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UniProtKB/Swiss-Prot entry P06733


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

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Entry information
Entry name ENOA_HUMAN
Primary accession number P06733
Secondary accession numbers P22712 Q16704 Q4TUS4 Q658M5 Q6GMP2 Q71V37 Q7Z3V6 Q8WU71 Q9UM55
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 23, 2008 (Entry version 115)
Name and origin of the protein
Protein name Alpha-enolase
Synonyms EC 4.2.1.11
2-phospho-D-glycerate hydro-lyase
Non-neural enolase
NNE
Enolase 1
Phosphopyruvate hydratase
C-myc promoter-binding protein
MBP-1
MPB-1
Plasminogen-binding protein
Gene name
Name: ENO1
Synonyms: ENO1L1, MBPB1, MPB1
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] (ISOFORM ALPHA-ENOLASE).
PubMed=3529090 [NCBI, ExPASy, EBI, Israel, Japan]
Giallongo A., Feo S., Moore R., Croce C.M., Showe L.C.;
"Molecular cloning and nucleotide sequence of a full-length cDNA for human alpha enolase.";
Proc. Natl. Acad. Sci. U.S.A. 83:6741-6745(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-ENOLASE).
TISSUE=T-cell;
PubMed=2373081 [NCBI, ExPASy, EBI, Israel, Japan]
Giallongo A., Oliva D., Cali L., Barba G., Barbieri G., Feo S.;
"Structure of the human gene for alpha-enolase.";
Eur. J. Biochem. 190:567-573(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MBP-1), AND FUNCTION.
TISSUE=Cervix carcinoma;
PubMed=2005901 [NCBI, ExPASy, EBI, Israel, Japan]
Ray R., Miller D.M.;
"Cloning and characterization of a human c-myc promoter-binding protein.";
Mol. Cell. Biol. 11:2154-2161(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-ENOLASE), AND MARKER FOR ENDOMETRIOSIS.
TISSUE=Endometrium;
DOI=10.1016/S0896-8411(95)80027-1; PubMed=8824716 [NCBI, ExPASy, EBI, Israel, Japan]
Walter M., Berg H., Leidenberger F.A., Schweppe K.W., Northemann W.;
"Autoreactive epitopes within the human alpha-enolase and their recognition by sera from patients with endometriosis.";
J. Autoimmun. 8:931-945(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
TISSUE=Retina, and Stomach;
The German cDNA consortium;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-177.
Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
TISSUE=Brain, Eye, Lung, Ovary, Placenta, and Skin;
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).
[9]
PROTEIN SEQUENCE OF 33-50; 163-179; 240-253 AND 307-326, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 166-434.
DOI=10.1006/geno.1997.5186; PubMed=9653645 [NCBI, ExPASy, EBI, Israel, Japan]
Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.;
"Molecular cloning and expression analysis of five novel genes in chromosome 1p36.";
Genomics 50:187-198(1998).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-434.
TISSUE=Brain;
PubMed=9110174 [NCBI, ExPASy, EBI, Israel, Japan]
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
[12]
PROTEIN SEQUENCE OF 2-9 (ISOFORM ALPHA-ENOLASE).
TISSUE=Colon carcinoma;
PubMed=9150948 [NCBI, ExPASy, EBI, Israel, Japan]
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[13]
PROTEIN SEQUENCE OF 270-281 AND 307-321, AND INDUCTION IN DIFFUSE LARGE CELL LYMPHOMA.
PubMed=7787969 [NCBI, ExPASy, EBI, Israel, Japan]
Mohamad R.M., Hamdan M.Y., Maki A., Al-Katib A.;
"Induced expression of alpha-enolase in differentiated diffuse large cell lymphoma.";
Enzyme Protein 48:37-44(1995).
[14]
FUNCTION OF MBP1, IDENTIFICATION OF REPRESSOR DOMAINS, AND MUTAGENESIS OF LEU-384 AND LEU-388.
PubMed=10082554 [NCBI, ExPASy, EBI, Israel, Japan]
Ghosh A.K., Steele R., Ray R.B.;
"Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation.";
Mol. Cell. Biol. 19:2880-2886(1999).
[15]
FUNCTION AS A C-MYC TRANSCRIPTIONAL REPRESSOR, AND SUBCELLULAR LOCATION.
DOI=10.1016/S0014-5793(00)01494-0; PubMed=10802057 [NCBI, ExPASy, EBI, Israel, Japan]
Feo S., Arcuri D., Piddini E., Passantino R., Giallongo A.;
"ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1).";
FEBS Lett. 473:47-52(2000).
[16]
FUNCTION IN PLASMINOGEN ACTIVATION.
DOI=10.1002/ajh.10299; PubMed=12666133 [NCBI, ExPASy, EBI, Israel, Japan]
Lopez-Alemany R., Longstaff C., Hawley S., Mirshahi M., Fabregas P., Jardi M., Merton E., Miles L.A., Felez J.;
"Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against alpha-enolase.";
Am. J. Hematol. 72:234-242(2003).
[17]
INTERACTION WITH PLG.
PubMed=9308760 [NCBI, ExPASy, EBI, Israel, Japan]
Arza B., Felez J., Lopez-Alemany R., Miles L.A., Munoz-Canoves P.;
"Identification of an epitope of alpha-enolase (a candidate plasminogen receptor) by phage display.";
Thromb. Haemost. 78:1097-1103(1997).
[18]
EPITOPE MAPPING, AND ASSOCIATION WITH CAR.
DOI=10.1006/jaut.1998.0239; PubMed=9878089 [NCBI, ExPASy, EBI, Israel, Japan]
Adamus G., Amundson D., Seigel G.M., Machnicki M.;
"Anti-enolase-alpha autoantibodies in cancer-associated retinopathy: epitope mapping and cytotoxicity on retinal cells.";
J. Autoimmun. 11:671-677(1998).
[19]
IDENTIFICATION OF MBP1 AS AN ALPHA-ENOLASE ALTERNATIVE INITIATION PRODUCT, AND MUTAGENESIS OF MET-94 AND MET-97.
DOI=10.1074/jbc.275.8.5958; PubMed=10681589 [NCBI, ExPASy, EBI, Israel, Japan]
Subramanian A., Miller D.M.;
"Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene.";
J. Biol. Chem. 275:5958-5965(2000).
[20]
REVIEW.
DOI=10.1007/PL00000910; PubMed=11497239 [NCBI, ExPASy, EBI, Israel, Japan]
Pancholi V.;
"Multifunctional alpha-enolase: its role in diseases.";
Cell. Mol. Life Sci. 58:902-920(2001).
[21]
INTERACTION OF MBP1 WITH SEDL.
DOI=10.1128/MCB.21.2.655-662.2001; PubMed=11134351 [NCBI, ExPASy, EBI, Israel, Japan]
Ghosh A.K., Majumder M., Steele R., White R.A., Ray R.B.;
"A novel 16-kilodalton cellular protein physically interacts with and antagonizes the functional activity of c-myc promoter-binding protein 1.";
Mol. Cell. Biol. 21:655-662(2001).
[22]
IDENTIFICATION AS AN AUTOANTIGEN IN HASHIMOTO ENCEPHALOPATHY.
DOI=10.1016/S0014-5793(02)03307-0; PubMed=12297304 [NCBI, ExPASy, EBI, Israel, Japan]
Ochi H., Horiuchi I., Araki N., Toda T., Araki T., Sato K., Murai H., Osoegawa M., Yamada T., Okamura K., Ogino T., Mizumoto K., Yamashita H., Saya H., Kira J.;
"Proteomic analysis of human brain identifies alpha-enolase as a novel autoantigen in Hashimoto's encephalopathy.";
FEBS Lett. 528:197-202(2002).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44 AND TYR-287, 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).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan]
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.";
Mol. Cell 23:607-618(2006).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44 AND TYR-287, 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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-57 AND SER-63, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Comments
  • FUNCTION: Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons.
  • FUNCTION: MBP1 binds to the c-myc promoter and acts as a transcriptional repressor. May be a tumor suppressor.
  • 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. ENO1 interacts with PLG in the neuronal plasma membrane and promotes its activation. The C-terminal lysine is required for this binding (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Cytoplasm, myofibril, sarcomere, M-band. Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M-band.
  • SUBCELLULAR LOCATION: Isoform MBP-1: Nucleus.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative initiation.
    Namealpha-enolase
    Isoform IDP06733-1
    This is the isoform sequence displayed in this entry.
    NameMBP-1
    Isoform IDP06733-2
    Note: It is uncertain whether the alternative initiation site is at Met-94 or at Met-97.
    Features which should be applied to build the isoform sequence: VSP_018725.
  • 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: Induced in diffuse large cell lymphoma (DLCL) after treatment with the natural biological agent, Bryo1.
  • DISEASE: ENO1 is identified as an autoantigen in Hashimoto encephalopathy (HE) a rare autoimmune disease associated with Hashimoto thyroiditis (HT). HT is a disorder in which destructive processes overcome the potential capacity of thyroid replacement leading to hypothyroidism.
  • DISEASE: Antibodies against alpha-enolase are present in sera from patients with cancer-associated retinopathy syndrome (CAR), a progressive blinding disease which occurs in the presence of systemic tumor growth, primarily small-cell carcinoma of the lung and other malignancies.
  • MISCELLANEOUS: Used as a diagnostic marker for many tumors and, in the heterodimeric form, alpha/gamma, as a marker for hypoxic brain injury after cardiac arrest. Also marker for endometriosis.
  • SIMILARITY: Belongs to the enolase family.
  • SEQUENCE CAUTION:
    • Sequence=AAA35698.1; Type=Frameshift; Positions=Several;
    • Sequence=AAA35698.1; Type=Miscellaneous discrepancy; Note=Sequencing errors
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
M14328; AAA52387.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X16288; CAA34360.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X16289; CAA34360.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X16290; CAA34360.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55914; AAA35698.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84907; CAA59331.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007163; AAP35827.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL833741; CAH56247.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX537400; CAD97642.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ056744; AAY43128.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139415; CAC42425.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001810; AAH01810.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004458; AAH04458.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009912; AAH09912.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011130; AAH11130.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015641; AAH15641.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021166; AAH21166.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022545; AAH22545.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027725; AAH27725.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050642; AAH50642.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U88968; AAC39935.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF035286; AAB88178.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39579; A39579.
S11696; A29170.
RefSeq NP_001419.1; -.
UniGene Hs.517145
3D structure databases
PDB
2PSN; X-ray; 2.20 A; A/B/C/D=1-434.[ExPASy / RCSB / EBI]
PDBsum 2PSN; -.
ModBase P06733.
PTM databases
PhosphoSite P06733; -.
Enzyme and pathway databases
Reactome REACT_1709; Metabolism of small molecules.
Polymorphism databases
NIEHS-SNPs ENO1.
2D gel databases
SWISS-2DPAGE P06733; -.
Aarhus/Ghent-2DPAGE 1325; IEF.
5406; NEPHGE.
Cornea-2DPAGE P06733; -.
DOSAC-COBS-2DPAGE P06733; -.
OGP P06733; -.
REPRODUCTION-2DPAGE IPI00465248; -.
P06733; -.
Organism-specific databases
H-InvDB HIX0000101; -.
HGNC HGNC:3350; ENO1.
GenAtlas ENO1.
MIM 172430; gene. [NCBI / EBI]
Orphanet 299; Enolase deficiency.
PharmGKB PA27786; -.
GeneCards P06733.
Gene expression databases
ArrayExpress P06733; -.
GermOnline ENSG00000074800; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from LIFEdb).
GO:0005634; Cellular component: nucleus (inferred by curator from UniProtKB).
GO:0004634; Molecular function: phosphopyruvate hydratase activity (traceable author statement from ProtInc).
GO:0003714; Molecular function: transcription corepressor activity (traceable author statement from ProtInc).
GO:0003700; Molecular function: transcription factor activity (traceable author statement from ProtInc).
GO:0030308; Biological process: negative regulation of cell growth (inferred from direct assay from UniProtKB).
GO:0000122; Biological process: negative regulation of transcription from RNA polymerase II promoter (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 P06733.
Proteomic databases
PeptideAtlas P06733; -.
Genome annotation databases
Ensembl ENSG00000074800; Homo sapiens. [Contig view]
GeneID 2023; -.
KEGG hsa:2023; -.
Phylogenomic databases
HOVERGEN P06733; -.
Other
LinkHub P06733; -.
SOURCE ENO1; Homo sapiens.
ProtoNet P06733.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative initiation; Cell membrane; Cytoplasm; Direct protein sequencing; DNA-binding; Glycolysis; Lyase; Magnesium; Membrane; Metal-binding; Nucleus; Phosphoprotein; Plasminogen activation; Polymorphism; Repressor; Transcription; Transcription regulation.
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     Alpha-enolase. PRO_0000134097
REGION   31    38  8     Epitope recognized by CAR and healthy patient antibodies. 
REGION   56    63  8     Epitope recognized by CAR antibodies. 
REGION   97   237  141     Required for repression of c-myc promoter activity. 
REGION   370   373  4     Substrate binding (By similarity). 
REGION   405   434  30     Required for interaction with PLG (By similarity). 
ACT_SITE   210   210        Proton donor (By similarity). 
ACT_SITE   343   343        Proton acceptor (By similarity). 
METAL   245   245        Magnesium (By similarity). 
METAL   293   293        Magnesium (By similarity). 
METAL   318   318        Magnesium (By similarity). 
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   44    44        Phosphotyrosine. 
MOD_RES   57    57        Phosphotyrosine. 
MOD_RES   63    63        Phosphoserine. 
MOD_RES   71    71        N6-acetyllysine. 
MOD_RES   72    72        Phosphothreonine. 
MOD_RES   263   263        Phosphoserine (By similarity). 
MOD_RES   287   287        Phosphotyrosine. 
VAR_SEQ   1    93        Missing (in isoform MBP-1). VSP_018725
VARIANT   177   177  1     N -> K. VAR_025172 [3D]
MUTAGEN   94    94        M->I: MBP1 protein production. No MBP1 protein production; when associated with I-97. 
MUTAGEN   97    97        M->I: MBP1 protein production. No MBP1 protein production; when associated with I-94. 
MUTAGEN   384   384        L->A: Loss of transcriptional repression and cell growth inhibition; when associated with A-388. 
MUTAGEN   388   388        L->A: Loss of transcriptional repression and cell growth inhibition; when associated with A-384.&nbs