##gff-version 3 Q92794 UniProtKB Chain 1 2004 . . . ID=PRO_0000051572;Note=Histone acetyltransferase KAT6A Q92794 UniProtKB Domain 1 77 . . . Note=SAMD1-like winged helix (WH);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01358 Q92794 UniProtKB Domain 95 171 . . . Note=H15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00837 Q92794 UniProtKB Domain 504 778 . . . Note=MYST-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 Q92794 UniProtKB Zinc finger 206 265 . . . Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q92794 UniProtKB Zinc finger 259 313 . . . Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q92794 UniProtKB Zinc finger 537 562 . . . Note=C2HC MYST-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 Q92794 UniProtKB Region 1 144 . . . Note=Required for activation of RUNX1-1 Q92794 UniProtKB Region 52 166 . . . Note=Required for nuclear localization Q92794 UniProtKB Region 144 664 . . . Note=Interaction with PML;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23431171;Dbxref=PMID:23431171 Q92794 UniProtKB Region 312 664 . . . Note=Interaction with RUNX1-1 Q92794 UniProtKB Region 334 375 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Region 441 464 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Region 488 778 . . . Note=Catalytic Q92794 UniProtKB Region 507 810 . . . Note=Mediates interaction with BRPF1%2C required for histone H3 acetyltransferase activity;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18794358;Dbxref=PMID:18794358 Q92794 UniProtKB Region 785 1445 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Region 1461 1621 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Region 1517 1741 . . . Note=Interaction with PML;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23431171;Dbxref=PMID:23431171 Q92794 UniProtKB Region 1517 1642 . . . Note=Interaction with RUNX1-2 Q92794 UniProtKB Region 1637 1721 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Region 1913 1948 . . . Note=Required for activation of RUNX1-2 Q92794 UniProtKB Compositional bias 339 353 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 786 803 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 804 832 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 842 862 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 873 888 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 889 926 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 930 946 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 952 987 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1011 1029 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1124 1148 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1149 1171 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1201 1226 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1227 1245 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1271 1286 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1287 1320 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1321 1347 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1355 1369 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1390 1420 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1423 1437 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1478 1621 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Compositional bias 1646 1701 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q92794 UniProtKB Active site 680 680 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 Q92794 UniProtKB Binding site 645 649 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.27 Q92794 UniProtKB Binding site 654 660 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.27 Q92794 UniProtKB Binding site 684 684 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.27 Q92794 UniProtKB Site 813 814 . . . Note=Breakpoint for translocation to form KAT6A-ASXL2 Q92794 UniProtKB Site 1117 1118 . . . Note=Breakpoint for translocation to form KAT6A-EP300 and KAT6A-NCOA2 Q92794 UniProtKB Site 1546 1547 . . . Note=Breakpoint for translocation to form KAT6A-CREBBP Q92794 UniProtKB Modified residue 172 172 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8BZ21 Q92794 UniProtKB Modified residue 350 350 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q92794 UniProtKB Modified residue 355 355 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q92794 UniProtKB Modified residue 369 369 . . . Note=Phosphothreonine%3B by PKB/AKT1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23431171;Dbxref=PMID:23431171 Q92794 UniProtKB Modified residue 420 420 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q92794 UniProtKB Modified residue 473 473 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:20068231,PMID:23186163 Q92794 UniProtKB Modified residue 604 604 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.27 Q92794 UniProtKB Modified residue 787 787 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8BZ21 Q92794 UniProtKB Modified residue 812 812 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q92794 UniProtKB Modified residue 815 815 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8BZ21 Q92794 UniProtKB Modified residue 899 899 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5TKR9 Q92794 UniProtKB Modified residue 941 941 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q92794 UniProtKB Modified residue 954 954 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q92794 UniProtKB Modified residue 974 974 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q92794 UniProtKB Modified residue 1007 1007 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 Q92794 UniProtKB Modified residue 1089 1089 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q92794 UniProtKB Modified residue 1090 1090 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q92794 UniProtKB Modified residue 1113 1113 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:23186163 Q92794 UniProtKB Cross-link 834 834 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q92794 UniProtKB Cross-link 1342 1342 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 Q92794 UniProtKB Natural variant 134 134 . . . ID=VAR_047548;Note=L->S;Dbxref=dbSNP:rs3824276 Q92794 UniProtKB Mutagenesis 543 543 . . . Note=Abrogates HAT activity. C->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12676584;Dbxref=PMID:12676584 Q92794 UniProtKB Mutagenesis 545 545 . . . Note=Reduced affinity for DNA. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17925393;Dbxref=PMID:17925393 Q92794 UniProtKB Mutagenesis 657 657 . . . Note=Abrogates HAT activity. G->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12676584;Dbxref=PMID:12676584 Q92794 UniProtKB Mutagenesis 727 727 . . . Note=Slightly reduced affinity for DNA. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17925393;Dbxref=PMID:17925393 Q92794 UniProtKB Mutagenesis 732 732 . . . Note=Reduced affinity for DNA. H->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17925393;Dbxref=PMID:17925393 Q92794 UniProtKB Sequence conflict 401 401 . . . Note=K->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q92794 UniProtKB Helix 7 22 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Y43 Q92794 UniProtKB Helix 29 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Y43 Q92794 UniProtKB Helix 44 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Y43 Q92794 UniProtKB Beta strand 59 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Y43 Q92794 UniProtKB Beta strand 68 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Y43 Q92794 UniProtKB Helix 195 197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Beta strand 198 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B76 Q92794 UniProtKB Beta strand 207 209 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Turn 210 212 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Turn 231 233 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Helix 239 242 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Helix 246 252 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Turn 253 256 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Turn 260 262 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Turn 266 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Helix 275 277 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Beta strand 278 280 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4LK9 Q92794 UniProtKB Turn 282 284 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Beta strand 287 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4LK9 Q92794 UniProtKB Helix 290 292 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Beta strand 293 295 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Turn 308 310 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5B78 Q92794 UniProtKB Beta strand 511 514 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Beta strand 517 520 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Helix 529 532 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RC4 Q92794 UniProtKB Beta strand 535 539 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Turn 541 543 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Beta strand 546 549 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Helix 550 559 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Beta strand 566 573 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Beta strand 576 582 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Turn 583 585 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Helix 587 598 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Beta strand 613 622 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Beta strand 625 637 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Beta strand 642 649 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Helix 651 653 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Beta strand 655 657 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2RC4 Q92794 UniProtKB Helix 658 672 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Beta strand 677 679 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Helix 685 705 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Helix 713 720 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Helix 724 733 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Helix 750 759 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU Q92794 UniProtKB Helix 771 773 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2OZU