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P17182

- ENOA_MOUSE

UniProt

P17182 - ENOA_MOUSE

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Protein
Alpha-enolase
Gene
Eno1, Eno-1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses By similarity. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production By similarity.UniRule annotation

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.UniRule annotation

Cofactori

Magnesium. Binds two Mg2+ per subunit. Required for catalysis and for stabilizing the dimer.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Magnesium 1 By similarity
Binding sitei158 – 1581Substrate By similarity
Binding sitei167 – 1671Substrate By similarity
Active sitei210 – 2101Proton donor By similarity
Metal bindingi245 – 2451Magnesium 2 By similarity
Metal bindingi293 – 2931Magnesium 2 By similarity
Binding sitei293 – 2931Substrate By similarity
Metal bindingi318 – 3181Magnesium 2 By similarity
Binding sitei318 – 3181Substrate By similarity
Active sitei343 – 3431Proton acceptor By similarity
Binding sitei394 – 3941Substrate By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. phosphopyruvate hydratase activity Source: MGI

GO - Biological processi

  1. glycolytic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.1.11. 3474.
SABIO-RKP17182.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 1
Non-neural enolase
Short name:
NNE
Gene namesi
Name:Eno1
Synonyms:Eno-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:95393. Eno1.

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. ENO1 is localized to the M-band.1 Publication

GO - Cellular componenti

  1. phosphopyruvate hydratase complex Source: InterPro
  2. 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 – 11Removed By similarity
Chaini2 – 434433Alpha-enolaseUniRule annotation
PRO_0000134098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei44 – 441Phosphotyrosine1 Publication
Modified residuei60 – 601N6-acetyllysine; alternate1 Publication
Modified residuei60 – 601N6-succinyllysine; alternate1 Publication
Modified residuei71 – 711N6-acetyllysine By similarity
Modified residuei89 – 891N6-acetyllysine; alternate1 Publication
Modified residuei89 – 891N6-succinyllysine; alternate1 Publication
Modified residuei92 – 921N6-acetyllysine1 Publication
Modified residuei126 – 1261N6-acetyllysine1 Publication
Modified residuei193 – 1931N6-acetyllysine1 Publication
Modified residuei199 – 1991N6-acetyllysine By similarity
Modified residuei202 – 2021N6-acetyllysine1 Publication
Modified residuei228 – 2281N6-acetyllysine; alternate1 Publication
Modified residuei228 – 2281N6-succinyllysine; alternate1 Publication
Modified residuei233 – 2331N6-acetyllysine; alternate By similarity
Modified residuei233 – 2331N6-malonyllysine; alternate By similarity
Modified residuei254 – 2541Phosphoserine By similarity
Modified residuei256 – 2561N6-acetyllysine1 Publication
Modified residuei263 – 2631Phosphoserine By similarity
Modified residuei281 – 2811N6-acetyllysine By similarity
Modified residuei287 – 2871Phosphotyrosine By similarity
Modified residuei335 – 3351N6-acetyllysine1 Publication
Modified residuei343 – 3431N6-acetyllysine1 Publication
Modified residuei406 – 4061N6-acetyllysine1 Publication
Modified residuei420 – 4201N6-acetyllysine; alternate By similarity
Modified residuei420 – 4201N6-malonyllysine; alternate By similarity
Modified residuei420 – 4201N6-succinyllysine; alternate1 Publication

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP17182.
PaxDbiP17182.
PRIDEiP17182.

2D gel databases

REPRODUCTION-2DPAGEIPI00462072.
P17182.
SWISS-2DPAGEP17182.
UCD-2DPAGEP17182.

PTM databases

PhosphoSiteiP17182.

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. In striated muscle, expression of ENO1 appears to be independent of fiber type.1 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. In embryonic muscle, ENO1 is highly expressed until E17. Decreased levels from P5.1 Publication

Gene expression databases

ArrayExpressiP17182.
BgeeiP17182.
GenevestigatoriP17182.

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. ENO1 interacts with PLG in the neuronal plasma membrane and promotes its activation. The C-terminal lysine is required for this binding By similarity. In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and aldolase. Also binds troponin, in vitro.1 Publication

Protein-protein interaction databases

BioGridi199451. 16 interactions.
241069. 8 interactions.
IntActiP17182. 13 interactions.
MINTiMINT-4996502.

Structurei

3D structure databases

ProteinModelPortaliP17182.
SMRiP17182. Positions 2-434.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3734Substrate binding By similarity
Regioni405 – 43430Required for interaction with PLG By similarity
Add
BLAST

Sequence similaritiesi

Belongs to the enolase family.

Phylogenomic databases

eggNOGiCOG0148.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP17182.
KOiK01689.
OMAiVSEKSCN.
OrthoDBiEOG776SQ1.
PhylomeDBiP17182.
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.

P17182-1 [UniParc]FASTAAdd to Basket

« Hide

MSILRIHARE IFDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR    50
DNDKTRFMGK GVSQAVEHIN KTIAPALVSK KVNVVEQEKI DKLMIEMDGT 100
ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN PEVILPVPAF 150
NVINGGSHAG NKLAMQEFMI LPVGASSFRE AMRIGAEVYH NLKNVIKEKY 200
GKDATNVGDE GGFAPNILEN KEALELLKTA IAKAGYTDQV VIGMDVAASE 250
FYRSGKYDLD FKSPDDPSRY ITPDQLADLY KSFVQNYPVV SIEDPFDQDD 300
WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AASEKSCNCL LLKVNQIGSV 350
TESLQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR 400
SERLAKYNQI LRIEEELGSK AKFAGRSFRN PLAK 434
Length:434
Mass (Da):47,141
Last modified:January 23, 2007 - v3
Checksum:iDBEF6270A70DE3A6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti359 – 3591L → P in CAA36605. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52379 mRNA. Translation: CAA36605.1.
AK002336 mRNA. Translation: BAB22021.1.
BC003891 mRNA. Translation: AAH03891.1.
BC004017 mRNA. Translation: AAH04017.1.
BC010685 mRNA. Translation: AAH10685.1.
BC024644 mRNA. Translation: AAH24644.1.
BC085098 mRNA. Translation: AAH85098.1.
CCDSiCCDS18971.1.
PIRiS10246.
RefSeqiNP_001020559.1. NM_001025388.1.
NP_075608.2. NM_023119.2.
UniGeneiMm.372357.
Mm.372389.
Mm.70666.

Genome annotation databases

EnsembliENSMUST00000076155; ENSMUSP00000075513; ENSMUSG00000059040.
ENSMUST00000080926; ENSMUSP00000079727; ENSMUSG00000063524.
GeneIDi13806.
433182.
KEGGimmu:13806.
mmu:433182.
UCSCiuc008ewh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X52379 mRNA. Translation: CAA36605.1 .
AK002336 mRNA. Translation: BAB22021.1 .
BC003891 mRNA. Translation: AAH03891.1 .
BC004017 mRNA. Translation: AAH04017.1 .
BC010685 mRNA. Translation: AAH10685.1 .
BC024644 mRNA. Translation: AAH24644.1 .
BC085098 mRNA. Translation: AAH85098.1 .
CCDSi CCDS18971.1.
PIRi S10246.
RefSeqi NP_001020559.1. NM_001025388.1.
NP_075608.2. NM_023119.2.
UniGenei Mm.372357.
Mm.372389.
Mm.70666.

3D structure databases

ProteinModelPortali P17182.
SMRi P17182. Positions 2-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199451. 16 interactions.
241069. 8 interactions.
IntActi P17182. 13 interactions.
MINTi MINT-4996502.

PTM databases

PhosphoSitei P17182.

2D gel databases

REPRODUCTION-2DPAGE IPI00462072.
P17182.
SWISS-2DPAGE P17182.
UCD-2DPAGE P17182.

Proteomic databases

MaxQBi P17182.
PaxDbi P17182.
PRIDEi P17182.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000076155 ; ENSMUSP00000075513 ; ENSMUSG00000059040 .
ENSMUST00000080926 ; ENSMUSP00000079727 ; ENSMUSG00000063524 .
GeneIDi 13806.
433182.
KEGGi mmu:13806.
mmu:433182.
UCSCi uc008ewh.1. mouse.

Organism-specific databases

CTDi 2023.
433182.
MGIi MGI:95393. Eno1.

Phylogenomic databases

eggNOGi COG0148.
HOGENOMi HOG000072174.
HOVERGENi HBG000067.
InParanoidi P17182.
KOi K01689.
OMAi VSEKSCN.
OrthoDBi EOG776SQ1.
PhylomeDBi P17182.
TreeFami TF300391.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00187 .
BRENDAi 4.2.1.11. 3474.
SABIO-RK P17182.

Miscellaneous databases

NextBioi 284584.
PROi P17182.
SOURCEi Search...

Gene expression databases

ArrayExpressi P17182.
Bgeei P17182.
Genevestigatori P17182.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  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].
    Strain: Czech II and FVB/N.
    Tissue: Mammary gland and Mammary tumor.
  4. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 10-28; 33-50; 61-120; 133-179; 184-193; 203-228; 234-253; 257-262; 270-281; 307-326; 344-358; 373-394 AND 413-420, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. "Cholesteryl ester loading of mouse peritoneal macrophages is associated with changes in the expression or modification of specific cellular proteins, including increase in an alpha-enolase isoform."
    Bottalico L.A., Kendrick N.C., Keller A., Li Y., Tabas I.
    Arterioscler. Thromb. 13:264-275(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 60-71; 100-114; 184-198 AND 246-259.
    Tissue: Macrophage.
  6. "Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins."
    Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F., Lazar M., Keller A.
    Biochem. J. 323:791-800(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PKM; PGM; CKM; ALDO AND TROPONIN, DEVELOPMENTAL STAGE.
  7. "Fibre-type distribution and subcellular localisation of alpha and beta enolase in mouse striated muscle."
    Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C., Lucas M., Chatelet F.-P.
    Biol. Cell 92:527-535(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. Cited for: ISGYLATION.
  9. "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-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-89; LYS-92; LYS-126; LYS-193; LYS-202; LYS-228; LYS-256; LYS-335; LYS-343 AND LYS-406, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-89; LYS-228 AND LYS-420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiENOA_MOUSE
AccessioniPrimary (citable) accession number: P17182
Secondary accession number(s): Q99KT7, Q9DCY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 156 of the entry and version 3 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

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