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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-)

 G3P_HUMAN               Reviewed;         335 AA.
P04406; E7EUT4; P00354; Q53X65;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 239.
RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
Short=GAPDH;
EC=1.2.1.12;
AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH;
EC=2.6.99.-;
Name=GAPDH; Synonyms=GAPD; ORFNames=CDABP0047, OK/SW-cl.12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6096136;
Hanauer A., Mandel J.-L.;
"The glyceraldehyde 3 phosphate dehydrogenase gene family: structure
of a human cDNA and of an X chromosome linked pseudogene; amazing
complexity of the gene family in mouse.";
EMBO J. 3:2627-2633(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6096821; DOI=10.1093/nar/12.23.9179;
Arcari P., Martinelli R., Salvatore F.;
"The complete sequence of a full length cDNA for human liver
glyceraldehyde-3-phosphate dehydrogenase: evidence for multiple mRNA
species.";
Nucleic Acids Res. 12:9179-9189(1984).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2987855; DOI=10.1093/nar/13.7.2485;
Tso J.Y., Sun X.-H., Kao T.-H., Reece K.S., Wu R.;
"Isolation and characterization of rat and human glyceraldehyde-3-
phosphate dehydrogenase cDNAs: genomic complexity and molecular
evolution of the gene.";
Nucleic Acids Res. 13:2485-2502(1985).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=3664468;
Tokunaga K., Nakamura Y., Sakata K., Fujimori K., Ohkubo M.,
Sawada K., Sakiyama S.;
"Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase
gene in human lung cancers.";
Cancer Res. 47:5616-5619(1987).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3027061;
Allen R.W., Trach K.A., Hoch J.A.;
"Identification of the 37-kDa protein displaying a variable
interaction with the erythroid cell membrane as glyceraldehyde-3-
phosphate dehydrogenase.";
J. Biol. Chem. 262:649-653(1987).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=3170585;
Ercolani L., Florence B., Denaro M., Alexander M.;
"Isolation and complete sequence of a functional human glyceraldehyde-
3-phosphate dehydrogenase gene.";
J. Biol. Chem. 263:15335-15341(1988).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=1924305; DOI=10.1073/pnas.88.19.8460;
Meyer-Siegler K., Mauro D.J., Seal G., Wurzer J., Deriel J.K.,
Sirover M.A.;
"A human nuclear uracil DNA glycosylase is the 37-kDa subunit of
glyceraldehyde-3-phosphate dehydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 88:8460-8464(1991).
[8]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Astrocytoma;
PubMed=10944468; DOI=10.1006/bbrc.2000.3282;
Ye Z., Connor J.R.;
"cDNA cloning by amplification of circularized first strand cDNAs
reveals non-IRE-regulated iron-responsive mRNAs.";
Biochem. Biophys. Res. Commun. 275:223-227(2000).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Leukemia;
Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
Margolin J.F.;
"Pediatric leukemia cDNA sequencing project.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-22.
NIEHS SNPs program;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, Kidney, Lung, Lymph, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[17]
PRELIMINARY PROTEIN SEQUENCE OF 2-335.
TISSUE=Muscle;
PubMed=7030790; DOI=10.1016/0014-5793(81)80587-X;
Nowak K., Wolny M., Banas T.;
"The complete amino acid sequence of human muscle glyceraldehyde 3-
phosphate dehydrogenase.";
FEBS Lett. 134:143-146(1981).
[18]
PROTEIN SEQUENCE OF 2-13.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[19]
PROTEIN SEQUENCE OF 2-13; 62-84; 118-139; 198-215; 220-227; 235-248
AND 310-335, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Prostatic carcinoma;
Bienvenut W.V., Gao M., Leug H.;
Submitted (JUL-2009) to UniProtKB.
[20]
PROTEIN SEQUENCE OF 67-80; 87-107; 119-139; 146-186; 201-215; 235-248
AND 310-334, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[21]
PROTEIN SEQUENCE OF 220-226 AND 242-246.
TISSUE=Heart;
PubMed=7498159; DOI=10.1002/elps.11501601192;
Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A.,
Ershova E.S., Egorov T.A., Musalyamov A.K.;
"The major protein expression profile and two-dimensional protein
database of human heart.";
Electrophoresis 16:1160-1169(1995).
[22]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Muscle;
PubMed=1193541;
Nowak K., Kuczek M., Ostropolska L., Malarska A., Wolny M.,
Branowski T.;
"The covalent structure of glyceraldehyde-phosphate dehydrogenase from
human muscles. Isolation and amino acid sequences of peptides from
tryptic digest.";
Hoppe-Seyler's Z. Physiol. Chem. 356:1181-1183(1975).
[23]
FUNCTION, AND INTERACTION WITH PRKCI.
PubMed=11724794; DOI=10.1074/jbc.M109744200;
Tisdale E.J.;
"Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein
kinase Ciota /lambda and plays a role in microtubule dynamics in the
early secretory pathway.";
J. Biol. Chem. 277:3334-3341(2002).
[24]
SUBCELLULAR LOCATION.
PubMed=12829261; DOI=10.1016/S0304-4165(03)00117-X;
Mazzola J.L., Sirover M.A.;
"Subcellular localization of human glyceraldehyde-3-phosphate
dehydrogenase is independent of its glycolytic function.";
Biochim. Biophys. Acta 1622:50-56(2003).
[25]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[26]
IDENTIFICATION IN THE GAIT COMPLEX.
PubMed=15479637; DOI=10.1016/j.cell.2004.09.030;
Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L.,
Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.;
"Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-
specific silencing of translation.";
Cell 119:195-208(2004).
[27]
INTERACTION WITH WARS.
PubMed=15628863; DOI=10.1021/bi048313k;
Wakasugi K., Nakano T., Morishima I.;
"Oxidative stress-responsive intracellular regulation specific for the
angiostatic form of human tryptophanyl-tRNA synthetase.";
Biochemistry 44:225-232(2005).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[30]
INTERACTION WITH USP25.
PubMed=16501887; DOI=10.1007/s00018-005-5533-1;
Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G.,
Marfany G.;
"The ubiquitin-specific protease USP25 interacts with three sarcomeric
proteins.";
Cell. Mol. Life Sci. 63:723-734(2006).
[31]
ISGYLATION.
PubMed=16815975; DOI=10.1073/pnas.0600397103;
Wong J.J., Pung Y.F., Sze N.S., Chin K.C.;
"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates
type I IFN-induced ISGylation of protein targets.";
Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006).
[32]
PHOSPHORYLATION AT THR-75; SER-122; SER-148; THR-229; THR-237 AND
SER-312, DEAMIDATION AT ASN-9; ASN-64; ASN-70; ASN-149; ASN-155;
ASN-225 AND ASN-316, AND METHYLATION AT LYS-5; LYS-66; LYS-194;
LYS-215; LYS-227; LYS-260; LYS-263 AND LYS-334.
PubMed=18183946; DOI=10.1021/pr700657y;
Seo J., Jeong J., Kim Y.M., Hwang N., Paek E., Lee K.-J.;
"Strategy for comprehensive identification of post-translational
modifications in cellular proteins, including low abundant
modifications: application to glyceraldehyde-3-phosphate
dehydrogenase.";
J. Proteome Res. 7:587-602(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-151 AND THR-184,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[35]
INTERACTION WITH FKBP6.
PubMed=19001379; DOI=10.1074/jbc.M709779200;
Jarczowski F., Jahreis G., Erdmann F., Schierhorn A., Fischer G.,
Edlich F.;
"FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate
dehydrogenase inhibitor.";
J. Biol. Chem. 284:766-773(2009).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-184; THR-211 AND
SER-312, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[37]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-194; LYS-219;
LYS-227 AND LYS-254, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[38]
INTERACTION WITH EIF1AD.
PubMed=20644585; DOI=10.1134/S1068162010030027;
Rakitina T.V., Bogatova O.V., Smirnova E.V., Pozdeev V.I.,
Kostanian I.A., Lipkin V.M.;
"Haponin (eIF1AD) interacts with glyceraldehyde 3-phosphate
dehydrogenase in the CHO-K1 cell line.";
Bioorg. Khim. 36:312-318(2010).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75; SER-83 AND THR-184,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[41]
MALONYLATION AT LYS-194 AND LYS-215.
PubMed=21908771; DOI=10.1074/mcp.M111.012658;
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
Dai J., Verdin E., Ye Y., Zhao Y.;
"The first identification of lysine malonylation substrates and its
regulatory enzyme.";
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[44]
INTERACTION WITH RPL13A, AND S-NITROSYLATION AT CYS-247.
PubMed=22771119; DOI=10.1016/j.molcel.2012.06.006;
Jia J., Arif A., Willard B., Smith J.D., Stuehr D.J., Hazen S.L.,
Fox P.L.;
"Protection of extraribosomal RPL13a by GAPDH and dysregulation by S-
nitrosylation.";
Mol. Cell 47:656-663(2012).
[45]
FUNCTION, AND RECONSTITUTION OF THE GAIT COMPLEX.
PubMed=23071094; DOI=10.1128/MCB.01168-12;
Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
"Heterotrimeric GAIT complex drives transcript-selective translation
inhibition in murine macrophages.";
Mol. Cell. Biol. 32:5046-5055(2012).
[46]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-151; THR-153;
THR-229 AND SER-333, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[48]
S-NITROSYLATION AT CYS-247, MUTAGENESIS OF LEU-245 AND GLU-250, AND
DOMAIN.
PubMed=25417112; DOI=10.1016/j.cell.2014.09.032;
Jia J., Arif A., Terenzi F., Willard B., Plow E.F., Hazen S.L.,
Fox P.L.;
"Target-selective protein S-nitrosylation by sequence motif
recognition.";
Cell 159:623-634(2014).
[49]
MECHANISM OF FREE RADICAL-INDUCED AGGREGATION, OXIDATION AT MET-46,
AND MUTAGENESIS OF MET-46; MET-105; CYS-152; CYS-156; TRP-196; CYS-247
AND TYR-320.
PubMed=25086035; DOI=10.1074/jbc.M114.570275;
Samson A.L., Knaupp A.S., Kass I., Kleifeld O., Marijanovic E.M.,
Hughes V.A., Lupton C.J., Buckle A.M., Bottomley S.P., Medcalf R.L.;
"Oxidation of an exposed methionine instigates the aggregation of
glyceraldehyde-3-phosphate dehydrogenase.";
J. Biol. Chem. 289:26922-26936(2014).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177; THR-182; THR-184
AND SER-241, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[52]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-186, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[53]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
PubMed=957435; DOI=10.1016/0022-2836(76)90013-9;
Mercer W.D., Winn S.I., Watson H.C.;
"Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-
phosphate dehydrogenase.";
J. Mol. Biol. 104:277-283(1976).
[54]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, AND
SUBUNIT.
PubMed=16239728; DOI=10.1107/S0907444905026740;
Ismail S.A., Park H.W.;
"Structural analysis of human liver glyceraldehyde-3-phosphate
dehydrogenase.";
Acta Crystallogr. D 61:1508-1513(2005).
[55]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD, AND
SUBUNIT.
PubMed=16510976; DOI=10.1107/S0907444905042289;
Jenkins J.L., Tanner J.J.;
"High-resolution structure of human D-glyceraldehyde-3-phosphate
dehydrogenase.";
Acta Crystallogr. D 62:290-301(2006).
-!- FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and
nitrosylase activities, thereby playing a role in glycolysis and
nuclear functions, respectively. Participates in nuclear events
including transcription, RNA transport, DNA replication and
apoptosis. Nuclear functions are probably due to the nitrosylase
activity that mediates cysteine S-nitrosylation of nuclear target
proteins such as SIRT1, HDAC2 and PRKDC. Modulates the
organization and assembly of the cytoskeleton. Facilitates the
CHP1-dependent microtubule and membrane associations through its
ability to stimulate the binding of CHP1 to microtubules (By
similarity). Glyceraldehyde-3-phosphate dehydrogenase is a key
enzyme in glycolysis that catalyzes the first step of the pathway
by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-
glyceroyl phosphate. Component of the GAIT (gamma interferon-
activated inhibitor of translation) complex which mediates
interferon-gamma-induced transcript-selective translation
inhibition in inflammation processes. Upon interferon-gamma
treatment assembles into the GAIT complex which binds to stem
loop-containing GAIT elements in the 3'-UTR of diverse
inflammatory mRNAs (such as ceruplasmin) and suppresses their
translation. {ECO:0000250, ECO:0000269|PubMed:11724794,
ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:3170585}.
-!- CATALYTIC ACTIVITY:
Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = 3-
phospho-D-glyceroyl phosphate + H(+) + NADH;
Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945,
ChEBI:CHEBI:59776; EC=1.2.1.12; Evidence={ECO:0000255|PROSITE-
ProRule:PRU10009, ECO:0000269|PubMed:3170585};
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 1/5.
-!- SUBUNIT: Homotetramer. Interacts with TPPP; the interaction is
direct. Interacts (when S-nitrosylated) with SIAH1; leading to
nuclear translocation. Interacts with RILPL1/GOSPEL, leading to
prevent the interaction between GAPDH and SIAH1 and prevent
nuclear translocation. Interacts with CHP1; the interaction
increases the binding of CHP1 with microtubules. Associates with
microtubules (By similarity). Interacts with EIF1AD, USP25, PRKCI
and WARS. Interacts with phosphorylated RPL13A; inhibited by
oxidatively-modified low-densitity lipoprotein (LDL(ox)).
Component of the GAIT complex. Interacts with FKBP6; leading to
inhibit GAPDH catalytic activity. {ECO:0000250,
ECO:0000269|PubMed:11724794, ECO:0000269|PubMed:15479637,
ECO:0000269|PubMed:15628863, ECO:0000269|PubMed:16239728,
ECO:0000269|PubMed:16501887, ECO:0000269|PubMed:16510976,
ECO:0000269|PubMed:19001379, ECO:0000269|PubMed:20644585,
ECO:0000269|PubMed:22771119}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-354056, EBI-354056;
Q60823:Akt2 (xeno); NbExp=2; IntAct=EBI-354056, EBI-400263;
P00533:EGFR; NbExp=6; IntAct=EBI-354056, EBI-297353;
P35228:NOS2; NbExp=8; IntAct=EBI-354056, EBI-6662224;
P12004:PCNA; NbExp=3; IntAct=EBI-354056, EBI-358311;
P00558:PGK1; NbExp=2; IntAct=EBI-354056, EBI-709599;
P48147:PREP; NbExp=5; IntAct=EBI-354056, EBI-1049962;
P15927:RPA2; NbExp=2; IntAct=EBI-354056, EBI-621404;
P05109:S100A8; NbExp=6; IntAct=EBI-354056, EBI-355281;
P00441:SOD1; NbExp=3; IntAct=EBI-354056, EBI-990792;
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-354056, EBI-717399;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:12829261}. Nucleus {ECO:0000250}. Cytoplasm,
perinuclear region {ECO:0000269|PubMed:12829261}. Membrane
{ECO:0000269|PubMed:12829261}. Cytoplasm, cytoskeleton
{ECO:0000250}. Note=Translocates to the nucleus following S-
nitrosylation and interaction with SIAH1, which contains a nuclear
localization signal (By similarity). Postnuclear and Perinuclear
regions. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P04406-1; Sequence=Displayed;
Name=2;
IsoId=P04406-2; Sequence=VSP_047289;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
transnitrosylase complex. {ECO:0000305|PubMed:25417112}.
-!- PTM: S-nitrosylation of Cys-152 leads to interaction with SIAH1,
followed by translocation to the nucleus (By similarity). S-
nitrosylation of Cys-247 is induced by interferon-gamma and
LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and
seems to prevent interaction with phosphorylated RPL13A and to
interfere with GAIT complex activity.
{ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:22771119,
ECO:0000269|PubMed:25417112}.
-!- PTM: ISGylated. {ECO:0000305|PubMed:16815975}.
-!- PTM: Sulfhydration at Cys-152 increases catalytic activity.
{ECO:0000250}.
-!- PTM: Oxidative stress can promote the formation of high molecular
weight disulfide-linked GAPDH aggregates, through a process called
nucleocytoplasmic coagulation. Such aggregates can be observed in
vivo in the affected tissues of patients with Alzheimer disease or
alcoholic liver cirrhosis, or in cell cultures during necrosis.
Oxidation at Met-46 may play a pivotal role in the formation of
these insoluble structures. This modification has been detected in
vitro following treatment with free radical donor (+/-)-(E)-4-
ethyl-2-[(E)-hydroxyimino]-5-nitro-3-hexenamide. It has been
proposed to destabilize nearby residues, increasing the likelihood
of secondary oxidative damages, including oxidation of Tyr-45 and
Met-105. This cascade of oxidations may augment GAPDH misfolding,
leading to intermolecular disulfide cross-linking and aggregation.
{ECO:0000305|PubMed:25086035}.
-!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
dehydrogenase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/gapd/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Glyceraldehyde 3-phosphate
dehydrogenase entry;
URL="https://en.wikipedia.org/wiki/Glyceraldehyde_3-phosphate_dehydrogenase";
-----------------------------------------------------------------------
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EMBL; X01677; CAA25833.1; -; mRNA.
EMBL; M17851; AAA86283.1; -; mRNA.
EMBL; M33197; AAA52518.1; -; mRNA.
EMBL; J02642; AAA52496.1; -; mRNA.
EMBL; J04038; AAA53191.1; -; Genomic_DNA.
EMBL; X53778; CAA37794.1; -; mRNA.
EMBL; AF261085; AAF99678.1; -; mRNA.
EMBL; AY007133; AAG01996.1; -; mRNA.
EMBL; AB062273; BAB93466.1; -; mRNA.
EMBL; BT006893; AAP35539.1; -; mRNA.
EMBL; AY340484; AAP88932.1; -; Genomic_DNA.
EMBL; CR407671; CAG28599.1; -; mRNA.
EMBL; AC006064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471116; EAW88787.1; -; Genomic_DNA.
EMBL; BC001601; AAH01601.1; -; mRNA.
EMBL; BC004109; AAH04109.1; -; mRNA.
EMBL; BC009081; AAH09081.1; -; mRNA.
EMBL; BC013310; AAH13310.1; -; mRNA.
EMBL; BC023632; AAH23632.1; -; mRNA.
EMBL; BC025925; AAH25925.1; -; mRNA.
EMBL; BC026907; AAH26907.1; -; mRNA.
EMBL; BC029618; AAH29618.1; -; mRNA.
EMBL; BC083511; AAH83511.1; -; mRNA.
CCDS; CCDS58201.1; -. [P04406-2]
CCDS; CCDS8549.1; -. [P04406-1]
PIR; A31988; DEHUG3.
RefSeq; NP_001243728.1; NM_001256799.2. [P04406-2]
RefSeq; NP_001276674.1; NM_001289745.1. [P04406-1]
RefSeq; NP_001276675.1; NM_001289746.1. [P04406-1]
RefSeq; NP_002037.2; NM_002046.5. [P04406-1]
UniGene; Hs.544577; -.
UniGene; Hs.592355; -.
UniGene; Hs.598320; -.
PDB; 1U8F; X-ray; 1.75 A; O/P/Q/R=1-335.
PDB; 1ZNQ; X-ray; 2.50 A; O/P/Q/R=1-335.
PDB; 2FEH; Model; -; O/P/Q/R=1-335.
PDB; 3GPD; X-ray; 3.50 A; G/R=2-335.
PDB; 4WNC; X-ray; 1.99 A; A/B/C/D/E/F/G/O=1-335.
PDB; 4WNI; X-ray; 2.30 A; A/B/C/O=1-335.
PDB; 6ADE; X-ray; 3.15 A; A/B/C=1-335.
PDBsum; 1U8F; -.
PDBsum; 1ZNQ; -.
PDBsum; 2FEH; -.
PDBsum; 3GPD; -.
PDBsum; 4WNC; -.
PDBsum; 4WNI; -.
PDBsum; 6ADE; -.
ProteinModelPortal; P04406; -.
SMR; P04406; -.
BioGrid; 108868; 213.
CORUM; P04406; -.
DIP; DIP-32521N; -.
IntAct; P04406; 104.
MINT; P04406; -.
STRING; 9606.ENSP00000229239; -.
BindingDB; P04406; -.
ChEMBL; CHEMBL2284; -.
DrugBank; DB07347; 4-(2-AMINOETHYL)BENZENESULFONYL FLUORIDE.
DrugBank; DB02059; Adenosine-5-Diphosphoribose.
DrugBank; DB00157; NADH.
DrugBank; DB03893; Thionicotinamide-Adenine-Dinucleotide.
MoonDB; P04406; Curated.
MoonProt; P04406; -.
iPTMnet; P04406; -.
PhosphoSitePlus; P04406; -.
SwissPalm; P04406; -.
BioMuta; GAPDH; -.
DMDM; 120649; -.
DOSAC-COBS-2DPAGE; P04406; -.
OGP; P04406; -.
REPRODUCTION-2DPAGE; IPI00219018; -.
REPRODUCTION-2DPAGE; P04406; -.
SWISS-2DPAGE; P04406; -.
UCD-2DPAGE; P04406; -.
EPD; P04406; -.
PaxDb; P04406; -.
PeptideAtlas; P04406; -.
PRIDE; P04406; -.
ProteomicsDB; 51703; -.
TopDownProteomics; P04406-1; -. [P04406-1]
DNASU; 2597; -.
Ensembl; ENST00000229239; ENSP00000229239; ENSG00000111640. [P04406-1]
Ensembl; ENST00000396858; ENSP00000380067; ENSG00000111640. [P04406-2]
Ensembl; ENST00000396859; ENSP00000380068; ENSG00000111640. [P04406-1]
Ensembl; ENST00000396861; ENSP00000380070; ENSG00000111640. [P04406-1]
Ensembl; ENST00000619601; ENSP00000478864; ENSG00000111640. [P04406-2]
GeneID; 2597; -.
KEGG; hsa:2597; -.
UCSC; uc031qfw.3; human. [P04406-1]
CTD; 2597; -.
DisGeNET; 2597; -.
EuPathDB; HostDB:ENSG00000111640.14; -.
GeneCards; GAPDH; -.
H-InvDB; HIX0000949; -.
H-InvDB; HIX0024996; -.
HGNC; HGNC:4141; GAPDH.
HPA; CAB005197; -.
HPA; CAB016392; -.
HPA; HPA040067; -.
HPA; HPA061280; -.
MIM; 138400; gene.
neXtProt; NX_P04406; -.
OpenTargets; ENSG00000111640; -.
PharmGKB; PA28554; -.
eggNOG; KOG0657; Eukaryota.
eggNOG; COG0057; LUCA.
GeneTree; ENSGT00940000153298; -.
HOGENOM; HOG000071678; -.
HOVERGEN; HBG000227; -.
InParanoid; P04406; -.
KO; K00134; -.
OMA; NCVAPMA; -.
OrthoDB; EOG091G0B1Y; -.
PhylomeDB; P04406; -.
TreeFam; TF300533; -.
BioCyc; MetaCyc:HS03433-MONOMER; -.
BRENDA; 1.2.1.12; 2681.
Reactome; R-HSA-70171; Glycolysis.
Reactome; R-HSA-70263; Gluconeogenesis.
SABIO-RK; P04406; -.
UniPathway; UPA00109; UER00184.
ChiTaRS; GAPDH; human.
EvolutionaryTrace; P04406; -.
GeneWiki; Glyceraldehyde_3-phosphate_dehydrogenase; -.
GenomeRNAi; 2597; -.
PRO; PR:P04406; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111640; Expressed in 236 organ(s), highest expression level in smooth muscle tissue.
CleanEx; HS_GAPDH; -.
ExpressionAtlas; P04406; baseline and differential.
Genevisible; P04406; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; EXP:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; ISS:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0061621; P:canonical glycolysis; TAS:Reactome.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
GO; GO:0051873; P:killing by host of symbiont cells; IDA:UniProtKB.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISS:UniProtKB.
GO; GO:0052501; P:positive regulation by organism of apoptotic process in other organism involved in symbiotic interaction; IDA:UniProtKB.
GO; GO:0050715; P:positive regulation of cytokine secretion; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
InterPro; IPR020830; GlycerAld_3-P_DH_AS.
InterPro; IPR020829; GlycerAld_3-P_DH_cat.
InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR10836; PTHR10836; 1.
Pfam; PF02800; Gp_dh_C; 1.
Pfam; PF00044; Gp_dh_N; 1.
PIRSF; PIRSF000149; GAP_DH; 1.
PRINTS; PR00078; G3PDHDRGNASE.
SMART; SM00846; Gp_dh_N; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01534; GAPDH-I; 1.
PROSITE; PS00071; GAPDH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
Apoptosis; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Glycolysis; Isopeptide bond; Membrane;
Methylation; NAD; Nucleus; Oxidation; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome; S-nitrosylation; Transferase;
Translation regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.19}.
CHAIN 2 335 Glyceraldehyde-3-phosphate dehydrogenase.
/FTId=PRO_0000145486.
NP_BIND 13 14 NAD. {ECO:0000269|PubMed:16239728,
ECO:0000269|PubMed:16510976}.
REGION 2 148 Interaction with WARS.
{ECO:0000269|PubMed:15628863}.
REGION 151 153 Glyceraldehyde 3-phosphate binding.
{ECO:0000250}.
REGION 211 212 Glyceraldehyde 3-phosphate binding.
{ECO:0000250}.
MOTIF 245 250 [IL]-x-C-x-x-[DE] motif.
{ECO:0000305|PubMed:25417112}.
ACT_SITE 152 152 Nucleophile.
BINDING 35 35 NAD. {ECO:0000269|PubMed:16239728,
ECO:0000269|PubMed:16510976}.
BINDING 80 80 NAD; via carbonyl oxygen.
{ECO:0000269|PubMed:16239728,
ECO:0000269|PubMed:16510976}.
BINDING 122 122 NAD. {ECO:0000269|PubMed:16239728,
ECO:0000269|PubMed:16510976}.
BINDING 182 182 Glyceraldehyde 3-phosphate.
{ECO:0000250}.
BINDING 234 234 Glyceraldehyde 3-phosphate.
{ECO:0000250}.
BINDING 316 316 NAD. {ECO:0000269|PubMed:16239728,
ECO:0000269|PubMed:16510976}.
SITE 179 179 Activates thiol group during catalysis.
MOD_RES 5 5 N6,N6-dimethyllysine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 9 9 Deamidated asparagine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 42 42 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 46 46 Methionine sulfoxide; in vitro.
{ECO:0000305|PubMed:25086035}.
MOD_RES 61 61 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 64 64 Deamidated asparagine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 66 66 N6,N6-dimethyllysine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 70 70 Deamidated asparagine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 75 75 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:18183946}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 148 148 Phosphoserine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 149 149 Deamidated asparagine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 152 152 ADP-ribosylcysteine; by autocatalysis; in
irreversibly inhibited form.
{ECO:0000250}.
MOD_RES 152 152 Cysteine persulfide. {ECO:0000250}.
MOD_RES 152 152 S-nitrosocysteine; in reversibly
inhibited form.
{ECO:0000250|UniProtKB:P04797}.
MOD_RES 153 153 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 155 155 Deamidated asparagine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 177 177 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 182 182 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 184 184 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 194 194 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:18183946}.
MOD_RES 194 194 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 194 194 N6-malonyllysine; alternate.
{ECO:0000269|PubMed:21908771}.
MOD_RES 211 211 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 215 215 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:18183946}.
MOD_RES 215 215 N6-malonyllysine; alternate.
{ECO:0000269|PubMed:21908771}.
MOD_RES 219 219 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 225 225 Deamidated asparagine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 227 227 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:18183946}.
MOD_RES 227 227 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 229 229 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18183946}.
MOD_RES 237 237 Phosphothreonine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 247 247 S-nitrosocysteine.
{ECO:0000269|PubMed:22771119,
ECO:0000269|PubMed:25417112}.
MOD_RES 254 254 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 260 260 N6,N6-dimethyllysine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 263 263 N6,N6-dimethyllysine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 312 312 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:18183946}.
MOD_RES 316 316 Deamidated asparagine.
{ECO:0000269|PubMed:18183946}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 334 334 N6,N6-dimethyllysine.
{ECO:0000269|PubMed:18183946}.
CROSSLNK 186 186 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 42 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_047289.
VARIANT 22 22 A -> G (in dbSNP:rs45541435).
{ECO:0000269|Ref.12}.
/FTId=VAR_018889.
VARIANT 251 251 K -> N (in dbSNP:rs1062429).
/FTId=VAR_049218.
MUTAGEN 46 46 M->L: Drastic reduction of the extent and
significant prolongation of the lag phase
of free radical-induced aggregation.
{ECO:0000269|PubMed:25086035}.
MUTAGEN 105 105 M->L: Increased resistance to free
radical-induced aggregation.
{ECO:0000269|PubMed:25086035}.
MUTAGEN 152 152 C->S: Markedly reduced glycolytic
activity; when associated with S-156 and
S-247. Forms free radical-induced
aggregates, but to a lesser extent than
wild-type protein; when associated with
S-156 and S-247.
{ECO:0000269|PubMed:25086035}.
MUTAGEN 156 156 C->S: Markedly reduced glycolytic
activity; when associated with S-152 and
S-247. Forms free radical-induced
aggregates, but to a lesser extent than
wild-type protein; when associated with
S-156 and S-247.
{ECO:0000269|PubMed:25086035}.
MUTAGEN 196 196 W->F: Increased free radical-induced
aggregation.
{ECO:0000269|PubMed:25086035}.
MUTAGEN 245 245 L->M: Inhibits S-nitrosylation of Cys-
247; when associated with M-250.
{ECO:0000269|PubMed:25417112}.
MUTAGEN 247 247 C->S: Markedly reduced glycolytic
activity; when associated with S-152 and
S-156. Forms free radical-induced
aggregates, but to a lesser extent than
wild-type protein; when associated with
S-156 and S-247.
{ECO:0000269|PubMed:25086035}.
MUTAGEN 250 250 E->M: Inhibits S-nitrosylation of Cys-
247; when associated with M-245.
{ECO:0000269|PubMed:25417112}.
MUTAGEN 320 320 Y->F: No effect on free radical-induced
aggregation.
{ECO:0000269|PubMed:25086035}.
CONFLICT 225 225 N -> D (in Ref. 2; CAA25833).
{ECO:0000305}.
STRAND 5 9 {ECO:0000244|PDB:1U8F}.
HELIX 13 25 {ECO:0000244|PDB:1U8F}.
STRAND 27 34 {ECO:0000244|PDB:1U8F}.
STRAND 36 38 {ECO:0000244|PDB:1U8F}.
HELIX 40 48 {ECO:0000244|PDB:1U8F}.
TURN 51 53 {ECO:0000244|PDB:1U8F}.
STRAND 60 63 {ECO:0000244|PDB:1U8F}.
STRAND 66 69 {ECO:0000244|PDB:1U8F}.
STRAND 72 77 {ECO:0000244|PDB:1U8F}.
HELIX 82 84 {ECO:0000244|PDB:1U8F}.
TURN 87 91 {ECO:0000244|PDB:1U8F}.
STRAND 94 97 {ECO:0000244|PDB:1U8F}.
STRAND 99 101 {ECO:0000244|PDB:1U8F}.
HELIX 105 108 {ECO:0000244|PDB:1U8F}.
HELIX 109 114 {ECO:0000244|PDB:1U8F}.
STRAND 117 123 {ECO:0000244|PDB:1U8F}.
STRAND 126 128 {ECO:0000244|PDB:1U8F}.
TURN 133 135 {ECO:0000244|PDB:1U8F}.
HELIX 137 139 {ECO:0000244|PDB:1U8F}.
STRAND 145 148 {ECO:0000244|PDB:1U8F}.
HELIX 152 168 {ECO:0000244|PDB:1U8F}.
STRAND 170 180 {ECO:0000244|PDB:1U8F}.
STRAND 185 189 {ECO:0000244|PDB:1U8F}.
HELIX 196 199 {ECO:0000244|PDB:1U8F}.
TURN 202 204 {ECO:0000244|PDB:1U8F}.
STRAND 207 210 {ECO:0000244|PDB:1U8F}.
TURN 213 216 {ECO:0000244|PDB:1U8F}.
HELIX 217 220 {ECO:0000244|PDB:1U8F}.
HELIX 222 224 {ECO:0000244|PDB:1U8F}.
STRAND 227 236 {ECO:0000244|PDB:1U8F}.
STRAND 241 251 {ECO:0000244|PDB:1U8F}.
HELIX 255 267 {ECO:0000244|PDB:1U8F}.
TURN 268 273 {ECO:0000244|PDB:1U8F}.
STRAND 274 277 {ECO:0000244|PDB:1U8F}.
HELIX 283 286 {ECO:0000244|PDB:1U8F}.
STRAND 292 296 {ECO:0000244|PDB:1U8F}.
TURN 297 299 {ECO:0000244|PDB:1U8F}.
STRAND 301 304 {ECO:0000244|PDB:1U8F}.
STRAND 307 314 {ECO:0000244|PDB:1U8F}.
HELIX 318 333 {ECO:0000244|PDB:1U8F}.
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


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