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Reviewed, UniProtKB/Swiss-Prot P13929 (ENOB_HUMAN)

Last modified June 16, 2009. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Beta-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Muscle-specific enolase
      Short name=MSE
    Skeletal muscle enolase
    Enolase 3
Gene names
Name: ENO3
OrganismHomo sapiens (Human)
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

Appears to have a function in striated muscle development and regeneration.

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 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. Interacts with PNKD. Ref.6

Subcellular location

Cytoplasm. Note: Localized to the Z line. Some colocalization with CKM at M-band 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.

Involvement in disease

Defects in ENO3 are the cause of muscle-specific enolase-beta deficiency (glycogenesis type XIII) [MIM:131370]. It is a glycogen storage myopathy which results in exercise-induced myalgias, generalized muscle weakness and fatigability. Dramatically reduced protein levels with focal sarcoplasmic accumulation of glycogen-beta particles are detected in patients.

Sequence similarities

Belongs to the enolase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandMagnesium
Metal-binding
   Molecular functionLyase
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentphosphopyruvate hydratase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphopyruvate hydratase activity Ref.4

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 434433Beta-enolase
PRO_0000134107

Regions

Region370 – 3734Substrate binding By similarity

Sites

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

Natural variations

Natural variant711N → S: dbSNP rs238238. Ref.5
VAR_020618
Natural variant851V → A: dbSNP rs238239. Ref.5 Ref.2
VAR_020619
Natural variant1561G → D in muscle-specific beta-enolase deficiency; when associated with E-374. Ref.8
VAR_020620
Natural variant3741G → E in muscle-specific beta-enolase deficiency; when associated with D-156. Ref.8
VAR_020621

Sequences

Sequence LengthMass (Da)Tools
P13929-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4D9D8DCF32CF153F

FASTA43446,987
        10         20         30         40         50         60 
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKGRYLGK 

        70         80         90        100        110        120 
GVLKAVENIN NTLGPALLQK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK 

       130        140        150        160        170        180 
AGAAEKGVPL YRHIADLAGN PDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE 

       190        200        210        220        230        240 
AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV 

       250        260        270        280        290        300 
VIGMDVAASE FYRNGKYDLD FKSPDDPARH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD 

       310        320        330        340        350        360 
WATWTSFLSG VNIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA 

       370        380        390        400        410        420 
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK 

       430 
AIFAGRKFRN PKAK 

« Hide

References

« Hide 'large scale' references
[1]"Structure of human muscle (beta) enolase mRNA and protein deduced from a genomic clone."
Peshavaria M., Hinks L.J., Day I.N.M.
Nucleic Acids Res. 17:8862-8862(1989) [PubMed: 2587223] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE)."
Cali L., Feo S., Oliva D., Giallongo A.
Nucleic Acids Res. 18:1893-1893(1990) [PubMed: 2336366] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-85.
[3]"Molecular structure of the human muscle-specific enolase gene (ENO3)."
Peshavaria M., Day I.N.M.
Biochem. J. 275:427-433(1991) [PubMed: 1840492] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structural features of the human gene for muscle-specific enolase. Differential splicing in the 5'-untranslated sequence generates two forms of mRNA."
Giallongo A., Venturella S., Oliva D., Barbieri G., Rubino P., Feo S.
Eur. J. Biochem. 214:367-374(1993) [PubMed: 8513787] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS SER-71 AND ALA-85.
Tissue: Muscle.
[6]"Characterization of MR-1, a novel myofibrillogenesis regulator in human muscle."
Li T.-B., Liu X.-H., Feng S., Hu Y., Yang W.-X., Han Y., Wang Y.-G., Gong L.-M.
Acta Biochim. Biophys. Sin. 36:412-418(2004) [PubMed: 15188056] [Abstract]
Cited for: INTERACTION WITH PNKD.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"Beta-enolase deficiency, a new metabolic myopathy of distal glycolysis."
Comi G.P., Fortunato F., Lucchiari S., Bordoni A., Prelle A., Jann S., Keller A., Ciscato P., Galbiati S., Chiveri L., Torrente Y., Scarlato G., Bresolin N.
Ann. Neurol. 50:202-207(2001) [PubMed: 11506403] [Abstract]
Cited for: VARIANTS MUSCLE-SPECIFIC BETA-ENOLASE DEFICIENCY ASP-156 AND GLU-374.

Cross-references

Sequence databases

X16504 mRNA. Translation: CAA34513.1.
X51957 mRNA. Translation: CAA36216.1.
X55976 Genomic DNA. Translation: CAA39446.1.
X56832 Genomic DNA. Translation: CAA40163.1.
BC017249 mRNA. Translation: AAH17249.1.
IPIIPI00218474.
PIRS06756.
RefSeqNP_001967.2.
NP_443739.2.
UniGeneHs.224171

3D structure databases

HSSPHSSP built from PDB template 1PDZ based on UniProtKB P56252.
SMRP13929. Positions 2-431.
ModBaseSearch...

PTM databases

PhosphoSiteP13929.

Proteomic databases

PRIDEP13929.

Genome annotation databases

EnsemblENSG00000108515. Homo sapiens. [Contig view]
GeneID2027.
KEGGhsa:2027.

Organism-specific databases

GeneCardsGC17P004795.
HGNCHGNC:3354. ENO3.
HPAHPA000793.
MIM131370. gene+phenotype.
Orphanet299. Enolase deficiency.
PharmGKBPA27789.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP13929.
HOVERGENP13929.

Enzyme and pathway databases

BRENDA4.2.1.11. 247.
ReactomeREACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpressP13929.
BgeeP13929.
CleanExHS_ENO3.
GermOnlineENSG00000108515. Homo sapiens.

Family and domain databases

InterProIPR000941. Enolase.
[Graphical view]
PANTHERPTHR11902. Enolase. 1 hit.
PfamPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFPIRSF001400. Enolase. 1 hit.
PRINTSPR00148. ENOLASE.
ProDomPD000902. Enolase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01060. eno. 1 hit.
PROSITEPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio8207.
SOURCESearch...

Entry information

Entry nameENOB_HUMAN
AccessionPrimary (citable) accession number: P13929
Secondary accession number(s): Q96AE2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents