ID G3P_HUMAN Reviewed; 335 AA. AC P04406; E7EUT4; P00354; Q53X65; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-NOV-2024, entry version 275. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:6096136}; DE Short=GAPDH {ECO:0000303|PubMed:2987855}; DE EC=1.2.1.12 {ECO:0000269|PubMed:3170585}; DE AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH {ECO:0000305}; DE EC=2.6.99.- {ECO:0000250|UniProtKB:P04797}; GN Name=GAPDH {ECO:0000303|PubMed:2987855, ECO:0000312|HGNC:HGNC:4141}; GN Synonyms=GAPD {ECO:0000303|PubMed:6096136}; GN ORFNames=CDABP0047, OK/SW-cl.12; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6096136; DOI=10.1002/j.1460-2075.1984.tb02185.x; RA Hanauer A., Mandel J.-L.; RT "The glyceraldehyde 3 phosphate dehydrogenase gene family: structure of a RT human cDNA and of an X chromosome linked pseudogene; amazing complexity of RT the gene family in mouse."; RL EMBO J. 3:2627-2633(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6096821; DOI=10.1093/nar/12.23.9179; RA Arcari P., Martinelli R., Salvatore F.; RT "The complete sequence of a full length cDNA for human liver RT glyceraldehyde-3-phosphate dehydrogenase: evidence for multiple mRNA RT species."; RL Nucleic Acids Res. 12:9179-9189(1984). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lung; RX PubMed=3664468; RA Tokunaga K., Nakamura Y., Sakata K., Fujimori K., Ohkubo M., Sawada K., RA Sakiyama S.; RT "Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in RT human lung cancers."; RL Cancer Res. 47:5616-5619(1987). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3027061; DOI=10.1016/s0021-9258(19)75833-5; RA Allen R.W., Trach K.A., Hoch J.A.; RT "Identification of the 37-kDa protein displaying a variable interaction RT with the erythroid cell membrane as glyceraldehyde-3-phosphate RT dehydrogenase."; RL J. Biol. Chem. 262:649-653(1987). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=3170585; DOI=10.1016/s0021-9258(19)37593-3; RA Ercolani L., Florence B., Denaro M., Alexander M.; RT "Isolation and complete sequence of a functional human glyceraldehyde-3- RT phosphate dehydrogenase gene."; RL J. Biol. Chem. 263:15335-15341(1988). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX PubMed=1924305; DOI=10.1073/pnas.88.19.8460; RA Meyer-Siegler K., Mauro D.J., Seal G., Wurzer J., Deriel J.K., RA Sirover M.A.; RT "A human nuclear uracil DNA glycosylase is the 37-kDa subunit of RT glyceraldehyde-3-phosphate dehydrogenase."; RL Proc. Natl. Acad. Sci. U.S.A. 88:8460-8464(1991). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Astrocytoma; RX PubMed=10944468; DOI=10.1006/bbrc.2000.3282; RA Ye Z., Connor J.R.; RT "cDNA cloning by amplification of circularized first strand cDNAs reveals RT non-IRE-regulated iron-responsive mRNAs."; RL Biochem. Biophys. Res. Commun. 275:223-227(2000). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Leukemia; RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., RA Margolin J.F.; RT "Pediatric leukemia cDNA sequencing project."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-22. RG NIEHS SNPs program; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [16] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye, Kidney, Lung, Lymph, and Placenta; 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 [17] RP PRELIMINARY PROTEIN SEQUENCE OF 2-335. RC TISSUE=Muscle; RX PubMed=7030790; DOI=10.1016/0014-5793(81)80587-x; RA Nowak K., Wolny M., Banas T.; RT "The complete amino acid sequence of human muscle glyceraldehyde 3- RT phosphate dehydrogenase."; RL FEBS Lett. 134:143-146(1981). RN [18] RP PROTEIN SEQUENCE OF 2-13. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [19] RP PROTEIN SEQUENCE OF 2-13; 62-84; 118-139; 198-215; 220-227; 235-248 AND RP 310-335, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Prostatic carcinoma; RA Bienvenut W.V., Gao M., Leug H.; RL Submitted (JUL-2009) to UniProtKB. RN [20] RP PROTEIN SEQUENCE OF 67-80; 87-107; 119-139; 146-186; 201-215; 235-248 AND RP 310-334, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [21] RP PROTEIN SEQUENCE OF 220-226 AND 242-246. RC TISSUE=Heart; RX PubMed=7498159; DOI=10.1002/elps.11501601192; RA Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., RA Ershova E.S., Egorov T.A., Musalyamov A.K.; RT "The major protein expression profile and two-dimensional protein database RT of human heart."; RL Electrophoresis 16:1160-1169(1995). RN [22] RP PARTIAL PROTEIN SEQUENCE. RC TISSUE=Muscle; RX PubMed=1193541; RA Nowak K., Kuczek M., Ostropolska L., Malarska A., Wolny M., Branowski T.; RT "The covalent structure of glyceraldehyde-phosphate dehydrogenase from RT human muscles. Isolation and amino acid sequences of peptides from tryptic RT digest."; RL Hoppe-Seyler's Z. Physiol. Chem. 356:1181-1183(1975). RN [23] RP FUNCTION, AND INTERACTION WITH PRKCI. RX PubMed=11724794; DOI=10.1074/jbc.m109744200; RA Tisdale E.J.; RT "Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein RT kinase Ciota /lambda and plays a role in microtubule dynamics in the early RT secretory pathway."; RL J. Biol. Chem. 277:3334-3341(2002). RN [24] RP SUBCELLULAR LOCATION. RX PubMed=12829261; DOI=10.1016/s0304-4165(03)00117-x; RA Mazzola J.L., Sirover M.A.; RT "Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase RT is independent of its glycolytic function."; RL Biochim. Biophys. Acta 1622:50-56(2003). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [26] RP IDENTIFICATION IN THE GAIT COMPLEX. RX PubMed=15479637; DOI=10.1016/j.cell.2004.09.030; RA Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L., Kinter M., RA Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.; RT "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific RT silencing of translation."; RL Cell 119:195-208(2004). RN [27] RP INTERACTION WITH WARS1. RX PubMed=15628863; DOI=10.1021/bi048313k; RA Wakasugi K., Nakano T., Morishima I.; RT "Oxidative stress-responsive intracellular regulation specific for the RT angiostatic form of human tryptophanyl-tRNA synthetase."; RL Biochemistry 44:225-232(2005). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [30] RP INTERACTION WITH USP25. RX PubMed=16501887; DOI=10.1007/s00018-005-5533-1; RA Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G., Marfany G.; RT "The ubiquitin-specific protease USP25 interacts with three sarcomeric RT proteins."; RL Cell. Mol. Life Sci. 63:723-734(2006). RN [31] RP ISGYLATION. RX PubMed=16815975; DOI=10.1073/pnas.0600397103; RA Wong J.J., Pung Y.F., Sze N.S., Chin K.C.; RT "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I RT IFN-induced ISGylation of protein targets."; RL Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006). RN [32] RP PHOSPHORYLATION AT THR-75; SER-122; SER-148; THR-229; THR-237 AND SER-312, RP DEAMIDATION AT ASN-9; ASN-64; ASN-70; ASN-149; ASN-155; ASN-225 AND RP ASN-316, AND METHYLATION AT LYS-5; LYS-66; LYS-194; LYS-215; LYS-227; RP LYS-260; LYS-263 AND LYS-334. RX PubMed=18183946; DOI=10.1021/pr700657y; RA Seo J., Jeong J., Kim Y.M., Hwang N., Paek E., Lee K.-J.; RT "Strategy for comprehensive identification of post-translational RT modifications in cellular proteins, including low abundant modifications: RT application to glyceraldehyde-3-phosphate dehydrogenase."; RL J. Proteome Res. 7:587-602(2008). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-151 AND THR-184, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [34] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [35] RP INTERACTION WITH FKBP6. RX PubMed=19001379; DOI=10.1074/jbc.m709779200; RA Jarczowski F., Jahreis G., Erdmann F., Schierhorn A., Fischer G., RA Edlich F.; RT "FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate RT dehydrogenase inhibitor."; RL J. Biol. Chem. 284:766-773(2009). RN [36] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-184; THR-211 AND SER-312, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [37] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-194; LYS-219; LYS-227 AND RP LYS-254, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [38] RP INTERACTION WITH EIF1AD. RX PubMed=20644585; DOI=10.1134/s1068162010030027; RA Rakitina T.V., Bogatova O.V., Smirnova E.V., Pozdeev V.I., Kostanian I.A., RA Lipkin V.M.; RT "Haponin (eIF1AD) interacts with glyceraldehyde 3-phosphate dehydrogenase RT in the CHO-K1 cell line."; RL Bioorg. Khim. 36:312-318(2010). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75; SER-83 AND THR-184, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [40] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [41] RP MALONYLATION AT LYS-194 AND LYS-215. RX PubMed=21908771; DOI=10.1074/mcp.m111.012658; RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., RA Verdin E., Ye Y., Zhao Y.; RT "The first identification of lysine malonylation substrates and its RT regulatory enzyme."; RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). RN [42] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [43] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [44] RP INTERACTION WITH RPL13A, AND S-NITROSYLATION AT CYS-247. RX PubMed=22771119; DOI=10.1016/j.molcel.2012.06.006; RA Jia J., Arif A., Willard B., Smith J.D., Stuehr D.J., Hazen S.L., Fox P.L.; RT "Protection of extraribosomal RPL13a by GAPDH and dysregulation by S- RT nitrosylation."; RL Mol. Cell 47:656-663(2012). RN [45] RP FUNCTION, 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). RN [46] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [47] RP FUNCTION, GLYCOSYLATION (MICROBIAL INFECTION), INTERACTION WITH TRAF2, AND RP MUTAGENESIS OF CYS-152; THR-211; THR-229; SER-241; THR-246 AND THR-277. RX PubMed=23332158; DOI=10.1016/j.chom.2012.11.010; RA Gao X., Wang X., Pham T.H., Feuerbacher L.A., Lubos M.L., Huang M., RA Olsen R., Mushegian A., Slawson C., Hardwidge P.R.; RT "NleB, a bacterial effector with glycosyltransferase activity, targets RT GAPDH function to inhibit NF-kappaB activation."; RL Cell Host Microbe 13:87-99(2013). RN [48] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-151; THR-153; THR-229 RP AND SER-333, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [49] RP S-NITROSYLATION AT CYS-247, MUTAGENESIS OF LEU-245 AND GLU-250, AND DOMAIN. RX PubMed=25417112; DOI=10.1016/j.cell.2014.09.032; RA Jia J., Arif A., Terenzi F., Willard B., Plow E.F., Hazen S.L., Fox P.L.; RT "Target-selective protein S-nitrosylation by sequence motif recognition."; RL Cell 159:623-634(2014). RN [50] RP MECHANISM OF FREE RADICAL-INDUCED AGGREGATION, ACTIVE SITE, OXIDATION AT RP MET-46, AND MUTAGENESIS OF MET-46; MET-105; CYS-152; CYS-156; TRP-196; RP CYS-247 AND TYR-320. RX PubMed=25086035; DOI=10.1074/jbc.m114.570275; RA Samson A.L., Knaupp A.S., Kass I., Kleifeld O., Marijanovic E.M., RA Hughes V.A., Lupton C.J., Buckle A.M., Bottomley S.P., Medcalf R.L.; RT "Oxidation of an exposed methionine instigates the aggregation of RT glyceraldehyde-3-phosphate dehydrogenase."; RL J. Biol. Chem. 289:26922-26936(2014). RN [51] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177; THR-182; THR-184 AND RP SER-241, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [52] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [53] RP FUNCTION, GLYCOSYLATION (MICROBIAL INFECTION), INTERACTION WITH TRAF2, AND RP MUTAGENESIS OF CYS-152. RX PubMed=27387501; DOI=10.1074/jbc.m116.738278; RA Gao X., Pham T.H., Feuerbacher L.A., Chen K., Hays M.P., Singh G., RA Rueter C., Hurtado-Guerrero R., Hardwidge P.R.; RT "Citrobacter rodentium NleB protein inhibits tumor necrosis factor (TNF) RT receptor-associated factor 3 (TRAF3) ubiquitination to reduce host type I RT interferon production."; RL J. Biol. Chem. 291:18232-18238(2016). RN [54] RP GLYCOSYLATION AT ARG-197 AND ARG-200 (MICROBIAL INFECTION). RX PubMed=28522607; DOI=10.1074/jbc.m117.790675; RA El Qaidi S., Chen K., Halim A., Siukstaite L., Rueter C., RA Hurtado-Guerrero R., Clausen H., Hardwidge P.R.; RT "NleB/SseK effectors from Citrobacter rodentium, Escherichia coli, and RT Salmonella enterica display distinct differences in host substrate RT specificity."; RL J. Biol. Chem. 292:11423-11430(2017). RN [55] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-186, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [56] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS). RX PubMed=957435; DOI=10.1016/0022-2836(76)90013-9; RA Mercer W.D., Winn S.I., Watson H.C.; RT "Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate RT dehydrogenase."; RL J. Mol. Biol. 104:277-283(1976). RN [57] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT. RX PubMed=16239728; DOI=10.1107/s0907444905026740; RA Ismail S.A., Park H.W.; RT "Structural analysis of human liver glyceraldehyde-3-phosphate RT dehydrogenase."; RL Acta Crystallogr. D 61:1508-1513(2005). RN [58] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT. RX PubMed=16510976; DOI=10.1107/s0907444905042289; RA Jenkins J.L., Tanner J.J.; RT "High-resolution structure of human D-glyceraldehyde-3-phosphate RT dehydrogenase."; RL Acta Crystallogr. D 62:290-301(2006). CC -!- FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and CC nitrosylase activities, thereby playing a role in glycolysis and CC nuclear functions, respectively (PubMed:11724794, PubMed:3170585). CC Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis CC that catalyzes the first step of the pathway by converting D- CC glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate CC (PubMed:11724794, PubMed:3170585). Modulates the organization and CC assembly of the cytoskeleton (By similarity). Facilitates the CHP1- CC dependent microtubule and membrane associations through its ability to CC stimulate the binding of CHP1 to microtubules (By similarity). CC Component of the GAIT (gamma interferon-activated inhibitor of CC translation) complex which mediates interferon-gamma-induced CC transcript-selective translation inhibition in inflammation processes CC (PubMed:23071094). Upon interferon-gamma treatment assembles into the CC GAIT complex which binds to stem loop-containing GAIT elements in the CC 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and CC suppresses their translation (PubMed:23071094). Also plays a role in CC innate immunity by promoting TNF-induced NF-kappa-B activation and type CC I interferon production, via interaction with TRAF2 and TRAF3, CC respectively (PubMed:23332158, PubMed:27387501). Participates in CC nuclear events including transcription, RNA transport, DNA replication CC and apoptosis (By similarity). 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:0000269|PubMed:11724794, CC ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:23332158, CC ECO:0000269|PubMed:27387501, ECO:0000269|PubMed:3170585}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = (2R)-3- CC phospho-glyceroyl phosphate + NADH + H(+); 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:3170585}; CC -!- CATALYTIC ACTIVITY: CC Reaction=S-nitroso-L-cysteinyl-[GAPDH] + L-cysteinyl-[protein] = 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:16239728, PubMed:16510976). Interacts CC with TPPP; the interaction is direct (By similarity). Interacts (when CC S-nitrosylated) with SIAH1; leading to nuclear translocation (By CC similarity). Interacts with RILPL1/GOSPEL, leading to prevent the CC interaction between GAPDH and SIAH1 and prevent nuclear translocation CC (By similarity). Interacts with CHP1; the interaction increases the CC binding of CHP1 with microtubules (By similarity). Associates with CC microtubules (By similarity). Interacts with EIF1AD, USP25, PRKCI and CC WARS1 (PubMed:11724794, PubMed:15628863, PubMed:16501887, CC PubMed:20644585). Interacts with phosphorylated RPL13A; inhibited by CC oxidatively-modified low-densitity lipoprotein (LDL(ox)) CC (PubMed:22771119). Component of the GAIT complex (PubMed:15479637). CC Interacts with FKBP6; leading to inhibit GAPDH catalytic activity CC (PubMed:19001379). Interacts with TRAF2, promoting TRAF2 ubiquitination CC (PubMed:23332158). Interacts with TRAF3, promoting TRAF3 ubiquitination CC (PubMed:27387501). {ECO:0000250|UniProtKB:P04797, CC ECO:0000250|UniProtKB:P10096, ECO:0000269|PubMed:11724794, CC ECO:0000269|PubMed:15479637, ECO:0000269|PubMed:15628863, CC ECO:0000269|PubMed:16239728, ECO:0000269|PubMed:16501887, CC ECO:0000269|PubMed:16510976, ECO:0000269|PubMed:19001379, CC ECO:0000269|PubMed:20644585, ECO:0000269|PubMed:22771119, CC ECO:0000269|PubMed:23332158, ECO:0000269|PubMed:27387501}. CC -!- INTERACTION: CC P04406; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-354056, EBI-10173507; CC P04406; Q9UIJ7: AK3; NbExp=3; IntAct=EBI-354056, EBI-3916527; CC P04406; P05067: APP; NbExp=3; IntAct=EBI-354056, EBI-77613; CC P04406; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-354056, EBI-1383687; CC P04406; Q14194: CRMP1; NbExp=3; IntAct=EBI-354056, EBI-473101; CC P04406; P35222: CTNNB1; NbExp=3; IntAct=EBI-354056, EBI-491549; CC P04406; Q9BPW9-4: DHRS9; NbExp=3; IntAct=EBI-354056, EBI-19157435; CC P04406; P00533: EGFR; NbExp=7; IntAct=EBI-354056, EBI-297353; CC P04406; O00471: EXOC5; NbExp=3; IntAct=EBI-354056, EBI-949824; CC P04406; O75344: FKBP6; NbExp=3; IntAct=EBI-354056, EBI-744771; CC P04406; P06241: FYN; NbExp=3; IntAct=EBI-354056, EBI-515315; CC P04406; P04406: GAPDH; NbExp=2; IntAct=EBI-354056, EBI-354056; CC P04406; O14556: GAPDHS; NbExp=3; IntAct=EBI-354056, EBI-1057431; CC P04406; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-354056, EBI-745707; CC P04406; P42858: HTT; NbExp=7; IntAct=EBI-354056, EBI-466029; CC P04406; Q92993-2: KAT5; NbExp=3; IntAct=EBI-354056, EBI-20795332; CC P04406; P42695: NCAPD3; NbExp=2; IntAct=EBI-354056, EBI-722805; CC P04406; P35228: NOS2; NbExp=8; IntAct=EBI-354056, EBI-6662224; CC P04406; P12004: PCNA; NbExp=3; IntAct=EBI-354056, EBI-358311; CC P04406; P00558: PGK1; NbExp=2; IntAct=EBI-354056, EBI-709599; CC P04406; P48147: PREP; NbExp=5; IntAct=EBI-354056, EBI-1049962; CC P04406; P17612: PRKACA; NbExp=3; IntAct=EBI-354056, EBI-476586; CC P04406; Q8WUY3: PRUNE2; NbExp=3; IntAct=EBI-354056, EBI-743880; CC P04406; Q9UHX1-2: PUF60; NbExp=3; IntAct=EBI-354056, EBI-11529177; CC P04406; P15927: RPA2; NbExp=2; IntAct=EBI-354056, EBI-621404; CC P04406; P05109: S100A8; NbExp=6; IntAct=EBI-354056, EBI-355281; CC P04406; Q96GZ6: SLC41A3; NbExp=3; IntAct=EBI-354056, EBI-7225508; CC P04406; P00441: SOD1; NbExp=3; IntAct=EBI-354056, EBI-990792; CC P04406; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-354056, EBI-717399; CC P04406; P10599: TXN; NbExp=3; IntAct=EBI-354056, EBI-594644; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12829261}. CC Nucleus {ECO:0000250|UniProtKB:P04797}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:12829261}. Membrane {ECO:0000269|PubMed:12829261}. CC Cytoplasm, cytoskeleton {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 (By similarity). Postnuclear and Perinuclear regions (PubMed:12829261). CC {ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:12829261}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P04406-1; Sequence=Displayed; CC Name=2; CC IsoId=P04406-2; Sequence=VSP_047289; 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:0000305|PubMed:25417112}. CC -!- PTM: S-nitrosylation of Cys-152 leads to interaction with SIAH1, CC followed by translocation to the nucleus (By similarity). S- CC nitrosylation of Cys-247 is induced by interferon-gamma and LDL(ox) CC implicating the iNOS-S100A8/9 transnitrosylase complex and seems to CC prevent interaction with phosphorylated RPL13A and to interfere with CC GAIT complex activity (PubMed:22771119, PubMed:25417112). CC {ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:22771119, CC ECO:0000269|PubMed:25417112}. CC -!- PTM: ISGylated. {ECO:0000305|PubMed:16815975}. CC -!- PTM: Sulfhydration at Cys-152 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. Such aggregates can be observed in vivo CC in the affected tissues of patients with Alzheimer disease or alcoholic CC liver cirrhosis, or in cell cultures during necrosis. Oxidation at Met- CC 46 may play a pivotal role in the formation of these insoluble CC structures. This modification has been detected in vitro following CC treatment with free radical donor (+/-)-(E)-4-ethyl-2-[(E)- CC hydroxyimino]-5-nitro-3-hexenamide. It has been proposed to destabilize CC nearby residues, increasing the likelihood of secondary oxidative CC damages, including oxidation of Tyr-45 and Met-105. This cascade of CC oxidations may augment GAPDH misfolding, leading to intermolecular CC disulfide cross-linking and aggregation. {ECO:0000305|PubMed:25086035}. CC -!- PTM: Succination of Cys-152 and Cys-247 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 -!- PTM: (Microbial infection) Glycosylated by C.rodentium protein NleB, CC enteropathogenic E.coli protein NleB1 and S.typhimurium protein Ssek1: CC arginine GlcNAcylation prevents the interaction with TRAF2 and TRAF3 CC (PubMed:23332158, PubMed:27387501, PubMed:28522607). This leads to CC reduced ubiquitination of TRAF2 and TRAF3, and subsequent inhibition of CC NF-kappa-B signaling and type I interferon production, respectively CC (PubMed:23332158, PubMed:27387501). {ECO:0000269|PubMed:23332158, CC ECO:0000269|PubMed:27387501, ECO:0000269|PubMed:28522607}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Glyceraldehyde 3-phosphate CC dehydrogenase entry; CC URL="https://en.wikipedia.org/wiki/Glyceraldehyde_3-phosphate_dehydrogenase"; 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; X01677; CAA25833.1; -; mRNA. DR EMBL; M17851; AAA86283.1; -; mRNA. DR EMBL; M33197; AAA52518.1; -; mRNA. DR EMBL; J02642; AAA52496.1; -; mRNA. DR EMBL; J04038; AAA53191.1; -; Genomic_DNA. DR EMBL; X53778; CAA37794.1; -; mRNA. DR EMBL; AF261085; AAF99678.1; -; mRNA. DR EMBL; AY007133; AAG01996.1; -; mRNA. DR EMBL; AB062273; BAB93466.1; -; mRNA. DR EMBL; BT006893; AAP35539.1; -; mRNA. DR EMBL; AY340484; AAP88932.1; -; Genomic_DNA. DR EMBL; CR407671; CAG28599.1; -; mRNA. DR EMBL; AC006064; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471116; EAW88787.1; -; Genomic_DNA. DR EMBL; BC001601; AAH01601.1; -; mRNA. DR EMBL; BC004109; AAH04109.1; -; mRNA. DR EMBL; BC009081; AAH09081.1; -; mRNA. DR EMBL; BC013310; AAH13310.1; -; mRNA. DR EMBL; BC023632; AAH23632.1; -; mRNA. DR EMBL; BC025925; AAH25925.1; -; mRNA. DR EMBL; BC026907; AAH26907.1; -; mRNA. DR EMBL; BC029618; AAH29618.1; -; mRNA. DR EMBL; BC083511; AAH83511.1; -; mRNA. DR CCDS; CCDS58201.1; -. [P04406-2] DR CCDS; CCDS8549.1; -. [P04406-1] DR PIR; A31988; DEHUG3. DR RefSeq; NP_001243728.1; NM_001256799.2. [P04406-2] DR RefSeq; NP_001276674.1; NM_001289745.1. [P04406-1] DR RefSeq; NP_001276675.1; NM_001289746.1. [P04406-1] DR RefSeq; NP_002037.2; NM_002046.5. [P04406-1] DR PDB; 1U8F; X-ray; 1.75 A; O/P/Q/R=1-335. DR PDB; 1ZNQ; X-ray; 2.50 A; O/P/Q/R=1-335. DR PDB; 3GPD; X-ray; 3.50 A; G/R=2-335. DR PDB; 4WNC; X-ray; 1.99 A; A/B/C/D/E/F/G/O=1-335. DR PDB; 4WNI; X-ray; 2.30 A; A/B/C/O=1-335. DR PDB; 6ADE; X-ray; 3.15 A; A/B/C=1-335. DR PDB; 6IQ6; X-ray; 2.29 A; A/B/C/D/E/F/G/H=1-335. DR PDB; 6M61; X-ray; 1.82 A; O/P/Q/R=1-335. DR PDB; 6YND; X-ray; 1.52 A; A/B/C/D/E/F/G/H=1-335. DR PDB; 6YNE; X-ray; 1.85 A; A/B/C/D=1-335. DR PDB; 6YNF; X-ray; 2.39 A; A/B/C/D/E/F/G/H=2-335. DR PDB; 6YNH; X-ray; 2.62 A; B/D/F/G=1-335. DR PDB; 8DNS; EM; 3.22 A; O/P/Q/R=1-335. DR PDB; 8G12; EM; 2.17 A; A/B/C/D=2-335. DR PDB; 8G13; EM; 2.30 A; A/B/C/D=2-335. DR PDB; 8G14; EM; 2.30 A; A/B/C/D=2-335. DR PDB; 8G15; EM; 2.07 A; A/B/C/D=2-335. DR PDB; 8G16; EM; 2.07 A; A/B/C/D=2-335. DR PDB; 8G17; EM; 1.98 A; A/B/C/D=2-335. DR PDB; 8P5F; X-ray; 1.82 A; AAA/DDD/EEE/GGG=1-335. DR PDBsum; 1U8F; -. DR PDBsum; 1ZNQ; -. DR PDBsum; 3GPD; -. DR PDBsum; 4WNC; -. DR PDBsum; 4WNI; -. DR PDBsum; 6ADE; -. DR PDBsum; 6IQ6; -. DR PDBsum; 6M61; -. DR PDBsum; 6YND; -. DR PDBsum; 6YNE; -. DR PDBsum; 6YNF; -. DR PDBsum; 6YNH; -. DR PDBsum; 8DNS; -. DR PDBsum; 8G12; -. DR PDBsum; 8G13; -. DR PDBsum; 8G14; -. DR PDBsum; 8G15; -. DR PDBsum; 8G16; -. DR PDBsum; 8G17; -. DR PDBsum; 8P5F; -. DR AlphaFoldDB; P04406; -. DR EMDB; EMD-27579; -. DR EMDB; EMD-29659; -. DR EMDB; EMD-29660; -. DR EMDB; EMD-29661; -. DR EMDB; EMD-29662; -. DR EMDB; EMD-29663; -. DR EMDB; EMD-29664; -. DR EMDB; EMD-32162; -. DR SMR; P04406; -. DR BioGRID; 108868; 643. DR ComplexPortal; CPX-2476; GAIT complex. DR CORUM; P04406; -. DR DIP; DIP-32521N; -. DR IntAct; P04406; 236. DR MINT; P04406; -. DR STRING; 9606.ENSP00000380070; -. DR BindingDB; P04406; -. DR ChEMBL; CHEMBL2284; -. DR DrugBank; DB07347; 4-(2-Aminoethyl)Benzenesulfonyl Fluoride. DR DrugBank; DB02059; Adenosine-5-Diphosphoribose. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB09130; Copper. DR DrugBank; DB00157; NADH. DR DrugBank; DB03893; Thionicotinamide-Adenine-Dinucleotide. DR DrugBank; DB09092; Xanthinol. DR DrugCentral; P04406; -. DR MoonDB; P04406; Curated. DR MoonProt; P04406; -. DR GlyConnect; 1941; 7 N-Linked glycans (2 sites). DR GlyCosmos; P04406; 6 sites, 9 glycans. DR GlyGen; P04406; 4 sites, 16 N-linked glycans (2 sites), 2 O-linked glycans (2 sites). DR iPTMnet; P04406; -. DR MetOSite; P04406; -. DR PhosphoSitePlus; P04406; -. DR SwissPalm; P04406; -. DR BioMuta; GAPDH; -. DR DMDM; 120649; -. DR OGP; P04406; -. DR REPRODUCTION-2DPAGE; IPI00219018; -. DR REPRODUCTION-2DPAGE; P04406; -. DR CPTAC; CPTAC-2733; -. DR CPTAC; CPTAC-5855; -. DR CPTAC; CPTAC-5880; -. DR CPTAC; CPTAC-5942; -. DR jPOST; P04406; -. DR MassIVE; P04406; -. DR PaxDb; 9606-ENSP00000229239; -. DR PeptideAtlas; P04406; -. DR PRIDE; P04406; -. DR ProteomicsDB; 18491; -. DR ProteomicsDB; 51703; -. [P04406-1] DR Pumba; P04406; -. DR TopDownProteomics; P04406-1; -. [P04406-1] DR ABCD; P04406; 1 sequenced antibody. DR Antibodypedia; 3923; 2630 antibodies from 59 providers. DR CPTC; P04406; 1 antibody. DR DNASU; 2597; -. DR Ensembl; ENST00000229239.10; ENSP00000229239.5; ENSG00000111640.15. [P04406-1] DR Ensembl; ENST00000396858.5; ENSP00000380067.1; ENSG00000111640.15. [P04406-2] DR Ensembl; ENST00000396859.5; ENSP00000380068.1; ENSG00000111640.15. [P04406-1] DR Ensembl; ENST00000396861.5; ENSP00000380070.1; ENSG00000111640.15. [P04406-1] DR Ensembl; ENST00000619601.1; ENSP00000478864.1; ENSG00000111640.15. [P04406-2] DR GeneID; 2597; -. DR KEGG; hsa:2597; -. DR MANE-Select; ENST00000229239.10; ENSP00000229239.5; NM_002046.7; NP_002037.2. DR UCSC; uc031qfw.3; human. [P04406-1] DR AGR; HGNC:4141; -. DR CTD; 2597; -. DR DisGeNET; 2597; -. DR GeneCards; GAPDH; -. DR HGNC; HGNC:4141; GAPDH. DR HPA; ENSG00000111640; Group enriched (skeletal muscle, tongue). DR MalaCards; GAPDH; -. DR MIM; 138400; gene. DR neXtProt; NX_P04406; -. DR OpenTargets; ENSG00000111640; -. DR PharmGKB; PA28554; -. DR VEuPathDB; HostDB:ENSG00000111640; -. DR eggNOG; KOG0657; Eukaryota. DR GeneTree; ENSGT00940000153298; -. DR HOGENOM; CLU_030140_0_3_1; -. DR InParanoid; P04406; -. DR OMA; YGYTCNM; -. DR OrthoDB; 275384at2759; -. DR PhylomeDB; P04406; -. DR TreeFam; TF300533; -. DR BioCyc; MetaCyc:HS03433-MONOMER; -. DR BRENDA; 1.2.1.12; 2681. DR PathwayCommons; P04406; -. DR Reactome; R-HSA-70171; Glycolysis. DR Reactome; R-HSA-70263; Gluconeogenesis. DR SABIO-RK; P04406; -. DR SignaLink; P04406; -. DR SIGNOR; P04406; -. DR UniPathway; UPA00109; UER00184. DR BioGRID-ORCS; 2597; 626 hits in 1149 CRISPR screens. DR ChiTaRS; GAPDH; human. DR EvolutionaryTrace; P04406; -. DR GeneWiki; Glyceraldehyde_3-phosphate_dehydrogenase; -. DR GenomeRNAi; 2597; -. DR Pharos; P04406; Tchem. DR PRO; PR:P04406; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P04406; protein. DR Bgee; ENSG00000111640; Expressed in frontal pole and 218 other cell types or tissues. DR ExpressionAtlas; P04406; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0097452; C:GAIT complex; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:CACAO. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0031982; C:vesicle; HDA:UniProtKB. DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IDA:UniProtKB. DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. 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; IDA:UniProtKB. DR GO; GO:0071346; P:cellular response to type II interferon; IDA:UniProtKB. DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR GO; GO:0051873; P:killing by host of symbiont cells; IDA:UniProtKB. DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB. DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB. DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB. 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:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IDA:UniProtKB. DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB. DR GO; GO:0032481; P:positive regulation of type I interferon production; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB. DR GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL. DR FunFam; 3.30.360.10:FF:000001; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:001161; Glyceraldehyde-3-phosphate dehydrogenase; 1. 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. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing; KW Apoptosis; Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycolysis; KW Glycoprotein; Immunity; Innate immunity; Isopeptide bond; Membrane; KW Methylation; NAD; Nucleus; Oxidation; Oxidoreductase; Phosphoprotein; KW Proteomics identification; Reference proteome; S-nitrosylation; KW Transferase; Translation regulation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.19" FT CHAIN 2..335 FT /note="Glyceraldehyde-3-phosphate dehydrogenase" FT /id="PRO_0000145486" FT REGION 2..148 FT /note="Interaction with WARS1" FT /evidence="ECO:0000269|PubMed:15628863" FT MOTIF 245..250 FT /note="[IL]-x-C-x-x-[DE] motif" FT /evidence="ECO:0000305|PubMed:25417112" FT ACT_SITE 152 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:25086035" FT BINDING 13..14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16239728, FT ECO:0000269|PubMed:16510976" FT BINDING 35 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16239728, FT ECO:0000269|PubMed:16510976" FT BINDING 80 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16239728, FT ECO:0000269|PubMed:16510976" FT BINDING 122 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16239728, FT ECO:0000269|PubMed:16510976" FT BINDING 151..153 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P22513" FT BINDING 182 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P22513" FT BINDING 211..212 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P22513" FT BINDING 234 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:P22513" FT BINDING 316 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:16239728, FT ECO:0000269|PubMed:16510976" FT SITE 179 FT /note="Activates thiol group during catalysis" FT /evidence="ECO:0000305|PubMed:16239728, FT ECO:0000305|PubMed:16510976" FT MOD_RES 5 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 9 FT /note="Deamidated asparagine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 42 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 46 FT /note="Methionine sulfoxide; in vitro" FT /evidence="ECO:0000305|PubMed:25086035" FT MOD_RES 61 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 64 FT /note="Deamidated asparagine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 66 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 70 FT /note="Deamidated asparagine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 75 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18183946, FT ECO:0007744|PubMed:20068231" FT MOD_RES 83 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 122 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 148 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 149 FT /note="Deamidated asparagine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 151 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 152 FT /note="ADP-ribosylcysteine; by autocatalysis; in FT irreversibly inhibited form" FT /evidence="ECO:0000250|UniProtKB:P04797" FT MOD_RES 152 FT /note="Cysteine persulfide" FT /evidence="ECO:0000250|UniProtKB:P16858" FT MOD_RES 152 FT /note="S-(2-succinyl)cysteine" FT /evidence="ECO:0000250|UniProtKB:P04797" FT MOD_RES 152 FT /note="S-nitrosocysteine; in reversibly inhibited form" FT /evidence="ECO:0000250|UniProtKB:P04797" FT MOD_RES 153 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 155 FT /note="Deamidated asparagine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 177 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 182 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 184 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 194 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 194 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 194 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21908771" FT MOD_RES 211 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 215 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 215 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21908771" FT MOD_RES 219 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 225 FT /note="Deamidated asparagine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 227 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 227 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 229 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18183946, FT ECO:0007744|PubMed:23186163" FT MOD_RES 237 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 241 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 247 FT /note="S-(2-succinyl)cysteine" FT /evidence="ECO:0000250|UniProtKB:P04797" FT MOD_RES 247 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000269|PubMed:22771119, FT ECO:0000269|PubMed:25417112" FT MOD_RES 254 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 260 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 263 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 312 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18183946, FT ECO:0007744|PubMed:19690332" FT MOD_RES 316 FT /note="Deamidated asparagine" FT /evidence="ECO:0000269|PubMed:18183946" FT MOD_RES 333 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 334 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000269|PubMed:18183946" FT CARBOHYD 197 FT /note="(Microbial infection) N-beta-linked (GlcNAc) FT arginine" FT /evidence="ECO:0000269|PubMed:28522607" FT CARBOHYD 200 FT /note="(Microbial infection) N-beta-linked (GlcNAc) FT arginine" FT /evidence="ECO:0000269|PubMed:28522607" FT CROSSLNK 186 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..42 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_047289" FT VARIANT 22 FT /note="A -> G (in dbSNP:rs45541435)" FT /evidence="ECO:0000269|Ref.12" FT /id="VAR_018889" FT VARIANT 251 FT /note="K -> N (in dbSNP:rs1062429)" FT /id="VAR_049218" FT MUTAGEN 46 FT /note="M->L: Drastic reduction of the extent and FT significant prolongation of the lag phase of free FT radical-induced aggregation." FT /evidence="ECO:0000269|PubMed:25086035" FT MUTAGEN 105 FT /note="M->L: Increased resistance to free radical-induced FT aggregation." FT /evidence="ECO:0000269|PubMed:25086035" FT MUTAGEN 152 FT /note="C->S: Markedly reduced glycolytic activity; when FT associated with S-156 and S-247. Forms free radical-induced FT aggregates, but to a lesser extent than wild-type protein; FT when associated with S-156 and S-247. Abolished interaction FT with TRAF2 and TRAF3." FT /evidence="ECO:0000269|PubMed:23332158, FT ECO:0000269|PubMed:25086035, ECO:0000269|PubMed:27387501" FT MUTAGEN 156 FT /note="C->S: Markedly reduced glycolytic activity; when FT associated with S-152 and S-247. Forms free radical-induced FT aggregates, but to a lesser extent than wild-type protein; FT when associated with S-156 and S-247." FT /evidence="ECO:0000269|PubMed:25086035" FT MUTAGEN 196 FT /note="W->F: Increased free radical-induced aggregation." FT /evidence="ECO:0000269|PubMed:25086035" FT MUTAGEN 211 FT /note="T->A: Does not affect glycosylation by C.rodentium FT protein NleB." FT /evidence="ECO:0000269|PubMed:23332158" FT MUTAGEN 229 FT /note="T->A: Does not affect glycosylation by C.rodentium FT protein NleB." FT /evidence="ECO:0000269|PubMed:23332158" FT MUTAGEN 241 FT /note="S->A: Does not affect glycosylation by C.rodentium FT protein NleB." FT /evidence="ECO:0000269|PubMed:23332158" FT MUTAGEN 245 FT /note="L->M: Inhibits S-nitrosylation of Cys-247; when FT associated with M-250." FT /evidence="ECO:0000269|PubMed:25417112" FT MUTAGEN 246 FT /note="T->A: Does not affect glycosylation by C.rodentium FT protein NleB." FT /evidence="ECO:0000269|PubMed:23332158" FT MUTAGEN 247 FT /note="C->S: Markedly reduced glycolytic activity; when FT associated with S-152 and S-156. Forms free radical-induced FT aggregates, but to a lesser extent than wild-type protein; FT when associated with S-156 and S-247." FT /evidence="ECO:0000269|PubMed:25086035" FT MUTAGEN 250 FT /note="E->M: Inhibits S-nitrosylation of Cys-247; when FT associated with M-245." FT /evidence="ECO:0000269|PubMed:25417112" FT MUTAGEN 277 FT /note="T->A: Does not affect glycosylation by C.rodentium FT protein NleB." FT /evidence="ECO:0000269|PubMed:23332158" FT MUTAGEN 320 FT /note="Y->F: No effect on free radical-induced FT aggregation." FT /evidence="ECO:0000269|PubMed:25086035" FT CONFLICT 225 FT /note="N -> D (in Ref. 2; CAA25833)" FT /evidence="ECO:0000305" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 13..25 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 27..34 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 40..48 FT /evidence="ECO:0007829|PDB:6YND" FT TURN 51..53 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 72..77 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 94..97 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 105..108 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 110..113 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 117..123 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:6YND" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 152..168 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 170..179 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 185..189 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 196..199 FT /evidence="ECO:0007829|PDB:6YND" FT TURN 202..204 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 207..210 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 213..220 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 227..234 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 241..251 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 255..267 FT /evidence="ECO:0007829|PDB:6YND" FT TURN 268..273 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 274..277 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 283..286 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:6YND" FT TURN 297..299 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 301..304 FT /evidence="ECO:0007829|PDB:6YND" FT STRAND 307..314 FT /evidence="ECO:0007829|PDB:6YND" FT HELIX 318..333 FT /evidence="ECO:0007829|PDB:6YND" SQ SEQUENCE 335 AA; 36053 MW; C9C135E8AE3E8744 CRC64; MGKVKVGVNG FGRIGRLVTR AAFNSGKVDI VAINDPFIDL NYMVYMFQYD STHGKFHGTV KAENGKLVIN GNPITIFQER DPSKIKWGDA GAEYVVESTG VFTTMEKAGA HLQGGAKRVI ISAPSADAPM FVMGVNHEKY DNSLKIISNA SCTTNCLAPL AKVIHDNFGI VEGLMTTVHA ITATQKTVDG PSGKLWRDGR GALQNIIPAS TGAAKAVGKV IPELNGKLTG MAFRVPTANV SVVDLTCRLE KPAKYDDIKK VVKQASEGPL KGILGYTEHQ VVSSDFNSDT HSSTFDAGAG IALNDHFVKL ISWYDNEFGY SNRVVDLMAH MASKE //