##gff-version 3 P17244 UniProtKB Chain 1 333 . . . ID=PRO_0000145484;Note=Glyceraldehyde-3-phosphate dehydrogenase P17244 UniProtKB Region 1 146 . . . Note=Interaction with WARS1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Motif 243 248 . . . Note=[IL]-x-C-x-x-[DE] motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Active site 150 150 . . . Note=Nucleophile;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10009 P17244 UniProtKB Binding site 11 12 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Binding site 33 33 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Binding site 78 78 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Binding site 120 120 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Binding site 149 151 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22513 P17244 UniProtKB Binding site 180 180 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22513 P17244 UniProtKB Binding site 209 210 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22513 P17244 UniProtKB Binding site 232 232 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22513 P17244 UniProtKB Binding site 314 314 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Site 177 177 . . . Note=Activates thiol group during catalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 3 3 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 7 7 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 40 40 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 59 59 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 62 62 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 64 64 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 68 68 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 73 73 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 120 120 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 146 146 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 147 147 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 149 149 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 150 150 . . . Note=ADP-ribosylcysteine%3B by autocatalysis%3B in irreversibly inhibited form;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04797 P17244 UniProtKB Modified residue 150 150 . . . Note=Cysteine persulfide;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16858 P17244 UniProtKB Modified residue 150 150 . . . Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04797 P17244 UniProtKB Modified residue 150 150 . . . Note=S-nitrosocysteine%3B in reversibly inhibited form;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04797 P17244 UniProtKB Modified residue 151 151 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 153 153 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 175 175 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 180 180 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 182 182 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 192 192 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 192 192 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 192 192 . . . Note=N6-malonyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 209 209 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 213 213 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 213 213 . . . Note=N6-malonyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 217 217 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 223 223 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 225 225 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 225 225 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 227 227 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 235 235 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 239 239 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 245 245 . . . Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04797 P17244 UniProtKB Modified residue 245 245 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 252 252 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 258 258 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 261 261 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 310 310 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 314 314 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 331 331 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Modified residue 332 332 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406 P17244 UniProtKB Cross-link 184 184 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04406