-A"
                     /REGION_NAME="DOMAIN"
                     /NOTE="CYTOPLASMIC TAIL."
ORIGIN      
        1 MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF
       61 DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAHSQTDRE SLRIALRYYN QSEDGSHTIQ
      121 RMYGCDVGPD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WETAHEAEQW
      181 RAYLEGRCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT
      241 WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP
      301 SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDMSL
      361 TACKV
//



REVISED: JULY 5, 2002.
 
 


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1: P01591. IMMUNOGLOBULIN J ...[GI:400044] LINKS  


LOCUS       IGJ_HUMAN                137 AA            LINEAR   PRI 16-OCT-2001
DEFINITION  IMMUNOGLOBULIN J CHAIN.
ACCESSION   P01591
VERSION     P01591  GI:400044
DBSOURCE    SWISSPROT: LOCUS IGJ_HUMAN, ACCESSION P01591;
            CLASS: STANDARD.
            CREATED: JUL 21, 1986.
            SEQUENCE UPDATED: JUL 1, 1993.
            ANNOTATION UPDATED: OCT 16, 2001.
            XREFS: GI: 532596, GI: 532598, GI: 185792, GI: 69716
            XREFS (NON-SEQUENCE DATABASES): GLYCOSUITEDBP01591,
            SWISS-2DPAGEP01591, SIENA-2DPAGEP01591, MIM 147790
KEYWORDS    GLYCOPROTEIN.
SOURCE      HOMO SAPIENS
  ORGANISM  HOMO SAPIENS
            EUKARYOTA; METAZOA; CHORDATA; CRANIATA; VERTEBRATA; EUTELEOSTOMI;
            MAMMALIA; EUTHERIA; PRIMATES; CATARRHINI; HOMINIDAE; HOMO.
REFERENCE   1  (RESIDUES 1 TO 137)
  AUTHORS   MAX,E.E. AND KORSMEYER,S.J.
  TITLE     HUMAN J CHAIN GENE. STRUCTURE AND EXPRESSION IN B LYMPHOID CELLS
  JOURNAL   J. EXP. MED. 161 (4), 832-849 (1985)
  MEDLINE   85159425
   PUBMED   2984306
  REMARK    SEQUENCE FROM N.A.
REFERENCE   2  (RESIDUES 1 TO 137)
  AUTHORS   MOLE,J.E., BHOWN,A.S. AND BENNETT,J.C.
  TITLE     PRIMARY STRUCTURE OF HUMAN J CHAIN: ALIGNMENT OF PEPTIDES FROM
            CHEMICAL AND ENZYMATIC HYDROLYSES
  JOURNAL   BIOCHEMISTRY 16 (16), 3507-3513 (1977)
  MEDLINE   77242318
   PUBMED   407930
  REMARK    PRELIMINARY SEQUENCE.
REFERENCE   3  (RESIDUES 1 TO 137)
  AUTHORS   FRUTIGER,S., HUGHES,G.J., PAQUET,N., LUTHY,R. AND JATON,J.C.
  TITLE     DISULFIDE BOND ASSIGNMENT IN HUMAN J CHAIN AND ITS COVALENT PAIRING
            WITH IMMUNOGLOBULIN M
  JOURNAL   BIOCHEMISTRY 31 (50), 12643-12647 (1992)
  MEDLINE   93112606
   PUBMED   1472500
  REMARK    DISULFIDE BONDS, AND PARTIAL SEQUENCE.
COMMENT     ON SEP 14, 1993 THIS SEQUENCE VERSION REPLACED GI:124269.
            -------------------------------------------------------------------
            THIS SWISS-PROT ENTRY IS COPYRIGHT. IT IS PRODUCED THROUGH A
            COLLABORATION BETWEEN THE SWISS INSTITUTE OF BIOINFORMATICS AND
            THE EMBL OUTSTATION - THE EUROPEAN BIOINFORMATICS INSTITUTE.
            THE ORIGINAL ENTRY IS AVAILABLE FROM HTTP://WWW.EXPASY.CH/SPROT
            AND HTTP://WWW.EBI.AC.UK/SPROT
            ------------------------------------------------------------------.
            [FUNCTION] SERVES TO LINK TWO MONOMER UNITS OF EITHER IGM OR IGA.
            IN THE CASE OF IGM, THE J CHAIN-JOINED DIMER IS A NUCLEATING UNIT
            FOR THE IGM PENTAMER, AND IN THE CASE OF IGA IT INDUCES LARGER
            POLYMERS. IT ALSO HELP TO BIND THESE IMMUNOGLOBULINS TO SECRETORY
            COMPONENT.
FEATURES             LOCATION/QUALIFIERS
     SOURCE          1..137
                     /ORGANISM="HOMO SAPIENS"
                     /DB_XREF="TAXON:9606"
     GENE            1..137
                     /GENE="IGJ"
                     /NOTE="IGCJ"
     PROTEIN         1..137
                     /GENE="IGJ"
                     /PRODUCT="IMMUNOGLOBULIN J CHAIN"
     SITE            1
                     /GENE="IGJ"
                     /SITE_TYPE="PYRROLIDONE-CARBOXYLIC-ACID"
     BOND            BOND(13,101)
                     /GENE="IGJ"
                     /BOND_TYPE="DISULFIDE"
     BOND            BOND(15)
                     /GENE="IGJ"
                     /BOND_TYPE="DISULFIDE"
                     /NOTE="INTERCHAIN (WITH IG HEAVY CHAIN)."
     SITE            49
                     /GENE="IGJ"
                     /SITE_TYPE="GLYCOSYLATION"
                     /NOTE="N-LINKED (GLCNAC...). /FTID=CAR_000167."
     BOND            BOND(69)
                     /GENE="IGJ"
                     /BOND_TYPE="DISULFIDE"
                     /NOTE="INTERCHAIN (WITH IG HEAVY CHAIN)."
     BOND            BOND(72,92)
                     /GENE="IGJ"
                     /BOND_TYPE="DISULFIDE"
     BOND            BOND(109,134)
                     /GENE="IGJ"
                     /BOND_TYPE="DISULFIDE"
ORIGIN      
        1 QEDERIVLVD NKCKCARITS RIIRSSEDPN EDIVERNIRI IVPLNNRENI SDPTSPLRTR
       61 FVYHLSDLCK KCDPTEVELD NQIVTATQSN ICDEDSATET CYTYDRNKCY TAVVPLVYGG
      121 ETKMVETALT PDACYPD
//



REVISED: JULY 5, 2002.
 
 


DISCLAIMER | WRITE TO THE HELP DESK
NCBI | NLM | NIH 

 

OCT 21 2002 11:56:56 

BLINKBLINKRELATED SEQUENCESRELATED SEQUENCESPUBMEDPUBMEDTAXONOMYTAXONOMYLINKOUTLINKOUTHELPHELP  


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