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UniProtKB/Swiss-Prot entry P09104


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

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Entry information
Entry name ENOG_HUMAN
Primary accession number P09104
Secondary accession number Q96J33
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 114)
Name and origin of the protein
Protein name Gamma-enolase
Synonyms EC 4.2.1.11
2-phospho-D-glycerate hydro-lyase
Neural enolase
Neuron-specific enolase
NSE
Enolase 2
Gene name
Name: ENO2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Retina;
PubMed=3208766 [NCBI, ExPASy, EBI, Israel, Japan]
McAleese S.M., Dunbar B., Fothergill J., Hinks L., Day I.N.M.;
"Complete amino acid sequence of the neurone-specific gamma isozyme of enolase (NSE) from human brain and comparison with the non-neuronal alpha form (NNE).";
Eur. J. Biochem. 178:413-417(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0378-1119(89)90217-5; PubMed=2792767 [NCBI, ExPASy, EBI, Israel, Japan]
Oliva D., Barba G., Barbieri G., Giallongo A., Feo S.;
"Cloning, expression and sequence homologies of cDNA for human gamma enolase.";
Gene 79:355-360(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=3385803 [NCBI, ExPASy, EBI, Israel, Japan]
van Obberghen E., Kamholz J., Bishop J.G. III, Zomzely-Neurath C., Lazzarini R.A.;
"Human gamma enolase: isolation of a cDNA clone and expression in normal and tumor tissues of human origin.";
J. Neurosci. Res. 19:450-456(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Hematopoietic;
DOI=10.1016/0888-7543(91)90496-2; PubMed=2045099 [NCBI, ExPASy, EBI, Israel, Japan]
Oliva D., Cali L., Feo S., Giallongo A.;
"Complete structure of the human gene encoding neuron-specific enolase.";
Genomics 10:157-165(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
PubMed=9074930 [NCBI, ExPASy, EBI, Israel, Japan]
Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
"Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination.";
Genome Res. 7:268-280(1997).
[6]
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
PROTEIN SEQUENCE OF 33-50; 163-179 AND 270-285, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE OF 425-434.
DOI=10.1016/0014-5793(87)80207-7; PubMed=3653393 [NCBI, ExPASy, EBI, Israel, Japan]
Day I.N.M., Allsopp M.T.E.P., Moore D.C.M., Thompson R.J.;
"Sequence conservation in the 3'-untranslated regions of neurone-specific enolase, lymphokine and protooncogene mRNAs.";
FEBS Lett. 222:139-143(1987).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[13]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
DOI=10.1016/j.jmb.2004.05.068; PubMed=15289101 [NCBI, ExPASy, EBI, Israel, Japan]
Chai G., Brewer J.M., Lovelace L.L., Aoki T., Minor W., Lebioda L.;
"Expression, purification and the 1.8 angstroms resolution crystal structure of human neuron specific enolase.";
J. Mol. Biol. 341:1015-1021(2004).
Comments
  • FUNCTION: Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity).
  • CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O.
  • COFACTOR: Magnesium. Required for catalysis and for stabilizing the dimer.
  • PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
  • SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific.
  • SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form (By similarity).
  • TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.
  • DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells.
  • INDUCTION: Levels of ENO2 increase dramatically in cardiovascular accidents, cerebral trauma, brain tumors and Creutzfeldt-Jacob disease.
  • SIMILARITY: Belongs to the enolase family.
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
X13120; CAA31512.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22349; AAB59554.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M36768; AAA52388.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X51956; CAA36215.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U47924; AAB51320.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007383; AAP36047.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002745; AAH02745.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14327; CAA32505.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JU0060; NOHUG.
RefSeq NP_001966.1; -.
UniGene Hs.511915
3D structure databases
PDB
1TE6; X-ray; 1.80 A; A/B=1-434.[ExPASy / RCSB / EBI]
2AKM; X-ray; 1.92 A; A/B=2-434.[ExPASy / RCSB / EBI]
2AKZ; X-ray; 1.36 A; A/B=2-434.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1TE6; -.
2AKM; -.
2AKZ; -.
ModBase P09104.
PTM databases
PhosphoSite P09104; -.
Enzyme and pathway databases
Reactome REACT_1709; Metabolism of small molecules.
2D gel databases
Cornea-2DPAGE P09104; -.
OGP P09104; -.
Organism-specific databases
H-InvDB HIX0010392; -.
HGNC HGNC:3353; ENO2.
GenAtlas ENO2.
HPA CAB000063; -.
MIM 131360; gene. [NCBI / EBI]
Orphanet 299; Enolase deficiency.
PharmGKB PA27788; -.
GeneCards P09104.
Gene expression databases
ArrayExpress P09104; -.
CleanEx HS_ENO2; -.
GermOnline ENSG00000111674; Homo sapiens.
Ontologies
GO
GO:0004634; Molecular function: phosphopyruvate hydratase activity (traceable author statement from ProtInc).
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 P09104.
Genome annotation databases
Ensembl ENSG00000111674; Homo sapiens. [Contig view]
GeneID 2026; -.
KEGG hsa:2026; -.
Phylogenomic databases
HOGENOM P09104; -.
HOVERGEN P09104; -.
Other
SOURCE ENO2; Homo sapiens.
ProtoNet P09104.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Membrane; Metal-binding; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   434  433     Gamma-enolase. PRO_0000134112
REGION   370   373  4     Substrate binding (By similarity). 
ACT_SITE   210   210        Proton donor (By similarity). 
ACT_SITE   343   343        Proton acceptor (By similarity). 
METAL   245   245        Magnesium. 
METAL   293   293        Magnesium. 
METAL   318   318        Magnesium. 
BINDING   158   158        Substrate (By similarity). 
BINDING   167   167        Substrate (By similarity). 
BINDING   293   293        Substrate (By similarity). 
BINDING   318   318        Substrate (By similarity). 
BINDING   394   394        Substrate (By similarity). 
MOD_RES   25    25        Phosphotyrosine (By similarity). 
MOD_RES   44    44        Phosphotyrosine. 
MOD_RES   80    80        Phosphoserine (By similarity). 
VARIANT   264   264  1     P -> A. VAR_002354 [3D]
VARIANT   395   395  1     T -> A. VAR_002355 [3D]
CONFLICT   4     4        E -> Q (in Ref. 1 and 3). 
CONFLICT   27    28        AK -> GC (in Ref. 3; AAA52388). 
CONFLICT   127   127        E -> N (in Ref. 3; AAA52388). 
CONFLICT   240   240        I -> M (in Ref. 1; CAA31512/CAA32505). 
STRAND   5    12  8      
STRAND   18    26  9      
STRAND   29    34  6      
HELIX   57    59  3      
HELIX   63    71  9      
HELIX   73    80  8      
HELIX   87    98  12      
TURN   104   106  3      
HELIX   108   126  19      
HELIX   130   138  9      
STRAND   147   154  8      
HELIX   156   158  3      
STRAND   159   162  4      
STRAND   167   171  5      
HELIX   178   200  23      
HELIX   202   205  4      
HELIX   220   234  15      
TURN   237   239  3      
STRAND   241   245  5      
HELIX   248   251  4      
TURN   259   262  4      
HELIX   267   269  3      
HELIX   273   286  14      
STRAND   289   293  5      
HELIX   301   309  9      
STRAND   312   318  7      
TURN   319   323  5      
HELIX   325   333  9      
STRAND   338   342  5      
HELIX   344   347  4      
HELIX   350   362  13      
STRAND   366   370  5      
HELIX   380   388  9      
STRAND   391   394  4      
HELIX   401   417  17      
HELIX   418   420  3      
HELIX   425   427  3      
HELIX   431   433  3      
Sequence information
Length: 434 AA [This is the length of the unprocessed precursor] Molecular weight: 47269 Da [This is the MW of the unprocessed precursor] CRC64: 6163DE81F5C67744 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK 

        70         80         90        100        110        120 
GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAERELPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD 

       190        200        210        220        230        240 
AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI 

       250        260        270        280        290        300 
VIGMDVAASE FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA 

       370        380        390        400        410        420 
QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE 

       430 
ARFAGHNFRN PSVL 

P09104 in FASTA format

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