##gff-version 3 Q92993 UniProtKB Chain 1 513 . . . ID=PRO_0000051580;Note=Histone acetyltransferase KAT5 Q92993 UniProtKB Domain 8 65 . . . Note=Tudor-knot;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q92993 UniProtKB Domain 227 504 . . . Note=MYST-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 Q92993 UniProtKB Zinc finger 260 285 . . . Note=C2HC MYST-type;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|PROSITE-ProRule:PRU01063,ECO:0000305|Ref.69 Q92993 UniProtKB Region 69 106 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92993 UniProtKB Region 122 220 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92993 UniProtKB Region 368 513 . . . Note=Interaction with ATF2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18397884;Dbxref=PMID:18397884 Q92993 UniProtKB Active site 403 403 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 Q92993 UniProtKB Binding site 370 372 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.69 Q92993 UniProtKB Binding site 377 383 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.69 Q92993 UniProtKB Binding site 407 407 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.69 Q92993 UniProtKB Binding site 416 416 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 Q92993 UniProtKB Modified residue 52 52 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q92993 UniProtKB Modified residue 86 86 . . . Note=Phosphoserine%3B by GSK3;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:12468530,ECO:0000269|PubMed:22539723,ECO:0000269|PubMed:29335245,ECO:0000269|PubMed:30704899,ECO:0007744|PubMed:23186163;Dbxref=PMID:12468530,PMID:22539723,PMID:23186163,PMID:29335245,PMID:30704899 Q92993 UniProtKB Modified residue 90 90 . . . Note=Phosphoserine%3B by CDK1 and CDK9;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:12468530,ECO:0000269|PubMed:22539723,ECO:0000269|PubMed:26829474,ECO:0000269|PubMed:29335245,ECO:0007744|PubMed:23186163;Dbxref=PMID:12468530,PMID:22539723,PMID:23186163,PMID:26829474,PMID:29335245 Q92993 UniProtKB Modified residue 104 104 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25301942,ECO:0000269|PubMed:29174981;Dbxref=PMID:25301942,PMID:29174981 Q92993 UniProtKB Modified residue 120 120 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25301942;Dbxref=PMID:25301942 Q92993 UniProtKB Modified residue 148 148 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25301942;Dbxref=PMID:25301942 Q92993 UniProtKB Modified residue 150 150 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25301942;Dbxref=PMID:25301942 Q92993 UniProtKB Modified residue 187 187 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25301942;Dbxref=PMID:25301942 Q92993 UniProtKB Modified residue 189 189 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25301942;Dbxref=PMID:25301942 Q92993 UniProtKB Modified residue 199 199 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q92993 UniProtKB Modified residue 327 327 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24835996,ECO:0000269|Ref.69;Dbxref=PMID:24835996 Q92993 UniProtKB Cross-link 430 430 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704809;Dbxref=PMID:17704809 Q92993 UniProtKB Cross-link 430 430 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32832608;Dbxref=PMID:32832608 Q92993 UniProtKB Cross-link 451 451 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704809;Dbxref=PMID:17704809 Q92993 UniProtKB Alternative sequence 4 4 . . . ID=VSP_009104;Note=In isoform 3 and isoform 4. V->VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:12801643,ECO:0000303|PubMed:14702039;Dbxref=PMID:12801643,PMID:14702039 Q92993 UniProtKB Alternative sequence 96 147 . . . ID=VSP_007438;Note=In isoform 1 and isoform 4. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:11416127,ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:11416127,PMID:14702039,PMID:15489334 Q92993 UniProtKB Natural variant 53 53 . . . ID=VAR_085192;Note=In NEDFASB%3B decreased histone acetyltransferase activity. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32822602;Dbxref=dbSNP:rs1857071943,PMID:32822602 Q92993 UniProtKB Natural variant 78 78 . . . ID=VAR_059456;Note=P->T;Dbxref=dbSNP:rs11541271 Q92993 UniProtKB Natural variant 369 369 . . . ID=VAR_085193;Note=In NEDFASB%3B decreased histone acetyltransferase activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32822602;Dbxref=dbSNP:rs1857215256,PMID:32822602 Q92993 UniProtKB Natural variant 413 413 . . . ID=VAR_085194;Note=In NEDFASB%3B decreased histone acetyltransferase activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32822602;Dbxref=dbSNP:rs1857290083,PMID:32822602 Q92993 UniProtKB Mutagenesis 86 86 . . . Note=Reduced phosphorylation. Abolishes phosphorylation%3B when associated with A-90. Reduced histone acetyltransferase activity. Abolished phosphorylation by GSK3 and decreased acetyltransferase activity. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12468530,ECO:0000269|PubMed:22539723,ECO:0000269|PubMed:30704899;Dbxref=PMID:12468530,PMID:22539723,PMID:30704899 Q92993 UniProtKB Mutagenesis 90 90 . . . Note=Reduced phosphorylation%2C leading to reduced protein acetyltransferase activity. Abolishes phosphorylation%3B when associated with A-86. Reduced histone acetyltransferase activity. Abolished phosphorylation by GSK3 at S-86. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12468530,ECO:0000269|PubMed:22539723,ECO:0000269|PubMed:26829474,ECO:0000269|PubMed:29335245;Dbxref=PMID:12468530,PMID:22539723,PMID:26829474,PMID:29335245 Q92993 UniProtKB Mutagenesis 90 90 . . . Note=Mimics phosphorylation%2C promoting protein acetyltransferase activity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26829474;Dbxref=PMID:26829474 Q92993 UniProtKB Mutagenesis 104 104 . . . Note=Impaired acetylation%2C leading to reduced histone acetyltransferase activity. In K6R%3B abolished autoacetylation%3B when associated with R-120%2C R-148%2C R-150%2C R-187 and R-189. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25301942,ECO:0000269|PubMed:29174981;Dbxref=PMID:25301942,PMID:29174981 Q92993 UniProtKB Mutagenesis 120 120 . . . Note=In K6R%3B abolished autoacetylation%3B when associated with R-104%2C R-148%2C R-150%2C R-187 and R-189. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25301942;Dbxref=PMID:25301942 Q92993 UniProtKB Mutagenesis 148 148 . . . Note=In K6R%3B abolished autoacetylation%3B when associated with R-104%2C R-120%2C R-150%2C R-187 and R-189. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25301942;Dbxref=PMID:25301942 Q92993 UniProtKB Mutagenesis 150 150 . . . Note=In K6R%3B abolished autoacetylation%3B when associated with R-104%2C R-120%2C R-148%2C R-187 and R-189. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25301942;Dbxref=PMID:25301942 Q92993 UniProtKB Mutagenesis 187 187 . . . Note=In K6R%3B abolished autoacetylation%3B when associated with R-104%2C R-120%2C R-148%2C R-150 and R-189. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25301942;Dbxref=PMID:25301942 Q92993 UniProtKB Mutagenesis 189 189 . . . Note=In K6R%3B abolished autoacetylation%3B when associated with R-104%2C R-120%2C R-148%2C R-150 and R-187. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25301942;Dbxref=PMID:25301942 Q92993 UniProtKB Mutagenesis 254 254 . . . Note=Does not affect phosphorylation%3B when associated with A-257. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12468530;Dbxref=PMID:12468530 Q92993 UniProtKB Mutagenesis 257 257 . . . Note=Does not affect phosphorylation%3B when associated with A-254. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12468530;Dbxref=PMID:12468530 Q92993 UniProtKB Mutagenesis 327 327 . . . Note=Mimics acetylation%3B promoting interaction with FOXP3 and subsequent acetylation. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835996;Dbxref=PMID:24835996 Q92993 UniProtKB Mutagenesis 327 327 . . . Note=Decreased autoacetylation%3B leading to decreased acetyltransferase activity and ability to acetylate FOXP3. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24835996;Dbxref=PMID:24835996 Q92993 UniProtKB Mutagenesis 377 380 . . . Note=In KAT5(QG/EE) mutant%3B abolished acetyltransferase activity. Impaired ability to activate CGAS. QRRG->ERRE;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24835996,ECO:0000269|PubMed:26291311,ECO:0000269|PubMed:32034146,ECO:0000269|PubMed:32817552,ECO:0000269|PubMed:33938178;Dbxref=PMID:24835996,PMID:26291311,PMID:32034146,PMID:32817552,PMID:33938178 Q92993 UniProtKB Mutagenesis 380 380 . . . Note=Loss of function. Does not affect phosphorylation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12468530;Dbxref=PMID:12468530 Q92993 UniProtKB Mutagenesis 430 430 . . . Note=Abrogates sumoylation. Abolished sumoylation by PIAS4%2C promoting interaction with PRKDC%2C leading to decreased repair of DNA double-strand breaks (DSBs) via homologous recombination (HR). K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17704809,ECO:0000269|PubMed:32832608;Dbxref=PMID:17704809,PMID:32832608 Q92993 UniProtKB Mutagenesis 451 451 . . . Note=Abrogates sumoylation. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17704809;Dbxref=PMID:17704809 Q92993 UniProtKB Sequence conflict 382 382 . . . Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q92993 UniProtKB Helix 4 6 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4QQG Q92993 UniProtKB Beta strand 12 15 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4QQG Q92993 UniProtKB Beta strand 28 35 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4QQG Q92993 UniProtKB Beta strand 37 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4QQG Q92993 UniProtKB Beta strand 42 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4QQG Q92993 UniProtKB Helix 52 54 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4QQG Q92993 UniProtKB Beta strand 56 58 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4QQG Q92993 UniProtKB Helix 60 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4QQG Q92993 UniProtKB Helix 65 67 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2EKO Q92993 UniProtKB Beta strand 235 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Beta strand 240 242 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Helix 252 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Beta strand 260 262 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Turn 264 266 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Beta strand 269 271 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Helix 273 282 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Beta strand 289 296 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Beta strand 299 305 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Turn 306 308 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Helix 310 321 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Beta strand 336 345 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Beta strand 348 360 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Beta strand 365 368 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Beta strand 370 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Helix 374 376 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Helix 381 395 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Beta strand 400 402 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Helix 408 425 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Helix 441 448 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Helix 452 461 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Beta strand 469 474 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Helix 497 499 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OU2 Q92993 UniProtKB Sequence conflict 32 32 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305