ENOG_HUMAN
ID ENOG_HUMAN Reviewed; 434 AA.
AC P09104; B7Z2X9; Q96J33;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 241.
DE RecName: Full=Gamma-enolase;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=Enolase 2;
DE AltName: Full=Neural enolase;
DE AltName: Full=Neuron-specific enolase;
DE Short=NSE;
GN Name=ENO2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Retina;
RX PubMed=3208766; DOI=10.1111/j.1432-1033.1988.tb14465.x;
RA McAleese S.M., Dunbar B., Fothergill J., Hinks L., Day I.N.M.;
RT "Complete amino acid sequence of the neurone-specific gamma isozyme of
RT enolase (NSE) from human brain and comparison with the non-neuronal alpha
RT form (NNE).";
RL Eur. J. Biochem. 178:413-417(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=3385803; DOI=10.1002/jnr.490190409;
RA van Obberghen E., Kamholz J., Bishop J.G. III, Zomzely-Neurath C.,
RA Lazzarini R.A.;
RT "Human gamma enolase: isolation of a cDNA clone and expression in normal
RT and tumor tissues of human origin.";
RL J. Neurosci. Res. 19:450-456(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2792767; DOI=10.1016/0378-1119(89)90217-5;
RA Oliva D., Barba G., Barbieri G., Giallongo A., Feo S.;
RT "Cloning, expression and sequence homologies of cDNA for human gamma
RT enolase.";
RL Gene 79:355-360(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Hematopoietic;
RX PubMed=2045099; DOI=10.1016/0888-7543(91)90496-2;
RA Oliva D., Cali L., Feo S., Giallongo A.;
RT "Complete structure of the human gene encoding neuron-specific enolase.";
RL Genomics 10:157-165(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=9074930; DOI=10.1101/gr.7.3.268;
RA Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
RT "Large-scale sequencing in human chromosome 12p13: experimental and
RT computational gene structure determination.";
RL Genome Res. 7:268-280(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 16-28; 33-50; 90-103; 163-179; 184-193; 240-262;
RP 270-285; 336-372 AND 413-422, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 425-434 (ISOFORM 1/2).
RX PubMed=3653393; DOI=10.1016/0014-5793(87)80207-7;
RA Day I.N.M., Allsopp M.T.E.P., Moore D.C.M., Thompson R.J.;
RT "Sequence conservation in the 3'-untranslated regions of neurone-specific
RT enolase, lymphokine and protooncogene mRNAs.";
RL FEBS Lett. 222:139-143(1987).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP HYDROXYBUTYRYLATION AT LYS-233.
RX PubMed=29775581; DOI=10.1016/j.molcel.2018.04.011;
RA Huang H., Tang S., Ji M., Tang Z., Shimada M., Liu X., Qi S.,
RA Locasale J.W., Roeder R.G., Zhao Y., Li X.;
RT "p300-mediated lysine 2-hydroxyisobutyrylation regulates glycolysis.";
RL Mol. Cell 70:663-678(2018).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
RX PubMed=15289101; DOI=10.1016/j.jmb.2004.05.068;
RA Chai G., Brewer J.M., Lovelace L.L., Aoki T., Minor W., Lebioda L.;
RT "Expression, purification and the 1.8 angstroms resolution crystal
RT structure of human neuron specific enolase.";
RL J. Mol. Biol. 341:1015-1021(2004).
CC -!- FUNCTION: Has neurotrophic and neuroprotective properties on a broad
CC spectrum of central nervous system (CNS) neurons. Binds, in a calcium-
CC dependent manner, to cultured neocortical neurons and promotes cell
CC survival (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC ChEBI:CHEBI:58702; EC=4.2.1.11;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5.
CC -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha,
CC beta and gamma, which can form homodimers or heterodimers which are
CC cell-type and development-specific. {ECO:0000269|PubMed:15289101}.
CC -!- INTERACTION:
CC P09104; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-713154, EBI-717399;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Can translocate to the plasma membrane in either
CC the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P09104-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09104-2; Sequence=VSP_055482;
CC -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in embryo
CC and in most adult tissues. The alpha/beta heterodimer and the beta/beta
CC homodimer are found in striated muscle, and the alpha/gamma heterodimer
CC and the gamma/gamma homodimer in neurons.
CC -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the
CC alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle
CC cells, and to the alpha/gamma heterodimer in nerve cells.
CC -!- INDUCTION: Levels of ENO2 increase dramatically in cardiovascular
CC accidents, cerebral trauma, brain tumors and Creutzfeldt-Jakob disease.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA52388.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X13120; CAA31512.1; -; mRNA.
DR EMBL; X14327; CAA32505.1; -; mRNA.
DR EMBL; M36768; AAA52388.1; ALT_INIT; mRNA.
DR EMBL; M22349; AAB59554.1; -; mRNA.
DR EMBL; X51956; CAA36215.1; -; Genomic_DNA.
DR EMBL; AK295220; BAH12015.1; -; mRNA.
DR EMBL; BT007383; AAP36047.1; -; mRNA.
DR EMBL; U47924; AAB51320.1; -; Genomic_DNA.
DR EMBL; BC002745; AAH02745.1; -; mRNA.
DR CCDS; CCDS8570.1; -. [P09104-1]
DR PIR; JU0060; NOHUG.
DR RefSeq; NP_001966.1; NM_001975.2. [P09104-1]
DR PDB; 1TE6; X-ray; 1.80 A; A/B=2-434.
DR PDB; 2AKM; X-ray; 1.92 A; A/B=2-434.
DR PDB; 2AKZ; X-ray; 1.36 A; A/B=2-434.
DR PDB; 3UCC; X-ray; 1.50 A; A/B=2-434.
DR PDB; 3UCD; X-ray; 1.41 A; A/B=2-434.
DR PDB; 3UJE; X-ray; 1.55 A; A/B=2-434.
DR PDB; 3UJF; X-ray; 2.10 A; A/B=2-434.
DR PDB; 3UJR; X-ray; 1.40 A; A/B=2-434.
DR PDB; 3UJS; X-ray; 1.65 A; A/B=2-434.
DR PDB; 4ZA0; X-ray; 2.31 A; A/B=1-434.
DR PDB; 4ZCW; X-ray; 1.99 A; A/B=1-434.
DR PDB; 5EU9; X-ray; 2.05 A; A/B/C/D/E/F/G/H=1-434.
DR PDB; 5IDZ; X-ray; 2.63 A; A/B=1-434.
DR PDB; 5TD9; X-ray; 2.32 A; A/B=1-434.
DR PDB; 5TIJ; X-ray; 2.63 A; A/B=1-434.
DR PDBsum; 1TE6; -.
DR PDBsum; 2AKM; -.
DR PDBsum; 2AKZ; -.
DR PDBsum; 3UCC; -.
DR PDBsum; 3UCD; -.
DR PDBsum; 3UJE; -.
DR PDBsum; 3UJF; -.
DR PDBsum; 3UJR; -.
DR PDBsum; 3UJS; -.
DR PDBsum; 4ZA0; -.
DR PDBsum; 4ZCW; -.
DR PDBsum; 5EU9; -.
DR PDBsum; 5IDZ; -.
DR PDBsum; 5TD9; -.
DR PDBsum; 5TIJ; -.
DR AlphaFoldDB; P09104; -.
DR SMR; P09104; -.
DR BioGRID; 108340; 116.
DR IntAct; P09104; 43.
DR MINT; P09104; -.
DR STRING; 9606.ENSP00000437402; -.
DR BindingDB; P09104; -.
DR DrugBank; DB02726; 2-Phosphoglycolic Acid.
DR GlyGen; P09104; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P09104; -.
DR MetOSite; P09104; -.
DR PhosphoSitePlus; P09104; -.
DR SwissPalm; P09104; -.
DR BioMuta; ENO2; -.
DR DMDM; 20981682; -.
DR OGP; P09104; -.
DR UCD-2DPAGE; P09104; -.
DR EPD; P09104; -.
DR jPOST; P09104; -.
DR MassIVE; P09104; -.
DR MaxQB; P09104; -.
DR PaxDb; P09104; -.
DR PeptideAtlas; P09104; -.
DR PRIDE; P09104; -.
DR ProteomicsDB; 52198; -. [P09104-1]
DR ProteomicsDB; 6473; -.
DR Antibodypedia; 3514; 2106 antibodies from 52 providers.
DR DNASU; 2026; -.
DR Ensembl; ENST00000229277.6; ENSP00000229277.1; ENSG00000111674.9. [P09104-1]
DR Ensembl; ENST00000535366.5; ENSP00000437402.1; ENSG00000111674.9. [P09104-1]
DR Ensembl; ENST00000538763.5; ENSP00000441490.1; ENSG00000111674.9. [P09104-2]
DR Ensembl; ENST00000541477.5; ENSP00000438873.1; ENSG00000111674.9. [P09104-1]
DR GeneID; 2026; -.
DR KEGG; hsa:2026; -.
DR MANE-Select; ENST00000229277.6; ENSP00000229277.1; NM_001975.3; NP_001966.1.
DR UCSC; uc058knm.1; human. [P09104-1]
DR CTD; 2026; -.
DR DisGeNET; 2026; -.
DR GeneCards; ENO2; -.
DR HGNC; HGNC:3353; ENO2.
DR HPA; ENSG00000111674; Group enriched (brain, retina).
DR MIM; 131360; gene.
DR neXtProt; NX_P09104; -.
DR OpenTargets; ENSG00000111674; -.
DR PharmGKB; PA27788; -.
DR VEuPathDB; HostDB:ENSG00000111674; -.
DR eggNOG; KOG2670; Eukaryota.
DR GeneTree; ENSGT00950000182805; -.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P09104; -.
DR OMA; QHLGGAF; -.
DR PhylomeDB; P09104; -.
DR TreeFam; TF300391; -.
DR BioCyc; MetaCyc:HS10646-MON; -.
DR BRENDA; 4.2.1.11; 2681.
DR PathwayCommons; P09104; -.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SABIO-RK; P09104; -.
DR SignaLink; P09104; -.
DR SIGNOR; P09104; -.
DR UniPathway; UPA00109; UER00187.
DR BioGRID-ORCS; 2026; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; ENO2; human.
DR EvolutionaryTrace; P09104; -.
DR GeneWiki; Enolase_2; -.
DR GenomeRNAi; 2026; -.
DR Pharos; P09104; Tbio.
DR PRO; PR:P09104; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P09104; protein.
DR Bgee; ENSG00000111674; Expressed in cerebellar hemisphere and 170 other tissues.
DR ExpressionAtlas; P09104; baseline and differential.
DR Genevisible; P09104; HS.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:CAFA.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IBA:GO_Central.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; ISS:CAFA.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0061621; P:canonical glycolysis; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR GO; GO:0006096; P:glycolytic process; ISS:CAFA.
DR GO; GO:0048609; P:multicellular organismal reproductive process; IEA:Ensembl.
DR GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR CDD; cd03313; enolase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_00318; Enolase; 1.
DR InterPro; IPR000941; Enolase.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR020810; Enolase_C.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR PANTHER; PTHR11902; PTHR11902; 1.
DR Pfam; PF00113; Enolase_C; 1.
DR Pfam; PF03952; Enolase_N; 1.
DR PIRSF; PIRSF001400; Enolase; 1.
DR PRINTS; PR00148; ENOLASE.
DR SFLD; SFLDF00002; enolase; 1.
DR SMART; SM01192; Enolase_C; 1.
DR SMART; SM01193; Enolase_N; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Glycolysis; Hydroxylation; Isopeptide bond;
KW Lyase; Magnesium; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT CHAIN 2..434
FT /note="Gamma-enolase"
FT /id="PRO_0000134112"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT ACT_SITE 343
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 370..373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00924"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 26
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 44
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 60
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 60
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 64
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 89
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 89
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 197
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17183"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17183"
FT MOD_RES 202
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 228
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 228
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 233
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:29775581"
FT MOD_RES 233
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 287
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT MOD_RES 335
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 343
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 406
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P06733"
FT VAR_SEQ 61..104
FT /note="GVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKS -> A
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055482"
FT VARIANT 264
FT /note="P -> A"
FT /id="VAR_002354"
FT VARIANT 395
FT /note="T -> A"
FT /id="VAR_002355"
FT CONFLICT 4
FT /note="E -> Q (in Ref. 1; CAA31512/CAA32505)"
FT /evidence="ECO:0000305"
FT CONFLICT 27..28
FT /note="AK -> GC (in Ref. 2; AAA52388)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="E -> N (in Ref. 2; AAA52388)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="I -> M (in Ref. 1; CAA31512/CAA32505)"
FT /evidence="ECO:0000305"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5TD9"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:5TD9"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5TD9"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 108..126
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 178..200
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:3UJF"
FT HELIX 220..234
FT /evidence="ECO:0007829|PDB:2AKZ"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:2AKM"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:2AKZ"
FT TURN 319..323
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 350..362
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 380..388
FT /evidence="ECO:0007829|PDB:2AKZ"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 401..417
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:2AKZ"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:2AKZ"
SQ 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
