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UniProtKB/Swiss-Prot entry P00360


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

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Entry information
Entry name G3P1_YEAST
Primary accession number P00360
Secondary accession numbers None
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 102)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase 1
Synonyms GAPDH 1
EC 1.2.1.12
Gene name
Name: TDH1
Synonyms: GPD1, SSS2
OrderedLocusNames: YJL052W
ORFNames: J1154
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=6833300 [NCBI, ExPASy, EBI, Israel, Japan]
Holland J.P., Labieniec L., Swimmer C., Holland M.J.;
"Homologous nucleotide sequences at the 5' termini of messenger RNAs synthesized from the yeast enolase and glyceraldehyde-3-phosphate dehydrogenase gene families. The primary structure of a third yeast glyceraldehyde-3-phosphate dehydrogenase gene.";
J. Biol. Chem. 258:5291-5299(1983).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8641269 [NCBI, ExPASy, EBI, Israel, Japan]
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
EMBO J. 15:2031-2049(1996).
[3]
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).
[4]
PROTEIN SEQUENCE OF 64-70 AND 218-225.
STRAIN=ATCC 44827 / SKQ2N;
DOI=10.1002/(SICI)1097-0061(199712)13:16<1519::AID-YEA211>3.0.CO;2-U; PubMed=9509572 [NCBI, ExPASy, EBI, Israel, Japan]
Norbeck J., Blomberg A.;
"Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins.";
Yeast 13:1519-1534(1997).
[5]
PROTEIN SEQUENCE OF N-TERMINUS.
PubMed=10930071 [NCBI, ExPASy, EBI, Israel, Japan]
Kadokura T., Ito T., Takano S., Nakazato A., Hara H., Watanabe S., Kudo T., Takeda M., Kaneko T.;
"Divergence of glyceraldehyde-3-phosphate dehydrogenase isozymes in Saccharomyces cerevisiae complex.";
Syst. Appl. Microbiol. 23:198-205(2000).
[6]
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).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-199; SER-201; SER-207; SER-208; SER-291 AND SER-310, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43; SER-124; SER-125 AND THR-182, 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
V01302; CAA24609.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49327; CAA89343.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY693001; AAT93020.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S56824; DEBYG3.
RefSeq NP_012483.1; -.
3D structure databases
HSSP P06977; 1DC5. [HSSP ENTRY / PDB]
SMR P00360; 1-330.
ModBase P00360.
Protein-protein interaction databases
DIP DIP:4304N; -.
IntAct P00360; -.
2D gel databases
SWISS-2DPAGE P00360; -.
COMPLUYEAST-2DPAGE P00360; -.
Organism-specific databases
CYGD YJL052w; -.
SGD S000003588; TDH1.
Yeast-GFP YJL052W.
Gene expression databases
GermOnline YJL052W; 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:0006094; Biological process: gluconeogenesis (inferred from expression pattern from SGD).
GO:0006096; Biological process: glycolysis (inferred from expression pattern 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 P00360.
ProtoNet P00360.
Proteomic databases
PeptideAtlas P00360; -.
Genome annotation databases
Ensembl YJL052W; Saccharomyces cerevisiae. [Contig view]
GeneID 853395; -.
GenomeReviews Y13136_GR; YJL052W.
KEGG sce:YJL052W; -.
NMPDR fig|4932.3.peg.3456; -.
Phylogenomic databases
HOGENOM P00360; -.
Other
LinkHub P00360; -.
NextBio 973876; -.
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
CHAIN   1   332  332     Glyceraldehyde-3-phosphate dehydrogenase 1. PRO_0000145589
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   43    43        Phosphotyrosine. 
MOD_RES   124   124        Phosphoserine. 
MOD_RES   125   125        Phosphoserine. 
MOD_RES   149   149        Phosphoserine. 
MOD_RES   182   182        Phosphothreonine. 
MOD_RES   199   199        Phosphothreonine. 
MOD_RES   201   201        Phosphoserine. 
MOD_RES   207   207        Phosphoserine. 
MOD_RES   208   208        Phosphoserine. 
MOD_RES   291   291        Phosphoserine. 
MOD_RES   310   310        Phosphoserine. 
CONFLICT   248   248        E -> A (in Ref. 1; CAA24609). 
Sequence information
Length: 332 AA [This is the length of the unprocessed precursor] Molecular weight: 35750 Da [This is the MW of the unprocessed precursor] CRC64: 4C116C86EAF3DB70 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIRIAINGFG RIGRLVLRLA LQRKDIEVVA VNDPFISNDY AAYMVKYDST HGRYKGTVSH 

        70         80         90        100        110        120 
DDKHIIIDGV KIATYQERDP ANLPWGSLKI DVAVDSTGVF KELDTAQKHI DAGAKKVVIT 

       130        140        150        160        170        180 
APSSSAPMFV VGVNHTKYTP DKKIVSNASC TTNCLAPLAK VINDAFGIEE GLMTTVHSMT 

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

       250        260        270        280        290        300 
VDLTVKLEKE ATYDQIKKAV KAAAEGPMKG VLGYTEDAVV SSDFLGDTHA SIFDASAGIQ 

       310        320        330 
LSPKFVKLIS WYDNEYGYSA RVVDLIEYVA KA 

P00360 in FASTA format

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