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Protein

Beta-enolase

Gene

ENO3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Mg2+Note: Mg2+ is required for catalysis and for stabilizing the dimer.

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-162eP), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-278), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (GAPDHS)
  2. Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase 1 (PGK1)
  3. no protein annotated in this organism
  4. Beta-enolase (ENO3), Alpha-enolase (ENO1), Enolase 4 (ENO4), Gamma-enolase (ENO2)
  5. Pyruvate kinase, Pyruvate kinase PKM (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase PKLR (PKLR), Pyruvate kinase, Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (HEL-S-30), Pyruvate kinase (PKM2)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei158SubstrateBy similarity1
Binding sitei167SubstrateBy similarity1
Active sitei210Proton donorBy similarity1
Metal bindingi245MagnesiumBy similarity1
Metal bindingi293MagnesiumBy similarity1
Binding sitei293SubstrateBy similarity1
Metal bindingi318MagnesiumBy similarity1
Binding sitei318SubstrateBy similarity1
Active sitei343Proton acceptorBy similarity1
Binding sitei394SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000108515-MONOMER.
ZFISH:ENSG00000108515-MONOMER.
ReactomeiR-HSA-70171. Glycolysis.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP13929.
SIGNORiP13929.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ENO3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:3354. ENO3.

Subcellular locationi

  • Cytoplasm

  • Note: Localized to the Z line. Some colocalization with CKM at M-band (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • phosphopyruvate hydratase complex Source: InterPro
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Glycogen storage disease 13 (GSD13)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:612932
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_020620156G → D in GSD13; when associated with E-374. 1 PublicationCorresponds to variant rs121918403dbSNPEnsembl.1
Natural variantiVAR_020621374G → E in GSD13; when associated with D-156. 1 PublicationCorresponds to variant rs121918404dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Glycogen storage disease

Organism-specific databases

DisGeNETi2027.
MalaCardsiENO3.
MIMi612932. phenotype.
OpenTargetsiENSG00000108515.
Orphaneti99849. Glycogen storage disease due to muscle beta-enolase deficiency.
PharmGKBiPA27789.

Polymorphism and mutation databases

BioMutaiENO3.
DMDMi425906077.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001341072 – 434Beta-enolaseAdd BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei26PhosphothreonineBy similarity1
Modified residuei44PhosphotyrosineBy similarity1
Modified residuei72PhosphothreonineBy similarity1
Modified residuei83PhosphoserineBy similarity1
Modified residuei157PhosphoserineBy similarity1
Modified residuei176PhosphoserineCombined sources1
Modified residuei197N6-acetyllysineBy similarity1
Modified residuei199N6-acetyllysineBy similarity1
Modified residuei205PhosphothreonineBy similarity1
Modified residuei229PhosphothreonineBy similarity1
Modified residuei236PhosphotyrosineBy similarity1
Modified residuei263PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP13929.
MaxQBiP13929.
PaxDbiP13929.
PeptideAtlasiP13929.
PRIDEiP13929.

2D gel databases

UCD-2DPAGEP13929.

PTM databases

iPTMnetiP13929.
PhosphoSitePlusiP13929.
SwissPalmiP13929.

Expressioni

Tissue specificityi

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 stagei

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.

Gene expression databases

BgeeiENSG00000108515.
CleanExiHS_ENO3.
ExpressionAtlasiP13929. baseline and differential.
GenevisibleiP13929. HS.

Organism-specific databases

HPAiHPA000793.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi108341. 43 interactors.
IntActiP13929. 20 interactors.
STRINGi9606.ENSP00000324105.

Structurei

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 12Combined sources8
Beta strandi18 – 26Combined sources9
Beta strandi29 – 34Combined sources6
Beta strandi43 – 45Combined sources3
Helixi57 – 59Combined sources3
Helixi63 – 71Combined sources9
Helixi73 – 79Combined sources7
Helixi87 – 98Combined sources12
Turni104 – 106Combined sources3
Helixi108 – 125Combined sources18
Helixi130 – 138Combined sources9
Beta strandi150 – 154Combined sources5
Helixi156 – 158Combined sources3
Beta strandi159 – 162Combined sources4
Beta strandi167 – 171Combined sources5
Helixi178 – 200Combined sources23
Helixi220 – 234Combined sources15
Turni237 – 239Combined sources3
Beta strandi241 – 245Combined sources5
Helixi248 – 251Combined sources4
Turni259 – 262Combined sources4
Helixi267 – 269Combined sources3
Helixi273 – 286Combined sources14
Beta strandi289 – 293Combined sources5
Helixi301 – 309Combined sources9
Beta strandi313 – 318Combined sources6
Turni319 – 323Combined sources5
Helixi325 – 334Combined sources10
Beta strandi338 – 342Combined sources5
Helixi344 – 347Combined sources4
Helixi350 – 362Combined sources13
Beta strandi366 – 370Combined sources5
Helixi380 – 388Combined sources9
Beta strandi391 – 394Combined sources4
Helixi401 – 417Combined sources17
Helixi418 – 420Combined sources3
Helixi425 – 427Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XSXX-ray1.70A/B1-434[»]
ProteinModelPortaliP13929.
SMRiP13929.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 373Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP13929.
KOiK01689.
OMAiETEDTFM.
OrthoDBiEOG091G07NH.
PhylomeDBiP13929.
TreeFamiTF300391.

Family and domain databases

CDDicd03313. enolase. 1 hit.
Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P13929-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DGDKGRYLGK GVLKAVENIN NTLGPALLQK KLSVVDQEKV DKFMIELDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGN PDLILPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGASSFKE AMRIGAEVYH HLKGVIKAKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV VIGMDVAASE
260 270 280 290 300
FYRNGKYDLD FKSPDDPARH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD
310 320 330 340 350
WATWTSFLSG VNIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV
360 370 380 390 400
TESIQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL MRIEEALGDK AIFAGRKFRN PKAK
Length:434
Mass (Da):46,987
Last modified:November 28, 2012 - v5
Checksum:i4D9D8DCF32CF153F
GO
Isoform 2 (identifier: P13929-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     150-177: Missing.

Note: No experimental confirmation available.
Show »
Length:406
Mass (Da):44,115
Checksum:iE0D4621669448D46
GO
Isoform 3 (identifier: P13929-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-104: GVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKS → A

Note: No experimental confirmation available.
Show »
Length:391
Mass (Da):42,248
Checksum:i0B6DB38924087E00
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02061871N → S.3 PublicationsCorresponds to variant rs238238dbSNPEnsembl.1
Natural variantiVAR_02061985V → A.4 PublicationsCorresponds to variant rs238239dbSNPEnsembl.1
Natural variantiVAR_020620156G → D in GSD13; when associated with E-374. 1 PublicationCorresponds to variant rs121918403dbSNPEnsembl.1
Natural variantiVAR_020621374G → E in GSD13; when associated with D-156. 1 PublicationCorresponds to variant rs121918404dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03775261 – 104GVLKA…TENKS → A in isoform 3. 1 PublicationAdd BLAST44
Alternative sequenceiVSP_037753150 – 177Missing in isoform 2. 1 PublicationAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11062.1. [P13929-1]
CCDS54070.1. [P13929-3]
PIRiS06756.
RefSeqiNP_001180432.1. NM_001193503.1. [P13929-3]
NP_001967.3. NM_001976.4. [P13929-1]
NP_443739.3. NM_053013.3. [P13929-1]
XP_011522031.1. XM_011523729.1. [P13929-1]
XP_016879835.1. XM_017024346.1. [P13929-1]
UniGeneiHs.224171.

Genome annotation databases

EnsembliENST00000323997; ENSP00000324105; ENSG00000108515. [P13929-1]
ENST00000518175; ENSP00000431087; ENSG00000108515. [P13929-1]
ENST00000519584; ENSP00000430636; ENSG00000108515. [P13929-3]
GeneIDi2027.
KEGGihsa:2027.
UCSCiuc002gac.5. human. [P13929-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11062.1. [P13929-1]
CCDS54070.1. [P13929-3]
PIRiS06756.
RefSeqiNP_001180432.1. NM_001193503.1. [P13929-3]
NP_001967.3. NM_001976.4. [P13929-1]
NP_443739.3. NM_053013.3. [P13929-1]
XP_011522031.1. XM_011523729.1. [P13929-1]
XP_016879835.1. XM_017024346.1. [P13929-1]
UniGeneiHs.224171.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XSXX-ray1.70A/B1-434[»]
ProteinModelPortaliP13929.
SMRiP13929.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108341. 43 interactors.
IntActiP13929. 20 interactors.
STRINGi9606.ENSP00000324105.

PTM databases

iPTMnetiP13929.
PhosphoSitePlusiP13929.
SwissPalmiP13929.

Polymorphism and mutation databases

BioMutaiENO3.
DMDMi425906077.

2D gel databases

UCD-2DPAGEP13929.

Proteomic databases

EPDiP13929.
MaxQBiP13929.
PaxDbiP13929.
PeptideAtlasiP13929.
PRIDEiP13929.

Protocols and materials databases

DNASUi2027.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323997; ENSP00000324105; ENSG00000108515. [P13929-1]
ENST00000518175; ENSP00000431087; ENSG00000108515. [P13929-1]
ENST00000519584; ENSP00000430636; ENSG00000108515. [P13929-3]
GeneIDi2027.
KEGGihsa:2027.
UCSCiuc002gac.5. human. [P13929-1]

Organism-specific databases

CTDi2027.
DisGeNETi2027.
GeneCardsiENO3.
H-InvDBHIX0013457.
HGNCiHGNC:3354. ENO3.
HPAiHPA000793.
MalaCardsiENO3.
MIMi131370. gene.
612932. phenotype.
neXtProtiNX_P13929.
OpenTargetsiENSG00000108515.
Orphaneti99849. Glycogen storage disease due to muscle beta-enolase deficiency.
PharmGKBiPA27789.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2670. Eukaryota.
COG0148. LUCA.
GeneTreeiENSGT00840000129817.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP13929.
KOiK01689.
OMAiETEDTFM.
OrthoDBiEOG091G07NH.
PhylomeDBiP13929.
TreeFamiTF300391.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciMetaCyc:ENSG00000108515-MONOMER.
ZFISH:ENSG00000108515-MONOMER.
ReactomeiR-HSA-70171. Glycolysis.
R-HSA-70263. Gluconeogenesis.
SABIO-RKP13929.
SIGNORiP13929.

Miscellaneous databases

ChiTaRSiENO3. human.
GeneWikiiENO3.
GenomeRNAii2027.
PROiP13929.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000108515.
CleanExiHS_ENO3.
ExpressionAtlasiP13929. baseline and differential.
GenevisibleiP13929. HS.

Family and domain databases

CDDicd03313. enolase. 1 hit.
Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase. 1 hit.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N-like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SMARTiSM01192. Enolase_C. 1 hit.
SM01193. Enolase_N. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENOB_HUMAN
AccessioniPrimary (citable) accession number: P13929
Secondary accession number(s): B4DUI6
, B4DUM6, D3DTL2, E7ENK8, Q96AE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 28, 2012
Last modified: November 2, 2016
This is version 180 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.