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UniProtKB/Swiss-Prot entry P00358


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

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Entry information
Entry name G3P2_YEAST
Primary accession number P00358
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    July 22, 2008 (Entry version 97)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase 2
Synonyms GAPDH 2
EC 1.2.1.12
Gene name
Name: TDH2
Synonyms: GPD2
OrderedLocusNames: YJR009C
ORFNames: J1433
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].
STRAIN=ATCC 204508 / S288c;
PubMed=1789010 [NCBI, ExPASy, EBI, Israel, Japan]
Mountain H.A., Korch C.;
"TDH2 is linked to MET3 on chromosome X of Saccharomyces cerevisiae.";
Yeast 7:873-880(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6244283 [NCBI, ExPASy, EBI, Israel, Japan]
Holland J.P., Holland M.J.;
"Structural comparison of two nontandemly repeated yeast glyceraldehyde-3-phosphate dehydrogenase genes.";
J. Biol. Chem. 255:2596-2605(1980).
[3]
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).
[4]
PROTEIN SEQUENCE OF 24-37; 72-77; 81-86; 199-213; 226-232 AND 322-331.
STRAIN=ATCC 38531 / Y41;
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).
[5]
PROTEIN SEQUENCE OF 2-13.
STRAIN=ATCC 26786 / X2180-1A;
Frutiger S., Hughes G.J., Sanchez J.-C., Hochstrasser D.F.;
Submitted (FEB-1996) to UniProtKB.
[6]
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).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; THR-50; TYR-54; SER-59; SER-310; SER-319 AND THR-320, 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).
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
X60157; CAA42725.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
V01301; CAA24608.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X87611; CAA60931.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49509; CAA89531.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S57024; DEBYG1.
RefSeq NP_012542.1; -.
3D structure databases
HSSP P06977; 1DC5. [HSSP ENTRY / PDB]
SMR P00358; 1-330.
ModBase P00358.
Protein-protein interaction databases
DIP DIP:1951N; -.
IntAct P00358; -.
2D gel databases
SWISS-2DPAGE P00358; -.
COMPLUYEAST-2DPAGE P00358; -.
Organism-specific databases
CYGD YJR009c; -.
SGD S000003769; TDH2.
Yeast-GFP YJR009C.
Gene expression databases
ArrayExpress P00358; -.
GermOnline YJR009C; 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: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 P00358.
Proteomic databases
PeptideAtlas P00358; -.
Genome annotation databases
Ensembl YJR009C; Saccharomyces cerevisiae. [Contig view]
GeneID 853465; -.
GenomeReviews Y13136_GR; YJR009C.
KEGG sce:YJR009C; -.
NMPDR fig|4932.3.peg.3516; -.
Phylogenomic databases
HOGENOM P00358; -.
Other
LinkHub P00358; -.
ProtoNet P00358.
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 2. PRO_0000145590
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   49    49        Phosphoserine. 
MOD_RES   50    50        Phosphothreonine. 
MOD_RES   54    54        Phosphotyrosine. 
MOD_RES   59    59        Phosphoserine. 
MOD_RES   149   149        Phosphoserine. 
MOD_RES   201   201        Phosphoserine. 
MOD_RES   310   310        Phosphoserine. 
MOD_RES   319   319        Phosphoserine. 
MOD_RES   320   320        Phosphothreonine. 
CONFLICT   77    77        E -> A (in Ref. 4; AA sequence). 
Sequence information
Length: 332 AA [This is the length of the unprocessed precursor] Molecular weight: 35847 Da [This is the MW of the unprocessed precursor] CRC64: 9A99DCB26672541E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVRVAINGFG RIGRLVMRIA LQRKNVEVVA LNDPFISNDY SAYMFKYDST HGRYAGEVSH 

        70         80         90        100        110        120 
DDKHIIVDGH KIATFQERDP ANLPWASLNI DIAIDSTGVF KELDTAQKHI DAGAKKVVIT 

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

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

       250        260        270        280        290        300 
VDLTVKLNKE TTYDEIKKVV KAAAEGKLKG VLGYTEDAVV SSDFLGDSNS SIFDAAAGIQ 

       310        320        330 
LSPKFVKLVS WYDNEYGYST RVVDLVEHVA KA 

P00358 in FASTA format

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