P17183 (ENOG_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 130.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 434 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. |
| Catalytic activity | 2-phospho-D-glycerate = phosphoenolpyruvate + H2O. |
| Cofactor | Magnesium. Required for catalysis and for stabilizing the dimer. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. |
| Subunit structure | 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. |
| Subcellular location | 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. |
| Tissue specificity | 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 stage | 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. |
| Sequence similarities | Belongs to the enolase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Cell membrane Cytoplasm Membrane |
| Ligand | Magnesium Metal-binding |
| Molecular function | Lyase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | cytoplasm Inferred from direct assay PubMed 9758704. Source: MGI perikaryonInferred from direct assay PubMed 9671661. Source: MGI phosphopyruvate hydratase complexInferred from electronic annotation. Source: InterPro photoreceptor inner segmentInferred from direct assay PubMed 9364238. Source: MGI plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphopyruvate hydratase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 434 | 434 | Gamma-enolase | PRO_0000134113 | |||||
Regions | |||||||||
| Region | 370 – 373 | 4 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 210 | 1 | Proton donor By similarity | ||||||
| Active site | 343 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 245 | 1 | Magnesium By similarity | ||||||
| Metal binding | 293 | 1 | Magnesium By similarity | ||||||
| Metal binding | 318 | 1 | Magnesium By similarity | ||||||
| Binding site | 158 | 1 | Substrate By similarity | ||||||
| Binding site | 167 | 1 | Substrate By similarity | ||||||
| Binding site | 293 | 1 | Substrate By similarity | ||||||
| Binding site | 318 | 1 | Substrate By similarity | ||||||
| Binding site | 394 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 25 | 1 | Phosphotyrosine Ref.6 Ref.7 | ||||||
| Modified residue | 26 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 44 | 1 | Phosphotyrosine Ref.6 Ref.7 | ||||||
| Modified residue | 80 | 1 | Phosphoserine Ref.5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus. |
| [5] | "Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol." Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L. Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain. |
| [6] | "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25 AND TYR-44, MASS SPECTROMETRY. Tissue: Mast cell. |
| [7] | "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25 AND TYR-44, MASS SPECTROMETRY. Tissue: Brain. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X52380 mRNA. Translation: CAA36606.1. AC002397 Genomic DNA. Translation: AAC36002.1. BC031739 mRNA. Translation: AAH31739.1. |
| IPI | IPI00331704. |
| PIR | S10247. |
| RefSeq | NP_038537.1. NM_013509.2. |
| UniGene | Mm.3913. |
3D structure databases | |
| ProteinModelPortal | P17183. |
| SMR | P17183. Positions 2-434. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P17183. 2 interactions. |
PTM databases | |
| PhosphoSite | P17183. |
2D gel databases | |
| UCD-2DPAGE | P17183. |
Proteomic databases | |
| PaxDb | P17183. |
| PRIDE | P17183. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000004378; ENSMUSP00000004378; ENSMUSG00000004267. |
| GeneID | 13807. |
| KEGG | mmu:13807. |
Organism-specific databases | |
| CTD | 2026. |
| MGI | MGI:95394. Eno2. |
Phylogenomic databases | |
| eggNOG | COG0148. |
| HOGENOM | HOG000072174. |
| HOVERGEN | HBG000067. |
| InParanoid | P17183. |
| KO | K01689. |
| OMA | QAVDHIN. |
| OrthoDB | EOG4T783B. |
Enzyme and pathway databases | |
| SABIO-RK | P17183. |
| UniPathway | UPA00109; UER00187. |
Gene expression databases | |
| ArrayExpress | P17183. |
| Bgee | P17183. |
| CleanEx | MM_ENO2. |
| Genevestigator | P17183. |
| GermOnline | ENSMUSG00000004267. Mus musculus. |
Family and domain databases | |
| InterPro | IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view] |
| PANTHER | PTHR11902. PTHR11902. 1 hit. |
| Pfam | PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF001400. Enolase. 1 hit. |
| PRINTS | PR00148. ENOLASE. |
| TIGRFAMs | TIGR01060. eno. 1 hit. |
| PROSITE | PS00164. ENOLASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 284588. |
| SOURCE | Search... |
Entry information
| Entry name | ENOG_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P17183 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
