G3P_HUMAN
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 03-AUG-2022, entry version 262.
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:3170585, PubMed:11724794).
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:3170585, PubMed:11724794). 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 + 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:3170585};
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: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:16501887, PubMed:15628863,
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; 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; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-354056, EBI-25830870;
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=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gapd/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Glyceraldehyde 3-phosphate
CC dehydrogenase entry;
CC URL="https://en.wikipedia.org/wiki/Glyceraldehyde_3-phosphate_dehydrogenase";
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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 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 AlphaFoldDB; P04406; -.
DR SMR; P04406; -.
DR BioGRID; 108868; 394.
DR CORUM; P04406; -.
DR DIP; DIP-32521N; -.
DR IntAct; P04406; 211.
DR MINT; P04406; -.
DR STRING; 9606.ENSP00000229239; -.
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 GlyGen; P04406; 4 sites, 7 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 DOSAC-COBS-2DPAGE; P04406; -.
DR OGP; P04406; -.
DR REPRODUCTION-2DPAGE; IPI00219018; -.
DR REPRODUCTION-2DPAGE; P04406; -.
DR SWISS-2DPAGE; P04406; -.
DR UCD-2DPAGE; P04406; -.
DR EPD; P04406; -.
DR jPOST; P04406; -.
DR MassIVE; P04406; -.
DR MaxQB; P04406; -.
DR PaxDb; P04406; -.
DR PeptideAtlas; P04406; -.
DR PRIDE; P04406; -.
DR ProteomicsDB; 18491; -.
DR ProteomicsDB; 51703; -. [P04406-1]
DR TopDownProteomics; P04406-1; -. [P04406-1]
DR ABCD; P04406; 1 sequenced antibody.
DR Antibodypedia; 3923; 2677 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 CTD; 2597; -.
DR DisGeNET; 2597; -.
DR GeneCards; GAPDH; -.
DR HGNC; HGNC:4141; GAPDH.
DR HPA; ENSG00000111640; Group enriched (skeletal muscle, tongue).
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; NCVAPMA; -.
DR PhylomeDB; P04406; -.
DR TreeFam; TF300533; -.
DR BioCyc; MetaCyc:HS03433-MON; -.
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; 589 hits in 1056 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 216 other tissues.
DR ExpressionAtlas; P04406; baseline and differential.
DR Genevisible; P04406; HS.
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 interferon-gamma; 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:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; 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 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; 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 Reference proteome; S-nitrosylation; Transferase; Translation regulation;
KW 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 radical-
FT 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
