##gff-version 3 Q6RI85 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Chain 2 417 . . . ID=PRO_0000145838;Note=Phosphoglycerate kinase 2 Q6RI85 UniProtKB Binding site 24 26 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q6RI85 UniProtKB Binding site 39 39 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q6RI85 UniProtKB Binding site 63 66 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q6RI85 UniProtKB Binding site 123 123 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q6RI85 UniProtKB Binding site 171 171 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q6RI85 UniProtKB Binding site 220 220 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q6RI85 UniProtKB Binding site 344 344 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q6RI85 UniProtKB Binding site 373 376 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q6RI85 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 4 4 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 11 11 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 75 75 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 86 86 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 97 97 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 131 131 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 146 146 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 196 196 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 199 199 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 267 267 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Modified residue 291 291 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P00558 Q6RI85 UniProtKB Natural variant 102 102 . . . Note=In SNP-A%3B possible loss of CK2 phosphorylation site. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15599558;Dbxref=PMID:15599558 Q6RI85 UniProtKB Natural variant 264 264 . . . Note=In SNP-B%3B increased semen volume in ejaculate. T->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15599558;Dbxref=PMID:15599558 Q6RI85 UniProtKB Sequence conflict 324 324 . . . Note=Y->N;Ontology_term=ECO:0000305;evidence=ECO:0000305