Gapdh
entrez
24383
canonical
uniprot
P04797
canonical
ensembl
ENSRNOG00000018630
resolver
ensembl
ENSRNOG00055006222
resolver
ensembl
ENSRNOG00055009333
resolver
ensembl
ENSRNOG00055030697
resolver
ensembl
ENSRNOG00060032665
resolver
ensembl
ENSRNOG00065020177
resolver
ensembl
ENSRNOG00065032955
resolver
ensp
ENSRNOP00000040878
resolver
ensp
ENSRNOP00055007825
resolver
ensp
ENSRNOP00055012671
resolver
ensp
ENSRNOP00055044021
resolver
ensp
ENSRNOP00060046787
resolver
ensp
ENSRNOP00065027256
resolver
ensp
ENSRNOP00065046675
resolver
enst
ENSRNOT00000050443
resolver
enst
ENSRNOT00055010101
resolver
enst
ENSRNOT00055015786
resolver
enst
ENSRNOT00055053257
resolver
enst
ENSRNOT00060056622
resolver
enst
ENSRNOT00065034039
resolver
enst
ENSRNOT00065056696
resolver
genesymbol
Gapdh
resolver
genesymbol_syn
Gapd
resolver
uniprot
P09328
resolver
uniprot
Q5M916
resolver
uniprot
Q9QWU4
resolver
uniprot_entry
G3P_RAT
resolver
uniprot_sec
P09328
resolver
uniprot_sec
Q5M916
resolver
uniprot_sec
Q9QWU4
resolver
activity_regulation
ACTIVITY REGULATION: Glyceraldehyde-3-phosphate dehydrogenase activity is inhibited by fumarate, via the formation of S-(2-succinyl)cysteine residues. {ECO:0000269|PubMed:17934141}.
uniprot
proteins
amino_acid_sequence
MVKVGVNGFGRIGRLVTRAAFSCDKVDIVAINDPFIDLNYMVYMFQYDSTHGKFNGTVKAENGKLVINGKPITIFQERDPANIKWGDAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKKVVKQAAEGPLKGILGYTEDQVVSCDFNSNSHSSTFDAGAGIALNDNFVKLISWYDNEYGYSNRVVDLMAYMASKE
uniprot
proteins
ec_number
1.2.1.12
uniprot
proteins
ec_number
2.6.99.-
uniprot
proteins
function
FUNCTION: Catalyzes the conversion of D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate in glycolysis and the reverse reaction in gluconeogenesis (PubMed:17934141). Also shows nitrosylase activity, thereby playing a role in nuclear functions (PubMed:15951807, PubMed:20972425). Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (PubMed:15312048). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (By similarity). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (PubMed:10424669, PubMed:15951807, PubMed:20972425). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (PubMed:15951807, PubMed:20972425). {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P10096, ECO:0000269|PubMed:10424669, ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:17934141, ECO:0000269|PubMed:20972425}.
uniprot
proteins
mass_dalton
35828
uniprot
proteins
mutagenesis
MUTAGEN 149; /note="S->A: Does not affect interaction with SIRT1."; /evidence="ECO:0000269|PubMed:20972425"; MUTAGEN 150; /note="C->S: Abolishes S-nitrosylation and subsequent nuclear translocation."; /evidence="ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:20972425"; MUTAGEN 151; /note="T->A: Does not affect interaction with SIRT1."; /evidence="ECO:0000269|PubMed:20972425"; MUTAGEN 152; /note="T->A: Abolishes interaction and subsequent nitrosylation of SIRT1."; /evidence="ECO:0000269|PubMed:20972425"; MUTAGEN 225; /note="K->A: Abolishes interaction with SIAH1."; /evidence="ECO:0000269|PubMed:15951807"; MUTAGEN 234; /note="P->A: Does not affect interaction with SIAH1."; /evidence="ECO:0000269|PubMed:15951807"; MUTAGEN 235; /note="T->A: Does not affect interaction with SIAH1."; /evidence="ECO:0000269|PubMed:15951807
uniprot
proteins
pathway_participation
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
uniprot
proteins
post_translational_modification
PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus (PubMed:1281150, PubMed:15951807, PubMed:20972425, PubMed:8626764). The effect of S-nitrosylation on enzymatic activity is unclear: according to some authors, it inhibits enzymatic activity and increases endogenous ADP-ribosylation, inhibiting the enzyme in a non-reversible manner (PubMed:8626764). According to others, it does not affect glycolysis (PubMed:15951807). ADP-ribosylation is likely to be a pathophysiological event associated with inhibition of gluconeogenesis (PubMed:8626764). S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity (By similarity). {ECO:0000250|UniProtKB:P04406, ECO:0000269|PubMed:1281150, ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:20972425, ECO:0000269|PubMed:8626764}.; PTM: ISGylated. {ECO:0000250|UniProtKB:P04406}.; PTM: Sulfhydration at Cys-150 increases catalytic activity. {ECO:0000250|UniProtKB:P16858}.; PTM: Oxidative stress can promote the formation of high molecular weight disulfide-linked GAPDH aggregates, through a process called nucleocytoplasmic coagulation. {ECO:0000250|UniProtKB:P04406}.; PTM: Succination of Cys-150 and Cys-245 by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits glyceraldehyde-3-phosphate dehydrogenase activity. Fumarate concentration as well as succination of cysteine residues in GAPDH is significantly increased in muscle of diabetic rats. It was proposed that the S-(2-succinyl)cysteine chemical modification may be a useful biomarker of mitochondrial and oxidative stress in diabetes and that succination of GAPDH and other thiol proteins by fumarate may contribute to the metabolic changes underlying the development of diabetes complications. {ECO:0000269|PubMed:17934141}.
uniprot
proteins
protein_family
Glyceraldehyde-3-phosphate dehydrogenase family
uniprot
proteins
pubmed
10424669
uniprot
proteins
pubmed
1281150
uniprot
proteins
pubmed
15312048
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15951807
uniprot
proteins
pubmed
17934141
uniprot
proteins
pubmed
19607794
uniprot
proteins
pubmed
20972425
uniprot
proteins
pubmed
2413848
uniprot
proteins
pubmed
2987824
uniprot
proteins
pubmed
2987855
uniprot
proteins
pubmed
3585333
uniprot
proteins
pubmed
6548307
uniprot
proteins
pubmed
8626764
uniprot
proteins
sequence_length
333
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:19607794}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15312048}. Nucleus {ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:19607794, ECO:0000269|PubMed:20972425}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (PubMed:15951807). Colocalizes with CHP1 to small punctate structures along the microtubules tracks (PubMed:15312048). {ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15951807}.
uniprot
proteins