ENOA_HUMAN
ID ENOA_HUMAN Reviewed; 434 AA.
AC P06733; B2RD59; P22712; Q16704; Q4TUS4; Q53FT9; Q53HR3; Q658M5; Q6GMP2;
AC Q71V37; Q7Z3V6; Q8WU71; Q96GV1; Q9BT62; Q9UCH6; Q9UM55;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 253.
DE RecName: Full=Alpha-enolase;
DE EC=4.2.1.11 {ECO:0000269|PubMed:1369209, ECO:0000269|PubMed:29775581};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 human
RT 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; DOI=10.1128/mcb.11.4.2154-2161.1991;
RA Ray R., Miller D.M.;
RT "Cloning and characterization of a human c-myc promoter-binding 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 recognition
RT 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 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., 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 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 AND
RP 407-420, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
RP IDENTIFICATION BY 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 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 [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; DOI=10.1101/gr.7.4.353;
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,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
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 stimulating
RT 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 LARGE
RP CELL LYMPHOMA.
RX PubMed=7787969; DOI=10.1159/000474967;
RA Mohamad R.M., Hamdan M.Y., Maki A., Al-Katib A.;
RT "Induced expression of alpha-enolase in differentiated diffuse large cell
RT lymphoma.";
RL Enzyme Protein 48:37-44(1994).
RN [20]
RP FUNCTION OF MBP1, IDENTIFICATION OF REPRESSOR DOMAINS, AND MUTAGENESIS OF
RP LEU-384 AND LEU-388.
RX PubMed=10082554; DOI=10.1128/mcb.19.4.2880;
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 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 protein 1
RT (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 monoclonal
RT 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 plasminogen
RT 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 PRODUCT,
RP 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 WITH TRAPPC2B (ISOFORM MBP-1).
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 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., Yamashita H.,
RA 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
RP IDENTIFICATION BY 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 [31]
RP INDUCTION, AND IDENTIFICATION BY 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 reveal
RT differential cellular gene expression in response to enterovirus 71
RT 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 type I
RT 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 LYS-5; LYS-64; LYS-71; LYS-89;
RP LYS-126; LYS-193; LYS-199; LYS-228; LYS-233; LYS-256; LYS-281; LYS-285 AND
RP LYS-420, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., 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 [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., He W.,
RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA 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).
RN [39]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [40]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-254; SER-263 AND
RP SER-272, AND IDENTIFICATION BY 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 [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-291, AND
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 [42]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [43]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [44]
RP INTERACTION WITH CMTM6, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28813417; DOI=10.1038/nature23643;
RA Burr M.L., Sparbier C.E., Chan Y.C., Williamson J.C., Woods K.,
RA Beavis P.A., Lam E.Y.N., Henderson M.A., Bell C.C., Stolzenburg S.,
RA Gilan O., Bloor S., Noori T., Morgens D.W., Bassik M.C., Neeson P.J.,
RA Behren A., Darcy P.K., Dawson S.J., Voskoboinik I., Trapani J.A., Cebon J.,
RA Lehner P.J., Dawson M.A.;
RT "CMTM6 maintains the expression of PD-L1 and regulates anti-tumour
RT immunity.";
RL Nature 549:101-105(2017).
RN [45]
RP FUNCTION, CATALYTIC ACTIVITY, HYDROXYBUTYRYLATION AT LYS-228 AND LYS-281,
RP AND MUTAGENESIS OF LYS-281.
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 [46]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-434, SUBUNIT, COFACTOR, AND
RP METAL-BINDING SITES.
RX PubMed=18560153; DOI=10.1107/s0907444908008561;
RA Kang H.J., Jung S.K., Kim S.J., Chung S.J.;
RT "Structure of human alpha-enolase (hENO1), a multifunctional glycolytic
RT enzyme.";
RL Acta Crystallogr. D 64:651-657(2008).
CC -!- FUNCTION: Glycolytic enzyme the catalyzes the conversion of 2-
CC phosphoglycerate to phosphoenolpyruvate (PubMed:29775581,
CC PubMed:1369209). In addition to glycolysis, involved in various
CC processes such as growth control, hypoxia tolerance and allergic
CC responses (PubMed:2005901, PubMed:10802057, PubMed:12666133,
CC PubMed:29775581). May also function in the intravascular and
CC pericellular fibrinolytic system due to its ability to serve as a
CC receptor and activator of plasminogen on the cell surface of several
CC cell-types such as leukocytes and neurons (PubMed:12666133). Stimulates
CC immunoglobulin production (PubMed:1369209).
CC {ECO:0000269|PubMed:10802057, ECO:0000269|PubMed:12666133,
CC ECO:0000269|PubMed:1369209, ECO:0000269|PubMed:2005901,
CC ECO:0000269|PubMed:29775581}.
CC -!- FUNCTION: MBP1 binds to the myc promoter and acts as a transcriptional
CC repressor. May be a tumor suppressor. {ECO:0000269|PubMed:10082554}.
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; Evidence={ECO:0000269|PubMed:1369209,
CC ECO:0000269|PubMed:29775581};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18560153};
CC Note=Binds two Mg(2+) per subunit. Required for catalysis and for
CC stabilizing the dimer. {ECO:0000269|PubMed:18560153};
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 {ECO:0000269|PubMed:1369209};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000305|PubMed:1369209}.
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 (PubMed:18560153). ENO1 interacts
CC with PLG in the neuronal plasma membrane and promotes its activation.
CC The C-terminal lysine is required for this binding (PubMed:9308760).
CC Isoform MBP-1 interacts with TRAPPC2B (PubMed:11134351). Interacts with
CC ENO4 and PGAM2 (By similarity). Interacts with CMTM6 (PubMed:28813417).
CC {ECO:0000250|UniProtKB:P17182, ECO:0000269|PubMed:11134351,
CC ECO:0000269|PubMed:18560153, ECO:0000269|PubMed:28813417,
CC ECO:0000269|PubMed:9308760}.
CC -!- INTERACTION:
CC P06733; P22303: ACHE; NbExp=2; IntAct=EBI-353877, EBI-1637793;
CC P06733; P42858: HTT; NbExp=13; IntAct=EBI-353877, EBI-466029;
CC P06733; P12004: PCNA; NbExp=3; IntAct=EBI-353877, EBI-358311;
CC P06733; Q8WZ42: TTN; NbExp=3; IntAct=EBI-353877, EBI-681210;
CC P06733; P63104: YWHAZ; NbExp=2; IntAct=EBI-353877, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10802057}. Cell
CC membrane {ECO:0000269|PubMed:10802057}. Cytoplasm, myofibril,
CC sarcomere, M line {ECO:0000269|PubMed:10802057}. Note=Can translocate
CC to the plasma membrane in either the homodimeric (alpha/alpha) or
CC heterodimeric (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 -!- 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: Induced in diffuse large cell lymphoma (DLCL) after
CC treatment with the natural biological agent, Bryo1. Up-regulated in
CC response to enterovirus 71 (EV71) infection (at protein level).
CC {ECO:0000269|PubMed:16548883, ECO:0000269|PubMed:7787969}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798,
CC ECO:0000269|PubMed:16815975}.
CC -!- PTM: Lysine 2-hydroxyisobutyrylation (Khib) by p300/EP300 activates the
CC phosphopyruvate hydratase activity. {ECO:0000269|PubMed:29775581}.
CC -!- MISCELLANEOUS: Used as a diagnostic marker for many tumors and, in the
CC heterodimeric form, alpha/gamma, as a marker for hypoxic brain injury
CC after cardiac arrest. Also marker for endometriosis. Antibodies against
CC alpha-enolase are present in sera from patients with cancer-associated
CC retinopathy syndrome (CAR), a progressive blinding disease which occurs
CC in the presence of systemic tumor growth, primarily small-cell
CC carcinoma of the lung and other malignancies. Is identified as an
CC autoantigen in Hashimoto encephalopathy (HE) a rare autoimmune disease
CC associated with Hashimoto thyroiditis (HT). HT is a disorder in which
CC destructive processes overcome the potential capacity of thyroid
CC replacement leading to hypothyroidism.
CC -!- MISCELLANEOUS: [Isoform MBP-1]: It is uncertain whether the alternative
CC initiation site is at Met-94 or at Met-97. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35698.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA35698.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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 and
CC 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; BC004325; AAH04325.1; -; mRNA.
DR EMBL; BC004458; AAH04458.1; -; mRNA.
DR EMBL; BC009218; AAH09218.2; -; 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 CCDS; CCDS97.1; -. [P06733-1]
DR PIR; A39579; A39579.
DR PIR; S11696; A29170.
DR RefSeq; NP_001188412.1; NM_001201483.1. [P06733-2]
DR RefSeq; NP_001419.1; NM_001428.3. [P06733-1]
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 PDB; 5JLZ; X-ray; 1.99 A; E/F=26-40.
DR PDB; 5LAX; X-ray; 2.60 A; E/F=26-40.
DR PDB; 5NI9; X-ray; 1.33 A; C=326-340.
DR PDB; 5NIG; X-ray; 1.35 A; C=326-340.
DR PDB; 5OCK; X-ray; 1.60 A; A=5-21.
DR PDBsum; 2PSN; -.
DR PDBsum; 3B97; -.
DR PDBsum; 5JLZ; -.
DR PDBsum; 5LAX; -.
DR PDBsum; 5NI9; -.
DR PDBsum; 5NIG; -.
DR PDBsum; 5OCK; -.
DR AlphaFoldDB; P06733; -.
DR SMR; P06733; -.
DR BioGRID; 108338; 490.
DR IntAct; P06733; 139.
DR MINT; P06733; -.
DR STRING; 9606.ENSP00000234590; -.
DR BindingDB; P06733; -.
DR ChEMBL; CHEMBL3298; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR MoonDB; P06733; Predicted.
DR MoonProt; P06733; -.
DR GlyGen; P06733; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; P06733; -.
DR MetOSite; P06733; -.
DR PhosphoSitePlus; P06733; -.
DR SwissPalm; P06733; -.
DR BioMuta; ENO1; -.
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 CPTAC; CPTAC-70; -.
DR EPD; P06733; -.
DR jPOST; P06733; -.
DR MassIVE; P06733; -.
DR MaxQB; P06733; -.
DR PaxDb; P06733; -.
DR PeptideAtlas; P06733; -.
DR PRIDE; P06733; -.
DR ProteomicsDB; 51919; -. [P06733-1]
DR ProteomicsDB; 51920; -. [P06733-2]
DR TopDownProteomics; P06733-1; -. [P06733-1]
DR TopDownProteomics; P06733-2; -. [P06733-2]
DR ABCD; P06733; 5 sequenced antibodies.
DR Antibodypedia; 4351; 847 antibodies from 43 providers.
DR DNASU; 2023; -.
DR Ensembl; ENST00000234590.10; ENSP00000234590.4; ENSG00000074800.16. [P06733-1]
DR GeneID; 2023; -.
DR KEGG; hsa:2023; -.
DR MANE-Select; ENST00000234590.10; ENSP00000234590.4; NM_001428.5; NP_001419.1.
DR UCSC; uc001apj.3; human. [P06733-1]
DR CTD; 2023; -.
DR DisGeNET; 2023; -.
DR GeneCards; ENO1; -.
DR HGNC; HGNC:3350; ENO1.
DR HPA; ENSG00000074800; Low tissue specificity.
DR MIM; 172430; gene.
DR neXtProt; NX_P06733; -.
DR OpenTargets; ENSG00000074800; -.
DR PharmGKB; PA27786; -.
DR VEuPathDB; HostDB:ENSG00000074800; -.
DR eggNOG; KOG2670; Eukaryota.
DR GeneTree; ENSGT00950000182805; -.
DR HOGENOM; CLU_031223_0_0_1; -.
DR InParanoid; P06733; -.
DR OMA; EFMIIPV; -.
DR PhylomeDB; P06733; -.
DR TreeFam; TF300391; -.
DR BioCyc; MetaCyc:ENSG00000074800-MON; -.
DR BRENDA; 4.2.1.11; 2681.
DR PathwayCommons; P06733; -.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR Reactome; R-HSA-9636667; Manipulation of host energy metabolism.
DR SABIO-RK; P06733; -.
DR SignaLink; P06733; -.
DR SIGNOR; P06733; -.
DR UniPathway; UPA00109; UER00187.
DR BioGRID-ORCS; 2023; 430 hits in 1097 CRISPR screens.
DR ChiTaRS; ENO1; human.
DR EvolutionaryTrace; P06733; -.
DR GeneWiki; Alpha-enolase; -.
DR GenomeRNAi; 2023; -.
DR Pharos; P06733; Tchem.
DR PRO; PR:P06733; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P06733; protein.
DR Bgee; ENSG00000074800; Expressed in metanephros cortex and 218 other tissues.
DR ExpressionAtlas; P06733; baseline and differential.
DR Genevisible; P06733; HS.
DR GO; GO:0005938; C:cell cortex; IDA:CAFA.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:CAFA.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR GO; GO:0061621; P:canonical glycolysis; IDA:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IDA:CAFA.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:CAFA.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IDA:CAFA.
DR GO; GO:0045933; P:positive regulation of muscle contraction; IGI:CAFA.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; IMP:CAFA.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
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 initiation; Cell membrane;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Glycolysis;
KW Hydroxylation; Isopeptide bond; Lyase; Magnesium; Membrane; Metal-binding;
KW Nucleus; Phosphoprotein; Plasminogen activation; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.14, ECO:0007744|PubMed:25944712"
FT CHAIN 2..434
FT /note="Alpha-enolase"
FT /id="PRO_0000134097"
FT REGION 31..38
FT /note="Epitope recognized by CAR and healthy patient
FT antibodies"
FT REGION 56..63
FT /note="Epitope recognized by CAR antibodies"
FT REGION 97..237
FT /note="Required for repression of c-myc promoter activity"
FT REGION 405..434
FT /note="Required for interaction with PLG"
FT /evidence="ECO:0000250"
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:0000269|PubMed:18560153"
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:0000269|PubMed:18560153"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18560153"
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:0000269|PubMed:18560153"
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:0000269|Ref.14, ECO:0007744|PubMed:25944712"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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:0007744|PubMed:19608861"
FT MOD_RES 71
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 89
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 89
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 126
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 193
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 202
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 228
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:29775581"
FT MOD_RES 228
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 228
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17182"
FT MOD_RES 233
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 233
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 281
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:29775581"
FT MOD_RES 281
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 285
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 287
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
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 MOD_RES 420
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 420
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 420
FT /note="N6-succinyllysine; alternate"
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:0007744|PubMed:28112733"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform MBP-1)"
FT /evidence="ECO:0000303|PubMed:2005901"
FT /id="VSP_018725"
FT VARIANT 177
FT /note="N -> K (in dbSNP:rs11544513)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_025172"
FT VARIANT 325
FT /note="P -> Q (in dbSNP:rs11544514)"
FT /id="VAR_048936"
FT MUTAGEN 94
FT /note="M->I: MBP1 protein production. No MBP1 protein
FT production; when associated with I-97."
FT /evidence="ECO:0000269|PubMed:10681589"
FT MUTAGEN 97
FT /note="M->I: MBP1 protein production. No MBP1 protein
FT production; when associated with I-94."
FT /evidence="ECO:0000269|PubMed:10681589"
FT MUTAGEN 281
FT /note="K->R: Decreased 2-hydroxyisobutyrylation leading to
FT decreased phosphopyruvate hydratase activity."
FT /evidence="ECO:0000269|PubMed:29775581"
FT MUTAGEN 384
FT /note="L->A: Loss of transcriptional repression and cell
FT growth inhibition; when associated with A-388."
FT /evidence="ECO:0000269|PubMed:10082554"
FT MUTAGEN 388
FT /note="L->A: Loss of transcriptional repression and cell
FT growth inhibition; when associated with A-384."
FT /evidence="ECO:0000269|PubMed:10082554"
FT CONFLICT 55
FT /note="T -> A (in Ref. 8; CAD97642)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="V -> A (in Ref. 7; BAD96237)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="E -> G (in Ref. 8; CAD97642)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="K -> R (in Ref. 7; BAD96912)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="F -> S (in Ref. 4; CAA59331)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="S -> I (in Ref. 8; CAD97642)"
FT /evidence="ECO:0000305"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:2PSN"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:2PSN"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:2PSN"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 108..125
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:2PSN"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2PSN"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2PSN"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 178..200
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:2PSN"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:2PSN"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:2PSN"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:2PSN"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:2PSN"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:2PSN"
FT TURN 319..323
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:2PSN"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 350..362
FT /evidence="ECO:0007829|PDB:2PSN"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 380..387
FT /evidence="ECO:0007829|PDB:2PSN"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 401..417
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:2PSN"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:2PSN"
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
