##gff-version 3 Q810T5 UniProtKB Chain 1 612 . . . ID=PRO_0000051571;Note=Histone acetyltransferase KAT7 Q810T5 UniProtKB Domain 333 608 . . . Note=MYST-type HAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 Q810T5 UniProtKB Zinc finger 177 220 . . . Note=CCHHC-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01143 Q810T5 UniProtKB Zinc finger 366 391 . . . Note=C2HC MYST-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01063 Q810T5 UniProtKB Region 1 174 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810T5 UniProtKB Compositional bias 20 39 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810T5 UniProtKB Compositional bias 40 107 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810T5 UniProtKB Compositional bias 108 124 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810T5 UniProtKB Compositional bias 125 152 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810T5 UniProtKB Compositional bias 154 174 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q810T5 UniProtKB Active site 509 509 . . . Note=Proton donor/acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 Q810T5 UniProtKB Binding site 186 186 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01143 Q810T5 UniProtKB Binding site 191 191 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01143 Q810T5 UniProtKB Binding site 204 204 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01143 Q810T5 UniProtKB Binding site 210 210 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01143 Q810T5 UniProtKB Binding site 369 369 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Binding site 372 372 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Binding site 385 385 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Binding site 389 389 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Binding site 476 478 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Binding site 484 489 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Binding site 513 513 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Binding site 522 522 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 11 11 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 51 51 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 54 54 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 58 58 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 Q810T5 UniProtKB Modified residue 65 65 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 86 86 . . . Note=Phosphothreonine%3B by CDK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 89 89 . . . Note=Phosphothreonine%3B by CDK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 103 103 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903 Q810T5 UniProtKB Modified residue 105 105 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SVQ0 Q810T5 UniProtKB Modified residue 112 112 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 125 125 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 129 129 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SVQ0 Q810T5 UniProtKB Modified residue 159 159 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 163 163 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 165 165 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 179 179 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 200 200 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Modified residue 278 278 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5SVQ0 Q810T5 UniProtKB Modified residue 433 433 . . . Note=N6-acetyllysine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H7Z6 Q810T5 UniProtKB Modified residue 507 507 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Cross-link 324 324 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Cross-link 339 339 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O95251 Q810T5 UniProtKB Alternative sequence 223 252 . . . ID=VSP_014585;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|Ref.1