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Protein

Beta-enolase

Gene

ENO3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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), Glyceraldehyde-3-phosphate dehydrogenase (epd)
  2. Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase, Phosphoglycerate kinase, Phosphoglycerate kinase (HEL-S-68p), Phosphoglycerate kinase (HEL-S-272), Phosphoglycerate kinase, Phosphoglycerate kinase, Phosphoglycerate kinase (pgk), Phosphoglycerate kinase 1 (PGK1), Phosphoglycerate kinase
  3. no protein annotated in this organism
  4. Alpha-enolase (ENO1), Beta-enolase (ENO3), Enolase 4 (ENO4), Gamma-enolase (ENO2)
  5. Pyruvate kinase, Pyruvate kinase PKM (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (pyk), 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

Keywordsi

Molecular functionLyase
Biological processGlycolysis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000108515-MONOMER
ReactomeiR-HSA-70171 Glycolysis
R-HSA-70263 Gluconeogenesis
SABIO-RKiP13929
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

EuPathDBiHostDB:ENSG00000108515.17
HGNCiHGNC:3354 ENO3
MIMi131370 gene
neXtProtiNX_P13929

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 dbSNP:rs121918403EnsemblClinVar.1
Natural variantiVAR_020621374G → E in GSD13; when associated with D-156. 1 PublicationCorresponds to variant dbSNP:rs121918404EnsemblClinVar.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

Chemistry databases

DrugBankiDB03465 2-Phospho-D-Glyceric Acid
DB02726 2-Phosphoglycolic Acid
DB01819 Phosphoenolpyruvate
DB03645 Phosphonoacetohydroxamic Acid

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 residuei72PhosphothreonineBy similarity1
Modified residuei83PhosphoserineBy similarity1
Modified residuei157PhosphoserineBy similarity1
Modified residuei176PhosphoserineCombined sources1
Modified residuei205PhosphothreonineBy similarity1
Modified residuei229PhosphothreonineBy similarity1
Modified residuei236PhosphotyrosineBy similarity1
Modified residuei263PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP13929
MaxQBiP13929
PaxDbiP13929
PeptideAtlasiP13929
PRIDEiP13929
ProteomicsDBi52999
53000 [P13929-2]
53001 [P13929-3]

2D gel databases

UCD-2DPAGEiP13929

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
HPA068284
HPA068721

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi108341, 46 interactors
IntActiP13929, 21 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

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
GeneTreeiENSGT00910000144064
HOGENOMiHOG000072174
HOVERGENiHBG000067
InParanoidiP13929
KOiK01689
OMAiQEFLVVP
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
InterProiView protein in InterPro
IPR000941 Enolase
IPR036849 Enolase-like_C_sf
IPR029017 Enolase-like_N
IPR034390 Enolase-like_superfamily
IPR020810 Enolase_C
IPR020809 Enolase_CS
IPR020811 Enolase_N
PANTHERiPTHR11902 PTHR11902, 1 hit
PfamiView protein in Pfam
PF00113 Enolase_C, 1 hit
PF03952 Enolase_N, 1 hit
PIRSFiPIRSF001400 Enolase, 1 hit
PRINTSiPR00148 ENOLASE
SFLDiSFLDG00178 enolase, 1 hit
SFLDS00001 Enolase, 1 hit
SMARTiView protein in SMART
SM01192 Enolase_C, 1 hit
SM01193 Enolase_N, 1 hit
SUPFAMiSSF51604 SSF51604, 1 hit
TIGRFAMsiTIGR01060 eno, 1 hit
PROSITEiView protein in PROSITE
PS00164 ENOLASE, 1 hit

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 → S3 PublicationsCorresponds to variant dbSNP:rs238238EnsemblClinVar.1
Natural variantiVAR_02061985V → A4 PublicationsCorresponds to variant dbSNP:rs238239EnsemblClinVar.1
Natural variantiVAR_020620156G → D in GSD13; when associated with E-374. 1 PublicationCorresponds to variant dbSNP:rs121918403EnsemblClinVar.1
Natural variantiVAR_020621374G → E in GSD13; when associated with D-156. 1 PublicationCorresponds to variant dbSNP:rs121918404EnsemblClinVar.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

Similar proteinsi

Entry informationi

Entry nameiENOB_HUMAN
AccessioniPrimary (citable) accession number: P13929
Secondary accession number(s): B4DUI6
, B4DUM6, D3DTL2, E7ENK8, Q96AE2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 28, 2012
Last modified: June 20, 2018
This is version 193 of the entry and version 5 of the sequence. See 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

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