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Protein

Gamma-enolase

Gene

Eno2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity).By similarity

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 (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm10358), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839)
  2. Phosphoglycerate kinase (Pgk1), Phosphoglycerate kinase 2 (Pgk2), Phosphoglycerate kinase 1 (Pgk1), Phosphoglycerate kinase (Pgk1)
  3. no protein annotated in this organism
  4. Gamma-enolase (Eno2), Beta-enolase (Eno3), Alpha-enolase (Eno1), Enolase 4 (Eno4)
  5. Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKM (Pkm)
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

ReactomeiR-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.
SABIO-RKiP17183.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 2
Neural enolase
Neuron-specific enolase
Short name:
NSE
Gene namesi
Name:Eno2
Synonyms:Eno-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:95394. Eno2.

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

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001341131 – 434Gamma-enolaseAdd BLAST434

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei26PhosphothreonineBy similarity1
Modified residuei44PhosphotyrosineBy similarity1
Modified residuei60N6-acetyllysine; alternateBy similarity1
Modified residuei60N6-succinyllysine; alternateBy similarity1
Modified residuei89N6-acetyllysine; alternateBy similarity1
Modified residuei89N6-succinyllysine; alternateBy similarity1
Modified residuei193N6-acetyllysineBy similarity1
Modified residuei197N6-acetyllysineCombined sources1
Modified residuei199N6-acetyllysineCombined sources1
Modified residuei202N6-acetyllysineBy similarity1
Modified residuei228N6-acetyllysine; alternateBy similarity1
Modified residuei228N6-succinyllysine; alternateBy similarity1
Modified residuei256N6-acetyllysineBy similarity1
Modified residuei263PhosphoserineBy similarity1
Modified residuei335N6-acetyllysineBy similarity1
Modified residuei343N6-acetyllysineBy similarity1
Modified residuei406N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP17183.
PaxDbiP17183.
PeptideAtlasiP17183.
PRIDEiP17183.

2D gel databases

UCD-2DPAGEiP17183.

PTM databases

iPTMnetiP17183.
PhosphoSitePlusiP17183.
SwissPalmiP17183.

Expressioni

Tissue specificityi

Skeletal muscle (at protein level). 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.1 Publication1 Publication

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

BgeeiENSMUSG00000004267.
CleanExiMM_ENO2.
ExpressionAtlasiP17183. baseline and differential.
GenevisibleiP17183. MM.

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.

Protein-protein interaction databases

BioGridi199452. 2 interactors.
IntActiP17183. 3 interactors.
MINTiMINT-4094426.
STRINGi10090.ENSMUSP00000004378.

Structurei

3D structure databases

ProteinModelPortaliP17183.
SMRiP17183.
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.
GeneTreeiENSGT00900000141167.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP17183.
KOiK01689.
OMAiAEERACN.
OrthoDBiEOG091G07NH.
PhylomeDBiP17183.
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.
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.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiView protein in PROSITE
PS00164. ENOLASE. 1 hit.

Sequencei

Sequence statusi: Complete.

P17183-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DGDKQRYLGK GVLKAVDHIN SRIAPALISS GISVVEQEKL DNLMLELDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAAERDLPL YRHIAQLAGN SDLILPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGAESFRD AMRLGAEVYH TLKGVIKDKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKM VIGMDVAASE
260 270 280 290 300
FYRDGKYDLD FKSPADPSRY ITGDQLGALY QDFVRNYPVV SIEDPFDQDD
310 320 330 340 350
WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV
360 370 380 390 400
TEAIQACKLA QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL MRIEEELGDE ARFAGHNFRN PSVL
Length:434
Mass (Da):47,297
Last modified:January 23, 2007 - v2
Checksum:iA5C7F189E913392E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52380 mRNA. Translation: CAA36606.1.
AC002397 Genomic DNA. Translation: AAC36002.1.
BC031739 mRNA. Translation: AAH31739.1.
CCDSiCCDS20527.1.
PIRiS10247.
RefSeqiNP_001289571.1. NM_001302642.1.
NP_038537.1. NM_013509.3.
XP_006505566.1. XM_006505503.3.
XP_006505567.1. XM_006505504.2.
UniGeneiMm.3913.

Genome annotation databases

EnsembliENSMUST00000004378; ENSMUSP00000004378; ENSMUSG00000004267.
GeneIDi13807.
KEGGimmu:13807.
UCSCiuc009drs.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiENOG_MOUSE
AccessioniPrimary (citable) accession number: P17183
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 173 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families