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Gamma-enolase (EC 4 2 1 11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)

 ENOG_HUMAN              Reviewed;         434 AA.
P09104; B7Z2X9; Q96J33;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
26-FEB-2020, entry version 229.
RecName: Full=Gamma-enolase;
EC=4.2.1.11;
AltName: Full=2-phospho-D-glycerate hydro-lyase;
AltName: Full=Enolase 2;
AltName: Full=Neural enolase;
AltName: Full=Neuron-specific enolase;
Short=NSE;
Name=ENO2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Retina;
PubMed=3208766; DOI=10.1111/j.1432-1033.1988.tb14465.x;
McAleese S.M., Dunbar B., Fothergill J., Hinks L., Day I.N.M.;
"Complete amino acid sequence of the neurone-specific gamma isozyme of
enolase (NSE) from human brain and comparison with the non-neuronal alpha
form (NNE).";
Eur. J. Biochem. 178:413-417(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=3385803; DOI=10.1002/jnr.490190409;
van Obberghen E., Kamholz J., Bishop J.G. III, Zomzely-Neurath C.,
Lazzarini R.A.;
"Human gamma enolase: isolation of a cDNA clone and expression in normal
and tumor tissues of human origin.";
J. Neurosci. Res. 19:450-456(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2792767; DOI=10.1016/0378-1119(89)90217-5;
Oliva D., Barba G., Barbieri G., Giallongo A., Feo S.;
"Cloning, expression and sequence homologies of cDNA for human gamma
enolase.";
Gene 79:355-360(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Hematopoietic;
PubMed=2045099; DOI=10.1016/0888-7543(91)90496-2;
Oliva D., Cali L., Feo S., Giallongo A.;
"Complete structure of the human gene encoding neuron-specific enolase.";
Genomics 10:157-165(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
PubMed=9074930; DOI=10.1101/gr.7.3.268;
Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
"Large-scale sequencing in human chromosome 12p13: experimental and
computational gene structure determination.";
Genome Res. 7:268-280(1997).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Caudate nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 16-28; 33-50; 90-103; 163-179; 184-193; 240-262;
270-285; 336-372 AND 413-422, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 425-434 (ISOFORM 1/2).
PubMed=3653393; DOI=10.1016/0014-5793(87)80207-7;
Day I.N.M., Allsopp M.T.E.P., Moore D.C.M., Thompson R.J.;
"Sequence conservation in the 3'-untranslated regions of neurone-specific
enolase, lymphokine and protooncogene mRNAs.";
FEBS Lett. 222:139-143(1987).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
HYDROXYBUTYRYLATION AT LYS-233.
PubMed=29775581; DOI=10.1016/j.molcel.2018.04.011;
Huang H., Tang S., Ji M., Tang Z., Shimada M., Liu X., Qi S.,
Locasale J.W., Roeder R.G., Zhao Y., Li X.;
"p300-mediated lysine 2-hydroxyisobutyrylation regulates glycolysis.";
Mol. Cell 70:663-678(2018).
[18]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
PubMed=15289101; DOI=10.1016/j.jmb.2004.05.068;
Chai G., Brewer J.M., Lovelace L.L., Aoki T., Minor W., Lebioda L.;
"Expression, purification and the 1.8 angstroms resolution crystal
structure of human neuron specific enolase.";
J. Mol. Biol. 341:1015-1021(2004).
-!- 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
ChEBI:CHEBI:58702; EC=4.2.1.11;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 4/5.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:15289101}.
-!- INTERACTION:
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-713154, EBI-717399;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=Can translocate to the plasma membrane in either
the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P09104-1; Sequence=Displayed;
Name=2;
IsoId=P09104-2; Sequence=VSP_055482;
-!- 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.
-!- INDUCTION: Levels of ENO2 increase dramatically in cardiovascular
accidents, cerebral trauma, brain tumors and Creutzfeldt-Jakob disease.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA52388.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X13120; CAA31512.1; -; mRNA.
EMBL; X14327; CAA32505.1; -; mRNA.
EMBL; M36768; AAA52388.1; ALT_INIT; mRNA.
EMBL; M22349; AAB59554.1; -; mRNA.
EMBL; X51956; CAA36215.1; -; Genomic_DNA.
EMBL; AK295220; BAH12015.1; -; mRNA.
EMBL; BT007383; AAP36047.1; -; mRNA.
EMBL; U47924; AAB51320.1; -; Genomic_DNA.
EMBL; BC002745; AAH02745.1; -; mRNA.
CCDS; CCDS8570.1; -. [P09104-1]
PIR; JU0060; NOHUG.
RefSeq; NP_001966.1; NM_001975.2. [P09104-1]
PDB; 1TE6; X-ray; 1.80 A; A/B=2-434.
PDB; 2AKM; X-ray; 1.92 A; A/B=2-434.
PDB; 2AKZ; X-ray; 1.36 A; A/B=2-434.
PDB; 3UCC; X-ray; 1.50 A; A/B=2-434.
PDB; 3UCD; X-ray; 1.41 A; A/B=2-434.
PDB; 3UJE; X-ray; 1.55 A; A/B=2-434.
PDB; 3UJF; X-ray; 2.10 A; A/B=2-434.
PDB; 3UJR; X-ray; 1.40 A; A/B=2-434.
PDB; 3UJS; X-ray; 1.65 A; A/B=2-434.
PDB; 4ZA0; X-ray; 2.31 A; A/B=1-434.
PDB; 4ZCW; X-ray; 1.99 A; A/B=1-434.
PDB; 5EU9; X-ray; 2.05 A; A/B/C/D/E/F/G/H=1-434.
PDB; 5IDZ; X-ray; 2.63 A; A/B=1-434.
PDB; 5TD9; X-ray; 2.32 A; A/B=1-434.
PDB; 5TIJ; X-ray; 2.63 A; A/B=1-434.
PDBsum; 1TE6; -.
PDBsum; 2AKM; -.
PDBsum; 2AKZ; -.
PDBsum; 3UCC; -.
PDBsum; 3UCD; -.
PDBsum; 3UJE; -.
PDBsum; 3UJF; -.
PDBsum; 3UJR; -.
PDBsum; 3UJS; -.
PDBsum; 4ZA0; -.
PDBsum; 4ZCW; -.
PDBsum; 5EU9; -.
PDBsum; 5IDZ; -.
PDBsum; 5TD9; -.
PDBsum; 5TIJ; -.
SMR; P09104; -.
BioGrid; 108340; 91.
IntAct; P09104; 31.
MINT; P09104; -.
STRING; 9606.ENSP00000437402; -.
BindingDB; P09104; -.
DrugBank; DB02726; 2-Phosphoglycolic Acid.
iPTMnet; P09104; -.
PhosphoSitePlus; P09104; -.
SwissPalm; P09104; -.
BioMuta; ENO2; -.
DMDM; 20981682; -.
OGP; P09104; -.
UCD-2DPAGE; P09104; -.
EPD; P09104; -.
jPOST; P09104; -.
MassIVE; P09104; -.
PaxDb; P09104; -.
PeptideAtlas; P09104; -.
PRIDE; P09104; -.
ProteomicsDB; 52198; -. [P09104-1]
ProteomicsDB; 6473; -.
DNASU; 2026; -.
Ensembl; ENST00000229277; ENSP00000229277; ENSG00000111674. [P09104-1]
Ensembl; ENST00000535366; ENSP00000437402; ENSG00000111674. [P09104-1]
Ensembl; ENST00000538763; ENSP00000441490; ENSG00000111674. [P09104-2]
Ensembl; ENST00000541477; ENSP00000438873; ENSG00000111674. [P09104-1]
GeneID; 2026; -.
KEGG; hsa:2026; -.
UCSC; uc058knm.1; human. [P09104-1]
CTD; 2026; -.
DisGeNET; 2026; -.
GeneCards; ENO2; -.
HGNC; HGNC:3353; ENO2.
HPA; CAB000063; -.
HPA; CAB073539; -.
HPA; CAB079023; -.
HPA; HPA068284; -.
HPA; HPA068721; -.
MIM; 131360; gene.
neXtProt; NX_P09104; -.
OpenTargets; ENSG00000111674; -.
PharmGKB; PA27788; -.
eggNOG; KOG2670; Eukaryota.
eggNOG; COG0148; LUCA.
GeneTree; ENSGT00950000182805; -.
HOGENOM; CLU_031223_0_0_1; -.
InParanoid; P09104; -.
KO; K01689; -.
OMA; KHADNGI; -.
OrthoDB; 773373at2759; -.
PhylomeDB; P09104; -.
TreeFam; TF300391; -.
BioCyc; MetaCyc:HS10646-MONOMER; -.
BRENDA; 4.2.1.11; 2681.
Reactome; R-HSA-70171; Glycolysis.
Reactome; R-HSA-70263; Gluconeogenesis.
SABIO-RK; P09104; -.
UniPathway; UPA00109; UER00187.
ChiTaRS; ENO2; human.
EvolutionaryTrace; P09104; -.
GeneWiki; Enolase_2; -.
GenomeRNAi; 2026; -.
Pharos; P09104; Tbio.
PRO; PR:P09104; -.
Proteomes; UP000005640; Chromosome 12.
RNAct; P09104; protein.
Bgee; ENSG00000111674; Expressed in right hemisphere of cerebellum and 194 other tissues.
ExpressionAtlas; P09104; baseline and differential.
Genevisible; P09104; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:CAFA.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004634; F:phosphopyruvate hydratase activity; ISS:CAFA.
GO; GO:0061621; P:canonical glycolysis; TAS:Reactome.
GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
GO; GO:0006096; P:glycolytic process; ISS:CAFA.
CDD; cd03313; enolase; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
HAMAP; MF_00318; Enolase; 1.
InterPro; IPR000941; Enolase.
InterPro; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR020810; Enolase_C.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
PANTHER; PTHR11902; PTHR11902; 1.
Pfam; PF00113; Enolase_C; 1.
Pfam; PF03952; Enolase_N; 1.
PIRSF; PIRSF001400; Enolase; 1.
PRINTS; PR00148; ENOLASE.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
SUPFAM; SSF54826; SSF54826; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
Direct protein sequencing; Glycolysis; Hydroxylation; Isopeptide bond;
Lyase; Magnesium; Membrane; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:P06733"
CHAIN 2..434
/note="Gamma-enolase"
/id="PRO_0000134112"
REGION 370..373
/note="Substrate binding"
/evidence="ECO:0000250|UniProtKB:P00924"
ACT_SITE 210
/note="Proton donor"
/evidence="ECO:0000250|UniProtKB:P00924"
ACT_SITE 343
/note="Proton acceptor"
/evidence="ECO:0000250|UniProtKB:P00924"
METAL 40
/note="Magnesium 1"
/evidence="ECO:0000250|UniProtKB:P06733"
METAL 245
/note="Magnesium"
METAL 245
/note="Magnesium 2"
/evidence="ECO:0000250|UniProtKB:P06733"
METAL 293
/note="Magnesium"
METAL 293
/note="Magnesium 2"
/evidence="ECO:0000250|UniProtKB:P06733"
METAL 318
/note="Magnesium"
METAL 318
/note="Magnesium 2"
/evidence="ECO:0000250|UniProtKB:P06733"
BINDING 158
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 167
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 293
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 318
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 394
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 5
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 26
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:20068231"
MOD_RES 44
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:15592455"
MOD_RES 60
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 60
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 64
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 89
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 89
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 193
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 197
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P17183"
MOD_RES 199
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P17183"
MOD_RES 202
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 228
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 228
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 233
/note="N6-(2-hydroxyisobutyryl)lysine; alternate"
/evidence="ECO:0000269|PubMed:29775581"
MOD_RES 233
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 256
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 263
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 287
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 291
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 335
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 343
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P17182"
MOD_RES 406
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P17182"
CROSSLNK 202
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
VAR_SEQ 61..104
/note="GVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKS -> A
(in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_055482"
VARIANT 264
/note="P -> A"
/id="VAR_002354"
VARIANT 395
/note="T -> A"
/id="VAR_002355"
CONFLICT 4
/note="E -> Q (in Ref. 1; CAA31512/CAA32505)"
/evidence="ECO:0000305"
CONFLICT 27..28
/note="AK -> GC (in Ref. 2; AAA52388)"
/evidence="ECO:0000305"
CONFLICT 127
/note="E -> N (in Ref. 2; AAA52388)"
/evidence="ECO:0000305"
CONFLICT 240
/note="I -> M (in Ref. 1; CAA31512/CAA32505)"
/evidence="ECO:0000305"
STRAND 5..12
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 18..26
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 29..34
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 43..45
/evidence="ECO:0000244|PDB:5TD9"
TURN 54..56
/evidence="ECO:0000244|PDB:5TD9"
HELIX 57..59
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 63..71
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 73..80
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 87..98
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 100..102
/evidence="ECO:0000244|PDB:5TD9"
TURN 104..106
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 108..126
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 130..138
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 147..154
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 156..158
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 159..162
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 167..171
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 178..200
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 202..205
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 211..213
/evidence="ECO:0000244|PDB:3UJF"
HELIX 220..234
/evidence="ECO:0000244|PDB:2AKZ"
TURN 237..239
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 241..245
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 248..251
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 254..257
/evidence="ECO:0000244|PDB:2AKM"
TURN 259..262
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 267..269
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 273..286
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 289..293
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 301..309
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 312..318
/evidence="ECO:0000244|PDB:2AKZ"
TURN 319..323
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 325..333
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 338..342
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 344..347
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 350..362
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 366..370
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 380..388
/evidence="ECO:0000244|PDB:2AKZ"
STRAND 391..394
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 401..417
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 418..420
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 425..427
/evidence="ECO:0000244|PDB:2AKZ"
HELIX 431..433
/evidence="ECO:0000244|PDB:2AKZ"
SEQUENCE 434 AA; 47269 MW; 6163DE81F5C67744 CRC64;
MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK
GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK
AGAAERELPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD
AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI
VIGMDVAASE FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD
WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA
QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE
ARFAGHNFRN PSVL


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Pathways :
WP1946: Cori Cycle
WP253: Glycolysis
WP1030: Selenium metabolism Selenoproteins
WP548: neural crest development
WP1224: EBV LMP1 signaling
WP760: estrogen signalling
WP2064: Neural Crest Differentiation
WP2199: Seed Development
WP1358: Selenium metabolism Selenoproteins
WP1654: gamma-Hexachlorocyclohexane degradation
WP262: EBV LMP1 signaling
WP390: Serine-isocitrate lyase pathway
WP1718: Vitamin B6 metabolism
WP1886: Post-translational modification: gamma carboxylation and hypusine formation
WP542: Electron Transport Chain
WP1149: Selenium metabolism Selenoproteins
WP758: EBV LMP1 signaling
WP2006: Squamous cell TarBase
WP2152: BDNF
WP1293: Selenium metabolism Selenoproteins
WP868: estrogen signalling
WP1640: Cysteine and methionine metabolism
WP32: Translation Factors
WP1705: Sulfur metabolism
WP537: Translation Factors

Related Genes :
[ENO2] Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)
[Eno2 Eno-2] Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)
[Eno2 Eno-2] Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)
[Eno1 Eno-1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[Eno1 Eno-1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[ENO1 ENO1L1 MBPB1 MPB1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (C-myc promoter-binding protein) (Enolase 1) (MBP-1) (MPB-1) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase) (Plasminogen-binding protein)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[Eno3 Eno-3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[Eno3 Eno-3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[ENO1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (HAP47) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[ENO1 CAALFM_C108500CA CaO19.395 CaO19.8025] Enolase 1 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[ENO2 LOS2 At2g36530 F1O11.16] Bifunctional enolase 2/transcriptional activator (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 2) (2-phosphoglycerate dehydratase 2) (LOW EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 1)
[ENO1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[ENO1 QccE-14518] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[ENO1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE) (Fragments)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[eno MSMEG_5415 MSMEI_5267] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR1_00408] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno CBP06_04475 E4195_23395 EQ845_16830] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR214_00082] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR37_00362] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR16_24200] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno BJD20_17165 CW311_11095] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno Loa_02648] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno E4195_02605] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno1 eno ACTI_28410] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[emp-7 NCU10042] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (Embden-meyerhof pathway protein 7)
[eno HPHPP2_0250] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)

Bibliography :
[32021984] Characteristics of S100B and Neuron Specific Enolase in Differentiating Acute Vertigo Cases with Central Cause; a Diagnostic Accuracy Study.
[32012501] Laboratory criteria of perinatal damage of central nervous system at premature newborns
[31825363] [The possibility of using neuron-specific enolase as a biomarker in the acute period of stroke].
[31638583] NSE & S100B protein blood level assessment during a long-distance trail race.
[31487372] [Inflammation and Neurodegeneration in Patients with Early-Stageand Chronic Bipolar Disorder].
[31468657] Protective effect of vanillic acid against benzo(a)pyrene induced lung cancer in Swiss albino mice.
[31454201] Could Cerebrospinal Fluid Biomarkers Offer Better Predictive Value for Spinal Cord Ischaemia Than Current Neuromonitoring Techniques During Thoracoabdominal Aortic Aneurysm Repair - A Systematic Review.
[31450096] PtCu nanoprobe-initiated cascade reaction modulated iodide-responsive sensing interface for improved electrochemical immunosensor of neuron-specific enolase.
[31449996] Brain Injury Biomarker Behavior in Spontaneous Intracerebral Hemorrhage.
[31414753] Right Lung Consolidation Combined Elevated Serum Neuron Specific Enolase Misdiagnosed as Lung Carcinoma Ultimately Confirmed Pulmonary Cryptococcosis by CT-guided Percutaneous Lung Biopsy: a Case Report and Literature Review.