##gff-version 3 P04406 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12665801,ECO:0000269|Ref.19;Dbxref=PMID:12665801 P04406 UniProtKB Chain 2 335 . . . ID=PRO_0000145486;Note=Glyceraldehyde-3-phosphate dehydrogenase P04406 UniProtKB Region 2 148 . . . Note=Interaction with WARS1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15628863;Dbxref=PMID:15628863 P04406 UniProtKB Motif 245 250 . . . Note=[IL]-x-C-x-x-[DE] motif;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:25417112;Dbxref=PMID:25417112 P04406 UniProtKB Active site 152 152 . . . Note=Nucleophile;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25086035;Dbxref=PMID:25086035 P04406 UniProtKB Binding site 13 14 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16239728,ECO:0000269|PubMed:16510976;Dbxref=PMID:16239728,PMID:16510976 P04406 UniProtKB Binding site 35 35 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16239728,ECO:0000269|PubMed:16510976;Dbxref=PMID:16239728,PMID:16510976 P04406 UniProtKB Binding site 80 80 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16239728,ECO:0000269|PubMed:16510976;Dbxref=PMID:16239728,PMID:16510976 P04406 UniProtKB Binding site 122 122 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16239728,ECO:0000269|PubMed:16510976;Dbxref=PMID:16239728,PMID:16510976 P04406 UniProtKB Binding site 151 153 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22513 P04406 UniProtKB Binding site 182 182 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22513 P04406 UniProtKB Binding site 211 212 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22513 P04406 UniProtKB Binding site 234 234 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P22513 P04406 UniProtKB Binding site 316 316 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16239728,ECO:0000269|PubMed:16510976;Dbxref=PMID:16239728,PMID:16510976 P04406 UniProtKB Site 179 179 . . . Note=Activates thiol group during catalysis;Ontology_term=ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:16239728,ECO:0000305|PubMed:16510976;Dbxref=PMID:16239728,PMID:16510976 P04406 UniProtKB Modified residue 5 5 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 9 9 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 42 42 . . . Note=Phosphotyrosine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:15592455;Dbxref=PMID:15592455 P04406 UniProtKB Modified residue 46 46 . . . Note=Methionine sulfoxide%3B in vitro;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:25086035;Dbxref=PMID:25086035 P04406 UniProtKB Modified residue 61 61 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P04406 UniProtKB Modified residue 64 64 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 66 66 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 70 70 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 75 75 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18183946,ECO:0007744|PubMed:20068231;Dbxref=PMID:18183946,PMID:20068231 P04406 UniProtKB Modified residue 83 83 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:17081983,PMID:18669648,PMID:20068231,PMID:21406692,PMID:23186163 P04406 UniProtKB Modified residue 122 122 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 148 148 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 149 149 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 151 151 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:23186163 P04406 UniProtKB Modified residue 152 152 . . . Note=ADP-ribosylcysteine%3B by autocatalysis%3B in irreversibly inhibited form;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04797 P04406 UniProtKB Modified residue 152 152 . . . Note=Cysteine persulfide;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P16858 P04406 UniProtKB Modified residue 152 152 . . . Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04797 P04406 UniProtKB Modified residue 152 152 . . . Note=S-nitrosocysteine%3B in reversibly inhibited form;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04797 P04406 UniProtKB Modified residue 153 153 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P04406 UniProtKB Modified residue 155 155 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 177 177 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P04406 UniProtKB Modified residue 182 182 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P04406 UniProtKB Modified residue 184 184 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:24275569;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:24275569 P04406 UniProtKB Modified residue 194 194 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 194 194 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P04406 UniProtKB Modified residue 194 194 . . . Note=N6-malonyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21908771;Dbxref=PMID:21908771 P04406 UniProtKB Modified residue 211 211 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19690332;Dbxref=PMID:19690332 P04406 UniProtKB Modified residue 215 215 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 215 215 . . . Note=N6-malonyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21908771;Dbxref=PMID:21908771 P04406 UniProtKB Modified residue 219 219 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P04406 UniProtKB Modified residue 225 225 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 227 227 . . . Note=N6%2CN6-dimethyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 227 227 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P04406 UniProtKB Modified residue 229 229 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18183946,ECO:0007744|PubMed:23186163;Dbxref=PMID:18183946,PMID:23186163 P04406 UniProtKB Modified residue 237 237 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 241 241 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P04406 UniProtKB Modified residue 247 247 . . . Note=S-(2-succinyl)cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04797 P04406 UniProtKB Modified residue 247 247 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22771119,ECO:0000269|PubMed:25417112;Dbxref=PMID:22771119,PMID:25417112 P04406 UniProtKB Modified residue 254 254 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P04406 UniProtKB Modified residue 260 260 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 263 263 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 312 312 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18183946,ECO:0007744|PubMed:19690332;Dbxref=PMID:18183946,PMID:19690332 P04406 UniProtKB Modified residue 316 316 . . . Note=Deamidated asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Modified residue 333 333 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P04406 UniProtKB Modified residue 334 334 . . . Note=N6%2CN6-dimethyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18183946;Dbxref=PMID:18183946 P04406 UniProtKB Glycosylation 197 197 . . . Note=(Microbial infection) N-beta-linked (GlcNAc) arginine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28522607;Dbxref=PMID:28522607 P04406 UniProtKB Glycosylation 200 200 . . . Note=(Microbial infection) N-beta-linked (GlcNAc) arginine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28522607;Dbxref=PMID:28522607 P04406 UniProtKB Cross-link 186 186 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:28112733;Dbxref=PMID:28112733 P04406 UniProtKB Alternative sequence 1 42 . . . ID=VSP_047289;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04406 UniProtKB Natural variant 22 22 . . . ID=VAR_018889;Note=A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.12;Dbxref=dbSNP:rs45541435 P04406 UniProtKB Natural variant 251 251 . . . ID=VAR_049218;Note=K->N;Dbxref=dbSNP:rs1062429 P04406 UniProtKB Mutagenesis 46 46 . . . Note=Drastic reduction of the extent and significant prolongation of the lag phase of free radical-induced aggregation. M->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25086035;Dbxref=PMID:25086035 P04406 UniProtKB Mutagenesis 105 105 . . . Note=Increased resistance to free radical-induced aggregation. M->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25086035;Dbxref=PMID:25086035 P04406 UniProtKB Mutagenesis 152 152 . . . Note=Markedly reduced glycolytic activity%3B when associated with S-156 and S-247. Forms free radical-induced aggregates%2C but to a lesser extent than wild-type protein%3B when associated with S-156 and S-247. Abolished interaction with TRAF2 and TRAF3. C->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23332158,ECO:0000269|PubMed:25086035,ECO:0000269|PubMed:27387501;Dbxref=PMID:23332158,PMID:25086035,PMID:27387501 P04406 UniProtKB Mutagenesis 156 156 . . . Note=Markedly reduced glycolytic activity%3B when associated with S-152 and S-247. Forms free radical-induced aggregates%2C but to a lesser extent than wild-type protein%3B when associated with S-156 and S-247. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25086035;Dbxref=PMID:25086035 P04406 UniProtKB Mutagenesis 196 196 . . . Note=Increased free radical-induced aggregation. W->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25086035;Dbxref=PMID:25086035 P04406 UniProtKB Mutagenesis 211 211 . . . Note=Does not affect glycosylation by C.rodentium protein NleB. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23332158;Dbxref=PMID:23332158 P04406 UniProtKB Mutagenesis 229 229 . . . Note=Does not affect glycosylation by C.rodentium protein NleB. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23332158;Dbxref=PMID:23332158 P04406 UniProtKB Mutagenesis 241 241 . . . Note=Does not affect glycosylation by C.rodentium protein NleB. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23332158;Dbxref=PMID:23332158 P04406 UniProtKB Mutagenesis 245 245 . . . Note=Inhibits S-nitrosylation of Cys-247%3B when associated with M-250. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25417112;Dbxref=PMID:25417112 P04406 UniProtKB Mutagenesis 246 246 . . . Note=Does not affect glycosylation by C.rodentium protein NleB. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23332158;Dbxref=PMID:23332158 P04406 UniProtKB Mutagenesis 247 247 . . . Note=Markedly reduced glycolytic activity%3B when associated with S-152 and S-156. Forms free radical-induced aggregates%2C but to a lesser extent than wild-type protein%3B when associated with S-156 and S-247. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25086035;Dbxref=PMID:25086035 P04406 UniProtKB Mutagenesis 250 250 . . . Note=Inhibits S-nitrosylation of Cys-247%3B when associated with M-245. E->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25417112;Dbxref=PMID:25417112 P04406 UniProtKB Mutagenesis 277 277 . . . Note=Does not affect glycosylation by C.rodentium protein NleB. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23332158;Dbxref=PMID:23332158 P04406 UniProtKB Mutagenesis 320 320 . . . Note=No effect on free radical-induced aggregation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25086035;Dbxref=PMID:25086035 P04406 UniProtKB Sequence conflict 225 225 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P04406 UniProtKB Beta strand 5 9 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 13 25 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 27 34 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 36 38 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 40 48 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Turn 51 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 60 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 66 69 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 72 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 82 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 88 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 94 97 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 99 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 105 108 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 110 113 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 117 123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 126 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Turn 133 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 137 139 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 146 148 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 152 168 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 170 179 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 185 189 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 196 199 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Turn 202 204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 207 210 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 213 220 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 222 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 227 234 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 241 251 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 255 267 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Turn 268 273 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 274 277 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 283 286 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 292 296 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Turn 297 299 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 301 304 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Beta strand 307 314 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND P04406 UniProtKB Helix 318 333 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6YND