##gff-version 3 Q5RCH1 UniProtKB Chain 1 297 . . . ID=PRO_0000085726;Note=Cyclin-dependent kinase 1 Q5RCH1 UniProtKB Domain 4 287 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q5RCH1 UniProtKB Active site 128 128 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 Q5RCH1 UniProtKB Binding site 10 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q5RCH1 UniProtKB Binding site 33 33 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q5RCH1 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 4 4 . . . Note=Phosphotyrosine%3B by PKR;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 6 6 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 9 9 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11440 Q5RCH1 UniProtKB Modified residue 14 14 . . . Note=Phosphothreonine%3B by PKMYT1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 15 15 . . . Note=Phosphotyrosine%3B by PKMYT1%2C WEE1 and WEE2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 15 15 . . . Note=Phosphotyrosine%3B by WEE1 and WEE2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 19 19 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 39 39 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 77 77 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 141 141 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 161 161 . . . Note=Phosphothreonine%3B by CAK;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 178 178 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 222 222 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Modified residue 245 245 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11440 Q5RCH1 UniProtKB Modified residue 248 248 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Cross-link 6 6 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Cross-link 9 9 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Cross-link 20 20 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493 Q5RCH1 UniProtKB Cross-link 139 139 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06493