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). DOI=10.1073/pnas.83.18.6741; 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; DOI=10.1111/j.1432-1033.1990.tb15611.x; 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). 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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE). TISSUE=Umbilical cord blood; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE). TISSUE=Adipose tissue, and Kidney proximal tubule; Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE). TISSUE=Retina, and Stomach; DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan] Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.; "The full-ORF clone resource of the German cDNA consortium."; BMC Genomics 8:399-399(2007).
[9]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-177. NIEHS SNPs program; Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[10]	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).
[11]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.; Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]	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).
[13]	PROTEIN SEQUENCE OF 2-9 (ISOFORM ALPHA-ENOLASE). TISSUE=Colon carcinoma; DOI=10.1002/elps.1150180344; 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).
[14]	PROTEIN SEQUENCE OF 2-28; 65-80; 121-162; 234-253; 270-281; 331-394 AND 407-420, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY. TISSUE=Colon carcinoma; Bienvenut W.V., Lilla S., Zebisch A., Kolch W.; Submitted (MAR-2009) to UniProtKB.
[15]	PROTEIN SEQUENCE OF 16-28; 33-50; 93-103; 106-120; 163-179; 184-193; 203-221; 240-253; 257-262; 270-281; 286-326; 336-394 AND 407-412, AND MASS SPECTROMETRY. TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; Submitted (DEC-2008) to UniProtKB.
[16]	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).
[17]	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).
[18]	PROTEIN SEQUENCE OF 203-228, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. TISSUE=Lymphoma; DOI=10.1007/BF00570890; PubMed=1369209 [NCBI, ExPASy, EBI, Israel, Japan] Sugahara T., Nakajima H., Shirahata S., Murakami H.; "Purification and characterization of immunoglobulin production stimulating factor-II beta derived from Namalwa cells."; Cytotechnology 10:137-146(1992).
[19]	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).
[20]	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).
[21]	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).
[22]	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).
[23]	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).
[24]	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).
[25]	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).
[26]	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).
[27]	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).
[28]	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).
[29]	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).
[30]	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).
[31]	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).
[32]	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).
[33]	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).
[34]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 AND SER-263, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[35]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

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. Stimulates immunoglobulin production.
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.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Enolase activity is lost above pH 9.0. Immunoglobulin production stimulating activity is retained at pH 13.0;
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.

Name	alpha-enolase
Isoform ID	P06733-1
This is the isoform sequence displayed in this entry.

Name	MBP-1
Isoform ID	P06733-2
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
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/eno1/";.

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]
AK315417; BAG37806.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL833741; CAH56247.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX537400; CAD97642.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222517; BAD96237.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223192; BAD96912.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ056744; AAY43128.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139415; CAC42425.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471130; EAW71604.1; -; 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]

IPI

IPI00465248; -.
IPI00759806; -.

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]
3B97; X-ray; 2.20 A; A/B/C/D=2-434.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2PSN; -.
3B97; -.

ModBase

P06733.

Protein-protein interaction databases

IntAct

P06733; 6.

PTM databases

PhosphoSite

P06733; -.

Enzyme and pathway databases

BRENDA

4.2.1.11; 247.

Pathway_Interaction_DB

hif1_tfpathway; HIF-1-alpha transcription factor network.

Reactome

REACT_474; Metabolism of carbohydrates.

2D gel databases

SWISS-2DPAGE

P06733; -.

Aarhus/Ghent-2DPAGE

1325; IEF.
5406; NEPHGE.

P06733; -.

P06733; -.

P06733; -.

IPI00465248; -.
P06733; -.

Organism-specific databases

GC01M008855; -.

HIX0000101; -.

HGNC:3350; ENO1.

CAB018614; -.

172430; gene. [NCBI / EBI]

Orphanet

299; Enolase deficiency.

PharmGKB

PA27786; -.

Gene expression databases

ArrayExpress

P06733; -.

Bgee

P06733; -.

GermOnline

ENSG00000074800; Homo sapiens.

Ontologies

GO:0031430;	Cellular component: M band (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634;	Cellular component: nucleus (inferred by curator from UniProtKB).
GO:0000015;	Cellular component: phosphopyruvate hydratase complex (inferred from electronic annotation from InterPro).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004634;	Molecular function: phosphopyruvate hydratase activity (traceable author statement from ProtInc).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from UniProtKB-KW).
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:0006096;	Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
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).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
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.

Proteomic databases

PeptideAtlas

P06733; -.

PRIDE

P06733; -.

Genome annotation databases

Ensembl

ENSG00000074800; Homo sapiens. [Contig view]

GeneID

2023; -.

KEGG

hsa:2023; -.

Phylogenomic databases

HOVERGEN

P06733; -.

OMA

P06733; SDSSKWL.

Other

8197; -.

P06733; -.

ENO1; Homo sapiens.

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

Feature table viewer

Feature aligner

`Key`	`From 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`	`2 2`		`N-acetylserine.`
`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`	`254 254`		`Phosphoserine.`
`MOD_RES`	`263 263`		`Phosphoserine.`
`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]`
`VARIANT`	`325 325`	`1`	`P -> Q (in dbSNP:rs11544514 [NCBI]).`	`VAR_048936 [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.`
`CONFLICT`	`55 55`		`T -> A (in Ref. 8; CAD97642).`
`CONFLICT`	`78 78`		`V -> A (in Ref. 7; BAD96237).`
`CONFLICT`	`187 187`		`E -> G (in Ref. 8; CAD97642).`
`CONFLICT`	`199 199`		`K -> R (in Ref. 7; BAD96912).`
`CONFLICT`	`252 252`		`F -> S (in Ref. 4; CAA59331).`
`CONFLICT`	`310 310`		`S -> I (in Ref. 8; CAD97642).`
`STRAND`	`5 12`	`8`
`STRAND`	`18 26`	`9`
`STRAND`	`29 34`	`6`
`HELIX`	`57 59`	`3`
`HELIX`	`63 71`	`9`
`HELIX`	`73 79`	`7`
`HELIX`	`87 98`	`12`
`TURN`	`104 106`	`3`
`HELIX`	`108 125`	`18`
`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`	`202 204`	`3`
`HELIX`	`220 233`	`14`
`TURN`	`237 239`	`3`
`STRAND`	`241 245`	`5`
`HELIX`	`248 250`	`3`
`TURN`	`259 262`	`4`
`HELIX`	`267 269`	`3`
`HELIX`	`273 286`	`14`
`STRAND`	`289 293`	`5`
`HELIX`	`301 311`	`11`
`STRAND`	`313 318`	`6`
`TURN`	`319 323`	`5`
`HELIX`	`325 334`	`10`
`STRAND`	`338 342`	`5`
`HELIX`	`344 347`	`4`
`HELIX`	`350 362`	`13`
`STRAND`	`366 370`	`5`
`HELIX`	`380 387`	`8`
`STRAND`	`391 394`	`4`
`HELIX`	`401 417`	`17`
`HELIX`	`418 420`	`3`
`HELIX`	`425 427`	`3`

Sequence information

Length: 434 AA [This is the length of the unprocessed precursor]

Molecular weight: 47169 Da [This is the MW of the unprocessed precursor]

CRC64: A0ED663FCC15ADA5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK 

        70         80         90        100        110        120 
GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAVEKGVPL YRHIADLAGN SEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAANFRE 

       190        200        210        220        230        240 
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV 

       250        260        270        280        290        300 
VIGMDVAASE FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV TESLQACKLA 

       370        380        390        400        410        420 
QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK 

       430 
AKFAGRNFRN PLAK

P06733 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools