##gff-version 3 Q9Z2K9 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Chain 2 414 . . . ID=PRO_0000083576;Note=Isocitrate dehydrogenase [NADP] cytoplasmic Q9Z2K9 UniProtKB Binding site 75 77 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Binding site 77 77 . . . Note=In other chain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Binding site 82 82 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Binding site 94 100 . . . Note=In other chain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Binding site 109 109 . . . Note=In other chain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Binding site 132 132 . . . Note=In other chain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Binding site 212 212 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88844 Q9Z2K9 UniProtKB Binding site 252 252 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Binding site 260 260 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Binding site 275 275 . . . Note=In other chain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Binding site 279 279 . . . Note=In other chain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Binding site 310 315 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Binding site 328 328 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Site 139 139 . . . Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z2K9 UniProtKB Site 212 212 . . . Note=Critical for catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9Z2K9 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Modified residue 42 42 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Modified residue 81 81 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88844 Q9Z2K9 UniProtKB Modified residue 126 126 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88844 Q9Z2K9 UniProtKB Modified residue 224 224 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88844 Q9Z2K9 UniProtKB Modified residue 233 233 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88844 Q9Z2K9 UniProtKB Modified residue 243 243 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88844 Q9Z2K9 UniProtKB Modified residue 321 321 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O75874 Q9Z2K9 UniProtKB Modified residue 389 389 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88844 Q9Z2K9 UniProtKB Modified residue 400 400 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88844