##gff-version 3 Q5TKR9 UniProtKB Chain 1 1998 . . . ID=PRO_0000051574;Note=Histone acetyltransferase KAT6A Q5TKR9 UniProtKB Domain 1 77 . . . Note=SAMD1-like winged helix (WH);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01358 Q5TKR9 UniProtKB Domain 95 171 . . . Note=H15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00837 Q5TKR9 UniProtKB Domain 502 776 . . . Note=MYST-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 Q5TKR9 UniProtKB Zinc finger 199 258 . . . Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q5TKR9 UniProtKB Zinc finger 255 306 . . . Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146 Q5TKR9 UniProtKB Zinc finger 535 560 . . . Note=C2HC MYST-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 Q5TKR9 UniProtKB Region 1 144 . . . Note=Required for activation of RUNX1-1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Region 52 166 . . . Note=Required for nuclear localization;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5TKR9 UniProtKB Region 72 93 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Region 144 662 . . . Note=Interaction with PML;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5TKR9 UniProtKB Region 312 662 . . . Note=Interaction with RUNX1-1;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5TKR9 UniProtKB Region 336 377 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Region 440 464 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Region 486 776 . . . Note=Catalytic;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5TKR9 UniProtKB Region 505 808 . . . Note=Mediates interaction with BRPF1%2C required for histone H3 acetyltransferase activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5TKR9 UniProtKB Region 783 947 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Region 982 1079 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Region 1096 1175 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Region 1195 1436 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Region 1450 1567 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Region 1510 1735 . . . Note=Interaction with PML;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5TKR9 UniProtKB Region 1510 1635 . . . Note=Interaction with RUNX1-2;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5TKR9 UniProtKB Region 1630 1702 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Region 1907 1942 . . . Note=Required for activation of RUNX1-2;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q5TKR9 UniProtKB Compositional bias 444 457 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 785 797 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 798 840 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 865 874 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 875 886 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 903 916 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1008 1029 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1030 1041 . . . Note=Low complexity;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1042 1052 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1064 1077 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1106 1119 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1135 1146 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1147 1173 . . . Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1203 1228 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1229 1240 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1281 1298 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1316 1333 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1351 1360 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1392 1413 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1472 1496 . . . Note=Low complexity;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1501 1522 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1527 1541 . . . Note=Low complexity;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1549 1567 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1639 1658 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Compositional bias 1665 1693 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q5TKR9 UniProtKB Active site 678 678 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 Q5TKR9 UniProtKB Binding site 643 647 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Binding site 652 658 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Binding site 682 682 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 172 172 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8BZ21 Q5TKR9 UniProtKB Modified residue 350 350 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 355 355 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 369 369 . . . Note=Phosphothreonine%3B by PKB/AKT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 419 419 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 471 471 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 602 602 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 785 785 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8BZ21 Q5TKR9 UniProtKB Modified residue 815 815 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q8BZ21 Q5TKR9 UniProtKB Modified residue 900 900 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:16641100;Dbxref=PMID:16641100 Q5TKR9 UniProtKB Modified residue 940 940 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 953 953 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 1006 1006 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 1006 1006 . . . Note=N6-crotonyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 1013 1013 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 1013 1013 . . . Note=N6-crotonyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 1088 1088 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 1089 1089 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794 Q5TKR9 UniProtKB Modified residue 1114 1114 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 Q5TKR9 UniProtKB Cross-link 835 835 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92794