##gff-version 3 Q8IW19 UniProtKB Chain 1 511 . . . ID=PRO_0000089342;Note=Aprataxin and PNK-like factor Q8IW19 UniProtKB Domain 1 108 . . . Note=FHA-like Q8IW19 UniProtKB Zinc finger 377 398 . . . Note=PBZ-type 1 Q8IW19 UniProtKB Zinc finger 419 440 . . . Note=PBZ-type 2 Q8IW19 UniProtKB Region 223 370 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8IW19 UniProtKB Region 406 416 . . . Note=Flexible linker;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20439749;Dbxref=PMID:20439749 Q8IW19 UniProtKB Region 449 497 . . . Note=Disordered;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21211722;Dbxref=PMID:21211722 Q8IW19 UniProtKB Coiled coil 487 511 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8IW19 UniProtKB Motif 182 191 . . . Note=KBM;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23689425,ECO:0000269|PubMed:27063109;Dbxref=PMID:23689425,PMID:27063109 Q8IW19 UniProtKB Motif 476 500 . . . Note=NAP1L motif;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21211722;Dbxref=PMID:21211722 Q8IW19 UniProtKB Compositional bias 224 248 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8IW19 UniProtKB Compositional bias 249 263 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8IW19 UniProtKB Compositional bias 264 293 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8IW19 UniProtKB Compositional bias 299 323 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8IW19 UniProtKB Compositional bias 324 370 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8IW19 UniProtKB Compositional bias 465 497 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8IW19 UniProtKB Binding site 376 376 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18172500;Dbxref=PMID:18172500 Q8IW19 UniProtKB Binding site 381 381 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18172500;Dbxref=PMID:18172500 Q8IW19 UniProtKB Binding site 386 386 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18172500;Dbxref=PMID:18172500 Q8IW19 UniProtKB Binding site 387 387 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18172500;Dbxref=PMID:18172500 Q8IW19 UniProtKB Binding site 423 423 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18172500;Dbxref=PMID:18172500 Q8IW19 UniProtKB Binding site 428 428 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18172500;Dbxref=PMID:18172500 Q8IW19 UniProtKB Binding site 429 429 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18172500;Dbxref=PMID:18172500 Q8IW19 UniProtKB Modified residue 116 116 . . . Note=Phosphoserine%3B by ATM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17507382;Dbxref=PMID:17507382 Q8IW19 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9D842 Q8IW19 UniProtKB Natural variant 100 100 . . . ID=VAR_032299;Note=I->V;Dbxref=dbSNP:rs11902811 Q8IW19 UniProtKB Natural variant 224 224 . . . ID=VAR_061557;Note=S->T;Dbxref=dbSNP:rs35002937 Q8IW19 UniProtKB Natural variant 336 336 . . . ID=VAR_032300;Note=L->F;Dbxref=dbSNP:rs13404469 Q8IW19 UniProtKB Mutagenesis 27 27 . . . Note=Does not affect interaction with XRCC5 and XRCC6%3B decreased ability to promote non-homologous end-joining (NHEJ). R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23689425;Dbxref=PMID:23689425 Q8IW19 UniProtKB Mutagenesis 116 116 . . . Note=Decreases phosphorylation by ATM. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17507382;Dbxref=PMID:17507382 Q8IW19 UniProtKB Mutagenesis 182 184 . . . Note=Abolished interaction with XRCC5 and XRCC6. RKR->AKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23689425;Dbxref=PMID:23689425 Q8IW19 UniProtKB Mutagenesis 182 182 . . . Note=Reduced interaction with XRCC5 and XRCC6%3B impaired localization to the nucleus. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23689425;Dbxref=PMID:23689425 Q8IW19 UniProtKB Mutagenesis 184 184 . . . Note=Abolished interaction with XRCC5 and XRCC6%3B impaired localization to the nucleus. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23689425;Dbxref=PMID:23689425 Q8IW19 UniProtKB Mutagenesis 189 191 . . . Note=Abolished interaction with XRCC5 and XRCC6. WML->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23689425;Dbxref=PMID:23689425 Q8IW19 UniProtKB Mutagenesis 189 189 . . . Note=Abolished interaction with XRCC5 and XRCC6%3B impaired localization to the nucleus%3B decreased ability to promote non-homologous end-joining (NHEJ). W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23689425;Dbxref=PMID:23689425 Q8IW19 UniProtKB Mutagenesis 190 190 . . . Note=Reduced interaction with XRCC5 and XRCC6. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23689425;Dbxref=PMID:23689425 Q8IW19 UniProtKB Mutagenesis 191 191 . . . Note=Does not affect interaction with XRCC5 and XRCC6. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23689425;Dbxref=PMID:23689425 Q8IW19 UniProtKB Mutagenesis 376 376 . . . Note=Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1%3B when associated with A-421 and A-427. Does not affect histone chaperone activity%3B when associated with A-421 and A-427. R->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18172500,ECO:0000269|PubMed:21211722;Dbxref=PMID:18172500,PMID:21211722 Q8IW19 UniProtKB Mutagenesis 379 379 . . . Note=Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1%3B when associated with A-385%3B A-421 and A-427. Does not affect histone chaperone activity%3B when associated with A-385%3B A-421 and A-427. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18172500,ECO:0000269|PubMed:21211722;Dbxref=PMID:18172500,PMID:21211722 Q8IW19 UniProtKB Mutagenesis 385 385 . . . Note=Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1%3B when associated with A-379%3B A-421 and A-427. Does not affect histone chaperone activity%3B when associated with A-379%3B A-421 and A-427. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18172500,ECO:0000269|PubMed:21211722;Dbxref=PMID:18172500,PMID:21211722 Q8IW19 UniProtKB Mutagenesis 421 421 . . . Note=Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1%3B when associated with A-379%3B A-385 and A-427. Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1%3B when associated with A-376 and A-427. Does not affect histone chaperone activity%3B when associated with A-376 and A-427. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18172500,ECO:0000269|PubMed:21211722;Dbxref=PMID:18172500,PMID:21211722 Q8IW19 UniProtKB Mutagenesis 427 427 . . . Note=Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1%3B when associated with A-379%3B A-385 and A-421. Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1%3B when associated with A-376 and A-421. Does not affect histone chaperone activity%3B when associated with A-376 and A-421. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18172500,ECO:0000269|PubMed:21211722;Dbxref=PMID:18172500,PMID:21211722 Q8IW19 UniProtKB Mutagenesis 477 477 . . . Note=Impaired binding to histones and ability to mediate histone chaperone activity. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21211722,ECO:0000269|PubMed:29905837;Dbxref=PMID:21211722,PMID:29905837 Q8IW19 UniProtKB Mutagenesis 485 485 . . . Note=Impaired binding to histones and ability to mediate histone chaperone activity. W->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21211722,ECO:0000269|PubMed:29905837;Dbxref=PMID:21211722,PMID:29905837 Q8IW19 UniProtKB Sequence conflict 313 313 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8IW19 UniProtKB Beta strand 4 9 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W7W Q8IW19 UniProtKB Beta strand 16 18 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W7W Q8IW19 UniProtKB Beta strand 20 28 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W7W Q8IW19 UniProtKB Turn 29 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W7W Q8IW19 UniProtKB Beta strand 43 48 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W7W Q8IW19 UniProtKB Beta strand 51 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W7W Q8IW19 UniProtKB Beta strand 58 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W7W Q8IW19 UniProtKB Beta strand 63 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W7W Q8IW19 UniProtKB Beta strand 81 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5E50 Q8IW19 UniProtKB Beta strand 88 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W7W Q8IW19 UniProtKB Beta strand 95 102 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W7W Q8IW19 UniProtKB Helix 188 191 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6TYZ Q8IW19 UniProtKB Beta strand 371 374 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KQB Q8IW19 UniProtKB Turn 380 383 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KQB Q8IW19 UniProtKB Helix 392 395 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KQB Q8IW19 UniProtKB Turn 412 414 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KQB Q8IW19 UniProtKB Helix 424 426 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KQC Q8IW19 UniProtKB Helix 432 437 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2KQC