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P06733 (ENOA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-enolase

EC=4.2.1.11
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
C-myc promoter-binding protein
Enolase 1
MBP-1
MPB-1
Non-neural enolase
Short name=NNE
Phosphopyruvate hydratase
Plasminogen-binding protein
Gene names
Name:ENO1
Synonyms:ENO1L1, MBPB1, MPB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Ref.3 Ref.18 Ref.20 Ref.21 Ref.22

MBP1 binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor. Ref.3 Ref.18 Ref.20 Ref.21 Ref.22

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O. Ref.18

Cofactor

Magnesium. Binds two Mg2+ per subunit. Required for catalysis and for stabilizing the dimer. Ref.39

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. HAMAP-Rule MF_00318

Subunit structure

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. Ref.23 Ref.27 Ref.39

Subcellular location

Cytoplasm. Cell membrane. CytoplasmmyofibrilsarcomereM line. Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M line. Ref.21

Isoform MBP-1: Nucleus Ref.21.

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. HAMAP-Rule MF_00318

Induction

Induced in diffuse large cell lymphoma (DLCL) after treatment with the natural biological agent, Bryo1. Up-regulated in response to enterovirus 71 (EV71) infection (at protein level). Ref.19 Ref.31

Post-translational modification

ISGylated. Ref.29 Ref.32

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. 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. 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.

Sequence similarities

Belongs to the enolase family.

Biophysicochemical properties

pH dependence:

Enolase activity is lost above pH 9.0. Immunoglobulin production stimulating activity is retained at pH 13.0. Ref.18

Sequence caution

The sequence AAA35698.1 differs from that shown. Reason: Frameshift at several positions.

The sequence AAA35698.1 differs from that shown. Reason: Sequencing errors.

Ontologies

Keywords
   Biological processGlycolysis
Plasminogen activation
Transcription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative initiation
Polymorphism
   LigandDNA-binding
Magnesium
Metal-binding
   Molecular functionLyase
Repressor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

gluconeogenesis

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glycolysis

Traceable author statement. Source: Reactome

negative regulation of cell growth

Inferred from direct assay Ref.20. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.3. Source: ProtInc

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.20. Source: UniProtKB

response to virus

Inferred from expression pattern Ref.31. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentM band

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: LIFEdb

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 22664934PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

nucleus

Inferred by curator Ref.20. Source: UniProtKB

phosphopyruvate hydratase complex

Inferred from electronic annotation. Source: InterPro

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphopyruvate hydratase activity

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.3. Source: ProtInc

transcription corepressor activity

Traceable author statement Ref.3. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform alpha-enolase (identifier: P06733-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform MBP-1 (identifier: P06733-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: Missing.
Note: It is uncertain whether the alternative initiation site is at Met-94 or at Met-97.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13 Ref.14
Chain2 – 434433Alpha-enolase HAMAP-Rule MF_00318
PRO_0000134097

Regions

Region31 – 388Epitope recognized by CAR and healthy patient antibodies HAMAP-Rule MF_00318
Region56 – 638Epitope recognized by CAR antibodies HAMAP-Rule MF_00318
Region97 – 237141Required for repression of c-myc promoter activity HAMAP-Rule MF_00318
Region370 – 3734Substrate binding By similarity
Region405 – 43430Required for interaction with PLG By similarity

Sites

Active site2101Proton donor By similarity
Active site3431Proton acceptor By similarity
Metal binding401Magnesium 1
Metal binding2451Magnesium 2
Metal binding2931Magnesium 2
Metal binding3181Magnesium 2
Binding site1581Substrate By similarity
Binding site1671Substrate By similarity
Binding site2931Substrate By similarity
Binding site3181Substrate By similarity
Binding site3941Substrate By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.14 Ref.35
Modified residue51N6-acetyllysine Ref.35
Modified residue441Phosphotyrosine Ref.30
Modified residue601N6-acetyllysine; alternate By similarity
Modified residue601N6-succinyllysine; alternate By similarity
Modified residue641N6-acetyllysine Ref.35
Modified residue711N6-acetyllysine Ref.35
Modified residue891N6-acetyllysine; alternate Ref.35
Modified residue891N6-succinyllysine; alternate By similarity
Modified residue921N6-acetyllysine By similarity
Modified residue1261N6-acetyllysine Ref.35
Modified residue1931N6-acetyllysine Ref.35
Modified residue1991N6-acetyllysine Ref.35
Modified residue2021N6-acetyllysine By similarity
Modified residue2281N6-acetyllysine; alternate Ref.35
Modified residue2281N6-succinyllysine; alternate By similarity
Modified residue2331N6-acetyllysine; alternate Ref.35
Modified residue2331N6-malonyllysine; alternate Ref.38
Modified residue2541Phosphoserine Ref.33
Modified residue2561N6-acetyllysine Ref.35
Modified residue2631Phosphoserine Ref.33
Modified residue2721Phosphoserine Ref.34
Modified residue2811N6-acetyllysine Ref.35
Modified residue2851N6-acetyllysine Ref.35
Modified residue2871Phosphotyrosine Ref.30
Modified residue3351N6-acetyllysine By similarity
Modified residue3431N6-acetyllysine By similarity
Modified residue4061N6-acetyllysine By similarity
Modified residue4201N6-acetyllysine; alternate Ref.35
Modified residue4201N6-malonyllysine; alternate Ref.38
Modified residue4201N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence1 – 9393Missing in isoform MBP-1.
VSP_018725
Natural variant1771N → K. Ref.9
Corresponds to variant rs11544513 [ dbSNP | Ensembl ].
VAR_025172
Natural variant3251P → Q.
Corresponds to variant rs11544514 [ dbSNP | Ensembl ].
VAR_048936

Experimental info

Mutagenesis941M → I: MBP1 protein production. No MBP1 protein production; when associated with I-97. Ref.25
Mutagenesis971M → I: MBP1 protein production. No MBP1 protein production; when associated with I-94. Ref.25
Mutagenesis3841L → A: Loss of transcriptional repression and cell growth inhibition; when associated with A-388. Ref.20
Mutagenesis3881L → A: Loss of transcriptional repression and cell growth inhibition; when associated with A-384. Ref.20
Sequence conflict551T → A in CAD97642. Ref.8
Sequence conflict781V → A in BAD96237. Ref.7
Sequence conflict1871E → G in CAD97642. Ref.8
Sequence conflict1991K → R in BAD96912. Ref.7
Sequence conflict2521F → S in CAA59331. Ref.4
Sequence conflict3101S → I in CAD97642. Ref.8

Secondary structure

........................................................................ 434
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform alpha-enolase [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A0ED663FCC15ADA5

FASTA43447,169
        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 

« Hide

Isoform MBP-1 [UniParc].

Checksum: 96D437CF21772928
Show »

FASTA34136,928

References

« Hide 'large scale' references
[1]"Molecular cloning and nucleotide sequence of a full-length cDNA for human alpha enolase."
Giallongo A., Feo S., Moore R., Croce C.M., Showe L.C.
Proc. Natl. Acad. Sci. U.S.A. 83:6741-6745(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-ENOLASE).
[2]"Structure of the human gene for alpha-enolase."
Giallongo A., Oliva D., Cali L., Barba G., Barbieri G., Feo S.
Eur. J. Biochem. 190:567-573(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-ENOLASE).
Tissue: T-cell.
[3]"Cloning and characterization of a human c-myc promoter-binding protein."
Ray R., Miller D.M.
Mol. Cell. Biol. 11:2154-2161(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MBP-1), FUNCTION.
Tissue: Cervix carcinoma.
[4]"Autoreactive epitopes within the human alpha-enolase and their recognition by sera from patients with endometriosis."
Walter M., Berg H., Leidenberger F.A., Schweppe K.W., Northemann W.
J. Autoimmun. 8:931-945(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-ENOLASE), MARKER FOR ENDOMETRIOSIS.
Tissue: Endometrium.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
Tissue: Umbilical cord blood.
[7]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
Tissue: Adipose tissue and Kidney proximal tubule.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
Tissue: Retina and Stomach.
[9]NIEHS SNPs program
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-177.
[10]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
Tissue: Brain, Eye, Lung, Ovary, Placenta and Skin.
[13]"A two-dimensional gel database of human colon carcinoma proteins."
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-9 (ISOFORM ALPHA-ENOLASE).
Tissue: Colon carcinoma.
[14]Bienvenut W.V., Lilla S., Zebisch A., Kolch W.
Submitted (MAR-2009) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma.
[15]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[16]"Molecular cloning and expression analysis of five novel genes in chromosome 1p36."
Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.
Genomics 50:187-198(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 166-434.
[17]"Large-scale concatenation cDNA sequencing."
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.
Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-434.
Tissue: Brain.
[18]"Purification and characterization of immunoglobulin production stimulating factor-II beta derived from Namalwa cells."
Sugahara T., Nakajima H., Shirahata S., Murakami H.
Cytotechnology 10:137-146(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 203-228, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Tissue: Lymphoma.
[19]"Induced expression of alpha-enolase in differentiated diffuse large cell lymphoma."
Mohamad R.M., Hamdan M.Y., Maki A., Al-Katib A.
Enzyme Protein 48:37-44(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 270-281 AND 307-321, INDUCTION IN DIFFUSE LARGE CELL LYMPHOMA.
[20]"Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation."
Ghosh A.K., Steele R., Ray R.B.
Mol. Cell. Biol. 19:2880-2886(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF MBP1, IDENTIFICATION OF REPRESSOR DOMAINS, MUTAGENESIS OF LEU-384 AND LEU-388.
[21]"ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1)."
Feo S., Arcuri D., Piddini E., Passantino R., Giallongo A.
FEBS Lett. 473:47-52(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A C-MYC TRANSCRIPTIONAL REPRESSOR, SUBCELLULAR LOCATION.
[22]"Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against alpha-enolase."
Lopez-Alemany R., Longstaff C., Hawley S., Mirshahi M., Fabregas P., Jardi M., Merton E., Miles L.A., Felez J.
Am. J. Hematol. 72:234-242(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PLASMINOGEN ACTIVATION.
[23]"Identification of an epitope of alpha-enolase (a candidate plasminogen receptor) by phage display."
Arza B., Felez J., Lopez-Alemany R., Miles L.A., Munoz-Canoves P.
Thromb. Haemost. 78:1097-1103(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLG.
[24]"Anti-enolase-alpha autoantibodies in cancer-associated retinopathy: epitope mapping and cytotoxicity on retinal cells."
Adamus G., Amundson D., Seigel G.M., Machnicki M.
J. Autoimmun. 11:671-677(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: EPITOPE MAPPING, ASSOCIATION WITH CAR.
[25]"Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene."
Subramanian A., Miller D.M.
J. Biol. Chem. 275:5958-5965(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF MBP1 AS AN ALPHA-ENOLASE ALTERNATIVE INITIATION PRODUCT, MUTAGENESIS OF MET-94 AND MET-97.
[26]"Multifunctional alpha-enolase: its role in diseases."
Pancholi V.
Cell. Mol. Life Sci. 58:902-920(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[27]"A novel 16-kilodalton cellular protein physically interacts with and antagonizes the functional activity of c-myc promoter-binding protein 1."
Ghosh A.K., Majumder M., Steele R., White R.A., Ray R.B.
Mol. Cell. Biol. 21:655-662(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION OF MBP1 WITH SEDL.
[28]"Proteomic analysis of human brain identifies alpha-enolase as a novel autoantigen in Hashimoto's encephalopathy."
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.
FEBS Lett. 528:197-202(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS AN AUTOANTIGEN IN HASHIMOTO ENCEPHALOPATHY.
[29]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[30]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44 AND TYR-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
Leong W.F., Chow V.T.
Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[32]"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[33]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 AND SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[35]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-5; LYS-64; LYS-71; LYS-89; LYS-126; LYS-193; LYS-199; LYS-228; LYS-233; LYS-256; LYS-281; LYS-285 AND LYS-420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[37]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MALONYLATION AT LYS-233 AND LYS-420.
[39]"Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme."
Kang H.J., Jung S.K., Kim S.J., Chung S.J.
Acta Crystallogr. D 64:651-657(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-434, SUBUNIT, COFACTOR, METAL-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14328 mRNA. Translation: AAA52387.1.
X16288, X16289, X16290 Genomic DNA. Translation: CAA34360.1.
M55914 mRNA. Translation: AAA35698.1. Frameshift.
X84907 mRNA. Translation: CAA59331.1.
BT007163 mRNA. Translation: AAP35827.1.
AK315417 mRNA. Translation: BAG37806.1.
AL833741 mRNA. Translation: CAH56247.1.
BX537400 mRNA. Translation: CAD97642.1.
AK222517 mRNA. Translation: BAD96237.1.
AK223192 mRNA. Translation: BAD96912.1.
DQ056744 Genomic DNA. Translation: AAY43128.1.
AL139415 Genomic DNA. Translation: CAC42425.1.
CH471130 Genomic DNA. Translation: EAW71604.1.
BC001810 mRNA. Translation: AAH01810.1.
BC004325 mRNA. Translation: AAH04325.1.
BC004458 mRNA. Translation: AAH04458.1.
BC009218 mRNA. Translation: AAH09218.2.
BC009912 mRNA. Translation: AAH09912.1.
BC011130 mRNA. Translation: AAH11130.1.
BC015641 mRNA. Translation: AAH15641.1.
BC021166 mRNA. Translation: AAH21166.2.
BC022545 mRNA. Translation: AAH22545.1.
BC027725 mRNA. Translation: AAH27725.1.
BC050642 mRNA. Translation: AAH50642.1.
U88968 mRNA. Translation: AAC39935.1.
AF035286 mRNA. Translation: AAB88178.1.
PIRA39579.
A29170. S11696.
RefSeqNP_001188412.1. NM_001201483.1.
NP_001419.1. NM_001428.3.
UniGeneHs.517145.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PSNX-ray2.20A/B/C/D1-434[»]
3B97X-ray2.20A/B/C/D2-434[»]
ProteinModelPortalP06733.
SMRP06733. Positions 2-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108338. 62 interactions.
IntActP06733. 59 interactions.
MINTMINT-155303.

PTM databases

PhosphoSiteP06733.

Polymorphism databases

DMDM119339.

2D gel databases

DOSAC-COBS-2DPAGEP06733.
OGPP06733.
REPRODUCTION-2DPAGEIPI00465248.
P06733.
SWISS-2DPAGEP06733.
UCD-2DPAGEP06733.

Proteomic databases

PaxDbP06733.
PeptideAtlasP06733.
PRIDEP06733.

Protocols and materials databases

DNASU2023.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234590; ENSP00000234590; ENSG00000074800. [P06733-1]
GeneID2023.
KEGGhsa:2023.
UCSCuc001api.2. human. [P06733-1]

Organism-specific databases

CTD2023.
GeneCardsGC01M008921.
HGNCHGNC:3350. ENO1.
HPACAB018614.
MIM172430. gene.
neXtProtNX_P06733.
PharmGKBPA27786.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0148.
HOVERGENHBG000067.
InParanoidP06733.
KOK01689.
OMAVSEKSCN.
OrthoDBEOG776SQ1.
PhylomeDBP06733.
TreeFamTF300391.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000074800-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP06733.
UniPathwayUPA00109; UER00187.

Gene expression databases

ArrayExpressP06733.
BgeeP06733.
GenevestigatorP06733.

Family and domain databases

HAMAPMF_00318. Enolase.
InterProIPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]
PANTHERPTHR11902. PTHR11902. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSENO1. human.
EvolutionaryTraceP06733.
GeneWikiAlpha-enolase.
GenomeRNAi2023.
NextBio8197.
PMAP-CutDBP06733.
PROP06733.
SOURCESearch...

Entry information

Entry nameENOA_HUMAN
AccessionPrimary (citable) accession number: P06733
Secondary accession number(s): B2RD59 expand/collapse secondary AC list , P22712, Q16704, Q4TUS4, Q53FT9, Q53HR3, Q658M5, Q6GMP2, Q71V37, Q7Z3V6, Q8WU71, Q96GV1, Q9BT62, Q9UCH6, Q9UM55
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 179 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM