##gff-version 3 Q8BZ21 UniProtKB Chain 1 2003 . . . ID=PRO_0000051573;Note=Histone acetyltransferase KAT6A Q8BZ21 UniProtKB Domain 1 77 . . . Note=SAMD1-like winged helix (WH);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01358 Q8BZ21 UniProtKB Domain 95 171 . . . Note=H15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00837 Q8BZ21 UniProtKB Domain 503 777 . . . Note=MYST-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 Q8BZ21 UniProtKB Zinc finger 206 265 . . . Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q8BZ21 UniProtKB Zinc finger 262 313 . . . Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q8BZ21 UniProtKB Zinc finger 536 561 . . . Note=C2HC MYST-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 Q8BZ21 UniProtKB Region 1 144 . . . Note=Required for activation of RUNX1-1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Region 52 166 . . . Note=Required for nuclear localization;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q8BZ21 UniProtKB Region 144 663 . . . Note=Interaction with PML;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q8BZ21 UniProtKB Region 312 663 . . . Note=Interaction with RUNX1-1;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q8BZ21 UniProtKB Region 336 377 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Region 439 466 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Region 487 777 . . . Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q8BZ21 UniProtKB Region 506 809 . . . Note=Mediates interaction with BRPF1%2C required for histone H3 acetyltransferase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q8BZ21 UniProtKB Region 784 939 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Region 983 1083 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Region 1096 1174 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Region 1197 1438 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Region 1455 1533 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Region 1511 1740 . . . Note=Interaction with PML;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q8BZ21 UniProtKB Region 1511 1636 . . . Note=Interaction with RUNX1-2;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q8BZ21 UniProtKB Region 1546 1568 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Region 1631 1707 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Region 1912 1947 . . . Note=Required for activation of RUNX1-2;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q8BZ21 UniProtKB Compositional bias 799 843 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 844 858 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 875 890 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 902 916 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 1011 1029 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 1065 1079 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 1151 1172 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 1202 1229 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 1262 1314 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 1315 1340 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 1396 1414 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 1417 1431 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 1472 1533 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Compositional bias 1638 1700 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8BZ21 UniProtKB Active site 679 679 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 Q8BZ21 UniProtKB Binding site 644 648 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Binding site 653 659 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Binding site 683 683 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 172 172 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 Q8BZ21 UniProtKB Modified residue 350 350 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 355 355 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 369 369 . . . Note=Phosphothreonine%3B by PKB/AKT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 419 419 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 472 472 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 603 603 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 786 786 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q8BZ21 UniProtKB Modified residue 813 813 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 Q8BZ21 UniProtKB Modified residue 816 816 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23806337;Dbxref=PMID:23806337 Q8BZ21 UniProtKB Modified residue 901 901 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5TKR9 Q8BZ21 UniProtKB Modified residue 941 941 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 954 954 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 1007 1007 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 1090 1090 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 1091 1091 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Modified residue 1115 1115 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Cross-link 836 836 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q8BZ21 UniProtKB Cross-link 1336 1336 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794