G3P_RAT
ID G3P_RAT Reviewed; 333 AA.
AC P04797; P09328; Q5M916; Q9QWU4;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12 {ECO:0000305|PubMed:17934141};
DE AltName: Full=38 kDa BFA-dependent ADP-ribosylation substrate;
DE AltName: Full=BARS-38;
DE AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH {ECO:0000305};
DE EC=2.6.99.- {ECO:0000269|PubMed:20972425};
GN Name=Gapdh; Synonyms=Gapd;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Muscle;
RX PubMed=2987824; DOI=10.1093/nar/13.5.1431;
RA Fort P., Marty L., Piechaczyk M., el Sabrouty S., Dani C., Jeanteur P.,
RA Blanchard J.-M.;
RT "Various rat adult tissues express only one major mRNA species from the
RT glyceraldehyde-3-phosphate-dehydrogenase multigenic family.";
RL Nucleic Acids Res. 13:1431-1442(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2987855; DOI=10.1093/nar/13.7.2485;
RA Tso J.Y., Sun X.-H., Kao T.-H., Reece K.S., Wu R.;
RT "Isolation and characterization of rat and human glyceraldehyde-3-phosphate
RT dehydrogenase cDNAs: genomic complexity and molecular evolution of the
RT gene.";
RL Nucleic Acids Res. 13:2485-2502(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
RX PubMed=10424669; DOI=10.1097/00001756-199907130-00007;
RA Tajima H., Tsuchiya K., Yamada M., Kondo K., Katsube N., Ishitani R.;
RT "Over-expression of GAPDH induces apoptosis in COS-7 cells transfected with
RT cloned GAPDH cDNAs.";
RL NeuroReport 10:2029-2033(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Zheng J., Ramirez V.D.;
RT "Isolation of a glyceraldehyde-3-phosphate dehydrogenase (GAPDH) cDNA
RT isoform from rat brain by a rapid PCR-based cloning method and its
RT expression by RT-PCR.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Pituitary anterior lobe;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 65-105; 116-137; 144-184; 233-246 AND 308-321, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 235-333.
RC TISSUE=Brain;
RX PubMed=3585333; DOI=10.1111/j.1471-4159.1987.tb03420.x;
RA Leung T.K.C., Hall C., Monfries C., Lim L.;
RT "Trifluoperazine activates and releases latent ATP-generating enzymes
RT associated with the synaptic plasma membrane.";
RL J. Neurochem. 49:232-238(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 261-323, AND TISSUE SPECIFICITY.
RC TISSUE=Glial tumor;
RX PubMed=6548307; DOI=10.1093/nar/12.18.6951;
RA Piechaczyk M., Blanchard J.-M., Marty L., Dani C., Panabieres F.,
RA el Sabrouty S., Fort P., Jeanteur P.;
RT "Post-transcriptional regulation of glyceraldehyde-3-phosphate-
RT dehydrogenase gene expression in rat tissues.";
RL Nucleic Acids Res. 12:6951-6963(1984).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 267-333.
RX PubMed=2413848; DOI=10.1016/0006-291x(85)91310-5;
RA Maehara Y., Fujiyoshi T., Takahashi K., Yamamoto M., Endo H.;
RT "1.5 kb mRNA abundantly expressed in rat tumors encodes a 37 kilodalton
RT protein in vitro.";
RL Biochem. Biophys. Res. Commun. 131:800-805(1985).
RN [10]
RP S-NITROSYLATION.
RX PubMed=1281150; DOI=10.1016/s0021-9258(19)73985-4;
RA Molina y Vedia L., McDonald B., Reep B., Brune B., Di Silvio M.,
RA Billiar T.R., Lapetina E.G.;
RT "Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate
RT dehydrogenase inhibits enzymatic activity and increases endogenous ADP-
RT ribosylation.";
RL J. Biol. Chem. 267:24929-24932(1992).
RN [11]
RP S-NITROSYLATION AT CYS-150, ADP-RIBOSYLATION AT CYS-150, LACK OF
RP S-NITROSYLATION AT CYS-154, AND ACTIVE SITE.
RX PubMed=8626764; DOI=10.1074/jbc.271.8.4209;
RA Mohr S., Stamler J.S., Brune B.;
RT "Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenase
RT by S-nitrosylation and subsequent NADH attachment.";
RL J. Biol. Chem. 271:4209-4214(1996).
RN [12]
RP FUNCTION, INTERACTION WITH CHP1, ASSOCIATION WITH MICROTUBULES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15312048; DOI=10.1042/bj20040622;
RA Andrade J., Pearce S.T., Zhao H., Barroso M.;
RT "Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and
RT microtubules.";
RL Biochem. J. 384:327-336(2004).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SIAH1, S-NITROSYLATION AT
RP CYS-150, AND MUTAGENESIS OF CYS-150; LYS-225; PRO-234 AND THR-235.
RX PubMed=15951807; DOI=10.1038/ncb1268;
RA Hara M.R., Agrawal N., Kim S.F., Cascio M.B., Fujimuro M., Ozeki Y.,
RA Takahashi M., Cheah J.H., Tankou S.K., Hester L.D., Ferris C.D.,
RA Hayward S.D., Snyder S.H., Sawa A.;
RT "S-nitrosylated GAPDH initiates apoptotic cell death by nuclear
RT translocation following Siah1 binding.";
RL Nat. Cell Biol. 7:665-674(2005).
RN [14]
RP SUCCINATION AT CYS-150 AND CYS-245, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=17934141; DOI=10.2337/db07-0838;
RA Blatnik M., Frizzell N., Thorpe S.R., Baynes J.W.;
RT "Inactivation of glyceraldehyde-3-phosphate dehydrogenase by fumarate in
RT diabetes: formation of S-(2-succinyl)cysteine, a novel chemical
RT modification of protein and possible biomarker of mitochondrial stress.";
RL Diabetes 57:41-49(2008).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RILPL1 AND SIAH1.
RX PubMed=19607794; DOI=10.1016/j.neuron.2009.05.024;
RA Sen N., Hara M.R., Ahmad A.S., Cascio M.B., Kamiya A., Ehmsen J.T.,
RA Agrawal N., Hester L., Dore S., Snyder S.H., Sawa A.;
RT "GOSPEL: a neuroprotective protein that binds to GAPDH upon S-
RT nitrosylation.";
RL Neuron 63:81-91(2009).
RN [16]
RP FUNCTION AS NITROSYLASE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP S-NITROSYLATION AT CYS-150, AND MUTAGENESIS OF SER-149; CYS-150; THR-151
RP AND THR-152.
RX PubMed=20972425; DOI=10.1038/ncb2114;
RA Kornberg M.D., Sen N., Hara M.R., Juluri K.R., Nguyen J.V., Snowman A.M.,
RA Law L., Hester L.D., Snyder S.H.;
RT "GAPDH mediates nitrosylation of nuclear proteins.";
RL Nat. Cell Biol. 12:1094-1100(2010).
CC -!- FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and
CC nitrosylase activities, thereby playing a role in glycolysis and
CC nuclear functions, respectively (PubMed:17934141, PubMed:15951807,
CC PubMed:20972425). Glyceraldehyde-3-phosphate dehydrogenase is a key
CC enzyme in glycolysis that catalyzes the first step of the pathway by
CC converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-
CC glyceroyl phosphate (PubMed:17934141). Modulates the organization and
CC assembly of the cytoskeleton. Facilitates the CHP1-dependent
CC microtubule and membrane associations through its ability to stimulate
CC the binding of CHP1 to microtubules (PubMed:15312048). Component of the
CC GAIT (gamma interferon-activated inhibitor of translation) complex
CC which mediates interferon-gamma-induced transcript-selective
CC translation inhibition in inflammation processes. Upon interferon-gamma
CC treatment assembles into the GAIT complex which binds to stem loop-
CC containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs
CC (such as ceruplasmin) and suppresses their translation (By similarity).
CC Also plays a role in innate immunity by promoting TNF-induced NF-kappa-
CC B activation and type I interferon production, via interaction with
CC TRAF2 and TRAF3, respectively (By similarity). Participates in nuclear
CC events including transcription, RNA transport, DNA replication and
CC apoptosis (PubMed:10424669, PubMed:15951807, PubMed:20972425). Nuclear
CC functions are probably due to the nitrosylase activity that mediates
CC cysteine S-nitrosylation of nuclear target proteins such as SIRT1,
CC HDAC2 and PRKDC (PubMed:15951807, PubMed:20972425).
CC {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P10096,
CC ECO:0000269|PubMed:10424669, ECO:0000269|PubMed:15312048,
CC ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:17934141,
CC ECO:0000269|PubMed:20972425}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10009,
CC ECO:0000305|PubMed:17934141};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-
CC cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089,
CC Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:149494; Evidence={ECO:0000269|PubMed:20972425};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685;
CC Evidence={ECO:0000269|PubMed:20972425};
CC -!- ACTIVITY REGULATION: Glyceraldehyde-3-phosphate dehydrogenase activity
CC is inhibited by fumarate, via the formation of S-(2-succinyl)cysteine
CC residues. {ECO:0000269|PubMed:17934141}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with TPPP; the
CC interaction is direct (By similarity). Interacts (when S-nitrosylated)
CC with SIAH1; leading to nuclear translocation (PubMed:15951807,
CC PubMed:19607794). Interacts with RILPL1/GOSPEL, leading to prevent the
CC interaction between GAPDH and SIAH1 and prevent nuclear translocation
CC (PubMed:19607794). Interacts with CHP1; the interaction increases the
CC binding of CHP1 with microtubules (PubMed:15312048). Associates with
CC microtubules (PubMed:15312048). Interacts with EIF1AD, USP25, PRKCI and
CC WARS1. Interacts with phosphorylated RPL13A; inhibited by oxidatively-
CC modified low-densitity lipoprotein (LDL(ox)). Component of the GAIT
CC complex. Interacts with FKBP6; leading to inhibit GAPDH catalytic
CC activity. Interacts with TRAF2, promoting TRAF2 ubiquitination.
CC Interacts with TRAF3, promoting TRAF3 ubiquitination (By similarity).
CC {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P10096,
CC ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15951807,
CC ECO:0000269|PubMed:19607794}.
CC -!- INTERACTION:
CC P04797; P47196: Akt1; NbExp=3; IntAct=EBI-349219, EBI-7204362;
CC P04797; P61023: Chp1; NbExp=3; IntAct=EBI-349219, EBI-917838;
CC P04797; Q80Z30: Ppm1e; NbExp=5; IntAct=EBI-349219, EBI-7473061;
CC P04797; P19357: Slc2a4; NbExp=2; IntAct=EBI-349219, EBI-915426;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15312048,
CC ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:19607794}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:15312048}. Nucleus
CC {ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:19607794,
CC ECO:0000269|PubMed:20972425}. Note=Translocates to the nucleus
CC following S-nitrosylation and interaction with SIAH1, which contains a
CC nuclear localization signal (PubMed:15951807). Colocalizes with CHP1 to
CC small punctate structures along the microtubules tracks
CC (PubMed:15312048). {ECO:0000269|PubMed:15312048,
CC ECO:0000269|PubMed:15951807}.
CC -!- TISSUE SPECIFICITY: High levels in skeletal muscle and heart, low
CC levels in liver, brain, and kidney. {ECO:0000269|PubMed:6548307}.
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000250|UniProtKB:P04406}.
CC -!- PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1,
CC followed by translocation to the nucleus (PubMed:1281150,
CC PubMed:15951807, PubMed:20972425, PubMed:8626764). The effect of S-
CC nitrosylation on enzymatic activity is unclear: according to some
CC authors, it inhibits enzymatic activity and increases endogenous ADP-
CC ribosylation, inhibiting the enzyme in a non-reversible manner
CC (PubMed:8626764). According to others, it does not affect glycolysis
CC (PubMed:15951807). ADP-ribosylation is likely to be a
CC pathophysiological event associated with inhibition of gluconeogenesis
CC (PubMed:8626764). S-nitrosylation of Cys-245 is induced by interferon-
CC gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase
CC complex and seems to prevent interaction with phosphorylated RPL13A and
CC to interfere with GAIT complex activity (By similarity).
CC {ECO:0000250|UniProtKB:P04406, ECO:0000269|PubMed:1281150,
CC ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:20972425,
CC ECO:0000269|PubMed:8626764}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P04406}.
CC -!- PTM: Sulfhydration at Cys-150 increases catalytic activity.
CC {ECO:0000250|UniProtKB:P16858}.
CC -!- PTM: Oxidative stress can promote the formation of high molecular
CC weight disulfide-linked GAPDH aggregates, through a process called
CC nucleocytoplasmic coagulation. {ECO:0000250|UniProtKB:P04406}.
CC -!- PTM: Succination of Cys-150 and Cys-245 by the Krebs cycle intermediate
CC fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits
CC glyceraldehyde-3-phosphate dehydrogenase activity. Fumarate
CC concentration as well as succination of cysteine residues in GAPDH is
CC significantly increased in muscle of diabetic rats. It was proposed
CC that the S-(2-succinyl)cysteine chemical modification may be a useful
CC biomarker of mitochondrial and oxidative stress in diabetes and that
CC succination of GAPDH and other thiol proteins by fumarate may
CC contribute to the metabolic changes underlying the development of
CC diabetes complications. {ECO:0000269|PubMed:17934141}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X02231; CAA26150.1; -; mRNA.
DR EMBL; M17701; AAA41193.1; -; mRNA.
DR EMBL; AB017801; BAB11748.1; -; mRNA.
DR EMBL; AF106860; AAD08929.2; -; mRNA.
DR EMBL; BC059110; AAH59110.1; -; mRNA.
DR EMBL; BC087743; AAH87743.1; -; mRNA.
DR EMBL; M29341; AAA40814.1; -; mRNA.
DR EMBL; M11561; AAA41795.1; -; mRNA.
DR PIR; A23013; DERTG.
DR RefSeq; NP_058704.1; NM_017008.4.
DR RefSeq; XP_017447924.1; XM_017592435.1.
DR RefSeq; XP_017458425.1; XM_017602936.1.
DR AlphaFoldDB; P04797; -.
DR SMR; P04797; -.
DR BioGRID; 246554; 12.
DR CORUM; P04797; -.
DR IntAct; P04797; 10.
DR MINT; P04797; -.
DR STRING; 10116.ENSRNOP00000040878; -.
DR ChEMBL; CHEMBL2176832; -.
DR MoonProt; P04797; -.
DR iPTMnet; P04797; -.
DR PhosphoSitePlus; P04797; -.
DR World-2DPAGE; 0004:P04797; -.
DR jPOST; P04797; -.
DR PaxDb; P04797; -.
DR PRIDE; P04797; -.
DR GeneID; 24383; -.
DR KEGG; rno:24383; -.
DR UCSC; RGD:2661; rat.
DR CTD; 2597; -.
DR RGD; 2661; Gapdh.
DR VEuPathDB; HostDB:ENSRNOG00000018630; -.
DR eggNOG; KOG0657; Eukaryota.
DR HOGENOM; CLU_030140_0_1_1; -.
DR InParanoid; P04797; -.
DR OMA; NCVAPMA; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; P04797; -.
DR TreeFam; TF300533; -.
DR BRENDA; 1.2.1.12; 5301.
DR Reactome; R-RNO-70171; Glycolysis.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR SABIO-RK; P04797; -.
DR UniPathway; UPA00109; UER00184.
DR PRO; PR:P04797; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000018630; Expressed in skeletal muscle tissue and 18 other tissues.
DR Genevisible; P04797; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0097452; C:GAIT complex; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005811; C:lipid droplet; ISO:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; ISO:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IMP:RGD.
DR GO; GO:0019933; P:cAMP-mediated signaling; IMP:RGD.
DR GO; GO:0061621; P:canonical glycolysis; ISO:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0050832; P:defense response to fungus; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0006094; P:gluconeogenesis; IDA:RGD.
DR GO; GO:0006096; P:glycolytic process; IDA:RGD.
DR GO; GO:0051873; P:killing by host of symbiont cells; ISO:RGD.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:RGD.
DR GO; GO:0017148; P:negative regulation of translation; ISO:RGD.
DR GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; IDA:UniProtKB.
DR GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; IDA:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0060359; P:response to ammonium ion; IDA:RGD.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Apoptosis; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Glycolysis; Immunity; Innate immunity;
KW Isopeptide bond; Methylation; NAD; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; S-nitrosylation; Transferase; Translation regulation;
KW Ubl conjugation.
FT CHAIN 1..333
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145494"
FT REGION 1..146
FT /note="Interaction with WARS1"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOTIF 243..248
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009,
FT ECO:0000269|PubMed:8626764"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT SITE 154
FT /note="Not nitrosylated"
FT /evidence="ECO:0000269|PubMed:8626764"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 3
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 7
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 40
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 62
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 64
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 68
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 147
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 150
FT /note="ADP-ribosylcysteine; by autocatalysis; in
FT irreversibly inhibited form"
FT /evidence="ECO:0000269|PubMed:8626764"
FT MOD_RES 150
FT /note="Cysteine persulfide"
FT /evidence="ECO:0000250|UniProtKB:P16858"
FT MOD_RES 150
FT /note="S-(2-succinyl)cysteine"
FT /evidence="ECO:0000269|PubMed:17934141"
FT MOD_RES 150
FT /note="S-nitrosocysteine; in reversibly inhibited form"
FT /evidence="ECO:0000269|PubMed:15951807,
FT ECO:0000269|PubMed:20972425, ECO:0000269|PubMed:8626764"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 153
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 192
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 192
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 192
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 213
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 213
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 217
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 223
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 225
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 225
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 245
FT /note="S-(2-succinyl)cysteine"
FT /evidence="ECO:0000269|PubMed:17934141"
FT MOD_RES 245
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 258
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 261
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 314
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 332
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MUTAGEN 149
FT /note="S->A: Does not affect interaction with SIRT1."
FT /evidence="ECO:0000269|PubMed:20972425"
FT MUTAGEN 150
FT /note="C->S: Abolishes S-nitrosylation and subsequent
FT nuclear translocation."
FT /evidence="ECO:0000269|PubMed:15951807,
FT ECO:0000269|PubMed:20972425"
FT MUTAGEN 151
FT /note="T->A: Does not affect interaction with SIRT1."
FT /evidence="ECO:0000269|PubMed:20972425"
FT MUTAGEN 152
FT /note="T->A: Abolishes interaction and subsequent
FT nitrosylation of SIRT1."
FT /evidence="ECO:0000269|PubMed:20972425"
FT MUTAGEN 225
FT /note="K->A: Abolishes interaction with SIAH1."
FT /evidence="ECO:0000269|PubMed:15951807"
FT MUTAGEN 234
FT /note="P->A: Does not affect interaction with SIAH1."
FT /evidence="ECO:0000269|PubMed:15951807"
FT MUTAGEN 235
FT /note="T->A: Does not affect interaction with SIAH1."
FT /evidence="ECO:0000269|PubMed:15951807"
FT CONFLICT 81..82
FT /note="AN -> VK (in Ref. 1; AAA41193)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="F -> L (in Ref. 5; AAH87743)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="F -> I (in Ref. 1; AAA41193 and 8; CAA26150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 35828 MW; D9E5ED4F38544C77 CRC64;
MVKVGVNGFG RIGRLVTRAA FSCDKVDIVA INDPFIDLNY MVYMFQYDST HGKFNGTVKA
ENGKLVINGK PITIFQERDP ANIKWGDAGA EYVVESTGVF TTMEKAGAHL KGGAKRVIIS
APSADAPMFV MGVNHEKYDN SLKIVSNASC TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT
ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV
VDLTCRLEKP AKYDDIKKVV KQAAEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA
LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE
