                         SEQUENCE LISTING

<110>  Albert-Ludwigs-Univ. Freiburg
 
<120>  Modified Cas9 System having a dominant negative effector on 
       non-homologous end-joining  fused thereto and its use for 
       improved gene editing

<130>  POW000352ALB

<150>  EP20194524.3
<151>  2020-09-04

<160>  2     

<170>  PatentIn version 3.5

<210>  1
<211>  498
<212>  PRT
<213>  artificial sequence

<220>
<223>  dn53BP1

<400>  1

Gly Glu Glu Glu Phe Asp Met Pro Gln Pro Pro His Gly His Val Leu 
1               5                   10                  15      


His Arg His Met Arg Thr Ile Arg Glu Val Arg Thr Leu Val Thr Arg 
            20                  25                  30          


Val Ile Thr Asp Val Tyr Tyr Val Asp Gly Thr Glu Val Glu Arg Lys 
        35                  40                  45              


Val Thr Glu Glu Thr Glu Glu Pro Ile Val Glu Cys Gln Glu Cys Glu 
    50                  55                  60                  


Thr Glu Val Ser Pro Ser Gln Thr Gly Gly Ser Ser Gly Asp Leu Gly 
65                  70                  75                  80  


Asp Ile Ser Ser Phe Ser Ser Lys Ala Ser Ser Leu His Arg Thr Ser 
                85                  90                  95      


Ser Gly Thr Ser Leu Ser Ala Met His Ser Ser Gly Ser Ser Gly Lys 
            100                 105                 110         


Gly Ala Gly Pro Leu Arg Gly Lys Thr Ser Gly Thr Glu Pro Ala Asp 
        115                 120                 125             


Phe Ala Leu Pro Ser Ser Arg Gly Gly Pro Gly Lys Leu Ser Pro Arg 
    130                 135                 140                 


Lys Gly Val Ser Gln Thr Gly Thr Pro Val Cys Glu Glu Asp Gly Asp 
145                 150                 155                 160 


Ala Gly Leu Gly Ile Arg Gln Gly Gly Lys Ala Pro Val Thr Pro Arg 
                165                 170                 175     


Gly Arg Gly Arg Arg Gly Arg Pro Pro Ser Arg Thr Thr Gly Thr Arg 
            180                 185                 190         


Glu Thr Ala Val Pro Gly Pro Leu Gly Ile Glu Asp Ile Ser Pro Asn 
        195                 200                 205             


Leu Ser Pro Asp Asp Lys Ser Phe Ser Arg Val Val Pro Arg Val Pro 
    210                 215                 220                 


Asp Ser Thr Arg Arg Thr Asp Val Gly Ala Gly Ala Leu Arg Arg Ser 
225                 230                 235                 240 


Asp Ser Pro Glu Ile Pro Phe Gln Ala Ala Ala Gly Pro Ser Asp Gly 
                245                 250                 255     


Leu Asp Ala Ser Ser Pro Gly Asn Ser Phe Val Gly Leu Arg Val Val 
            260                 265                 270         


Ala Lys Trp Ser Ser Asn Gly Tyr Phe Tyr Ser Gly Lys Ile Thr Arg 
        275                 280                 285             


Asp Val Gly Ala Gly Lys Tyr Lys Leu Leu Phe Asp Asp Gly Tyr Glu 
    290                 295                 300                 


Cys Asp Val Leu Gly Lys Asp Ile Leu Leu Cys Asp Pro Ile Pro Leu 
305                 310                 315                 320 


Asp Thr Glu Val Thr Ala Leu Ser Glu Asp Glu Tyr Phe Ser Ala Gly 
                325                 330                 335     


Val Val Lys Gly His Arg Lys Glu Ser Gly Glu Leu Tyr Tyr Ser Ile 
            340                 345                 350         


Glu Lys Glu Gly Gln Arg Lys Trp Tyr Lys Arg Met Ala Val Ile Leu 
        355                 360                 365             


Ser Leu Glu Gln Gly Asn Arg Leu Arg Glu Gln Tyr Gly Leu Gly Pro 
    370                 375                 380                 


Tyr Glu Ala Val Thr Pro Leu Thr Lys Ala Ala Asp Ile Ser Leu Asp 
385                 390                 395                 400 


Asn Leu Val Glu Gly Lys Arg Lys Arg Arg Ser Asn Val Ser Ser Pro 
                405                 410                 415     


Ala Thr Pro Thr Ala Ser Ser Ser Ser Ser Thr Thr Pro Thr Arg Lys 
            420                 425                 430         


Ile Thr Glu Ser Pro Arg Ala Ser Met Gly Val Leu Ser Gly Lys Arg 
        435                 440                 445             


Lys Leu Ile Thr Ser Glu Glu Glu Arg Ser Pro Ala Lys Arg Gly Arg 
    450                 455                 460                 


Lys Ser Ala Thr Val Lys Pro Gly Ala Val Gly Ala Gly Glu Phe Val 
465                 470                 475                 480 


Ser Pro Cys Glu Ser Gly Asp Asn Thr Gly Glu Pro Ser Ala Leu Glu 
                485                 490                 495     


Glu Gln 
        


<210>  2
<211>  527
<212>  PRT
<213>  artificial sequence

<220>
<223>  RNF 168 DRING

<400>  2

Met Ala Leu Pro Lys Asp Ala Ile Pro Ser Leu Ser Glu Cys Ser Ser 
1               5                   10                  15      


Trp Thr Arg Tyr His Thr Arg Arg Asn Ser Leu Val Asn Val Glu Leu 
            20                  25                  30          


Trp Thr Ile Ile Gln Lys His Tyr Pro Arg Glu Cys Lys Leu Arg Ala 
        35                  40                  45              


Ser Gly Gln Glu Ser Glu Glu Val Ala Asp Asp Tyr Gln Pro Val Arg 
    50                  55                  60                  


Leu Leu Ser Lys Pro Gly Glu Leu Arg Arg Glu Tyr Glu Glu Glu Ile 
65                  70                  75                  80  


Ser Lys Val Ala Ala Glu Arg Arg Ala Ser Glu Glu Glu Glu Asn Lys 
                85                  90                  95      


Ala Ser Glu Glu Tyr Ile Gln Arg Leu Leu Ala Glu Glu Glu Glu Glu 
            100                 105                 110         


Glu Lys Arg Gln Ala Glu Lys Arg Arg Arg Ala Met Glu Glu Gln Leu 
        115                 120                 125             


Lys Ser Asp Glu Glu Leu Ala Arg Lys Leu Ser Ile Asp Ile Asn Asn 
    130                 135                 140                 


Phe Cys Glu Gly Ser Ile Ser Ala Ser Pro Leu Asn Ser Arg Lys Ser 
145                 150                 155                 160 


Asp Pro Val Thr Pro Lys Ser Glu Lys Lys Ser Lys Asn Lys Gln Arg 
                165                 170                 175     


Asn Thr Gly Asp Ile Gln Lys Tyr Leu Thr Pro Lys Ser Gln Phe Gly 
            180                 185                 190         


Ser Ala Ser His Ser Glu Ala Val Gln Glu Val Arg Lys Asp Ser Val 
        195                 200                 205             


Ser Lys Asp Ile Asp Ser Ser Asp Arg Lys Ser Pro Thr Gly Gln Asp 
    210                 215                 220                 


Thr Glu Ile Glu Asp Met Pro Thr Leu Ser Pro Gln Ile Ser Leu Gly 
225                 230                 235                 240 


Val Gly Glu Gln Gly Ala Asp Ser Ser Ile Glu Ser Pro Met Pro Trp 
                245                 250                 255     


Leu Cys Ala Cys Gly Ala Glu Trp Tyr His Glu Gly Asn Val Lys Thr 
            260                 265                 270         


Arg Pro Ser Asn His Gly Lys Glu Leu Cys Val Leu Ser His Glu Arg 
        275                 280                 285             


Pro Lys Thr Arg Val Pro Tyr Ser Lys Glu Thr Ala Val Met Pro Cys 
    290                 295                 300                 


Gly Arg Thr Glu Ser Gly Cys Ala Pro Thr Ser Gly Val Thr Gln Thr 
305                 310                 315                 320 


Asn Gly Asn Asn Thr Gly Glu Thr Glu Asn Glu Glu Ser Cys Leu Leu 
                325                 330                 335     


Ile Ser Lys Glu Ile Ser Lys Arg Lys Asn Gln Glu Ser Ser Phe Glu 
            340                 345                 350         


Ala Val Lys Asp Pro Cys Phe Ser Ala Lys Arg Arg Lys Val Ser Pro 
        355                 360                 365             


Glu Ser Ser Pro Asp Gln Glu Glu Thr Glu Ile Asn Phe Thr Gln Lys 
    370                 375                 380                 


Leu Ile Asp Leu Glu His Leu Leu Phe Glu Arg His Lys Gln Glu Glu 
385                 390                 395                 400 


Gln Asp Arg Leu Leu Ala Leu Gln Leu Gln Lys Glu Val Asp Lys Glu 
                405                 410                 415     


Gln Met Val Pro Asn Arg Gln Lys Gly Ser Pro Asp Glu Tyr His Leu 
            420                 425                 430         


Arg Ala Thr Ser Ser Pro Pro Asp Lys Val Leu Asn Gly Gln Arg Lys 
        435                 440                 445             


Asn Pro Lys Asp Gly Asn Phe Lys Arg Gln Thr His Thr Lys His Pro 
    450                 455                 460                 


Thr Pro Glu Arg Gly Ser Arg Asp Lys Asn Arg Gln Val Ser Leu Lys 
465                 470                 475                 480 


Met Gln Leu Lys Gln Ser Val Asn Arg Arg Lys Met Pro Asn Ser Thr 
                485                 490                 495     


Arg Asp His Cys Lys Val Ser Lys Ser Ala His Ser Leu Gln Pro Ser 
            500                 505                 510         


Ile Ser Gln Lys Ser Val Phe Gln Met Phe Gln Arg Cys Thr Lys 
        515                 520                 525         


