Gapdh
entrez
14433
canonical
uniprot
P16858
canonical
ensembl
ENSMUSG00000057666
resolver
ensp
ENSMUSP00000073289
resolver
ensp
ENSMUSP00000113213
resolver
ensp
ENSMUSP00000113942
resolver
ensp
ENSMUSP00000138508
resolver
enst
ENSMUST00000073605
resolver
enst
ENSMUST00000117757
resolver
enst
ENSMUST00000118875
resolver
genesymbol
Gapdh
resolver
genesymbol_syn
GAPDH
resolver
genesymbol_syn
Gapd
resolver
uniprot
A0A0A0MQF6
resolver
uniprot
A6H6A8
resolver
uniprot
D2KHZ9
resolver
uniprot
Q0QEU0
resolver
uniprot
Q3THM2
resolver
uniprot
Q3TUI2
resolver
uniprot
Q3UMT2
resolver
uniprot
Q4V783
resolver
uniprot
Q569X2
resolver
uniprot
Q569X5
resolver
uniprot
Q5U410
resolver
uniprot_entry
A0A0A0MQF6_MOUSE
resolver
uniprot_entry
D2KHZ9_MOUSE
resolver
uniprot_entry
G3P_MOUSE
resolver
uniprot_sec
A6H6A8
resolver
uniprot_sec
Q0QEU0
resolver
uniprot_sec
Q3THM2
resolver
uniprot_sec
Q3TUI2
resolver
uniprot_sec
Q3UMT2
resolver
uniprot_sec
Q4V783
resolver
uniprot_sec
Q569X2
resolver
uniprot_sec
Q569X5
resolver
uniprot_sec
Q5U410
resolver
activity_regulation
ACTIVITY REGULATION: Glyceraldehyde-3-phosphate dehydrogenase activity is inhibited by fumarate, via the formation of S-(2-succinyl)cysteine residues. {ECO:0000250|UniProtKB:P04797}.
uniprot
proteins
amino_acid_sequence
MVKVGVNGFGRIGRLVTRAAICSGKVEIVAINDPFIDLNYMVYMFQYDSTHGKFNGTVKAENGKLVINGKPITIFQERDPTNIKWGEAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEDQVVSCDFNSNSHSSTFDAGAGIALNDNFVKLISWYDNEYGYSNRVVDLMAYMASKE
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:19903941). Also shows nitrosylase activity, thereby playing a role in nuclear functions (PubMed:19903941). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). 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 (PubMed:23071094). 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. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). {ECO:0000250|UniProtKB:P04797, ECO:0000250|UniProtKB:P10096, ECO:0000269|PubMed:19903941, ECO:0000269|PubMed:23071094}.
uniprot
proteins
mass_dalton
35810
uniprot
proteins
mutagenesis
MUTAGEN 150; /note="C->S: Abolishes sulfhydration and induces impaired enzyme activity."; /evidence="ECO:0000269|PubMed:19903941
uniprot
proteins
pathway_participation
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
uniprot
proteins
post_translational_modification
PTM: ISGylated. {ECO:0000250|UniProtKB:P04406}.; PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus 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:0000250|UniProtKB:P04797}.; PTM: Sulfhydration at Cys-150 increases catalytic activity. {ECO:0000269|PubMed:19903941}.; 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 mammals. 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:0000250|UniProtKB:P04797}.
uniprot
proteins
protein_family
Glyceraldehyde-3-phosphate dehydrogenase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16751257
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19903941
uniprot
proteins
pubmed
2145197
uniprot
proteins
pubmed
23071094
uniprot
proteins
sequence_length
333
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. Colocalizes with CHP1 to small punctate structures along the microtubules tracks. {ECO:0000250|UniProtKB:P04797}.
uniprot
proteins