G3P_MOUSE
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 03-AUG-2022, entry version 216.
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}.
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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; 54.
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 iPTMnet; P16858; -.
DR PhosphoSitePlus; P16858; -.
DR SwissPalm; P16858; -.
DR REPRODUCTION-2DPAGE; P16858; -.
DR REPRODUCTION-2DPAGE; Q5U410; -.
DR SWISS-2DPAGE; P16858; -.
DR EPD; P16858; -.
DR jPOST; P16858; -.
DR MaxQB; P16858; -.
DR PaxDb; P16858; -.
DR PRIDE; P16858; -.
DR ProteomicsDB; 267504; -.
DR TopDownProteomics; P16858; -.
DR DNASU; 14433; -.
DR Ensembl; ENSMUST00000073605; ENSMUSP00000073289; ENSMUSG00000057666.
DR Ensembl; ENSMUST00000118875; ENSMUSP00000113213; ENSMUSG00000057666.
DR GeneID; 14433; -.
DR KEGG; mmu:14433; -.
DR UCSC; uc007igj.1; mouse.
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; NCVAPMA; -.
DR OrthoDB; 945145at2759; -.
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 73 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 120 other tissues.
DR ExpressionAtlas; P16858; baseline and differential.
DR Genevisible; P16858; MM.
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:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0061621; P:canonical glycolysis; IDA:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
DR GO; GO:0050832; P:defense response to fungus; ISO:MGI.
DR GO; GO:0006094; P:gluconeogenesis; IDA: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:0010951; P:negative regulation of endopeptidase activity; ISO:MGI.
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:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0060359; P:response to ammonium ion; ISO:MGI.
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 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
