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UniProtKB/Swiss-Prot entry P00359


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name G3P3_YEAST
Primary accession number P00359
Secondary accession number Q6Q5P9
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 103)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase 3
Synonyms GAPDH 3
EC 1.2.1.12
Gene name
Name: TDH3
Synonyms: GPD3
OrderedLocusNames: YGR192C
ORFNames: G7576
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=385592 [NCBI, ExPASy, EBI, Israel, Japan]
Holland J.P., Holland M.J.;
"The primary structure of a glyceraldehyde-3-phosphate dehydrogenase gene from Saccharomyces cerevisiae.";
J. Biol. Chem. 254:9839-9845(1979).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7645350 [NCBI, ExPASy, EBI, Israel, Japan]
Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., Nombela C.;
"The complete sequence of a 9037 bp DNA fragment of the right arm of Saccharomyces cerevisiae chromosome VII.";
Yeast 11:587-591(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
PROTEIN SEQUENCE OF 47-58.
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/elps.11501501210; PubMed=7895733 [NCBI, ExPASy, EBI, Israel, Japan]
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein database.";
Electrophoresis 15:1466-1486(1994).
[6]
PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 38531 / Y41, and ATCC 44827 / SKQ2N;
DOI=10.1002/elps.1150160124; PubMed=7737086 [NCBI, ExPASy, EBI, Israel, Japan]
Norbeck J., Blomberg A.;
"Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides.";
Electrophoresis 16:149-156(1995).
[7]
SUBCELLULAR LOCATION.
DOI=10.1021/bi010277r; PubMed=11502169 [NCBI, ExPASy, EBI, Israel, Japan]
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.";
Biochemistry 40:9758-9769(2001).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-178 AND SER-201, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-175 AND SER-178, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-123; SER-124; THR-125; SER-149; THR-151; THR-152; SER-178; THR-182; SER-190; THR-199; SER-201; SER-207; SER-208; THR-209; THR-227; THR-235; SER-239; THR-252; SER-302; SER-310 AND TYR-312, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
V01300; CAA24607.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J01324; AAA88714.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X82408; CAA57803.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z72977; CAA97218.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY557831; AAS56157.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S55870; DEBYG2.
RefSeq NP_011708.1; -.
3D structure databases
HSSP P06977; 1DC5. [HSSP ENTRY / PDB]
SMR P00359; 1-330.
ModBase P00359.
Protein-protein interaction databases
DIP DIP:4309N; -.
IntAct P00359; -.
2D gel databases
SWISS-2DPAGE P00359; -.
COMPLUYEAST-2DPAGE P00359; -.
Organism-specific databases
CYGD YGR192c; -.
SGD S000003424; TDH3.
Yeast-GFP YGR192C.
Gene expression databases
GermOnline YGR192C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0009277; Cellular component: fungal-type cell wall (inferred from direct assay from SGD).
GO:0005811; Cellular component: lipid particle (inferred from direct assay from SGD).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006915; Biological process: apoptosis (inferred from mutant phenotype from SGD).
GO:0006094; Biological process: gluconeogenesis (inferred from expression pattern from SGD).
GO:0006096; Biological process: glycolysis (inferred from expression pattern from SGD).
GO:0006800; Biological process: oxygen and reactive oxygen species metabolic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
Graphical view of domain structure.
PANTHER PTHR10836; GAP_DH; 1.
Pfam PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000149; GAP_DH; 1.
PRINTS PR00078; G3PDHDRGNASE.
TIGRFAMs TIGR01534; GAPDH-I; 1.
PROSITE PS00071; GAPDH; 1.
BLOCKS P00359.
ProtoNet P00359.
Proteomic databases
PeptideAtlas P00359; -.
Genome annotation databases
Ensembl YGR192C; Saccharomyces cerevisiae. [Contig view]
GeneID 853106; -.
GenomeReviews Y13135_GR; YGR192C.
KEGG sce:YGR192C; -.
NMPDR fig|4932.3.peg.2835; -.
Phylogenomic databases
HOGENOM P00359; -.
Other
LinkHub P00359; -.
NextBio 973112; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   332  331     Glyceraldehyde-3-phosphate dehydrogenase 3. PRO_0000145591
NP_BIND   11    12  2     NAD (By similarity). 
REGION   149   151  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   209   210  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   150   150        Nucleophile (By similarity). 
BINDING   33    33        NAD (By similarity). 
BINDING   78    78        NAD; via carbonyl oxygen (By similarity). 
BINDING   180   180        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   232   232        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   314   314        NAD (By similarity). 
SITE   177   177  1     Activates thiol group during catalysis (By similarity). 
MOD_RES   22    22        Phosphoserine. 
MOD_RES   123   123        Phosphoserine. 
MOD_RES   124   124        Phosphoserine. 
MOD_RES   125   125        Phosphothreonine. 
MOD_RES   149   149        Phosphoserine. 
MOD_RES   151   151        Phosphothreonine. 
MOD_RES   152   152        Phosphothreonine. 
MOD_RES   175   175        Phosphothreonine. 
MOD_RES   178   178        Phosphoserine. 
MOD_RES   182   182        Phosphothreonine. 
MOD_RES   190   190        Phosphoserine. 
MOD_RES   199   199        Phosphothreonine. 
MOD_RES   201   201        Phosphoserine. 
MOD_RES   207   207        Phosphoserine. 
MOD_RES   208   208        Phosphoserine. 
MOD_RES   209   209        Phosphothreonine. 
MOD_RES   227   227        Phosphothreonine. 
MOD_RES   235   235        Phosphothreonine. 
MOD_RES   239   239        Phosphoserine. 
MOD_RES   252   252        Phosphothreonine. 
MOD_RES   302   302        Phosphoserine. 
MOD_RES   310   310        Phosphoserine. 
MOD_RES   312   312        Phosphotyrosine. 
CONFLICT   136   136        E -> V (in Ref. 1; CAA24607/AAA88714). 
CONFLICT   248   248        N -> D (in Ref. 1; CAA24607/AAA88714). 
CONFLICT   287   287        D -> G (in Ref. 4; AAS56157). 
CONFLICT   329   329        V -> I (in Ref. 1; CAA24607/AAA88714). 
Sequence information
Length: 332 AA [This is the length of the unprocessed precursor] Molecular weight: 35747 Da [This is the MW of the unprocessed precursor] CRC64: 6CFFFEE7061BC36F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVRVAINGFG RIGRLVMRIA LSRPNVEVVA LNDPFITNDY AAYMFKYDST HGRYAGEVSH 

        70         80         90        100        110        120 
DDKHIIVDGK KIATYQERDP ANLPWGSSNV DIAIDSTGVF KELDTAQKHI DAGAKKVVIT 

       130        140        150        160        170        180 
APSSTAPMFV MGVNEEKYTS DLKIVSNASC TTNCLAPLAK VINDAFGIEE GLMTTVHSLT 

       190        200        210        220        230        240 
ATQKTVDGPS HKDWRGGRTA SGNIIPSSTG AAKAVGKVLP ELQGKLTGMA FRVPTVDVSV 

       250        260        270        280        290        300 
VDLTVKLNKE TTYDEIKKVV KAAAEGKLKG VLGYTEDAVV SSDFLGDSHS SIFDASAGIQ 

       310        320        330 
LSPKFVKLVS WYDNEYGYST RVVDLVEHVA KA 

P00359 in FASTA format

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