##gff-version 3 O60934 UniProtKB Chain 1 754 . . . ID=PRO_0000231043;Note=Nibrin O60934 UniProtKB Domain 24 83 . . . Note=FHA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00086 O60934 UniProtKB Domain 105 181 . . . Note=BRCT O60934 UniProtKB Region 111 328 . . . Note=Mediates interaction with SP100;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9R207 O60934 UniProtKB Region 221 402 . . . Note=Interaction with MTOR%2C MAPKAP1 and RICTOR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23762398;Dbxref=PMID:23762398 O60934 UniProtKB Region 326 346 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O60934 UniProtKB Region 396 415 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O60934 UniProtKB Region 430 478 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O60934 UniProtKB Motif 461 467 . . . Note=Nuclear localization signal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16188882;Dbxref=PMID:16188882 O60934 UniProtKB Motif 736 743 . . . Note=EEXXXDDL motif;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15758953;Dbxref=PMID:15758953 O60934 UniProtKB Compositional bias 326 344 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O60934 UniProtKB Compositional bias 430 460 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O60934 UniProtKB Compositional bias 461 477 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O60934 UniProtKB Modified residue 278 278 . . . Note=Phosphoserine%3B by ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10839544;Dbxref=PMID:10839544 O60934 UniProtKB Modified residue 337 337 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O60934 UniProtKB Modified residue 343 343 . . . Note=Phosphoserine%3B by ATM;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10802669,ECO:0000269|PubMed:10839545,ECO:0007744|PubMed:23186163;Dbxref=PMID:10802669,PMID:10839545,PMID:23186163 O60934 UniProtKB Modified residue 347 347 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O60934 UniProtKB Modified residue 397 397 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:10839545,ECO:0007744|PubMed:17525332,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:10839545,PMID:17525332,PMID:18669648,PMID:20068231,PMID:23186163 O60934 UniProtKB Modified residue 402 402 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:20068231;Dbxref=PMID:20068231 O60934 UniProtKB Modified residue 432 432 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:16964243,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163,ECO:0007744|PubMed:24275569;Dbxref=PMID:16964243,PMID:18669648,PMID:20068231,PMID:23186163,PMID:24275569 O60934 UniProtKB Modified residue 509 509 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O60934 UniProtKB Modified residue 518 518 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O60934 UniProtKB Modified residue 615 615 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10839545;Dbxref=PMID:10839545 O60934 UniProtKB Modified residue 673 673 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 O60934 UniProtKB Cross-link 529 529 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 O60934 UniProtKB Cross-link 571 571 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 O60934 UniProtKB Cross-link 582 582 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 O60934 UniProtKB Natural variant 93 93 . . . ID=VAR_025792;Note=In some childhood acute lymphoblastic leukemia patients%3B uncertain significance%3B rare variant. S->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11325820;Dbxref=dbSNP:rs12721593,PMID:11325820 O60934 UniProtKB Natural variant 95 95 . . . ID=VAR_025793;Note=In some childhood acute lymphoblastic leukemia patients%3B uncertain significance%3B rare variant. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11325820;Dbxref=dbSNP:rs61753720,PMID:11325820 O60934 UniProtKB Natural variant 105 105 . . . ID=VAR_025794;Note=K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7;Dbxref=dbSNP:rs13312858 O60934 UniProtKB Natural variant 142 142 . . . ID=VAR_051226;Note=N->S;Dbxref=dbSNP:rs769414 O60934 UniProtKB Natural variant 150 150 . . . ID=VAR_025795;Note=In BC. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14684699;Dbxref=dbSNP:rs773119929,PMID:14684699 O60934 UniProtKB Natural variant 171 171 . . . ID=VAR_025796;Note=In some childhood acute lymphoblastic leukemia patients%3B uncertain significance%3B rare variant%3B associated with aplastic anemia at homozygosity. I->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11325820,ECO:0000269|PubMed:15338273;Dbxref=dbSNP:rs61754966,PMID:11325820,PMID:15338273 O60934 UniProtKB Natural variant 185 185 . . . ID=VAR_025797;Note=E->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14684699,ECO:0000269|PubMed:14688016,ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:9590180,ECO:0000269|PubMed:9590181,ECO:0000269|Ref.7;Dbxref=dbSNP:rs1805794,PMID:14684699,PMID:14688016,PMID:14702039,PMID:9590180,PMID:9590181 O60934 UniProtKB Natural variant 210 210 . . . ID=VAR_025798;Note=V->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11325820;Dbxref=dbSNP:rs61754796,PMID:11325820 O60934 UniProtKB Natural variant 215 215 . . . ID=VAR_025799;Note=R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11325820;Dbxref=dbSNP:rs34767364,PMID:11325820 O60934 UniProtKB Natural variant 216 216 . . . ID=VAR_025800;Note=Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7;Dbxref=dbSNP:rs769416 O60934 UniProtKB Natural variant 266 266 . . . ID=VAR_025801;Note=P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7;Dbxref=dbSNP:rs769420 O60934 UniProtKB Natural variant 408 408 . . . ID=VAR_051227;Note=K->E;Dbxref=dbSNP:rs34120922 O60934 UniProtKB Natural variant 497 497 . . . ID=VAR_025802;Note=T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.7;Dbxref=dbSNP:rs3026268 O60934 UniProtKB Natural variant 574 574 . . . ID=VAR_025803;Note=L->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14684699;Dbxref=dbSNP:rs142334798,PMID:14684699 O60934 UniProtKB Natural variant 679 679 . . . ID=VAR_064738;Note=Found in a renal cell carcinoma sample%3B somatic mutation. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21248752;Dbxref=PMID:21248752 O60934 UniProtKB Mutagenesis 28 28 . . . Note=Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10802669;Dbxref=PMID:10802669 O60934 UniProtKB Mutagenesis 45 45 . . . Note=Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10802669;Dbxref=PMID:10802669 O60934 UniProtKB Mutagenesis 136 137 . . . Note=Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. GG->EE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10802669;Dbxref=PMID:10802669 O60934 UniProtKB Mutagenesis 176 176 . . . Note=Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10802669;Dbxref=PMID:10802669 O60934 UniProtKB Mutagenesis 343 343 . . . Note=Abrogates ATM-dependent phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10839545;Dbxref=PMID:10839545 O60934 UniProtKB Mutagenesis 397 397 . . . Note=Abrogates ATM-dependent phosphorylation. No loss of interaction with KPNA2. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10839545,ECO:0000269|PubMed:16188882;Dbxref=PMID:10839545,PMID:16188882 O60934 UniProtKB Mutagenesis 465 466 . . . Note=Blocks the association with KPNA2%2C and reduces nuclear foci formation in response to ionizing radiation. KR->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16188882;Dbxref=PMID:16188882 O60934 UniProtKB Mutagenesis 583 583 . . . Note=No loss of interaction with KPNA2. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16188882;Dbxref=PMID:16188882 O60934 UniProtKB Mutagenesis 615 615 . . . Note=Abrogates ATM-dependent phosphorylation. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10839545;Dbxref=PMID:10839545 O60934 UniProtKB Mutagenesis 736 737 . . . Note=Decreases ATM binding. EE->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15758953;Dbxref=PMID:15758953 O60934 UniProtKB Mutagenesis 741 742 . . . Note=Decreases ATM binding. DD->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15758953;Dbxref=PMID:15758953 O60934 UniProtKB Mutagenesis 745 746 . . . Note=Decreases ATM binding. RY->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15758953;Dbxref=PMID:15758953 O60934 UniProtKB Sequence conflict 247 247 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 O60934 UniProtKB Turn 426 429 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5WQD O60934 UniProtKB Turn 742 744 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SID