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UniProtKB/Swiss-Prot entry P00925


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

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Entry information
Entry name ENO2_YEAST
Primary accession number P00925
Secondary accession number P99013
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 94)
Name and origin of the protein
Protein name Enolase 2
Synonyms EC 4.2.1.11
2-phosphoglycerate dehydratase 2
2-phospho-D-glycerate hydro-lyase 2
Gene name
Name: ENO2
Synonyms: ENOB
OrderedLocusNames: YHR174W
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=6256394 [NCBI, ExPASy, EBI, Israel, Japan]
Holland M.J., Holland J.P., Thill G.P., Jackson K.A.;
"The primary structures of two yeast enolase genes. Homology between the 5' noncoding flanking regions of yeast enolase and glyceraldehyde-3-phosphate dehydrogenase genes.";
J. Biol. Chem. 256:1385-1395(1981).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=8091229 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII.";
Science 265:2077-2082(1994).
[3]
PROTEIN SEQUENCE OF 2-12.
STRAIN=ATCC 26786 / X2180-1A;
Sanchez J.-C., Golaz O., Schaller D., Morch F., Frutiger S., Hughes G.J., Appel R.D., Deshusses J., Hochstrasser D.F.;
Submitted (AUG-1995) to UniProtKB.
[4]
PROTEIN SEQUENCE OF 2-21.
STRAIN=ATCC 38531 / Y41;
DOI=10.1016/0378-1097(96)00006-7; PubMed=8935650 [NCBI, ExPASy, EBI, Israel, Japan]
Norbeck J., Blomberg A.;
"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae.";
FEMS Microbiol. Lett. 137:1-8(1996).
[5]
PROTEIN SEQUENCE OF 16-24; 57-60; 89-103; 290-298 AND 424-432.
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).
[6]
PROTEIN SEQUENCE OF 127-139 AND 244-255.
STRAIN=ATCC 204508 / S288c;
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASS SPECTROMETRY.
DOI=10.1038/nbt0302-301; PubMed=11875433 [NCBI, ExPASy, EBI, Israel, Japan]
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.;
"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae.";
Nat. Biotechnol. 20:301-305(2002).
[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-10 AND SER-188, 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 SER-40; SER-188; SER-205; THR-221 AND SER-373, 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-324 AND THR-326, 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
J01323; AAA88713.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00027; AAB68019.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A01148; NOBY2.
RefSeq NP_012044.1; -.
3D structure databases
HSSP P00924; 4ENL. [HSSP ENTRY / PDB]
SMR P00925; 2-437.
ModBase P00925.
Protein-protein interaction databases
DIP DIP:4777N; -.
IntAct P00925; -.
2D gel databases
SWISS-2DPAGE P00925; -.
COMPLUYEAST-2DPAGE P00925; -.
Organism-specific databases
CYGD YHR174w; -.
SGD S000001217; ENO2.
Yeast-GFP YHR174W.
Gene expression databases
GermOnline YHR174W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0000324; Cellular component: fungal-type vacuole (inferred from direct assay from SGD).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0000015; Cellular component: phosphopyruvate hydratase complex (inferred from direct assay from SGD).
GO:0005625; Cellular component: soluble fraction (inferred from direct assay from SGD).
GO:0004634; Molecular function: phosphopyruvate hydratase activity (inferred from mutant phenotype from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006094; Biological process: gluconeogenesis (inferred from expression pattern from SGD).
GO:0006096; Biological process: glycolysis (inferred from mutant phenotype from SGD).
GO:0032889; Biological process: regulation of vacuole fusion, non-autophagic (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000941; Enolase.
Graphical view of domain structure.
PANTHER PTHR11902; Enolase; 1.
Pfam PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001400; Enolase; 1.
PRINTS PR00148; ENOLASE.
ProDom PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01060; eno; 1.
PROSITE PS00164; ENOLASE; 1.
BLOCKS P00925.
Proteomic databases
PeptideAtlas P00925; -.
Genome annotation databases
Ensembl YHR174W; Saccharomyces cerevisiae. [Contig view]
GeneID 856579; -.
GenomeReviews U00093_GR; YHR174W.
KEGG sce:YHR174W; -.
NMPDR fig|4932.3.peg.3209; -.
Phylogenomic databases
HOGENOM P00925; -.
Other
LinkHub P00925; -.
ProtoNet P00925.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   437  436     Enolase 2. PRO_0000134063
ACT_SITE   160   160        By similarity. 
METAL   247   247        Magnesium (By similarity). 
METAL   296   296        Magnesium (By similarity). 
METAL   321   321        Magnesium (By similarity). 
MOD_RES   10    10        Phosphoserine. 
MOD_RES   40    40        Phosphoserine. 
MOD_RES   188   188        Phosphoserine. 
MOD_RES   205   205        Phosphoserine. 
MOD_RES   221   221        Phosphothreonine. 
MOD_RES   324   324        Phosphothreonine. 
MOD_RES   326   326        Phosphothreonine. 
MOD_RES   373   373        Phosphoserine. 
Sequence information
Length: 437 AA [This is the length of the unprocessed precursor] Molecular weight: 46914 Da [This is the MW of the unprocessed precursor] CRC64: 04599565F58A7643 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR DEDKSKWMGK 

        70         80         90        100        110        120 
GVMNAVNNVN NVIAAAFVKA NLDVKDQKAV DDFLLSLDGT ANKSKLGANA ILGVSMAAAR 

       130        140        150        160        170        180 
AAAAEKNVPL YQHLADLSKS KTSPYVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAKTF 

       190        200        210        220        230        240 
AEAMRIGSEV YHNLKSLTKK RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG 

       250        260        270        280        290        300 
KVKIGLDCAS SEFFKDGKYD LDFKNPESDK SKWLTGVELA DMYHSLMKRY PIVSIEDPFA 

       310        320        330        340        350        360 
EDDWEAWSHF FKTAGIQIVA DDLTVTNPAR IATAIEKKAA DALLLKVNQI GTLSESIKAA 

       370        380        390        400        410        420 
QDSFAANWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL 

       430 
GDKAVYAGEN FHHGDKL 

P00925 in FASTA format

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