ID G3P_MOUSE Reviewed; 333 AA. AC P16858; A6H6A8; Q0QEU0; Q3THM2; Q3TUI2; Q3UMT2; Q4V783; Q569X2; Q569X5; AC Q5U410; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 224. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase; DE Short=GAPDH; DE EC=1.2.1.12 {ECO:0000269|PubMed:19903941}; DE AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH {ECO:0000305}; DE EC=2.6.99.- {ECO:0000250|UniProtKB:P04797}; GN Name=Gapdh; Synonyms=Gapd; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2145197; DOI=10.1016/0378-1119(90)90087-8; RA Sabath D.E., Broome H.E., Prystowsky M.B.; RT "Glyceraldehyde-3-phosphate dehydrogenase mRNA is a major interleukin 2- RT induced transcript in a cloned T-helper lymphocyte."; RL Gene 91:185-191(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=BALB/cJ, C57BL/6J, and DBA/2J; RC TISSUE=Cerebellum, Eye, Head, Kidney, and Lung; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=129, C57BL/6J, Czech II, FVB/N, and FVB/N-3; RC TISSUE=Brain, Colon, Embryo, Eye, Mammary gland, and Mammary tumor; 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 [5] RP PROTEIN SEQUENCE OF 4-11; 27-50; 65-78; 85-105; 116-137; 144-189; 199-213; RP 218-246 AND 262-333, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus; RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-249. RX PubMed=16751257; DOI=10.1093/molbev/msl027; RA Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.; RT "Housekeeping genes for phylogenetic analysis of eutherian relationships."; RL Mol. Biol. Evol. 23:1493-1503(2006). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, SULFHYDRATION AT CYS-150, AND MUTAGENESIS OF RP CYS-150. RX PubMed=19903941; DOI=10.1126/scisignal.2000464; RA Mustafa A.K., Gadalla M.M., Sen N., Kim S., Mu W., Gazi S.K., Barrow R.K., RA Yang G., Wang R., Snyder S.H.; RT "H2S signals through protein S-sulfhydration."; RL Sci. Signal. 2:RA72-RA72(2009). RN [8] RP FUNCTION, SUBUNIT, AND RECONSTITUTION OF THE GAIT COMPLEX. RX PubMed=23071094; DOI=10.1128/mcb.01168-12; RA Arif A., Chatterjee P., Moodt R.A., Fox P.L.; RT "Heterotrimeric GAIT complex drives transcript-selective translation RT inhibition in murine macrophages."; RL Mol. Cell. Biol. 32:5046-5055(2012). CC -!- FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and CC nitrosylase activities, thereby playing a role in glycolysis and CC nuclear functions, respectively (PubMed:19903941). Glyceraldehyde-3- CC phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes CC the first step of the pathway by converting D-glyceraldehyde 3- CC phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:19903941). CC Modulates the organization and assembly of the cytoskeleton (By CC similarity). Facilitates the CHP1-dependent microtubule and membrane CC associations through its ability to stimulate the binding of CHP1 to CC microtubules (By similarity). Component of the GAIT (gamma interferon- CC activated inhibitor of translation) complex which mediates interferon- CC gamma-induced transcript-selective translation inhibition in CC inflammation processes (PubMed:23071094). 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 CC (PubMed:23071094). Also plays a role in innate immunity by promoting CC TNF-induced NF-kappa-B activation and type I interferon production, via CC interaction with TRAF2 and TRAF3, respectively (By similarity). CC Participates in nuclear events including transcription, RNA transport, CC DNA replication and apoptosis. Nuclear functions are probably due to CC the nitrosylase activity that mediates cysteine S-nitrosylation of CC nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). CC {ECO:0000250|UniProtKB:P04797, ECO:0000250|UniProtKB:P10096, CC ECO:0000269|PubMed:19903941, ECO:0000269|PubMed:23071094}. 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:0000269|PubMed:19903941}; 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:0000250|UniProtKB:P04797}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685; CC Evidence={ECO:0000250|UniProtKB:P04797}; CC -!- ACTIVITY REGULATION: Glyceraldehyde-3-phosphate dehydrogenase activity CC is inhibited by fumarate, via the formation of S-(2-succinyl)cysteine CC residues. {ECO:0000250|UniProtKB:P04797}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. CC -!- SUBUNIT: Homotetramer (PubMed:23071094). Interacts with TPPP; the CC interaction is direct (By similarity). Interacts (when S-nitrosylated) CC with SIAH1; leading to nuclear translocation. Interacts with CC RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and CC SIAH1 and prevent nuclear translocation. Interacts with CHP1; the CC interaction increases the binding of CHP1 with microtubules. Associates CC with microtubules (By similarity). Interacts with EIF1AD, USP25, PRKCI CC and WARS1. Interacts with phosphorylated RPL13A; inhibited by CC oxidatively-modified low-densitity lipoprotein (LDL(ox)) (By CC similarity). Component of the GAIT complex. Interacts with FKBP6; CC leading to inhibit GAPDH catalytic activity (PubMed:23071094). CC Interacts with TRAF2, promoting TRAF2 ubiquitination (By similarity). CC Interacts with TRAF3, promoting TRAF3 ubiquitination (By similarity). CC {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P04797, CC ECO:0000250|UniProtKB:P10096, ECO:0000269|PubMed:23071094}. CC -!- INTERACTION: CC P16858; P23819: Gria2; NbExp=2; IntAct=EBI-444871, EBI-77538; CC P16858; Q08460: Kcnma1; NbExp=3; IntAct=EBI-444871, EBI-1633915; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}. CC Note=Translocates to the nucleus following S-nitrosylation and CC interaction with SIAH1, which contains a nuclear localization signal. CC Colocalizes with CHP1 to small punctate structures along the CC microtubules tracks. {ECO:0000250|UniProtKB:P04797}. 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: ISGylated. {ECO:0000250|UniProtKB:P04406}. CC -!- PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1, CC followed by translocation to the nucleus S-nitrosylation of Cys-245 is CC induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 CC transnitrosylase complex and seems to prevent interaction with CC phosphorylated RPL13A and to interfere with GAIT complex activity (By CC similarity). {ECO:0000250|UniProtKB:P04406, CC ECO:0000250|UniProtKB:P04797}. CC -!- PTM: Sulfhydration at Cys-150 increases catalytic activity. CC {ECO:0000269|PubMed:19903941}. 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 mammals. 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:0000250|UniProtKB:P04797}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M32599; AAA37659.1; -; mRNA. DR EMBL; AK002273; BAB21979.1; -; mRNA. DR EMBL; AK081405; BAC38211.1; -; mRNA. DR EMBL; AK140794; BAE24481.1; -; mRNA. DR EMBL; AK144690; BAE26016.1; -; mRNA. DR EMBL; AK146435; BAE27169.1; -; mRNA. DR EMBL; AK147738; BAE28105.1; -; mRNA. DR EMBL; AK147891; BAE28208.1; -; mRNA. DR EMBL; AK160399; BAE35768.1; -; mRNA. DR EMBL; AK160753; BAE35989.1; -; mRNA. DR EMBL; AK164415; BAE37778.1; -; mRNA. DR EMBL; AK168217; BAE40174.1; -; mRNA. DR EMBL; AL662926; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC082592; AAH82592.1; -; mRNA. DR EMBL; BC083065; AAH83065.1; -; mRNA. DR EMBL; BC083079; AAH83079.1; -; mRNA. DR EMBL; BC083080; AAH83080.1; -; mRNA. DR EMBL; BC083149; AAH83149.1; -; mRNA. DR EMBL; BC085274; AAH85274.1; -; mRNA. DR EMBL; BC085275; AAH85275.1; -; mRNA. DR EMBL; BC085315; AAH85315.1; -; mRNA. DR EMBL; BC091768; AAH91768.1; -; mRNA. DR EMBL; BC092252; AAH92252.1; -; mRNA. DR EMBL; BC092264; AAH92264.1; -; mRNA. DR EMBL; BC092267; AAH92267.1; -; mRNA. DR EMBL; BC092294; AAH92294.1; -; mRNA. DR EMBL; BC093508; AAH93508.1; -; mRNA. DR EMBL; BC094037; AAH94037.1; -; mRNA. DR EMBL; BC095932; AAH95932.1; -; mRNA. DR EMBL; BC096440; AAH96440.1; -; mRNA. DR EMBL; BC096590; AAH96590.1; -; mRNA. DR EMBL; BC110311; AAI10312.1; -; mRNA. DR EMBL; BC145810; AAI45811.1; -; mRNA. DR EMBL; BC145812; AAI45813.1; -; mRNA. DR EMBL; DQ403054; ABD77187.1; -; mRNA. DR CCDS; CCDS51913.1; -. DR PIR; JT0553; DEMSG. DR RefSeq; NP_001276655.1; NM_001289726.1. DR RefSeq; NP_032110.1; NM_008084.3. DR RefSeq; XP_001476757.1; XM_001476707.5. DR PDB; 6LGJ; X-ray; 2.40 A; A/B/C/D=1-333. DR PDB; 6LGK; X-ray; 2.00 A; A/B/C/D=1-333. DR PDB; 6LGM; X-ray; 2.40 A; A/B/C/D=1-333. DR PDBsum; 6LGJ; -. DR PDBsum; 6LGK; -. DR PDBsum; 6LGM; -. DR AlphaFoldDB; P16858; -. DR SMR; P16858; -. DR BioGRID; 199829; 58. DR BioGRID; 785307; 2. DR DIP; DIP-31404N; -. DR IntAct; P16858; 24. DR MINT; P16858; -. DR STRING; 10090.ENSMUSP00000113942; -. DR ChEMBL; CHEMBL3309048; -. DR MoonProt; P16858; -. DR GlyGen; P16858; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P16858; -. DR MetOSite; P16858; -. DR PhosphoSitePlus; P16858; -. DR SwissPalm; P16858; -. DR REPRODUCTION-2DPAGE; P16858; -. DR REPRODUCTION-2DPAGE; Q5U410; -. DR EPD; P16858; -. DR jPOST; P16858; -. DR MaxQB; P16858; -. DR PaxDb; 10090-ENSMUSP00000113942; -. DR ProteomicsDB; 267504; -. DR Pumba; P16858; -. DR TopDownProteomics; P16858; -. DR DNASU; 14433; -. DR Ensembl; ENSMUST00000073605.15; ENSMUSP00000073289.9; ENSMUSG00000057666.19. DR Ensembl; ENSMUST00000118875.8; ENSMUSP00000113213.2; ENSMUSG00000057666.19. DR GeneID; 14433; -. DR KEGG; mmu:14433; -. DR UCSC; uc007igj.1; mouse. DR AGR; MGI:95640; -. DR CTD; 2597; -. DR MGI; MGI:95640; Gapdh. DR VEuPathDB; HostDB:ENSMUSG00000057666; -. DR eggNOG; KOG0657; Eukaryota. DR GeneTree; ENSGT00940000153298; -. DR HOGENOM; CLU_030140_0_1_1; -. DR InParanoid; P16858; -. DR OMA; YGYTCNM; -. DR OrthoDB; 275384at2759; -. DR PhylomeDB; P16858; -. DR TreeFam; TF300533; -. DR BRENDA; 1.2.1.12; 3474. DR Reactome; R-MMU-70171; Glycolysis. DR Reactome; R-MMU-70263; Gluconeogenesis. DR SABIO-RK; P16858; -. DR UniPathway; UPA00109; UER00184. DR BioGRID-ORCS; 14433; 27 hits in 78 CRISPR screens. DR ChiTaRS; Gapdh; mouse. DR PRO; PR:P16858; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; P16858; Protein. DR Bgee; ENSMUSG00000057666; Expressed in epiblast (generic) and 123 other cell types or tissues. DR ExpressionAtlas; P16858; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0097452; C:GAIT complex; IDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0031906; C:late endosome lumen; TAS:Reactome. DR GO; GO:0005811; C:lipid droplet; ISO:MGI. DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI. DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI. DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; ISO:MGI. DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0008017; F:microtubule binding; ISS: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; ISS:UniProtKB. DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI. DR GO; GO:0019933; P:cAMP-mediated signaling; ISO:MGI. DR GO; GO:0061621; P:canonical glycolysis; IDA:MGI. DR GO; GO:0071346; P:cellular response to type II interferon; ISO:MGI. DR GO; GO:0050832; P:defense response to fungus; ISO:MGI. DR GO; GO:0006094; P:gluconeogenesis; IDA:MGI. DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; ISO:MGI. DR GO; GO:0006096; P:glycolytic process; ISO:MGI. DR GO; GO:0051873; P:killing by host of symbiont cells; ISO:MGI. DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB. DR GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; ISO:MGI. DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB. DR GO; GO:0007263; P:nitric oxide mediated signal transduction; ISO:MGI. DR GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISS:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB. DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI. DR GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB. DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. 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 NCBIfam; TIGR01534; GAPDH-I; 1. DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR10836:SF111; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00071; GAPDH; 1. DR SWISS-2DPAGE; P16858; -. DR Genevisible; P16858; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Apoptosis; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Glycolysis; Immunity; KW Innate immunity; Isopeptide bond; Methylation; NAD; Nucleus; KW Oxidoreductase; Phosphoprotein; Reference proteome; S-nitrosylation; KW Transferase; Translation regulation; Ubl conjugation. FT CHAIN 1..333 FT /note="Glyceraldehyde-3-phosphate dehydrogenase" FT /id="PRO_0000145490" 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 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 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:0000250|UniProtKB:P04797" FT MOD_RES 150 FT /note="Cysteine persulfide" FT /evidence="ECO:0000269|PubMed:19903941" FT MOD_RES 150 FT /note="S-(2-succinyl)cysteine" FT /evidence="ECO:0000250|UniProtKB:P04797" FT MOD_RES 150 FT /note="S-nitrosocysteine; in reversibly inhibited form" FT /evidence="ECO:0000250|UniProtKB:P04797" 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:0000250|UniProtKB:P04797" 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 150 FT /note="C->S: Abolishes sulfhydration and induces impaired FT enzyme activity." FT /evidence="ECO:0000269|PubMed:19903941" FT CONFLICT 3 FT /note="K -> E (in Ref. 2; BAE40174)" FT /evidence="ECO:0000305" FT CONFLICT 30 FT /note="A -> V (in Ref. 4; AAH92267)" FT /evidence="ECO:0000305" FT CONFLICT 82 FT /note="N -> S (in Ref. 2; BAE35989)" FT /evidence="ECO:0000305" FT CONFLICT 84 FT /note="K -> E (in Ref. 2; BAE40174)" FT /evidence="ECO:0000305" FT CONFLICT 89 FT /note="G -> S (in Ref. 2; BAE26016)" FT /evidence="ECO:0000305" FT CONFLICT 91 FT /note="E -> K (in Ref. 2; BAE35989)" FT /evidence="ECO:0000305" FT CONFLICT 134 FT /note="N -> D (in Ref. 4; AAH85315)" FT /evidence="ECO:0000305" FT CONFLICT 195 FT /note="R -> C (in Ref. 4; AAH85315)" FT /evidence="ECO:0000305" FT CONFLICT 300 FT /note="A -> S (in Ref. 4; AAH85315)" FT /evidence="ECO:0000305" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 11..22 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 25..32 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 38..46 FT /evidence="ECO:0007829|PDB:6LGK" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 58..61 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 70..75 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 85..88 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 103..106 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 108..111 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 115..121 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:6LGK" FT TURN 131..133 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 143..146 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 150..166 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 168..178 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 183..187 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 194..197 FT /evidence="ECO:0007829|PDB:6LGK" FT TURN 200..202 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 211..218 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 220..222 FT /evidence="ECO:0007829|PDB:6LGK" FT TURN 223..225 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 226..234 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 239..249 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 253..265 FT /evidence="ECO:0007829|PDB:6LGK" FT TURN 266..271 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 272..275 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 281..284 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 290..294 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 299..302 FT /evidence="ECO:0007829|PDB:6LGK" FT STRAND 305..312 FT /evidence="ECO:0007829|PDB:6LGK" FT HELIX 316..331 FT /evidence="ECO:0007829|PDB:6LGK" SQ SEQUENCE 333 AA; 35810 MW; F25131EFFA9F2BD6 CRC64; MVKVGVNGFG RIGRLVTRAA ICSGKVEIVA INDPFIDLNY MVYMFQYDST HGKFNGTVKA ENGKLVINGK PITIFQERDP TNIKWGEAGA EYVVESTGVF TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDN SLKIVSNASC TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKP AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE //