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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.

Pathway:iglycolysis

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 (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm7293), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839)
  2. Phosphoglycerate kinase 1 (Pgk1), Phosphoglycerate kinase 2 (Pgk2)
  3. no protein annotated in this organism
  4. Enolase (Eno3), Enolase (Eno2), Enolase (Eno1), Enolase (Eno2), Enolase (Eno3), Enolase (Eno2), Enolase, Gamma-enolase (Eno2), Alpha-enolase (Eno1), Beta-enolase (Eno3)
  5. Pyruvate kinase (Pklr), Pyruvate kinase PKM (Pkm), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581SubstrateBy similarity
Binding sitei167 – 1671SubstrateBy similarity
Active sitei210 – 2101Proton donorBy similarity
Metal bindingi245 – 2451MagnesiumBy similarity
Metal bindingi293 – 2931MagnesiumBy similarity
Binding sitei293 – 2931SubstrateBy similarity
Metal bindingi318 – 3181MagnesiumBy similarity
Binding sitei318 – 3181SubstrateBy similarity
Active sitei343 – 3431Proton acceptorBy similarity
Binding sitei394 – 3941SubstrateBy similarity

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

ReactomeiREACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.
SABIO-RKP17183.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:95394. Eno2.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

  • Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form.By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • intracellular Source: MGI
  • myelin sheath Source: UniProtKB
  • neuronal cell body Source: MGI
  • perikaryon Source: MGI
  • phosphopyruvate hydratase complex Source: InterPro
  • photoreceptor inner segment Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 434433Gamma-enolasePRO_0000134113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei26 – 261PhosphothreonineBy similarity
Modified residuei44 – 441PhosphotyrosineBy similarity
Modified residuei60 – 601N6-acetyllysine; alternateBy similarity
Modified residuei60 – 601N6-succinyllysine; alternateBy similarity
Modified residuei64 – 641N6-acetyllysineBy similarity
Modified residuei89 – 891N6-acetyllysine; alternateBy similarity
Modified residuei89 – 891N6-succinyllysine; alternateBy similarity
Modified residuei193 – 1931N6-acetyllysineBy similarity
Modified residuei197 – 1971N6-acetyllysine1 Publication
Modified residuei199 – 1991N6-acetyllysine1 Publication
Modified residuei202 – 2021N6-acetyllysineBy similarity
Modified residuei228 – 2281N6-acetyllysine; alternateBy similarity
Modified residuei228 – 2281N6-succinyllysine; alternateBy similarity
Modified residuei233 – 2331N6-acetyllysineBy similarity
Modified residuei256 – 2561N6-acetyllysineBy similarity
Modified residuei263 – 2631PhosphoserineBy similarity
Modified residuei287 – 2871PhosphotyrosineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei335 – 3351N6-acetyllysineBy similarity
Modified residuei343 – 3431N6-acetyllysineBy similarity
Modified residuei406 – 4061N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP17183.
PaxDbiP17183.
PRIDEiP17183.

2D gel databases

UCD-2DPAGEP17183.

PTM databases

PhosphoSiteiP17183.

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

BgeeiP17183.
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. 1 interaction.
IntActiP17183. 3 interactions.
MINTiMINT-4094426.
STRINGi10090.ENSMUSP00000004378.

Structurei

3D structure databases

ProteinModelPortaliP17183.
SMRiP17183. Positions 2-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3734Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiCOG0148.
GeneTreeiENSGT00550000074560.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP17183.
KOiK01689.
OMAiEAYAGNQ.
PhylomeDBiP17183.
TreeFamiTF300391.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
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.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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_006505503.2.
XP_006505567.1. XM_006505504.1.
UniGeneiMm.3913.

Genome annotation databases

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

Cross-referencesi

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_006505503.2.
XP_006505567.1. XM_006505504.1.
UniGeneiMm.3913.

3D structure databases

ProteinModelPortaliP17183.
SMRiP17183. Positions 2-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199452. 1 interaction.
IntActiP17183. 3 interactions.
MINTiMINT-4094426.
STRINGi10090.ENSMUSP00000004378.

PTM databases

PhosphoSiteiP17183.

2D gel databases

UCD-2DPAGEP17183.

Proteomic databases

MaxQBiP17183.
PaxDbiP17183.
PRIDEiP17183.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2026.
MGIiMGI:95394. Eno2.

Phylogenomic databases

eggNOGiCOG0148.
GeneTreeiENSGT00550000074560.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP17183.
KOiK01689.
OMAiEAYAGNQ.
PhylomeDBiP17183.
TreeFamiTF300391.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
ReactomeiREACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.
SABIO-RKP17183.

Miscellaneous databases

NextBioi284588.
PROiP17183.
SOURCEiSearch...

Gene expression databases

BgeeiP17183.
CleanExiMM_ENO2.
ExpressionAtlasiP17183. baseline and differential.
GenevisibleiP17183. MM.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
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.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequences of cDNAs alpha and gamma enolase mRNAs from mouse brain."
    Kaghad M., Dumont X., Chalon P., Lelias J.M., Lamande N., Lucas M., Lazar M., Caput D.
    Nucleic Acids Res. 18:3638-3638(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6."
    Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A.
    Genome Res. 8:29-40(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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].
    Tissue: Retina.
  4. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 16-28; 33-50; 73-89; 104-120; 163-179; 184-193; 203-228; 240-262; 270-285; 307-326; 336-358; 373-394 AND 413-429, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-197 AND LYS-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiENOG_MOUSE
AccessioniPrimary (citable) accession number: P17183
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 151 of the entry and version 2 of the sequence. [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

External Data

Dasty 3

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 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.