##gff-version 3 Q01831 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8168482;Dbxref=PMID:8168482 Q01831 UniProtKB Chain 2 940 . . . ID=PRO_0000218293;Note=DNA repair protein complementing XP-C cells Q01831 UniProtKB Region 1 78 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01831 UniProtKB Region 111 136 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01831 UniProtKB Region 327 519 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01831 UniProtKB Region 496 734 . . . Note=Interaction with RAD23B Q01831 UniProtKB Region 607 766 . . . Note=Minimal sensor domain involved in damage recognition Q01831 UniProtKB Region 607 741 . . . Note=DNA-binding%3B preference for heteroduplex DNA Q01831 UniProtKB Region 767 831 . . . Note=DNA-binding%3B preference for single stranded DNA%3B required for formation of stable nucleoprotein complex Q01831 UniProtKB Region 816 940 . . . Note=Interaction with ERCC2 and GTF2H1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12509233;Dbxref=PMID:12509233 Q01831 UniProtKB Region 847 866 . . . Note=Interaction with CETN2 Q01831 UniProtKB Region 866 940 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01831 UniProtKB Motif 390 395 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q01831 UniProtKB Compositional bias 1 46 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01831 UniProtKB Compositional bias 121 136 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01831 UniProtKB Compositional bias 342 359 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01831 UniProtKB Compositional bias 393 438 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01831 UniProtKB Compositional bias 496 510 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01831 UniProtKB Compositional bias 905 919 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q01831 UniProtKB Modified residue 94 94 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:24275569;Dbxref=PMID:17081983,PMID:18669648,PMID:20068231,PMID:21406692,PMID:24275569 Q01831 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:20068231;Dbxref=PMID:17081983,PMID:20068231 Q01831 UniProtKB Modified residue 140 140 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q01831 UniProtKB Modified residue 169 169 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q01831 UniProtKB Modified residue 397 397 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q01831 UniProtKB Modified residue 398 398 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q01831 UniProtKB Modified residue 399 399 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q01831 UniProtKB Modified residue 453 453 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q01831 UniProtKB Modified residue 460 460 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q01831 UniProtKB Modified residue 876 876 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21406692;Dbxref=PMID:21406692 Q01831 UniProtKB Modified residue 883 883 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:18669648,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569 Q01831 UniProtKB Modified residue 884 884 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:18669648,PMID:20068231,PMID:21406692,PMID:23186163,PMID:24275569 Q01831 UniProtKB Modified residue 891 891 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 Q01831 UniProtKB Modified residue 903 903 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q01831 UniProtKB Cross-link 41 41 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q01831 UniProtKB Cross-link 81 81 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:25755297,ECO:0007744|PubMed:25772364,ECO:0007744|PubMed:28112733;Dbxref=PMID:25755297,PMID:25772364,PMID:28112733 Q01831 UniProtKB Cross-link 89 89 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q01831 UniProtKB Cross-link 161 161 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q01831 UniProtKB Alternative sequence 136 172 . . . ID=VSP_046344;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q01831 UniProtKB Alternative sequence 138 140 . . . ID=VSP_055890;Note=In isoform 3. ELS->VKR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:24722188;Dbxref=PMID:24722188 Q01831 UniProtKB Alternative sequence 141 940 . . . ID=VSP_055891;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:24722188;Dbxref=PMID:24722188 Q01831 UniProtKB Natural variant 16 16 . . . ID=VAR_018894;Note=L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs1870134 Q01831 UniProtKB Natural variant 48 48 . . . ID=VAR_018895;Note=L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs2229089 Q01831 UniProtKB Natural variant 86 86 . . . ID=VAR_018896;Note=K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs3731063 Q01831 UniProtKB Natural variant 287 287 . . . ID=VAR_057475;Note=F->C;Dbxref=dbSNP:rs35629274 Q01831 UniProtKB Natural variant 314 314 . . . ID=VAR_018897;Note=R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs3731126 Q01831 UniProtKB Natural variant 334 334 . . . ID=VAR_005846;Note=In XP-C%3B severe%3B does not affect interaction with KAT2A and transcription coactivator activity in absence of DNA damage. P->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29973595,ECO:0000269|PubMed:8298653;Dbxref=dbSNP:rs74737358,PMID:29973595,PMID:8298653 Q01831 UniProtKB Natural variant 492 492 . . . ID=VAR_018898;Note=R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs2227999 Q01831 UniProtKB Natural variant 499 499 . . . ID=VAR_018899;Note=A->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12177305,ECO:0000269|PubMed:8168482,ECO:0000269|Ref.4;Dbxref=dbSNP:rs2228000,PMID:12177305,PMID:8168482 Q01831 UniProtKB Natural variant 511 511 . . . ID=VAR_059963;Note=K->Q;Dbxref=dbSNP:rs6413541 Q01831 UniProtKB Natural variant 513 513 . . . ID=VAR_018900;Note=M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs3731130 Q01831 UniProtKB Natural variant 514 514 . . . ID=VAR_057476;Note=C->S;Dbxref=dbSNP:rs3731130 Q01831 UniProtKB Natural variant 632 632 . . . ID=VAR_018901;Note=Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs3731139 Q01831 UniProtKB Natural variant 671 671 . . . ID=VAR_018902;Note=R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs3731140 Q01831 UniProtKB Natural variant 689 689 . . . ID=VAR_018903;Note=T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs3731152 Q01831 UniProtKB Natural variant 690 690 . . . ID=VAR_064039;Note=In XP-C%3B diminishes repair activity and impairs DNA binding. W->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10766188,ECO:0000269|PubMed:17355181,ECO:0000269|PubMed:17682058,ECO:0000269|PubMed:19609301;Dbxref=PMID:10766188,PMID:17355181,PMID:17682058,PMID:19609301 Q01831 UniProtKB Natural variant 697 697 . . . ID=VAR_005847;Note=In XP-C%3B mild. V->VV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8298653;Dbxref=PMID:8298653 Q01831 UniProtKB Natural variant 928 928 . . . ID=VAR_018904;Note=K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.4;Dbxref=dbSNP:rs3731177 Q01831 UniProtKB Natural variant 939 939 . . . ID=VAR_005848;Note=Q->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12177305,ECO:0000269|PubMed:8168482,ECO:0000269|Ref.4;Dbxref=dbSNP:rs2228001,PMID:12177305,PMID:8168482 Q01831 UniProtKB Mutagenesis 531 531 . . . Note=Slightly diminishes repair activity and slightly impairs DNA binding. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19609301;Dbxref=PMID:19609301 Q01831 UniProtKB Mutagenesis 542 542 . . . Note=Slightly diminishes repair activity and slightly impairs DNA binding. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19609301;Dbxref=PMID:19609301 Q01831 UniProtKB Mutagenesis 733 733 . . . Note=Diminishes repair activity and impairs DNA binding. F->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17355181,ECO:0000269|PubMed:19609301;Dbxref=PMID:17355181,PMID:19609301 Q01831 UniProtKB Mutagenesis 754 754 . . . Note=Reduces DNA repair activity%3B abolishes single-stranded DNA binding%3B reduces binding to homoduplex DNA%3B reduces localization at DNA damaged foci. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20649465;Dbxref=PMID:20649465 Q01831 UniProtKB Mutagenesis 755 755 . . . Note=Reduces nuclear mobility and impairs repair activity. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19609301;Dbxref=PMID:19609301 Q01831 UniProtKB Mutagenesis 756 756 . . . Note=Reduces DNA repair activity%3B abolishes single-stranded DNA binding%3B reduces binding to homoduplex DNA%3B reduces localization at DNA damaged foci. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20649465;Dbxref=PMID:20649465 Q01831 UniProtKB Mutagenesis 797 797 . . . Note=Reduces DNA repair activity%3B abolishes single-stranded DNA binding%3B reduces binding to homoduplex DNA%3B reduces localization at DNA damaged foci%3B decreases recruitment of TFIIH complex to lesion sites. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20649465;Dbxref=PMID:20649465 Q01831 UniProtKB Mutagenesis 799 799 . . . Note=Reduces DNA repair activity%3B abolishes single-stranded DNA binding%3B reduces binding to homoduplex DNA%3B greatly reduces localization at DNA damaged foci%3B decreases recruitment of TFIIH complex to lesion sites. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20649465;Dbxref=PMID:20649465 Q01831 UniProtKB Mutagenesis 848 848 . . . Note=Reduces NER activity and abolishes interaction with CETN2%3B when associated with A-851 and A-855. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15964821;Dbxref=PMID:15964821 Q01831 UniProtKB Mutagenesis 851 851 . . . Note=Reduces NER activity and abolishes interaction with CETN2%3B when associated with A-848 and A-855. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15964821;Dbxref=PMID:15964821 Q01831 UniProtKB Mutagenesis 855 855 . . . Note=Reduces NER activity and abolishes interaction with CETN2%3B when associated with A-848 and A-851. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15964821;Dbxref=PMID:15964821 Q01831 UniProtKB Sequence conflict 135 135 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01831 UniProtKB Sequence conflict 489 489 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q01831 UniProtKB Turn 120 123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RVB Q01831 UniProtKB Beta strand 124 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RVB Q01831 UniProtKB Beta strand 134 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RVB Q01831 UniProtKB Helix 150 153 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RVB Q01831 UniProtKB Helix 848 861 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OBH Q01831 UniProtKB Helix 890 901 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EBU Q01831 UniProtKB Turn 905 908 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EBU Q01831 UniProtKB Helix 909 915 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EBU Q01831 UniProtKB Helix 936 938 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EBU