Full text data of ENO1
ENO1
(ENO1L1, MBPB1, MPB1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Alpha-enolase; 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)
Alpha-enolase; 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)
hRBCD
IPI00215736
IPI00215736 Alpha enolase Alpha enolase membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a Glycolisis, cytoplasmic, can translocate to the plasma membrane n/a expected molecular weight found in band > 188 kDa together with ubiquitin
IPI00215736 Alpha enolase Alpha enolase membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a Glycolisis, cytoplasmic, can translocate to the plasma membrane n/a expected molecular weight found in band > 188 kDa together with ubiquitin
UniProt
P06733
ID ENOA_HUMAN Reviewed; 434 AA.
AC P06733; B2RD59; P22712; Q16704; Q4TUS4; Q53FT9; Q53HR3; Q658M5;
read moreAC Q6GMP2; Q71V37; Q7Z3V6; Q8WU71; Q9UCH6; Q9UM55;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 176.
DE RecName: Full=Alpha-enolase;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=C-myc promoter-binding protein;
DE AltName: Full=Enolase 1;
DE AltName: Full=MBP-1;
DE AltName: Full=MPB-1;
DE AltName: Full=Non-neural enolase;
DE Short=NNE;
DE AltName: Full=Phosphopyruvate hydratase;
DE AltName: Full=Plasminogen-binding protein;
GN Name=ENO1; Synonyms=ENO1L1, MBPB1, MPB1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-ENOLASE).
RX PubMed=3529090; DOI=10.1073/pnas.83.18.6741;
RA Giallongo A., Feo S., Moore R., Croce C.M., Showe L.C.;
RT "Molecular cloning and nucleotide sequence of a full-length cDNA for
RT human alpha enolase.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6741-6745(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-ENOLASE).
RC TISSUE=T-cell;
RX PubMed=2373081; DOI=10.1111/j.1432-1033.1990.tb15611.x;
RA Giallongo A., Oliva D., Cali L., Barba G., Barbieri G., Feo S.;
RT "Structure of the human gene for alpha-enolase.";
RL Eur. J. Biochem. 190:567-573(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MBP-1), AND FUNCTION.
RC TISSUE=Cervix carcinoma;
RX PubMed=2005901;
RA Ray R., Miller D.M.;
RT "Cloning and characterization of a human c-myc promoter-binding
RT protein.";
RL Mol. Cell. Biol. 11:2154-2161(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-ENOLASE), AND MARKER FOR
RP ENDOMETRIOSIS.
RC TISSUE=Endometrium;
RX PubMed=8824716; DOI=10.1016/S0896-8411(95)80027-1;
RA Walter M., Berg H., Leidenberger F.A., Schweppe K.W., Northemann W.;
RT "Autoreactive epitopes within the human alpha-enolase and their
RT recognition by sera from patients with endometriosis.";
RL J. Autoimmun. 8:931-945(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
RC TISSUE=Umbilical cord blood;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 ALPHA-ENOLASE).
RC TISSUE=Adipose tissue, and Kidney proximal tubule;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
RC TISSUE=Retina, and Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-177.
RG NIEHS SNPs program;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
RC TISSUE=Brain, Eye, Lung, Ovary, Placenta, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP PROTEIN SEQUENCE OF 2-9 (ISOFORM ALPHA-ENOLASE).
RC TISSUE=Colon carcinoma;
RX PubMed=9150948; DOI=10.1002/elps.1150180344;
RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
RT "A two-dimensional gel database of human colon carcinoma proteins.";
RL Electrophoresis 18:605-613(1997).
RN [14]
RP PROTEIN SEQUENCE OF 2-28; 65-80; 121-162; 234-253; 270-281; 331-394
RP AND 407-420, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2,
RP AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Lilla S., Zebisch A., Kolch W.;
RL Submitted (MAR-2009) to UniProtKB.
RN [15]
RP PROTEIN SEQUENCE OF 16-28; 33-50; 93-103; 106-120; 163-179; 184-193;
RP 203-221; 240-253; 257-262; 270-281; 286-326; 336-394 AND 407-412, AND
RP 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 [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 166-434.
RX PubMed=9653645; DOI=10.1006/geno.1997.5186;
RA Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.;
RT "Molecular cloning and expression analysis of five novel genes in
RT chromosome 1p36.";
RL Genomics 50:187-198(1998).
RN [17]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-434.
RC TISSUE=Brain;
RX PubMed=9110174;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [18]
RP PROTEIN SEQUENCE OF 203-228, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Lymphoma;
RX PubMed=1369209; DOI=10.1007/BF00570890;
RA Sugahara T., Nakajima H., Shirahata S., Murakami H.;
RT "Purification and characterization of immunoglobulin production
RT stimulating factor-II beta derived from Namalwa cells.";
RL Cytotechnology 10:137-146(1992).
RN [19]
RP PROTEIN SEQUENCE OF 270-281 AND 307-321, AND INDUCTION IN DIFFUSE
RP LARGE CELL LYMPHOMA.
RX PubMed=7787969;
RA Mohamad R.M., Hamdan M.Y., Maki A., Al-Katib A.;
RT "Induced expression of alpha-enolase in differentiated diffuse large
RT cell lymphoma.";
RL Enzyme Protein 48:37-44(1994).
RN [20]
RP FUNCTION OF MBP1, IDENTIFICATION OF REPRESSOR DOMAINS, AND MUTAGENESIS
RP OF LEU-384 AND LEU-388.
RX PubMed=10082554;
RA Ghosh A.K., Steele R., Ray R.B.;
RT "Functional domains of c-myc promoter binding protein 1 involved in
RT transcriptional repression and cell growth regulation.";
RL Mol. Cell. Biol. 19:2880-2886(1999).
RN [21]
RP FUNCTION AS A C-MYC TRANSCRIPTIONAL REPRESSOR, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10802057; DOI=10.1016/S0014-5793(00)01494-0;
RA Feo S., Arcuri D., Piddini E., Passantino R., Giallongo A.;
RT "ENO1 gene product binds to the c-myc promoter and acts as a
RT transcriptional repressor: relationship with Myc promoter-binding
RT protein 1 (MBP-1).";
RL FEBS Lett. 473:47-52(2000).
RN [22]
RP FUNCTION IN PLASMINOGEN ACTIVATION.
RX PubMed=12666133; DOI=10.1002/ajh.10299;
RA Lopez-Alemany R., Longstaff C., Hawley S., Mirshahi M., Fabregas P.,
RA Jardi M., Merton E., Miles L.A., Felez J.;
RT "Inhibition of cell surface mediated plasminogen activation by a
RT monoclonal antibody against alpha-enolase.";
RL Am. J. Hematol. 72:234-242(2003).
RN [23]
RP INTERACTION WITH PLG.
RX PubMed=9308760;
RA Arza B., Felez J., Lopez-Alemany R., Miles L.A., Munoz-Canoves P.;
RT "Identification of an epitope of alpha-enolase (a candidate
RT plasminogen receptor) by phage display.";
RL Thromb. Haemost. 78:1097-1103(1997).
RN [24]
RP EPITOPE MAPPING, AND ASSOCIATION WITH CAR.
RX PubMed=9878089; DOI=10.1006/jaut.1998.0239;
RA Adamus G., Amundson D., Seigel G.M., Machnicki M.;
RT "Anti-enolase-alpha autoantibodies in cancer-associated retinopathy:
RT epitope mapping and cytotoxicity on retinal cells.";
RL J. Autoimmun. 11:671-677(1998).
RN [25]
RP IDENTIFICATION OF MBP1 AS AN ALPHA-ENOLASE ALTERNATIVE INITIATION
RP PRODUCT, AND MUTAGENESIS OF MET-94 AND MET-97.
RX PubMed=10681589; DOI=10.1074/jbc.275.8.5958;
RA Subramanian A., Miller D.M.;
RT "Structural analysis of alpha-enolase. Mapping the functional domains
RT involved in down-regulation of the c-myc protooncogene.";
RL J. Biol. Chem. 275:5958-5965(2000).
RN [26]
RP REVIEW.
RX PubMed=11497239; DOI=10.1007/PL00000910;
RA Pancholi V.;
RT "Multifunctional alpha-enolase: its role in diseases.";
RL Cell. Mol. Life Sci. 58:902-920(2001).
RN [27]
RP INTERACTION OF MBP1 WITH SEDL.
RX PubMed=11134351; DOI=10.1128/MCB.21.2.655-662.2001;
RA Ghosh A.K., Majumder M., Steele R., White R.A., Ray R.B.;
RT "A novel 16-kilodalton cellular protein physically interacts with and
RT antagonizes the functional activity of c-myc promoter-binding protein
RT 1.";
RL Mol. Cell. Biol. 21:655-662(2001).
RN [28]
RP IDENTIFICATION AS AN AUTOANTIGEN IN HASHIMOTO ENCEPHALOPATHY.
RX PubMed=12297304; DOI=10.1016/S0014-5793(02)03307-0;
RA Ochi H., Horiuchi I., Araki N., Toda T., Araki T., Sato K., Murai H.,
RA Osoegawa M., Yamada T., Okamura K., Ogino T., Mizumoto K.,
RA Yamashita H., Saya H., Kira J.;
RT "Proteomic analysis of human brain identifies alpha-enolase as a novel
RT autoantigen in Hashimoto's encephalopathy.";
RL FEBS Lett. 528:197-202(2002).
RN [29]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44 AND TYR-287, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [31]
RP INDUCTION, AND MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
RT reveal differential cellular gene expression in response to
RT enterovirus 71 infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [32]
RP ISGYLATION.
RX PubMed=16815975; DOI=10.1073/pnas.0600397103;
RA Wong J.J., Pung Y.F., Sze N.S., Chin K.C.;
RT "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates
RT type I IFN-induced ISGylation of protein targets.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 AND SER-263, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [35]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-5; LYS-64; LYS-71;
RP LYS-89; LYS-126; LYS-193; LYS-199; LYS-228; LYS-233; LYS-256; LYS-281;
RP LYS-285 AND LYS-420, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [36]
RP IDENTIFICATION BY 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [37]
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.,
RA Buerckstuemmer T., 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 [38]
RP MALONYLATION AT LYS-233 AND LYS-420.
RX PubMed=21908771; DOI=10.1074/mcp.M111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
RA He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
RA Dai J., Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
CC -!- FUNCTION: Multifunctional enzyme that, as well as its role in
CC glycolysis, plays a part in various processes such as growth
CC control, hypoxia tolerance and allergic responses. May also
CC function in the intravascular and pericellular fibrinolytic system
CC due to its ability to serve as a receptor and activator of
CC plasminogen on the cell surface of several cell-types such as
CC leukocytes and neurons. Stimulates immunoglobulin production.
CC -!- FUNCTION: MBP1 binds to the myc promoter and acts as a
CC transcriptional repressor. May be a tumor suppressor.
CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC H(2)O.
CC -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC the dimer.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Enolase activity is lost above pH 9.0. Immunoglobulin production
CC stimulating activity is retained at pH 13.0;
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,
CC alpha, beta and gamma, which can form homodimers or heterodimers
CC which are cell-type and development-specific. ENO1 interacts with
CC PLG in the neuronal plasma membrane and promotes its activation.
CC The C-terminal lysine is required for this binding (By
CC similarity).
CC -!- INTERACTION:
CC P22303:ACHE; NbExp=2; IntAct=EBI-353877, EBI-1637793;
CC P12004:PCNA; NbExp=3; IntAct=EBI-353877, EBI-358311;
CC Q8WZ42:TTN; NbExp=3; IntAct=EBI-353877, EBI-681210;
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-353877, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Cytoplasm,
CC myofibril, sarcomere, M line. Note=Can translocate to the plasma
CC membrane in either the homodimeric (alpha/alpha) or heterodimeric
CC (alpha/gamma) form. ENO1 is localized to the M line.
CC -!- SUBCELLULAR LOCATION: Isoform MBP-1: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=alpha-enolase;
CC IsoId=P06733-1; Sequence=Displayed;
CC Name=MBP-1;
CC IsoId=P06733-2; Sequence=VSP_018725;
CC Note=It is uncertain whether the alternative initiation site is
CC at Met-94 or at Met-97;
CC -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in
CC embryo and in most adult tissues. The alpha/beta heterodimer and
CC the beta/beta homodimer are found in striated muscle, and the
CC alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.
CC -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition
CC from the alpha/alpha homodimer to the alpha/beta heterodimer in
CC striated muscle cells, and to the alpha/gamma heterodimer in nerve
CC cells.
CC -!- INDUCTION: Induced in diffuse large cell lymphoma (DLCL) after
CC treatment with the natural biological agent, Bryo1. Up-regulated
CC in response to enterovirus 71 (EV71) infection (at protein level).
CC -!- PTM: ISGylated.
CC -!- MISCELLANEOUS: Used as a diagnostic marker for many tumors and, in
CC the heterodimeric form, alpha/gamma, as a marker for hypoxic brain
CC injury after cardiac arrest. Also marker for endometriosis.
CC Antibodies against alpha-enolase are present in sera from patients
CC with cancer-associated retinopathy syndrome (CAR), a progressive
CC blinding disease which occurs in the presence of systemic tumor
CC growth, primarily small-cell carcinoma of the lung and other
CC malignancies. Is identified as an autoantigen in Hashimoto
CC encephalopathy (HE) a rare autoimmune disease associated with
CC Hashimoto thyroiditis (HT). HT is a disorder in which destructive
CC processes overcome the potential capacity of thyroid replacement
CC leading to hypothyroidism.
CC -!- SIMILARITY: Belongs to the enolase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35698.1; Type=Frameshift; Positions=Several;
CC Sequence=AAA35698.1; Type=Miscellaneous discrepancy; Note=Sequencing errors;
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/eno1/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ENO1ID40453ch1p36.html";
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DR EMBL; M14328; AAA52387.1; -; mRNA.
DR EMBL; X16288; CAA34360.1; -; Genomic_DNA.
DR EMBL; X16289; CAA34360.1; JOINED; Genomic_DNA.
DR EMBL; X16290; CAA34360.1; JOINED; Genomic_DNA.
DR EMBL; M55914; AAA35698.1; ALT_FRAME; mRNA.
DR EMBL; X84907; CAA59331.1; -; mRNA.
DR EMBL; BT007163; AAP35827.1; -; mRNA.
DR EMBL; AK315417; BAG37806.1; -; mRNA.
DR EMBL; AL833741; CAH56247.1; -; mRNA.
DR EMBL; BX537400; CAD97642.1; -; mRNA.
DR EMBL; AK222517; BAD96237.1; -; mRNA.
DR EMBL; AK223192; BAD96912.1; -; mRNA.
DR EMBL; DQ056744; AAY43128.1; -; Genomic_DNA.
DR EMBL; AL139415; CAC42425.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71604.1; -; Genomic_DNA.
DR EMBL; BC001810; AAH01810.1; -; mRNA.
DR EMBL; BC004458; AAH04458.1; -; mRNA.
DR EMBL; BC009912; AAH09912.1; -; mRNA.
DR EMBL; BC011130; AAH11130.1; -; mRNA.
DR EMBL; BC015641; AAH15641.1; -; mRNA.
DR EMBL; BC021166; AAH21166.2; -; mRNA.
DR EMBL; BC022545; AAH22545.1; -; mRNA.
DR EMBL; BC027725; AAH27725.1; -; mRNA.
DR EMBL; BC050642; AAH50642.1; -; mRNA.
DR EMBL; U88968; AAC39935.1; -; mRNA.
DR EMBL; AF035286; AAB88178.1; -; mRNA.
DR PIR; A39579; A39579.
DR PIR; S11696; A29170.
DR RefSeq; NP_001188412.1; NM_001201483.1.
DR RefSeq; NP_001419.1; NM_001428.3.
DR UniGene; Hs.517145; -.
DR PDB; 2PSN; X-ray; 2.20 A; A/B/C/D=1-434.
DR PDB; 3B97; X-ray; 2.20 A; A/B/C/D=2-434.
DR PDBsum; 2PSN; -.
DR PDBsum; 3B97; -.
DR ProteinModelPortal; P06733; -.
DR SMR; P06733; 2-434.
DR IntAct; P06733; 57.
DR MINT; MINT-155303; -.
DR PhosphoSite; P06733; -.
DR DMDM; 119339; -.
DR DOSAC-COBS-2DPAGE; P06733; -.
DR OGP; P06733; -.
DR REPRODUCTION-2DPAGE; IPI00465248; -.
DR REPRODUCTION-2DPAGE; P06733; -.
DR SWISS-2DPAGE; P06733; -.
DR UCD-2DPAGE; P06733; -.
DR PaxDb; P06733; -.
DR PeptideAtlas; P06733; -.
DR PRIDE; P06733; -.
DR DNASU; 2023; -.
DR Ensembl; ENST00000234590; ENSP00000234590; ENSG00000074800.
DR GeneID; 2023; -.
DR KEGG; hsa:2023; -.
DR UCSC; uc001api.2; human.
DR CTD; 2023; -.
DR GeneCards; GC01M008921; -.
DR HGNC; HGNC:3350; ENO1.
DR HPA; CAB018614; -.
DR MIM; 172430; gene.
DR neXtProt; NX_P06733; -.
DR PharmGKB; PA27786; -.
DR eggNOG; COG0148; -.
DR HOVERGEN; HBG000067; -.
DR InParanoid; P06733; -.
DR KO; K01689; -.
DR OMA; VSEKSCN; -.
DR OrthoDB; EOG776SQ1; -.
DR PhylomeDB; P06733; -.
DR BioCyc; MetaCyc:ENSG00000074800-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P06733; -.
DR UniPathway; UPA00109; UER00187.
DR ChiTaRS; ENO1; human.
DR EvolutionaryTrace; P06733; -.
DR GeneWiki; Alpha-enolase; -.
DR GenomeRNAi; 2023; -.
DR NextBio; 8197; -.
DR PMAP-CutDB; P06733; -.
DR PRO; PR:P06733; -.
DR ArrayExpress; P06733; -.
DR Bgee; P06733; -.
DR Genevestigator; P06733; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; TAS:ProtInc.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0006096; P:glycolysis; TAS:Reactome.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR000941; Enolase.
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 TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Cell membrane;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Glycolysis; Lyase; Magnesium; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Plasminogen activation; Polymorphism;
KW Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 434 Alpha-enolase.
FT /FTId=PRO_0000134097.
FT REGION 31 38 Epitope recognized by CAR and healthy
FT patient antibodies.
FT REGION 56 63 Epitope recognized by CAR antibodies.
FT REGION 97 237 Required for repression of c-myc promoter
FT activity.
FT REGION 370 373 Substrate binding (By similarity).
FT REGION 405 434 Required for interaction with PLG (By
FT similarity).
FT ACT_SITE 210 210 Proton donor (By similarity).
FT ACT_SITE 343 343 Proton acceptor (By similarity).
FT METAL 245 245 Magnesium (By similarity).
FT METAL 293 293 Magnesium (By similarity).
FT METAL 318 318 Magnesium (By similarity).
FT BINDING 158 158 Substrate (By similarity).
FT BINDING 167 167 Substrate (By similarity).
FT BINDING 293 293 Substrate (By similarity).
FT BINDING 318 318 Substrate (By similarity).
FT BINDING 394 394 Substrate (By similarity).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 5 5 N6-acetyllysine.
FT MOD_RES 44 44 Phosphotyrosine.
FT MOD_RES 64 64 N6-acetyllysine.
FT MOD_RES 71 71 N6-acetyllysine.
FT MOD_RES 89 89 N6-acetyllysine.
FT MOD_RES 126 126 N6-acetyllysine.
FT MOD_RES 193 193 N6-acetyllysine.
FT MOD_RES 199 199 N6-acetyllysine.
FT MOD_RES 228 228 N6-acetyllysine.
FT MOD_RES 233 233 N6-acetyllysine; alternate.
FT MOD_RES 233 233 N6-malonyllysine; alternate.
FT MOD_RES 254 254 Phosphoserine.
FT MOD_RES 256 256 N6-acetyllysine.
FT MOD_RES 263 263 Phosphoserine.
FT MOD_RES 272 272 Phosphoserine.
FT MOD_RES 281 281 N6-acetyllysine.
FT MOD_RES 285 285 N6-acetyllysine.
FT MOD_RES 287 287 Phosphotyrosine.
FT MOD_RES 420 420 N6-acetyllysine; alternate.
FT MOD_RES 420 420 N6-malonyllysine; alternate.
FT VAR_SEQ 1 93 Missing (in isoform MBP-1).
FT /FTId=VSP_018725.
FT VARIANT 177 177 N -> K (in dbSNP:rs11544513).
FT /FTId=VAR_025172.
FT VARIANT 325 325 P -> Q (in dbSNP:rs11544514).
FT /FTId=VAR_048936.
FT MUTAGEN 94 94 M->I: MBP1 protein production. No MBP1
FT protein production; when associated with
FT I-97.
FT MUTAGEN 97 97 M->I: MBP1 protein production. No MBP1
FT protein production; when associated with
FT I-94.
FT MUTAGEN 384 384 L->A: Loss of transcriptional repression
FT and cell growth inhibition; when
FT associated with A-388.
FT MUTAGEN 388 388 L->A: Loss of transcriptional repression
FT and cell growth inhibition; when
FT associated with A-384.
FT CONFLICT 55 55 T -> A (in Ref. 8; CAD97642).
FT CONFLICT 78 78 V -> A (in Ref. 7; BAD96237).
FT CONFLICT 187 187 E -> G (in Ref. 8; CAD97642).
FT CONFLICT 199 199 K -> R (in Ref. 7; BAD96912).
FT CONFLICT 252 252 F -> S (in Ref. 4; CAA59331).
FT CONFLICT 310 310 S -> I (in Ref. 8; CAD97642).
FT STRAND 5 12
FT STRAND 18 26
FT STRAND 29 34
FT HELIX 57 59
FT HELIX 63 71
FT HELIX 73 79
FT HELIX 87 98
FT TURN 104 106
FT HELIX 108 125
FT HELIX 130 138
FT STRAND 147 154
FT HELIX 156 158
FT STRAND 159 162
FT STRAND 167 171
FT HELIX 178 200
FT HELIX 202 204
FT HELIX 220 233
FT TURN 237 239
FT STRAND 241 245
FT HELIX 248 250
FT TURN 259 262
FT HELIX 267 269
FT HELIX 273 286
FT STRAND 289 293
FT HELIX 301 311
FT STRAND 313 318
FT TURN 319 323
FT HELIX 325 334
FT STRAND 338 342
FT HELIX 344 347
FT HELIX 350 362
FT STRAND 366 370
FT HELIX 380 387
FT STRAND 391 394
FT HELIX 401 417
FT HELIX 418 420
FT HELIX 425 427
SQ SEQUENCE 434 AA; 47169 MW; A0ED663FCC15ADA5 CRC64;
MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK
GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK
AGAVEKGVPL YRHIADLAGN SEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAANFRE
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV
VIGMDVAASE FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD
WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV TESLQACKLA
QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK
AKFAGRNFRN PLAK
//
ID ENOA_HUMAN Reviewed; 434 AA.
AC P06733; B2RD59; P22712; Q16704; Q4TUS4; Q53FT9; Q53HR3; Q658M5;
read moreAC Q6GMP2; Q71V37; Q7Z3V6; Q8WU71; Q9UCH6; Q9UM55;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 176.
DE RecName: Full=Alpha-enolase;
DE EC=4.2.1.11;
DE AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE AltName: Full=C-myc promoter-binding protein;
DE AltName: Full=Enolase 1;
DE AltName: Full=MBP-1;
DE AltName: Full=MPB-1;
DE AltName: Full=Non-neural enolase;
DE Short=NNE;
DE AltName: Full=Phosphopyruvate hydratase;
DE AltName: Full=Plasminogen-binding protein;
GN Name=ENO1; Synonyms=ENO1L1, MBPB1, MPB1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-ENOLASE).
RX PubMed=3529090; DOI=10.1073/pnas.83.18.6741;
RA Giallongo A., Feo S., Moore R., Croce C.M., Showe L.C.;
RT "Molecular cloning and nucleotide sequence of a full-length cDNA for
RT human alpha enolase.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6741-6745(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-ENOLASE).
RC TISSUE=T-cell;
RX PubMed=2373081; DOI=10.1111/j.1432-1033.1990.tb15611.x;
RA Giallongo A., Oliva D., Cali L., Barba G., Barbieri G., Feo S.;
RT "Structure of the human gene for alpha-enolase.";
RL Eur. J. Biochem. 190:567-573(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MBP-1), AND FUNCTION.
RC TISSUE=Cervix carcinoma;
RX PubMed=2005901;
RA Ray R., Miller D.M.;
RT "Cloning and characterization of a human c-myc promoter-binding
RT protein.";
RL Mol. Cell. Biol. 11:2154-2161(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-ENOLASE), AND MARKER FOR
RP ENDOMETRIOSIS.
RC TISSUE=Endometrium;
RX PubMed=8824716; DOI=10.1016/S0896-8411(95)80027-1;
RA Walter M., Berg H., Leidenberger F.A., Schweppe K.W., Northemann W.;
RT "Autoreactive epitopes within the human alpha-enolase and their
RT recognition by sera from patients with endometriosis.";
RL J. Autoimmun. 8:931-945(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
RC TISSUE=Umbilical cord blood;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 ALPHA-ENOLASE).
RC TISSUE=Adipose tissue, and Kidney proximal tubule;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
RC TISSUE=Retina, and Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-177.
RG NIEHS SNPs program;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
RC TISSUE=Brain, Eye, Lung, Ovary, Placenta, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP PROTEIN SEQUENCE OF 2-9 (ISOFORM ALPHA-ENOLASE).
RC TISSUE=Colon carcinoma;
RX PubMed=9150948; DOI=10.1002/elps.1150180344;
RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
RT "A two-dimensional gel database of human colon carcinoma proteins.";
RL Electrophoresis 18:605-613(1997).
RN [14]
RP PROTEIN SEQUENCE OF 2-28; 65-80; 121-162; 234-253; 270-281; 331-394
RP AND 407-420, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2,
RP AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Lilla S., Zebisch A., Kolch W.;
RL Submitted (MAR-2009) to UniProtKB.
RN [15]
RP PROTEIN SEQUENCE OF 16-28; 33-50; 93-103; 106-120; 163-179; 184-193;
RP 203-221; 240-253; 257-262; 270-281; 286-326; 336-394 AND 407-412, AND
RP 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 [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 166-434.
RX PubMed=9653645; DOI=10.1006/geno.1997.5186;
RA Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.;
RT "Molecular cloning and expression analysis of five novel genes in
RT chromosome 1p36.";
RL Genomics 50:187-198(1998).
RN [17]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-434.
RC TISSUE=Brain;
RX PubMed=9110174;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [18]
RP PROTEIN SEQUENCE OF 203-228, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Lymphoma;
RX PubMed=1369209; DOI=10.1007/BF00570890;
RA Sugahara T., Nakajima H., Shirahata S., Murakami H.;
RT "Purification and characterization of immunoglobulin production
RT stimulating factor-II beta derived from Namalwa cells.";
RL Cytotechnology 10:137-146(1992).
RN [19]
RP PROTEIN SEQUENCE OF 270-281 AND 307-321, AND INDUCTION IN DIFFUSE
RP LARGE CELL LYMPHOMA.
RX PubMed=7787969;
RA Mohamad R.M., Hamdan M.Y., Maki A., Al-Katib A.;
RT "Induced expression of alpha-enolase in differentiated diffuse large
RT cell lymphoma.";
RL Enzyme Protein 48:37-44(1994).
RN [20]
RP FUNCTION OF MBP1, IDENTIFICATION OF REPRESSOR DOMAINS, AND MUTAGENESIS
RP OF LEU-384 AND LEU-388.
RX PubMed=10082554;
RA Ghosh A.K., Steele R., Ray R.B.;
RT "Functional domains of c-myc promoter binding protein 1 involved in
RT transcriptional repression and cell growth regulation.";
RL Mol. Cell. Biol. 19:2880-2886(1999).
RN [21]
RP FUNCTION AS A C-MYC TRANSCRIPTIONAL REPRESSOR, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10802057; DOI=10.1016/S0014-5793(00)01494-0;
RA Feo S., Arcuri D., Piddini E., Passantino R., Giallongo A.;
RT "ENO1 gene product binds to the c-myc promoter and acts as a
RT transcriptional repressor: relationship with Myc promoter-binding
RT protein 1 (MBP-1).";
RL FEBS Lett. 473:47-52(2000).
RN [22]
RP FUNCTION IN PLASMINOGEN ACTIVATION.
RX PubMed=12666133; DOI=10.1002/ajh.10299;
RA Lopez-Alemany R., Longstaff C., Hawley S., Mirshahi M., Fabregas P.,
RA Jardi M., Merton E., Miles L.A., Felez J.;
RT "Inhibition of cell surface mediated plasminogen activation by a
RT monoclonal antibody against alpha-enolase.";
RL Am. J. Hematol. 72:234-242(2003).
RN [23]
RP INTERACTION WITH PLG.
RX PubMed=9308760;
RA Arza B., Felez J., Lopez-Alemany R., Miles L.A., Munoz-Canoves P.;
RT "Identification of an epitope of alpha-enolase (a candidate
RT plasminogen receptor) by phage display.";
RL Thromb. Haemost. 78:1097-1103(1997).
RN [24]
RP EPITOPE MAPPING, AND ASSOCIATION WITH CAR.
RX PubMed=9878089; DOI=10.1006/jaut.1998.0239;
RA Adamus G., Amundson D., Seigel G.M., Machnicki M.;
RT "Anti-enolase-alpha autoantibodies in cancer-associated retinopathy:
RT epitope mapping and cytotoxicity on retinal cells.";
RL J. Autoimmun. 11:671-677(1998).
RN [25]
RP IDENTIFICATION OF MBP1 AS AN ALPHA-ENOLASE ALTERNATIVE INITIATION
RP PRODUCT, AND MUTAGENESIS OF MET-94 AND MET-97.
RX PubMed=10681589; DOI=10.1074/jbc.275.8.5958;
RA Subramanian A., Miller D.M.;
RT "Structural analysis of alpha-enolase. Mapping the functional domains
RT involved in down-regulation of the c-myc protooncogene.";
RL J. Biol. Chem. 275:5958-5965(2000).
RN [26]
RP REVIEW.
RX PubMed=11497239; DOI=10.1007/PL00000910;
RA Pancholi V.;
RT "Multifunctional alpha-enolase: its role in diseases.";
RL Cell. Mol. Life Sci. 58:902-920(2001).
RN [27]
RP INTERACTION OF MBP1 WITH SEDL.
RX PubMed=11134351; DOI=10.1128/MCB.21.2.655-662.2001;
RA Ghosh A.K., Majumder M., Steele R., White R.A., Ray R.B.;
RT "A novel 16-kilodalton cellular protein physically interacts with and
RT antagonizes the functional activity of c-myc promoter-binding protein
RT 1.";
RL Mol. Cell. Biol. 21:655-662(2001).
RN [28]
RP IDENTIFICATION AS AN AUTOANTIGEN IN HASHIMOTO ENCEPHALOPATHY.
RX PubMed=12297304; DOI=10.1016/S0014-5793(02)03307-0;
RA Ochi H., Horiuchi I., Araki N., Toda T., Araki T., Sato K., Murai H.,
RA Osoegawa M., Yamada T., Okamura K., Ogino T., Mizumoto K.,
RA Yamashita H., Saya H., Kira J.;
RT "Proteomic analysis of human brain identifies alpha-enolase as a novel
RT autoantigen in Hashimoto's encephalopathy.";
RL FEBS Lett. 528:197-202(2002).
RN [29]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44 AND TYR-287, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [31]
RP INDUCTION, AND MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
RT reveal differential cellular gene expression in response to
RT enterovirus 71 infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [32]
RP ISGYLATION.
RX PubMed=16815975; DOI=10.1073/pnas.0600397103;
RA Wong J.J., Pung Y.F., Sze N.S., Chin K.C.;
RT "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates
RT type I IFN-induced ISGylation of protein targets.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 AND SER-263, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [35]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-5; LYS-64; LYS-71;
RP LYS-89; LYS-126; LYS-193; LYS-199; LYS-228; LYS-233; LYS-256; LYS-281;
RP LYS-285 AND LYS-420, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [36]
RP IDENTIFICATION BY 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [37]
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.,
RA Buerckstuemmer T., 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 [38]
RP MALONYLATION AT LYS-233 AND LYS-420.
RX PubMed=21908771; DOI=10.1074/mcp.M111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
RA He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
RA Dai J., Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
CC -!- FUNCTION: Multifunctional enzyme that, as well as its role in
CC glycolysis, plays a part in various processes such as growth
CC control, hypoxia tolerance and allergic responses. May also
CC function in the intravascular and pericellular fibrinolytic system
CC due to its ability to serve as a receptor and activator of
CC plasminogen on the cell surface of several cell-types such as
CC leukocytes and neurons. Stimulates immunoglobulin production.
CC -!- FUNCTION: MBP1 binds to the myc promoter and acts as a
CC transcriptional repressor. May be a tumor suppressor.
CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC H(2)O.
CC -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC the dimer.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Enolase activity is lost above pH 9.0. Immunoglobulin production
CC stimulating activity is retained at pH 13.0;
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,
CC alpha, beta and gamma, which can form homodimers or heterodimers
CC which are cell-type and development-specific. ENO1 interacts with
CC PLG in the neuronal plasma membrane and promotes its activation.
CC The C-terminal lysine is required for this binding (By
CC similarity).
CC -!- INTERACTION:
CC P22303:ACHE; NbExp=2; IntAct=EBI-353877, EBI-1637793;
CC P12004:PCNA; NbExp=3; IntAct=EBI-353877, EBI-358311;
CC Q8WZ42:TTN; NbExp=3; IntAct=EBI-353877, EBI-681210;
CC P63104:YWHAZ; NbExp=2; IntAct=EBI-353877, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Cytoplasm,
CC myofibril, sarcomere, M line. Note=Can translocate to the plasma
CC membrane in either the homodimeric (alpha/alpha) or heterodimeric
CC (alpha/gamma) form. ENO1 is localized to the M line.
CC -!- SUBCELLULAR LOCATION: Isoform MBP-1: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=alpha-enolase;
CC IsoId=P06733-1; Sequence=Displayed;
CC Name=MBP-1;
CC IsoId=P06733-2; Sequence=VSP_018725;
CC Note=It is uncertain whether the alternative initiation site is
CC at Met-94 or at Met-97;
CC -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in
CC embryo and in most adult tissues. The alpha/beta heterodimer and
CC the beta/beta homodimer are found in striated muscle, and the
CC alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.
CC -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition
CC from the alpha/alpha homodimer to the alpha/beta heterodimer in
CC striated muscle cells, and to the alpha/gamma heterodimer in nerve
CC cells.
CC -!- INDUCTION: Induced in diffuse large cell lymphoma (DLCL) after
CC treatment with the natural biological agent, Bryo1. Up-regulated
CC in response to enterovirus 71 (EV71) infection (at protein level).
CC -!- PTM: ISGylated.
CC -!- MISCELLANEOUS: Used as a diagnostic marker for many tumors and, in
CC the heterodimeric form, alpha/gamma, as a marker for hypoxic brain
CC injury after cardiac arrest. Also marker for endometriosis.
CC Antibodies against alpha-enolase are present in sera from patients
CC with cancer-associated retinopathy syndrome (CAR), a progressive
CC blinding disease which occurs in the presence of systemic tumor
CC growth, primarily small-cell carcinoma of the lung and other
CC malignancies. Is identified as an autoantigen in Hashimoto
CC encephalopathy (HE) a rare autoimmune disease associated with
CC Hashimoto thyroiditis (HT). HT is a disorder in which destructive
CC processes overcome the potential capacity of thyroid replacement
CC leading to hypothyroidism.
CC -!- SIMILARITY: Belongs to the enolase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35698.1; Type=Frameshift; Positions=Several;
CC Sequence=AAA35698.1; Type=Miscellaneous discrepancy; Note=Sequencing errors;
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/eno1/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ENO1ID40453ch1p36.html";
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DR EMBL; M14328; AAA52387.1; -; mRNA.
DR EMBL; X16288; CAA34360.1; -; Genomic_DNA.
DR EMBL; X16289; CAA34360.1; JOINED; Genomic_DNA.
DR EMBL; X16290; CAA34360.1; JOINED; Genomic_DNA.
DR EMBL; M55914; AAA35698.1; ALT_FRAME; mRNA.
DR EMBL; X84907; CAA59331.1; -; mRNA.
DR EMBL; BT007163; AAP35827.1; -; mRNA.
DR EMBL; AK315417; BAG37806.1; -; mRNA.
DR EMBL; AL833741; CAH56247.1; -; mRNA.
DR EMBL; BX537400; CAD97642.1; -; mRNA.
DR EMBL; AK222517; BAD96237.1; -; mRNA.
DR EMBL; AK223192; BAD96912.1; -; mRNA.
DR EMBL; DQ056744; AAY43128.1; -; Genomic_DNA.
DR EMBL; AL139415; CAC42425.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71604.1; -; Genomic_DNA.
DR EMBL; BC001810; AAH01810.1; -; mRNA.
DR EMBL; BC004458; AAH04458.1; -; mRNA.
DR EMBL; BC009912; AAH09912.1; -; mRNA.
DR EMBL; BC011130; AAH11130.1; -; mRNA.
DR EMBL; BC015641; AAH15641.1; -; mRNA.
DR EMBL; BC021166; AAH21166.2; -; mRNA.
DR EMBL; BC022545; AAH22545.1; -; mRNA.
DR EMBL; BC027725; AAH27725.1; -; mRNA.
DR EMBL; BC050642; AAH50642.1; -; mRNA.
DR EMBL; U88968; AAC39935.1; -; mRNA.
DR EMBL; AF035286; AAB88178.1; -; mRNA.
DR PIR; A39579; A39579.
DR PIR; S11696; A29170.
DR RefSeq; NP_001188412.1; NM_001201483.1.
DR RefSeq; NP_001419.1; NM_001428.3.
DR UniGene; Hs.517145; -.
DR PDB; 2PSN; X-ray; 2.20 A; A/B/C/D=1-434.
DR PDB; 3B97; X-ray; 2.20 A; A/B/C/D=2-434.
DR PDBsum; 2PSN; -.
DR PDBsum; 3B97; -.
DR ProteinModelPortal; P06733; -.
DR SMR; P06733; 2-434.
DR IntAct; P06733; 57.
DR MINT; MINT-155303; -.
DR PhosphoSite; P06733; -.
DR DMDM; 119339; -.
DR DOSAC-COBS-2DPAGE; P06733; -.
DR OGP; P06733; -.
DR REPRODUCTION-2DPAGE; IPI00465248; -.
DR REPRODUCTION-2DPAGE; P06733; -.
DR SWISS-2DPAGE; P06733; -.
DR UCD-2DPAGE; P06733; -.
DR PaxDb; P06733; -.
DR PeptideAtlas; P06733; -.
DR PRIDE; P06733; -.
DR DNASU; 2023; -.
DR Ensembl; ENST00000234590; ENSP00000234590; ENSG00000074800.
DR GeneID; 2023; -.
DR KEGG; hsa:2023; -.
DR UCSC; uc001api.2; human.
DR CTD; 2023; -.
DR GeneCards; GC01M008921; -.
DR HGNC; HGNC:3350; ENO1.
DR HPA; CAB018614; -.
DR MIM; 172430; gene.
DR neXtProt; NX_P06733; -.
DR PharmGKB; PA27786; -.
DR eggNOG; COG0148; -.
DR HOVERGEN; HBG000067; -.
DR InParanoid; P06733; -.
DR KO; K01689; -.
DR OMA; VSEKSCN; -.
DR OrthoDB; EOG776SQ1; -.
DR PhylomeDB; P06733; -.
DR BioCyc; MetaCyc:ENSG00000074800-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P06733; -.
DR UniPathway; UPA00109; UER00187.
DR ChiTaRS; ENO1; human.
DR EvolutionaryTrace; P06733; -.
DR GeneWiki; Alpha-enolase; -.
DR GenomeRNAi; 2023; -.
DR NextBio; 8197; -.
DR PMAP-CutDB; P06733; -.
DR PRO; PR:P06733; -.
DR ArrayExpress; P06733; -.
DR Bgee; P06733; -.
DR Genevestigator; P06733; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; TAS:ProtInc.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0006096; P:glycolysis; TAS:Reactome.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR000941; Enolase.
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 TIGRFAMs; TIGR01060; eno; 1.
DR PROSITE; PS00164; ENOLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Cell membrane;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Glycolysis; Lyase; Magnesium; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Plasminogen activation; Polymorphism;
KW Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 434 Alpha-enolase.
FT /FTId=PRO_0000134097.
FT REGION 31 38 Epitope recognized by CAR and healthy
FT patient antibodies.
FT REGION 56 63 Epitope recognized by CAR antibodies.
FT REGION 97 237 Required for repression of c-myc promoter
FT activity.
FT REGION 370 373 Substrate binding (By similarity).
FT REGION 405 434 Required for interaction with PLG (By
FT similarity).
FT ACT_SITE 210 210 Proton donor (By similarity).
FT ACT_SITE 343 343 Proton acceptor (By similarity).
FT METAL 245 245 Magnesium (By similarity).
FT METAL 293 293 Magnesium (By similarity).
FT METAL 318 318 Magnesium (By similarity).
FT BINDING 158 158 Substrate (By similarity).
FT BINDING 167 167 Substrate (By similarity).
FT BINDING 293 293 Substrate (By similarity).
FT BINDING 318 318 Substrate (By similarity).
FT BINDING 394 394 Substrate (By similarity).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 5 5 N6-acetyllysine.
FT MOD_RES 44 44 Phosphotyrosine.
FT MOD_RES 64 64 N6-acetyllysine.
FT MOD_RES 71 71 N6-acetyllysine.
FT MOD_RES 89 89 N6-acetyllysine.
FT MOD_RES 126 126 N6-acetyllysine.
FT MOD_RES 193 193 N6-acetyllysine.
FT MOD_RES 199 199 N6-acetyllysine.
FT MOD_RES 228 228 N6-acetyllysine.
FT MOD_RES 233 233 N6-acetyllysine; alternate.
FT MOD_RES 233 233 N6-malonyllysine; alternate.
FT MOD_RES 254 254 Phosphoserine.
FT MOD_RES 256 256 N6-acetyllysine.
FT MOD_RES 263 263 Phosphoserine.
FT MOD_RES 272 272 Phosphoserine.
FT MOD_RES 281 281 N6-acetyllysine.
FT MOD_RES 285 285 N6-acetyllysine.
FT MOD_RES 287 287 Phosphotyrosine.
FT MOD_RES 420 420 N6-acetyllysine; alternate.
FT MOD_RES 420 420 N6-malonyllysine; alternate.
FT VAR_SEQ 1 93 Missing (in isoform MBP-1).
FT /FTId=VSP_018725.
FT VARIANT 177 177 N -> K (in dbSNP:rs11544513).
FT /FTId=VAR_025172.
FT VARIANT 325 325 P -> Q (in dbSNP:rs11544514).
FT /FTId=VAR_048936.
FT MUTAGEN 94 94 M->I: MBP1 protein production. No MBP1
FT protein production; when associated with
FT I-97.
FT MUTAGEN 97 97 M->I: MBP1 protein production. No MBP1
FT protein production; when associated with
FT I-94.
FT MUTAGEN 384 384 L->A: Loss of transcriptional repression
FT and cell growth inhibition; when
FT associated with A-388.
FT MUTAGEN 388 388 L->A: Loss of transcriptional repression
FT and cell growth inhibition; when
FT associated with A-384.
FT CONFLICT 55 55 T -> A (in Ref. 8; CAD97642).
FT CONFLICT 78 78 V -> A (in Ref. 7; BAD96237).
FT CONFLICT 187 187 E -> G (in Ref. 8; CAD97642).
FT CONFLICT 199 199 K -> R (in Ref. 7; BAD96912).
FT CONFLICT 252 252 F -> S (in Ref. 4; CAA59331).
FT CONFLICT 310 310 S -> I (in Ref. 8; CAD97642).
FT STRAND 5 12
FT STRAND 18 26
FT STRAND 29 34
FT HELIX 57 59
FT HELIX 63 71
FT HELIX 73 79
FT HELIX 87 98
FT TURN 104 106
FT HELIX 108 125
FT HELIX 130 138
FT STRAND 147 154
FT HELIX 156 158
FT STRAND 159 162
FT STRAND 167 171
FT HELIX 178 200
FT HELIX 202 204
FT HELIX 220 233
FT TURN 237 239
FT STRAND 241 245
FT HELIX 248 250
FT TURN 259 262
FT HELIX 267 269
FT HELIX 273 286
FT STRAND 289 293
FT HELIX 301 311
FT STRAND 313 318
FT TURN 319 323
FT HELIX 325 334
FT STRAND 338 342
FT HELIX 344 347
FT HELIX 350 362
FT STRAND 366 370
FT HELIX 380 387
FT STRAND 391 394
FT HELIX 401 417
FT HELIX 418 420
FT HELIX 425 427
SQ SEQUENCE 434 AA; 47169 MW; A0ED663FCC15ADA5 CRC64;
MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK
GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK
AGAVEKGVPL YRHIADLAGN SEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAANFRE
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV
VIGMDVAASE FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD
WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV TESLQACKLA
QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK
AKFAGRNFRN PLAK
//
MIM
172430
*RECORD*
*FIELD* NO
172430
*FIELD* TI
*172430 ENOLASE 1; ENO1
;;ENOLASE, ALPHA;;
PHOSPHOPYRUVATE HYDRATASE; PPH
CRYSTALLIN, TAU, INCLUDED;;
read moreENOLASE, NONNEURONAL, INCLUDED; NNE, INCLUDED
*FIELD* TX
DESCRIPTION
Enolase is a glycolytic enzyme (2-phospho-D-glycerate hydrolyase; EC
4.2.1.11). Each of the 3 ENO isoenzymes is a homodimer composed of 2
alpha (ENO1), 2 gamma (ENO2; 131360), or 2 beta (ENO3; 131370) subunits.
Isoenzyme alpha (ENO1) is present in most tissues, whereas the beta form
(ENO3) is localized to muscle and the gamma form (ENO2) is found only in
nervous tissue (summary by Giallongo et al., 1986).
CLONING
Giallongo et al. (1986) cloned and sequenced a full-length cDNA for
human alpha-enolase. Its coding region was found to be 1,299 bases long.
The 433-amino acid protein shows 67% homology to yeast enolase and 94%
homology to rat nonneural enolase.
Wistow et al. (1988) presented evidence for the remarkable conclusion
that alpha-enolase is encoded by the same gene that encodes
tau-crystallin, a lens structural protein.
GENE STRUCTURE
Giallongo et al. (1990) determined that the ENO1 gene contains 12 exons.
MAPPING
Giblett et al. (1974) observed an electrophoretic variant of red cell
PPH among Cree Indians. Linkage was found with the Rhesus locus. Since
the Rh locus has been assigned to chromosome 1 and since cell
hybridization studies assign the PPH locus to chromosome 1, the new data
are consistent. The Goss-Harris method of mapping combines features of
recombinational study in families and synteny tests in hybrid cells. As
applied to chromosome 1, the method shows that AK2 and UMPK are distal
to PGM1 and that the order of the loci is PGM1: UMPK: (AK2, alpha-FUC):
ENO1 (Goss and Harris, 1977). Comings (1972) and Ohno (1973) suggested
that during vertebrate evolution tetraploidization occurred 2-3 hundred
million years ago and that chromosomal events that tend to preserve
ancestral linkage groups, such as Robertsonian fusions, inversions and
gene duplications, have been favored. Demonstration of linkage of
homologous genes supports this hypothesis.
D'Ancona et al. (1977) regionalized ENO1 to 1pter-p36.13. Lalley et al.
(1978) demonstrated synteny of enolase, PGD (172200), PGM1 (171900), and
AK2 (103020) on chromosome 4 of the mouse; they are on 1p of man.
- Pseudogene
Feo et al. (1990) concluded that there is a single alpha-enolase
pseudogene in the human genome. This intronless, processed pseudogene
was mapped to chromosome 1 by Southern blot analysis of rodent-human
hybrid cell DNAs; thus, it is on the same chromosome as the functional
gene. Ribaudo et al. (1996) confirmed the assignment of ENO1P to
chromosome 1. By fluorescence in situ hybridization, they found that it
is located on 1q41-q42, whereas the functional gene is located on the
short arm of that chromosome.
GENE FUNCTION
Lachant et al. (1986) and Lachant and Tanaka (1987) reported 4
generations of a Caucasian family with hereditary red cell enolase
deficiency. Partial deficiency in this kindred behaved as an autosomal
dominant and was associated with a spherocytic phenotype, although a
normal acidified glycerol lysis test suggested that the spherocytes of
enolase deficiency are different from those of hereditary spherocytosis
(see 182900). Clinical expression of enolase deficiency varied in this
family. Some had slightly low hematocrit with elevated reticulocytes,
while others had no evidence of anemia or hemolysis.
To identify the autoantigens related to Hashimoto encephalopathy, a rare
autoimmune disease associated with Hashimoto thyroiditis (140300), Ochi
et al. (2002) developed a human brain proteome map using 2-dimensional
electrophoresis and applied it to the immunoscreening of brain proteins
that react with autoantibodies in affected patients. They thereby
identified alpha-enolase as the autoantigen in that disorder.
MOLECULAR GENETICS
Muller et al. (2012) proposed that homozygous deletions in passenger
genes in cancer deletions can expose cancer-specific therapeutic
vulnerabilities when the collaterally deleted gene is a member of a
functionally redundant family of genes carrying out an essential
function. The glycolytic gene ENO1 in the 1p36 locus is deleted in
glioblastoma, which is tolerated by the expression of ENO2 (131360).
Muller et al. (2012) showed that short hairpin RNA-mediated silencing of
ENO2 selectively inhibits growth, survival, and the tumorigenic
potential of ENO1-deleted GBM cells, and that the enolase inhibitor
phosphonoacetohydroxamate is selectively toxic to ENO1-deleted GBM cells
relative to ENO1-intact GBM cells or normal astrocytes. Muller et al.
(2012) suggested that the principle of collateral vulnerability should
be applicable to other passenger-deleted genes encoding functionally
redundant essential activities and provide an effective treatment
strategy for cancers containing such genomic events.
*FIELD* SA
D'Ancona and Croce (1977); Feo et al. (1990); Van Cong et al. (1977)
*FIELD* RF
1. Comings, D. E.: Evidence for ancient tetraploidy and conservation
of linkage groups in mammalian chromosomes. Nature 238: 455-457,
1972.
2. D'Ancona, G. G.; Chern, C. J.; Benn, P.; Croce, C. M.: Assignment
of the human gene for enolase 1 to region pter-p36 of chromosome 1. Cytogenet.
Cell Genet. 18: 327-332, 1977.
3. D'Ancona, G. G.; Croce, C. M.: Assignment of the gene for enolase
to mouse chromosome 4 using somatic cell hybrids. Cytogenet. Cell
Genet. 19: 1-6, 1977.
4. Feo, S.; Oliva, D.; Arico, B.; Barba, G.; Cali, L.; Giallongo,
A.: The human genome contains a single processed pseudogene for alpha
enolase located on chromosome 1. DNA Sequence 1: 79-83, 1990.
5. Feo, S.; Oliva, D.; Barbieri, G.; Xu, W.; Fried, M.; Giallongo,
A.: The gene for the muscle-specific enolase is on the short arm
of human chromosome 17. Genomics 6: 192-194, 1990.
6. Giallongo, A.; Feo, S.; Moore, R.; Croce, C. M.; Showe, L. C.:
Molecular cloning and nucleotide sequence of a full-length cDNA for
human alpha enolase. Proc. Nat. Acad. Sci. 83: 6741-6745, 1986.
7. Giallongo, A.; Oliva, D.; Cali, L.; Barba, G.; Barbieri, G.; Feo,
S.: Structure of the human gene for alpha-enolase. Europ. J. Biochem. 190:
567-573, 1990.
8. Giblett, E. R.; Chen, S.-H.; Anderson, J. E.; Lewis, M.: A family
study suggesting genetic linkage of phosphopyruvate hydratase (enolase)
to the Rh blood group system. Cytogenet. Cell Genet. 13: 91-92,
1974.
9. Goss, S. J.; Harris, H.: Gene transfer by means of cell fusion.
II. The mapping of 8 loci on human chromosome 1 by statistical analysis
of gene assortment in somatic cell hybrids. J. Cell Sci. 25: 39-57,
1977.
10. Lachant, N. A.; Jennings, M. A.; Tanaka, K. R.: Partial erythrocyte
enolase deficiency: a hereditary disorder with variable clinical expression.
(Abstract) Blood 68: 55a only, 1986.
11. Lachant, N. A.; Tanaka, K. R.: Enolase kinetic properties in
partial erythrocyte enolase deficiency. (Abstract) Clin. Res. 35:
426A only, 1987.
12. Lalley, P. A.; Francke, U.; Minna, J. D.: Homologous genes for
enolase, phosphogluconate dehydrogenase, phosphoglucomutase, and adenylate
kinase are syntenic on mouse chromosome 4 and human chromosome 1p. Proc.
Nat. Acad. Sci. 75: 2382-2386, 1978.
13. Muller, F. L.; Colla, S.; Aquilanti, E.; Manzo, V. E.; Genovese,
G.; Lee, J.; Eisenson, D.; Narurkar, R.; Deng, P.; Nezi, L.; Lee,
M. A.; Hu, B.; and 10 others: Passenger deletions generate therapeutic
vulnerabilities in cancer. Nature 488: 337-342, 2012.
14. Ochi, H.; Horiuchi, I.; Araki, N.; Toda, T.; Araki, T.; Sato,
K.; Murai, H.; Osoegawa, M.; Yamada, T.; Okamura, K.; Ogino, T.; Mizumoto,
K.; Yamashita, H.; Saya, H.; Kira, J.: Proteomic analysis of human
brain identifies alpha-enolase as a novel autoantigen in Hashimoto's
encephalopathy. FEBS Lett. 528: 197-202, 2002.
15. Ohno, S.: Ancient linkage groups and frozen accidents. Nature 244:
259-262, 1973.
16. Ribaudo, M. R.; Di Leonardo, A.; Rubino, P.; Giallongo, A.; Feo,
S.: Assignment of enolase processed pseudogene (ENO1P) to human chromosome
1 bands 1q41-q42. Cytogenet. Cell Genet. 74: 201-202, 1996.
17. Van Cong, N.; Weil, D.; Rebourcet, R.; Frezal, J.: Localisation
des enolases 1 et 2 respectivement sur les chromosomes 1 et 12 par
l'analyse des hybrids homme-souris. Ann. Genet. 20: 153-157, 1977.
18. Wistow, G. J.; Lietman, T.; Williams, L. A.; Stapel, S. O.; de
Jong, W. W.; Horwitz, J.; Piatigorsky, J.: Tau-crystallin/alpha-enolase:
one gene encodes both an enzyme and a lens structural protein. J.
Cell Biol. 107: 2729-2736, 1988.
*FIELD* CN
Ada Hamosh - updated: 9/12/2012
Victor A. McKusick - updated: 2/24/2003
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
alopez: 09/13/2012
terry: 9/12/2012
carol: 8/28/2012
carol: 2/26/2009
carol: 3/3/2003
tkritzer: 2/25/2003
terry: 2/24/2003
carol: 1/13/1999
carol: 8/27/1998
dkim: 7/21/1998
alopez: 4/13/1998
terry: 1/13/1997
mimadm: 1/14/1995
carol: 4/21/1994
carol: 11/10/1993
supermim: 3/16/1992
carol: 1/22/1991
supermim: 3/20/1990
*RECORD*
*FIELD* NO
172430
*FIELD* TI
*172430 ENOLASE 1; ENO1
;;ENOLASE, ALPHA;;
PHOSPHOPYRUVATE HYDRATASE; PPH
CRYSTALLIN, TAU, INCLUDED;;
read moreENOLASE, NONNEURONAL, INCLUDED; NNE, INCLUDED
*FIELD* TX
DESCRIPTION
Enolase is a glycolytic enzyme (2-phospho-D-glycerate hydrolyase; EC
4.2.1.11). Each of the 3 ENO isoenzymes is a homodimer composed of 2
alpha (ENO1), 2 gamma (ENO2; 131360), or 2 beta (ENO3; 131370) subunits.
Isoenzyme alpha (ENO1) is present in most tissues, whereas the beta form
(ENO3) is localized to muscle and the gamma form (ENO2) is found only in
nervous tissue (summary by Giallongo et al., 1986).
CLONING
Giallongo et al. (1986) cloned and sequenced a full-length cDNA for
human alpha-enolase. Its coding region was found to be 1,299 bases long.
The 433-amino acid protein shows 67% homology to yeast enolase and 94%
homology to rat nonneural enolase.
Wistow et al. (1988) presented evidence for the remarkable conclusion
that alpha-enolase is encoded by the same gene that encodes
tau-crystallin, a lens structural protein.
GENE STRUCTURE
Giallongo et al. (1990) determined that the ENO1 gene contains 12 exons.
MAPPING
Giblett et al. (1974) observed an electrophoretic variant of red cell
PPH among Cree Indians. Linkage was found with the Rhesus locus. Since
the Rh locus has been assigned to chromosome 1 and since cell
hybridization studies assign the PPH locus to chromosome 1, the new data
are consistent. The Goss-Harris method of mapping combines features of
recombinational study in families and synteny tests in hybrid cells. As
applied to chromosome 1, the method shows that AK2 and UMPK are distal
to PGM1 and that the order of the loci is PGM1: UMPK: (AK2, alpha-FUC):
ENO1 (Goss and Harris, 1977). Comings (1972) and Ohno (1973) suggested
that during vertebrate evolution tetraploidization occurred 2-3 hundred
million years ago and that chromosomal events that tend to preserve
ancestral linkage groups, such as Robertsonian fusions, inversions and
gene duplications, have been favored. Demonstration of linkage of
homologous genes supports this hypothesis.
D'Ancona et al. (1977) regionalized ENO1 to 1pter-p36.13. Lalley et al.
(1978) demonstrated synteny of enolase, PGD (172200), PGM1 (171900), and
AK2 (103020) on chromosome 4 of the mouse; they are on 1p of man.
- Pseudogene
Feo et al. (1990) concluded that there is a single alpha-enolase
pseudogene in the human genome. This intronless, processed pseudogene
was mapped to chromosome 1 by Southern blot analysis of rodent-human
hybrid cell DNAs; thus, it is on the same chromosome as the functional
gene. Ribaudo et al. (1996) confirmed the assignment of ENO1P to
chromosome 1. By fluorescence in situ hybridization, they found that it
is located on 1q41-q42, whereas the functional gene is located on the
short arm of that chromosome.
GENE FUNCTION
Lachant et al. (1986) and Lachant and Tanaka (1987) reported 4
generations of a Caucasian family with hereditary red cell enolase
deficiency. Partial deficiency in this kindred behaved as an autosomal
dominant and was associated with a spherocytic phenotype, although a
normal acidified glycerol lysis test suggested that the spherocytes of
enolase deficiency are different from those of hereditary spherocytosis
(see 182900). Clinical expression of enolase deficiency varied in this
family. Some had slightly low hematocrit with elevated reticulocytes,
while others had no evidence of anemia or hemolysis.
To identify the autoantigens related to Hashimoto encephalopathy, a rare
autoimmune disease associated with Hashimoto thyroiditis (140300), Ochi
et al. (2002) developed a human brain proteome map using 2-dimensional
electrophoresis and applied it to the immunoscreening of brain proteins
that react with autoantibodies in affected patients. They thereby
identified alpha-enolase as the autoantigen in that disorder.
MOLECULAR GENETICS
Muller et al. (2012) proposed that homozygous deletions in passenger
genes in cancer deletions can expose cancer-specific therapeutic
vulnerabilities when the collaterally deleted gene is a member of a
functionally redundant family of genes carrying out an essential
function. The glycolytic gene ENO1 in the 1p36 locus is deleted in
glioblastoma, which is tolerated by the expression of ENO2 (131360).
Muller et al. (2012) showed that short hairpin RNA-mediated silencing of
ENO2 selectively inhibits growth, survival, and the tumorigenic
potential of ENO1-deleted GBM cells, and that the enolase inhibitor
phosphonoacetohydroxamate is selectively toxic to ENO1-deleted GBM cells
relative to ENO1-intact GBM cells or normal astrocytes. Muller et al.
(2012) suggested that the principle of collateral vulnerability should
be applicable to other passenger-deleted genes encoding functionally
redundant essential activities and provide an effective treatment
strategy for cancers containing such genomic events.
*FIELD* SA
D'Ancona and Croce (1977); Feo et al. (1990); Van Cong et al. (1977)
*FIELD* RF
1. Comings, D. E.: Evidence for ancient tetraploidy and conservation
of linkage groups in mammalian chromosomes. Nature 238: 455-457,
1972.
2. D'Ancona, G. G.; Chern, C. J.; Benn, P.; Croce, C. M.: Assignment
of the human gene for enolase 1 to region pter-p36 of chromosome 1. Cytogenet.
Cell Genet. 18: 327-332, 1977.
3. D'Ancona, G. G.; Croce, C. M.: Assignment of the gene for enolase
to mouse chromosome 4 using somatic cell hybrids. Cytogenet. Cell
Genet. 19: 1-6, 1977.
4. Feo, S.; Oliva, D.; Arico, B.; Barba, G.; Cali, L.; Giallongo,
A.: The human genome contains a single processed pseudogene for alpha
enolase located on chromosome 1. DNA Sequence 1: 79-83, 1990.
5. Feo, S.; Oliva, D.; Barbieri, G.; Xu, W.; Fried, M.; Giallongo,
A.: The gene for the muscle-specific enolase is on the short arm
of human chromosome 17. Genomics 6: 192-194, 1990.
6. Giallongo, A.; Feo, S.; Moore, R.; Croce, C. M.; Showe, L. C.:
Molecular cloning and nucleotide sequence of a full-length cDNA for
human alpha enolase. Proc. Nat. Acad. Sci. 83: 6741-6745, 1986.
7. Giallongo, A.; Oliva, D.; Cali, L.; Barba, G.; Barbieri, G.; Feo,
S.: Structure of the human gene for alpha-enolase. Europ. J. Biochem. 190:
567-573, 1990.
8. Giblett, E. R.; Chen, S.-H.; Anderson, J. E.; Lewis, M.: A family
study suggesting genetic linkage of phosphopyruvate hydratase (enolase)
to the Rh blood group system. Cytogenet. Cell Genet. 13: 91-92,
1974.
9. Goss, S. J.; Harris, H.: Gene transfer by means of cell fusion.
II. The mapping of 8 loci on human chromosome 1 by statistical analysis
of gene assortment in somatic cell hybrids. J. Cell Sci. 25: 39-57,
1977.
10. Lachant, N. A.; Jennings, M. A.; Tanaka, K. R.: Partial erythrocyte
enolase deficiency: a hereditary disorder with variable clinical expression.
(Abstract) Blood 68: 55a only, 1986.
11. Lachant, N. A.; Tanaka, K. R.: Enolase kinetic properties in
partial erythrocyte enolase deficiency. (Abstract) Clin. Res. 35:
426A only, 1987.
12. Lalley, P. A.; Francke, U.; Minna, J. D.: Homologous genes for
enolase, phosphogluconate dehydrogenase, phosphoglucomutase, and adenylate
kinase are syntenic on mouse chromosome 4 and human chromosome 1p. Proc.
Nat. Acad. Sci. 75: 2382-2386, 1978.
13. Muller, F. L.; Colla, S.; Aquilanti, E.; Manzo, V. E.; Genovese,
G.; Lee, J.; Eisenson, D.; Narurkar, R.; Deng, P.; Nezi, L.; Lee,
M. A.; Hu, B.; and 10 others: Passenger deletions generate therapeutic
vulnerabilities in cancer. Nature 488: 337-342, 2012.
14. Ochi, H.; Horiuchi, I.; Araki, N.; Toda, T.; Araki, T.; Sato,
K.; Murai, H.; Osoegawa, M.; Yamada, T.; Okamura, K.; Ogino, T.; Mizumoto,
K.; Yamashita, H.; Saya, H.; Kira, J.: Proteomic analysis of human
brain identifies alpha-enolase as a novel autoantigen in Hashimoto's
encephalopathy. FEBS Lett. 528: 197-202, 2002.
15. Ohno, S.: Ancient linkage groups and frozen accidents. Nature 244:
259-262, 1973.
16. Ribaudo, M. R.; Di Leonardo, A.; Rubino, P.; Giallongo, A.; Feo,
S.: Assignment of enolase processed pseudogene (ENO1P) to human chromosome
1 bands 1q41-q42. Cytogenet. Cell Genet. 74: 201-202, 1996.
17. Van Cong, N.; Weil, D.; Rebourcet, R.; Frezal, J.: Localisation
des enolases 1 et 2 respectivement sur les chromosomes 1 et 12 par
l'analyse des hybrids homme-souris. Ann. Genet. 20: 153-157, 1977.
18. Wistow, G. J.; Lietman, T.; Williams, L. A.; Stapel, S. O.; de
Jong, W. W.; Horwitz, J.; Piatigorsky, J.: Tau-crystallin/alpha-enolase:
one gene encodes both an enzyme and a lens structural protein. J.
Cell Biol. 107: 2729-2736, 1988.
*FIELD* CN
Ada Hamosh - updated: 9/12/2012
Victor A. McKusick - updated: 2/24/2003
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
alopez: 09/13/2012
terry: 9/12/2012
carol: 8/28/2012
carol: 2/26/2009
carol: 3/3/2003
tkritzer: 2/25/2003
terry: 2/24/2003
carol: 1/13/1999
carol: 8/27/1998
dkim: 7/21/1998
alopez: 4/13/1998
terry: 1/13/1997
mimadm: 1/14/1995
carol: 4/21/1994
carol: 11/10/1993
supermim: 3/16/1992
carol: 1/22/1991
supermim: 3/20/1990