V9HVZ4 · V9HVZ4_HUMAN
- ProteinGlyceraldehyde-3-phosphate dehydrogenase
- GeneHEL-S-162eP
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids335 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
Catalytic activity
- D-glyceraldehyde 3-phosphate + NAD+ + phosphate = (2R)-3-phospho-glyceroyl phosphate + H+ + NADH
- L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein]This reaction proceeds in the forward direction.
Pathway
Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 13-14 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: RI | ||||||
Binding site | 35 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 80 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 122 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 151-153 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: SCT | ||||||
Active site | 152 | Nucleophile | ||||
Sequence: C | ||||||
Site | 179 | Activates thiol group during catalysis | ||||
Sequence: H | ||||||
Binding site | 182 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 211-212 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: TG | ||||||
Binding site | 234 | D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 316 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | nuclear membrane | |
Cellular Component | plasma membrane | |
Molecular Function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | |
Molecular Function | NAD binding | |
Molecular Function | NADP binding | |
Molecular Function | peptidyl-cysteine S-nitrosylase activity | |
Biological Process | apoptotic process | |
Biological Process | glucose metabolic process | |
Biological Process | glycolytic process | |
Biological Process | regulation of translation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlyceraldehyde-3-phosphate dehydrogenase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionV9HVZ4
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Organism-specific databases
PTM/Processing
Keywords
- PTM
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-152 | Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding | ||||
Sequence: VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMVYMFQYDSTHGKFHGTVKAENGKLVINGNPITIFQERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASC |
Sequence similarities
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length335
- Mass (Da)36,053
- Last updated2014-03-19 v1
- ChecksumC9C135E8AE3E8744
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
EU668321 EMBL· GenBank· DDBJ | ACF94474.1 EMBL· GenBank· DDBJ | mRNA |