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P17183

- ENOG_MOUSE

UniProt

P17183 - ENOG_MOUSE

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Protein

Gamma-enolase

Gene

Eno2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Magnesium. Required for catalysis and for stabilizing the dimer.

Pathwayi

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

  1. magnesium ion binding Source: InterPro
  2. phosphopyruvate hydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

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: 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

  1. cytoplasm Source: MGI
  2. extracellular space Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. intracellular Source: MGI
  5. neuronal cell body Source: MGI
  6. perikaryon Source: MGI
  7. phosphopyruvate hydratase complex Source: InterPro
  8. photoreceptor inner segment Source: MGI
  9. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Gamma-enolasePRO_0000134113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261PhosphothreonineBy similarity
Modified residuei44 – 441PhosphotyrosineBy similarity
Modified residuei197 – 1971N6-acetyllysine1 Publication
Modified residuei199 – 1991N6-acetyllysine1 Publication

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.
GenevestigatoriP17183.

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

IntActiP17183. 3 interactions.
MINTiMINT-4094426.

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.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP17183.
KOiK01689.
OMAiHANWQGA.
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.

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:
EMBL
GenBank
DDBJ
Links Updated
X52380 mRNA. Translation: CAA36606.1.
AC002397 Genomic DNA. Translation: AAC36002.1.
BC031739 mRNA. Translation: AAH31739.1.
CCDSiCCDS20527.1.
PIRiS10247.
RefSeqiNP_038537.1. NM_013509.2.
XP_006505566.1. XM_006505503.1.
XP_006505567.1. XM_006505504.1.
UniGeneiMm.3913.

Genome annotation databases

EnsembliENSMUST00000004378; ENSMUSP00000004378; ENSMUSG00000004267.
GeneIDi13807.
KEGGimmu:13807.
UCSCiuc009drs.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52380 mRNA. Translation: CAA36606.1 .
AC002397 Genomic DNA. Translation: AAC36002.1 .
BC031739 mRNA. Translation: AAH31739.1 .
CCDSi CCDS20527.1.
PIRi S10247.
RefSeqi NP_038537.1. NM_013509.2.
XP_006505566.1. XM_006505503.1.
XP_006505567.1. XM_006505504.1.
UniGenei Mm.3913.

3D structure databases

ProteinModelPortali P17183.
SMRi P17183. Positions 2-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P17183. 3 interactions.
MINTi MINT-4094426.

PTM databases

PhosphoSitei P17183.

2D gel databases

UCD-2DPAGE P17183.

Proteomic databases

MaxQBi P17183.
PaxDbi P17183.
PRIDEi P17183.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004378 ; ENSMUSP00000004378 ; ENSMUSG00000004267 .
GeneIDi 13807.
KEGGi mmu:13807.
UCSCi uc009drs.1. mouse.

Organism-specific databases

CTDi 2026.
MGIi MGI:95394. Eno2.

Phylogenomic databases

eggNOGi COG0148.
HOGENOMi HOG000072174.
HOVERGENi HBG000067.
InParanoidi P17183.
KOi K01689.
OMAi HANWQGA.
PhylomeDBi P17183.
TreeFami TF300391.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00187 .
SABIO-RK P17183.

Miscellaneous databases

NextBioi 284588.
PROi P17183.
SOURCEi Search...

Gene expression databases

Bgeei P17183.
CleanExi MM_ENO2.
ExpressionAtlasi P17183. baseline and differential.
Genevestigatori P17183.

Family and domain databases

Gene3Di 3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPi MF_00318. Enolase.
InterProi IPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view ]
PANTHERi PTHR11902. PTHR11902. 1 hit.
Pfami PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001400. Enolase. 1 hit.
PRINTSi PR00148. ENOLASE.
SUPFAMi SSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsi TIGR01060. eno. 1 hit.
PROSITEi PS00164. ENOLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 143 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