MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Alpha-enolase; EC=4.2.1.11; AltName: Full=2-phospho-D-glycerate hydro-lyase; AltName: Full=C-myc promoter-binding protein; AltName: Full=Enolase 1; AltName: Full=MBP-1; AltName: Full=MPB-1; AltName: Full=Non-neural enolase; Short=NNE; AltName: Full=Phosphopyruvate hydratase; AltName: Full=Plasminogen-binding protein; |
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| MyHits synonyms | ENOA_HUMAN , P06733 , B2RD59 , P22712 , Q16704 , Q4TUS4 , Q53FT9 , Q53HR3 , Q658M5 , Q6GMP2 , Q71V37 , Q7Z3V6 , Q8WU71 , Q96GV1 , Q9BT62 , Q9UCH6 , Q9UM55 , A0ED663FCC15ADA5 |
 Legends: 1, INIT_MET Removed. {ECO:0000244|PubMed:25944712, ECO:0000269|Ref.14}; 2, ACT_SITE Proton donor. {ECO:0000250}; 3, ACT_SITE Proton acceptor. {ECO:0000250}; 4, BINDING Substrate. {ECO:0000250}; 5, N-acetylserine. {ECO:0000244|PubMed:25944712, ECO:0000269|Ref.14}; 6, N6-acetyllysine. {ECO:0000244|PubMed:19608861}; 7, Phosphoserine. {ECO:0000244|PubMed:23186163}; 8, Phosphotyrosine. {ECO:0000244|PubMed:15592455}; 9, N6-acetyllysine; alternate. {ECO:0000250|UniProtKB:P17182}; 10, N6-succinyllysine; alternate. {ECO:0000250|UniProtKB:P17182}; 11, N6-acetyllysine; alternate. {ECO:0000244|PubMed:19608861}; 12, N6-acetyllysine. {ECO:0000250|UniProtKB:P17182}; 13, N6-malonyllysine; alternate. {ECO:0000269|PubMed:21908771}; 14, Phosphoserine. {ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:23186163}; 15, Phosphoserine. {ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569}; 16, Phosphoserine. {ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:23186163}; 17, Phosphoserine. {ECO:0000244|PubMed:24275569}; 18, VARIANT N -> K (in dbSNP:rs11544513). {ECO:0000269|Ref.9}; 19, VARIANT P -> Q (in dbSNP:rs11544514); 20, MUTAGEN M->I: MBP1 protein production. No MBP1 protein production; when associated with I-97. {ECO:0000269|PubMed:10681589}; 21, MUTAGEN M->I: MBP1 protein production. No MBP1 protein production; when associated with I-94. {ECO:0000269|PubMed:10681589}; 22, MUTAGEN L->A: Loss of transcriptional repression and cell growth inhibition; when associated with A-388. {ECO:0000269|PubMed:10082554}; 23, MUTAGEN L->A: Loss of transcriptional repression and cell growth inhibition; when associated with A-384. {ECO:0000269|PubMed:10082554}; 24, CONFLICT T -> A (in Ref. 8; CAD97642). {ECO:0000305}; 25, CONFLICT V -> A (in Ref. 7; BAD96237). {ECO:0000305}; 26, CONFLICT E -> G (in Ref. 8; CAD97642). {ECO:0000305}; 27, CONFLICT K -> R (in Ref. 7; BAD96912). {ECO:0000305}; 28, CONFLICT F -> S (in Ref. 4; CAA59331). {ECO:0000305}; 29, CONFLICT S -> I (in Ref. 8; CAD97642). {ECO:0000305}; 30, REGION Epitope recognized by CAR and healthy patient antibodies; 31, REGION Epitope recognized by CAR antibodies; 32, REGION Required for repression of c-myc promoter activity; 33, REGION Substrate binding. {ECO:0000250}; 34, REGION Required for interaction with PLG. {ECO:0000250}; 35, VAR_SEQ Missing (in isoform MBP-1). {ECO:0000303|PubMed:2005901}; 36, ipat:ENOLASE [T]; 37, STRAND {ECO:0000244|PDB:2PSN}; 38, HELIX {ECO:0000244|PDB:2PSN}; 39, TURN {ECO:0000244|PDB:2PSN}.
| |
ID ENOA_HUMAN Reviewed; 434 AA.
AC P06733; B2RD59; P22712; Q16704; Q4TUS4; Q53FT9; Q53HR3; Q658M5;
AC Q6GMP2; Q71V37; Q7Z3V6; Q8WU71; Q96GV1; Q9BT62; Q9UCH6; Q9UM55;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 30-NOV-2016, entry version 208.
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; DOI=10.1128/MCB.11.4.2154;
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 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;
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; 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
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 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
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
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
RT 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
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 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
RP BY 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
RP AND LYS-420, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
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).
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.,
RA Fischer-Posovszky P., Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion
RT 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
RP 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.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver 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
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA Ayoub D., 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 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
RT glycolytic enzyme.";
RL Acta Crystallogr. D 64:651-657(2008).
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. {ECO:0000269|PubMed:1369209}.
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.
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 (PubMed:18560153).
CC ENO1 interacts with PLG in the neuronal plasma membrane and
CC promotes its activation. The C-terminal lysine is required for
CC this binding (PubMed:9308760). Isoform MBP-1 interacts with
CC TRAPPC2B (PubMed:11134351). Interacts with ENO4 and PGAM2 (By
CC similarity). {ECO:0000250|UniProtKB:P17182,
CC ECO:0000269|PubMed:11134351, ECO:0000269|PubMed:18560153,
CC ECO:0000269|PubMed:9308760}.
CC -!- INTERACTION:
CC P22303:ACHE; NbExp=2; IntAct=EBI-353877, EBI-1637793;
CC Q60823:Akt2 (xeno); NbExp=2; IntAct=EBI-353877, EBI-400263;
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 {ECO:0000269|PubMed:10802057}.
CC Cell membrane {ECO:0000269|PubMed:10802057}. Cytoplasm, myofibril,
CC sarcomere, M line {ECO:0000269|PubMed:10802057}. Note=Can
CC translocate to the plasma membrane in either the homodimeric
CC (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is
CC 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 {ECO:0000269|PubMed:16548883, ECO:0000269|PubMed:7787969}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798,
CC ECO:0000269|PubMed:16815975}.
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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35698.1; Type=Frameshift; Positions=Several; 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
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ENO1ID40453ch1p36.html";
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 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; -.
DR BioGrid; 108338; 284.
DR IntAct; P06733; 83.
DR MINT; MINT-155303; -.
DR STRING; 9606.ENSP00000234590; -.
DR ChEMBL; CHEMBL3298; -.
DR iPTMnet; 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 EPD; P06733; -.
DR MaxQB; P06733; -.
DR PaxDb; P06733; -.
DR PeptideAtlas; P06733; -.
DR PRIDE; P06733; -.
DR TopDownProteomics; P06733-1; -. [P06733-1]
DR TopDownProteomics; P06733-2; -. [P06733-2]
DR DNASU; 2023; -.
DR Ensembl; ENST00000234590; ENSP00000234590; ENSG00000074800. [P06733-1]
DR GeneID; 2023; -.
DR KEGG; hsa:2023; -.
DR UCSC; uc001apj.3; human. [P06733-1]
DR CTD; 2023; -.
DR DisGeNET; 2023; -.
DR GeneCards; ENO1; -.
DR HGNC; HGNC:3350; ENO1.
DR HPA; CAB018614; -.
DR HPA; CAB069394; -.
DR MIM; 172430; gene.
DR neXtProt; NX_P06733; -.
DR OpenTargets; ENSG00000074800; -.
DR PharmGKB; PA27786; -.
DR eggNOG; KOG2670; Eukaryota.
DR eggNOG; COG0148; LUCA.
DR GeneTree; ENSGT00840000129817; -.
DR HOVERGEN; HBG000067; -.
DR InParanoid; P06733; -.
DR KO; K01689; -.
DR OMA; NFRNPRI; -.
DR OrthoDB; EOG091G07NH; -.
DR PhylomeDB; P06733; -.
DR TreeFam; TF300391; -.
DR BioCyc; MetaCyc:ENSG00000074800-MONOMER; -.
DR BioCyc; ZFISH:ENSG00000074800-MONOMER; -.
DR BRENDA; 4.2.1.11; 2681.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SABIO-RK; P06733; -.
DR SIGNOR; P06733; -.
DR UniPathway; UPA00109; UER00187.
DR ChiTaRS; ENO1; human.
DR EvolutionaryTrace; P06733; -.
DR GeneWiki; Alpha-enolase; -.
DR GenomeRNAi; 2023; -.
DR PMAP-CutDB; P06733; -.
DR PRO; PR:P06733; -.
DR Proteomes; UP000005640; Chromosome 1.
DR Bgee; ENSG00000074800; -.
DR ExpressionAtlas; P06733; baseline and differential.
DR Genevisible; P06733; HS.
DR GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; TAS:Reactome.
DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR GO; GO:0061621; P:canonical glycolysis; TAS:Reactome.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; IPR020810; Enolase_C.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR020809; Enolase_CS.
DR InterPro; IPR020811; Enolase_N.
DR InterPro; IPR029017; Enolase_N-like.
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 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 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. {ECO:0000244|PubMed:25944712,
FT ECO:0000269|Ref.14}.
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. {ECO:0000250}.
FT REGION 405 434 Required for interaction with PLG.
FT {ECO:0000250}.
FT ACT_SITE 210 210 Proton donor. {ECO:0000250}.
FT ACT_SITE 343 343 Proton acceptor. {ECO:0000250}.
FT METAL 40 40 Magnesium 1.
FT METAL 245 245 Magnesium 2.
FT METAL 293 293 Magnesium 2.
FT METAL 318 318 Magnesium 2.
FT BINDING 158 158 Substrate. {ECO:0000250}.
FT BINDING 167 167 Substrate. {ECO:0000250}.
FT BINDING 293 293 Substrate. {ECO:0000250}.
FT BINDING 318 318 Substrate. {ECO:0000250}.
FT BINDING 394 394 Substrate. {ECO:0000250}.
FT MOD_RES 2 2 N-acetylserine.
FT {ECO:0000244|PubMed:25944712,
FT ECO:0000269|Ref.14}.
FT MOD_RES 5 5 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 27 27 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 44 44 Phosphotyrosine.
FT {ECO:0000244|PubMed:15592455}.
FT MOD_RES 60 60 N6-acetyllysine; alternate.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 60 60 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 64 64 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 71 71 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 89 89 N6-acetyllysine; alternate.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 89 89 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 92 92 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 126 126 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 193 193 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 199 199 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 202 202 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 228 228 N6-acetyllysine; alternate.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 228 228 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 233 233 N6-acetyllysine; alternate.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 233 233 N6-malonyllysine; alternate.
FT {ECO:0000269|PubMed:21908771}.
FT MOD_RES 254 254 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 256 256 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 263 263 Phosphoserine.
FT {ECO:0000244|PubMed:18669648,
FT ECO:0000244|PubMed:23186163,
FT ECO:0000244|PubMed:24275569}.
FT MOD_RES 272 272 Phosphoserine.
FT {ECO:0000244|PubMed:19690332,
FT ECO:0000244|PubMed:23186163}.
FT MOD_RES 281 281 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 285 285 N6-acetyllysine.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 287 287 Phosphotyrosine.
FT {ECO:0000244|PubMed:15592455}.
FT MOD_RES 291 291 Phosphoserine.
FT {ECO:0000244|PubMed:24275569}.
FT MOD_RES 335 335 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 343 343 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 406 406 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P17182}.
FT MOD_RES 420 420 N6-acetyllysine; alternate.
FT {ECO:0000244|PubMed:19608861}.
FT MOD_RES 420 420 N6-malonyllysine; alternate.
FT {ECO:0000269|PubMed:21908771}.
FT MOD_RES 420 420 N6-succinyllysine; alternate.
FT {ECO:0000250|UniProtKB:P17182}.
FT VAR_SEQ 1 93 Missing (in isoform MBP-1).
FT {ECO:0000303|PubMed:2005901}.
FT /FTId=VSP_018725.
FT VARIANT 177 177 N -> K (in dbSNP:rs11544513).
FT {ECO:0000269|Ref.9}.
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. {ECO:0000269|PubMed:10681589}.
FT MUTAGEN 97 97 M->I: MBP1 protein production. No MBP1
FT protein production; when associated with
FT I-94. {ECO:0000269|PubMed:10681589}.
FT MUTAGEN 384 384 L->A: Loss of transcriptional repression
FT and cell growth inhibition; when
FT associated with A-388.
FT {ECO:0000269|PubMed:10082554}.
FT MUTAGEN 388 388 L->A: Loss of transcriptional repression
FT and cell growth inhibition; when
FT associated with A-384.
FT {ECO:0000269|PubMed:10082554}.
FT CONFLICT 55 55 T -> A (in Ref. 8; CAD97642).
FT {ECO:0000305}.
FT CONFLICT 78 78 V -> A (in Ref. 7; BAD96237).
FT {ECO:0000305}.
FT CONFLICT 187 187 E -> G (in Ref. 8; CAD97642).
FT {ECO:0000305}.
FT CONFLICT 199 199 K -> R (in Ref. 7; BAD96912).
FT {ECO:0000305}.
FT CONFLICT 252 252 F -> S (in Ref. 4; CAA59331).
FT {ECO:0000305}.
FT CONFLICT 310 310 S -> I (in Ref. 8; CAD97642).
FT {ECO:0000305}.
FT STRAND 5 12 {ECO:0000244|PDB:2PSN}.
FT STRAND 18 26 {ECO:0000244|PDB:2PSN}.
FT STRAND 29 34 {ECO:0000244|PDB:2PSN}.
FT HELIX 57 59 {ECO:0000244|PDB:2PSN}.
FT HELIX 63 71 {ECO:0000244|PDB:2PSN}.
FT HELIX 73 79 {ECO:0000244|PDB:2PSN}.
FT HELIX 87 98 {ECO:0000244|PDB:2PSN}.
FT TURN 104 106 {ECO:0000244|PDB:2PSN}.
FT HELIX 108 125 {ECO:0000244|PDB:2PSN}.
FT HELIX 130 138 {ECO:0000244|PDB:2PSN}.
FT STRAND 147 154 {ECO:0000244|PDB:2PSN}.
FT HELIX 156 158 {ECO:0000244|PDB:2PSN}.
FT STRAND 159 162 {ECO:0000244|PDB:2PSN}.
FT STRAND 167 171 {ECO:0000244|PDB:2PSN}.
FT HELIX 178 200 {ECO:0000244|PDB:2PSN}.
FT HELIX 202 204 {ECO:0000244|PDB:2PSN}.
FT HELIX 220 233 {ECO:0000244|PDB:2PSN}.
FT TURN 237 239 {ECO:0000244|PDB:2PSN}.
FT STRAND 241 245 {ECO:0000244|PDB:2PSN}.
FT HELIX 248 250 {ECO:0000244|PDB:2PSN}.
FT TURN 259 262 {ECO:0000244|PDB:2PSN}.
FT HELIX 267 269 {ECO:0000244|PDB:2PSN}.
FT HELIX 273 286 {ECO:0000244|PDB:2PSN}.
FT STRAND 289 293 {ECO:0000244|PDB:2PSN}.
FT HELIX 301 311 {ECO:0000244|PDB:2PSN}.
FT STRAND 313 318 {ECO:0000244|PDB:2PSN}.
FT TURN 319 323 {ECO:0000244|PDB:2PSN}.
FT HELIX 325 334 {ECO:0000244|PDB:2PSN}.
FT STRAND 338 342 {ECO:0000244|PDB:2PSN}.
FT HELIX 344 347 {ECO:0000244|PDB:2PSN}.
FT HELIX 350 362 {ECO:0000244|PDB:2PSN}.
FT STRAND 366 370 {ECO:0000244|PDB:2PSN}.
FT HELIX 380 387 {ECO:0000244|PDB:2PSN}.
FT STRAND 391 394 {ECO:0000244|PDB:2PSN}.
FT HELIX 401 417 {ECO:0000244|PDB:2PSN}.
FT HELIX 418 420 {ECO:0000244|PDB:2PSN}.
FT HELIX 425 427 {ECO:0000244|PDB:2PSN}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 1 417 ihamap:Enolase [T]
FT MYHIT 3 134 ismart:Enolase_N [T]
FT MYHIT 340 353 ipat:ENOLASE [T]
FT MYHIT 143 430 ipfam:Enolase_C [T]
FT MYHIT 3 134 ipfam:Enolase_N [T]
FT MYHIT 142 431 ismart:Enolase_C [T]
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
//
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