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P13929 (ENOB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-enolase

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

Appears to have a function in striated muscle development and regeneration. HAMAP-Rule MF_00318

Catalytic activity

2-phospho-D-glycerate = phosphoenolpyruvate + H2O. HAMAP-Rule MF_00318

Cofactor

Magnesium. Required for catalysis and for stabilizing the dimer.

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. Interacts with PNKD. Ref.9

Subcellular location

Cytoplasm. Note: Localized to the Z line. Some colocalization with CKM at M-band By similarity. HAMAP-Rule MF_00318

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

Involvement in disease

Glycogen storage disease 13 (GSD13) [MIM:612932]: A metabolic disorder that results in exercise-induced myalgias, generalized muscle weakness and fatigability. It is characterized by increased serum creatine kinase and decreased enolase 3 activity. Dramatically reduced protein levels with focal sarcoplasmic accumulation of glycogen-beta particles are detected on ultrastructural analysis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

Belongs to the enolase family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P13929-1)

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 2 (identifier: P13929-2)

The sequence of this isoform differs from the canonical sequence as follows:
     150-177: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P13929-3)

The sequence of this isoform differs from the canonical sequence as follows:
     61-104: GVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKS → A
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 434433Beta-enolase HAMAP-Rule MF_00318
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

Amino acid modifications

Modified residue21N-acetylalanine Ref.11

Natural variations

Alternative sequence61 – 10444GVLKA…TENKS → A in isoform 3.
VSP_037752
Alternative sequence150 – 17728Missing in isoform 2.
VSP_037753
Natural variant711N → S. Ref.4 Ref.5 Ref.8
Corresponds to variant rs238238 [ dbSNP | Ensembl ].
VAR_020618
Natural variant851V → A. Ref.2 Ref.4 Ref.5 Ref.8
Corresponds to variant rs238239 [ dbSNP | Ensembl ].
VAR_020619
Natural variant1561G → D in GSD13; when associated with E-374. Ref.12
Corresponds to variant rs121918403 [ dbSNP | Ensembl ].
VAR_020620
Natural variant3741G → E in GSD13; when associated with D-156. Ref.12
VAR_020621

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2012. Version 5.
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

Isoform 2 [UniParc].

Checksum: E0D4621669448D46
Show »

FASTA40644,115
Isoform 3 [UniParc].

Checksum: 0B6DB38924087E00
Show »

FASTA39142,248

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS SER-71 AND ALA-85.
[5]"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] (ISOFORMS 2 AND 3), VARIANTS SER-71 AND ALA-85.
Tissue: Skeletal muscle.
[6]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 1), VARIANTS SER-71 AND ALA-85.
Tissue: Muscle.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PNKD.
[10]"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].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD13 ASP-156 AND GLU-374.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16504 mRNA. Translation: CAA34513.1.
X51957 mRNA. Translation: CAA36216.1.
X55976 Genomic DNA. Translation: CAA39446.1.
X56832 Genomic DNA. Translation: CAA40163.1.
AK300662 mRNA. Translation: BAG62348.1.
AK300709 mRNA. Translation: BAG62388.1.
AC004771 Genomic DNA. No translation available.
AC109333 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90375.1.
CH471108 Genomic DNA. Translation: EAW90379.1.
CH471108 Genomic DNA. Translation: EAW90380.1.
BC017249 mRNA. Translation: AAH17249.1.
PIRS06756.
RefSeqNP_001180432.1. NM_001193503.1.
NP_001967.3. NM_001976.4.
NP_443739.3. NM_053013.3.
UniGeneHs.224171.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XSXX-ray1.70A/B1-434[»]
ProteinModelPortalP13929.
SMRP13929. Positions 1-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108341. 10 interactions.
IntActP13929. 17 interactions.
STRING9606.ENSP00000324105.

PTM databases

PhosphoSiteP13929.

Polymorphism databases

DMDM425906077.

2D gel databases

UCD-2DPAGEP13929.

Proteomic databases

PaxDbP13929.
PRIDEP13929.

Protocols and materials databases

DNASU2027.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323997; ENSP00000324105; ENSG00000108515. [P13929-1]
ENST00000518175; ENSP00000431087; ENSG00000108515. [P13929-1]
ENST00000519584; ENSP00000430636; ENSG00000108515. [P13929-3]
GeneID2027.
KEGGhsa:2027.
UCSCuc002gab.4. human. [P13929-1]
uc010vss.2. human. [P13929-3]

Organism-specific databases

CTD2027.
GeneCardsGC17P004851.
H-InvDBHIX0013457.
HGNCHGNC:3354. ENO3.
HPAHPA000793.
MIM131370. gene.
612932. phenotype.
neXtProtNX_P13929.
Orphanet99849. Glycogen storage disease due to muscle beta-enolase deficiency.
PharmGKBPA27789.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0148.
HOGENOMHOG000072174.
HOVERGENHBG000067.
InParanoidP13929.
KOK01689.
OMAGELYKNF.
TreeFamTF300391.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000108515-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP13929.
UniPathwayUPA00109; UER00187.

Gene expression databases

ArrayExpressP13929.
BgeeP13929.
CleanExHS_ENO3.
GenevestigatorP13929.

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

GeneWikiENO3.
GenomeRNAi2027.
NextBio8207.
PROP13929.
SOURCESearch...

Entry information

Entry nameENOB_HUMAN
AccessionPrimary (citable) accession number: P13929
Secondary accession number(s): B4DUI6 expand/collapse secondary AC list , B4DUM6, D3DTL2, E7ENK8, Q96AE2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 28, 2012
Last modified: April 16, 2014
This is version 153 of the entry and version 5 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 17

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