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Alpha-enolase (EC 4 2 1 11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)

 ENOA_MOUSE              Reviewed;         434 AA.
P17182; Q99KT7; Q9DCY7;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
26-FEB-2020, entry version 209.
RecName: Full=Alpha-enolase;
EC=4.2.1.11;
AltName: Full=2-phospho-D-glycerate hydro-lyase;
AltName: Full=Enolase 1;
AltName: Full=Non-neural enolase;
Short=NNE;
Name=Eno1; Synonyms=Eno-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=2362815; DOI=10.1093/nar/18.12.3638;
Kaghad M., Dumont X., Chalon P., Lelias J.M., Lamande N., Lucas M.,
Lazar M., Caput D.;
"Nucleotide sequences of cDNAs alpha and gamma enolase mRNAs from mouse
brain.";
Nucleic Acids Res. 18:3638-3638(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 10-28; 33-50; 61-120; 133-179; 184-193; 203-228;
234-253; 257-262; 270-281; 307-326; 344-358; 373-394 AND 413-420, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 60-71; 100-114; 184-198 AND 246-259.
TISSUE=Macrophage;
PubMed=8427861; DOI=10.1161/01.atv.13.2.264;
Bottalico L.A., Kendrick N.C., Keller A., Li Y., Tabas I.;
"Cholesteryl ester loading of mouse peritoneal macrophages is associated
with changes in the expression or modification of specific cellular
proteins, including increase in an alpha-enolase isoform.";
Arterioscler. Thromb. 13:264-275(1993).
[6]
INTERACTION WITH PKM; PGM; CKM; ALDO AND TROPONIN, AND DEVELOPMENTAL STAGE.
PubMed=9169614; DOI=10.1042/bj3230791;
Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F.,
Lazar M., Keller A.;
"Biochemical characterization of the mouse muscle-specific enolase:
developmental changes in electrophoretic variants and selective binding to
other proteins.";
Biochem. J. 323:791-800(1997).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11229603; DOI=10.1016/s0248-4900(00)01103-5;
Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C.,
Lucas M., Chatelet F.-P.;
"Fibre-type distribution and subcellular localisation of alpha and beta
enolase in mouse striated muscle.";
Biol. Cell 92:527-535(2000).
[8]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[11]
INTERACTION WITH ENO4 AND PGAM2, AND TISSUE SPECIFICITY.
PubMed=23446454; DOI=10.1095/biolreprod.112.107128;
Nakamura N., Dai Q., Williams J., Goulding E.H., Willis W.D., Brown P.R.,
Eddy E.M.;
"Disruption of a spermatogenic cell-specific mouse enolase 4 (eno4) gene
causes sperm structural defects and male infertility.";
Biol. Reprod. 88:90-90(2013).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-89; LYS-92; LYS-126;
LYS-193; LYS-202; LYS-228; LYS-256; LYS-335; LYS-343 AND LYS-406,
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-89; LYS-228 AND
LYS-420, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Glycolytic enzyme the catalyzes the conversion of 2-
phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis,
involved in various processes such as growth control, hypoxia tolerance
and allergic responses. May also function in the intravascular and
pericellular fibrinolytic system due to its ability to serve as a
receptor and activator of plasminogen on the cell surface of several
cell-types such as leukocytes and neurons. Stimulates immunoglobulin
production. {ECO:0000250|UniProtKB:P06733}.
-!- CATALYTIC ACTIVITY:
Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
ChEBI:CHEBI:58702; EC=4.2.1.11;
Evidence={ECO:0000250|UniProtKB:P06733};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P06733};
Note=Binds two Mg(2+) per subunit. Required for catalysis and for
stabilizing the dimer. {ECO:0000250|UniProtKB:P06733};
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 4/5.
-!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits, alpha,
beta and gamma, which can form homodimers or heterodimers which are
cell-type and development-specific. ENO1 interacts with PLG in the
neuronal plasma membrane and promotes its activation. The C-terminal
lysine is required for this binding (By similarity). In vitro,
interacts with several glycolytic enzymes including PKM, PGM, CKM and
aldolase (PubMed:9169614). Also binds troponin, in vitro
(PubMed:9169614). Interacts with ENO4 and PGAM2 (PubMed:23446454).
Interacts with CMTM6 (By similarity). {ECO:0000250|UniProtKB:P06733,
ECO:0000269|PubMed:23446454, ECO:0000269|PubMed:9169614}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}. Note=Can translocate to the plasma membrane in either
the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form (By
similarity). ENO1 is localized to the M-band. {ECO:0000250,
ECO:0000269|PubMed:11229603}.
-!- TISSUE SPECIFICITY: Testis. Found in the principal piece of sperm tail
(at protein level). The alpha/alpha homodimer is expressed in embryo
and in most adult tissues. The alpha/beta heterodimer and the beta/beta
homodimer are found in striated muscle, and the alpha/gamma heterodimer
and the gamma/gamma homodimer in neurons. In striated muscle,
expression of ENO1 appears to be independent of fiber type.
{ECO:0000269|PubMed:11229603, ECO:0000269|PubMed:23446454}.
-!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition from the
alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle
cells, and to the alpha/gamma heterodimer in nerve cells. In embryonic
muscle, ENO1 is highly expressed until 17 dpc. Decreased levels from
P5. {ECO:0000269|PubMed:9169614}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: Lysine 2-hydroxyisobutyrylation (Khib) by p300/EP300 activates the
phosphopyruvate hydratase activity. {ECO:0000250|UniProtKB:P06733}.
-!- SIMILARITY: Belongs to the enolase family. {ECO:0000305}.
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EMBL; X52379; CAA36605.1; -; mRNA.
EMBL; AK002336; BAB22021.1; -; mRNA.
EMBL; BC003891; AAH03891.1; -; mRNA.
EMBL; BC004017; AAH04017.1; -; mRNA.
EMBL; BC010685; AAH10685.1; -; mRNA.
EMBL; BC024644; AAH24644.1; -; mRNA.
EMBL; BC085098; AAH85098.1; -; mRNA.
CCDS; CCDS18971.1; -.
PIR; S10246; S10246.
RefSeq; NP_001020559.1; NM_001025388.1.
RefSeq; NP_075608.2; NM_023119.2.
RefSeq; XP_006538588.2; XM_006538525.2.
SMR; P17182; -.
BioGrid; 199451; 19.
BioGrid; 241069; 4.
IntAct; P17182; 16.
MINT; P17182; -.
STRING; 10090.ENSMUSP00000079727; -.
CarbonylDB; P17182; -.
iPTMnet; P17182; -.
PhosphoSitePlus; P17182; -.
SwissPalm; P17182; -.
REPRODUCTION-2DPAGE; IPI00462072; -.
REPRODUCTION-2DPAGE; P17182; -.
SWISS-2DPAGE; P17182; -.
UCD-2DPAGE; P17182; -.
CPTAC; non-CPTAC-3347; -.
CPTAC; non-CPTAC-3348; -.
EPD; P17182; -.
jPOST; P17182; -.
PaxDb; P17182; -.
PeptideAtlas; P17182; -.
PRIDE; P17182; -.
Ensembl; ENSMUST00000076155; ENSMUSP00000075513; ENSMUSG00000059040.
Ensembl; ENSMUST00000080926; ENSMUSP00000079727; ENSMUSG00000063524.
Ensembl; ENSMUST00000235307; ENSMUSP00000157807; ENSMUSG00000059040.
GeneID; 13806; -.
GeneID; 433182; -.
KEGG; mmu:13806; -.
KEGG; mmu:433182; -.
UCSC; uc008ewh.1; mouse.
CTD; 2023; -.
CTD; 433182; -.
MGI; MGI:95393; Eno1.
eggNOG; KOG2670; Eukaryota.
eggNOG; COG0148; LUCA.
GeneTree; ENSGT00950000182805; -.
HOGENOM; CLU_031223_0_0_1; -.
InParanoid; P17182; -.
KO; K01689; -.
OMA; EFMIIPV; -.
OrthoDB; 773373at2759; -.
PhylomeDB; P17182; -.
TreeFam; TF300391; -.
BRENDA; 4.2.1.11; 3474.
Reactome; R-MMU-70171; Glycolysis.
Reactome; R-MMU-70263; Gluconeogenesis.
SABIO-RK; P17182; -.
UniPathway; UPA00109; UER00187.
ChiTaRS; Eno1; mouse.
PRO; PR:P17182; -.
Proteomes; UP000000589; Chromosome 18.
Proteomes; UP000000589; Chromosome 4.
RNAct; P17182; protein.
Bgee; ENSMUSG00000059040; Expressed in brown adipose tissue and 33 other tissues.
ExpressionAtlas; P17182; baseline and differential.
Genevisible; P17182; MM.
GO; GO:0099738; C:cell cortex region; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0000015; C:phosphopyruvate hydratase complex; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0097060; C:synaptic membrane; ISO:MGI.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0051020; F:GTPase binding; ISO:MGI.
GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004634; F:phosphopyruvate hydratase activity; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0061621; P:canonical glycolysis; ISS:UniProtKB.
GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
GO; GO:0006096; P:glycolytic process; IDA:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0051099; P:positive regulation of binding; IMP:MGI.
CDD; cd03313; enolase; 1.
Gene3D; 3.20.20.120; -; 1.
Gene3D; 3.30.390.10; -; 1.
HAMAP; MF_00318; Enolase; 1.
InterPro; IPR000941; Enolase.
InterPro; IPR036849; Enolase-like_C_sf.
InterPro; IPR029017; Enolase-like_N.
InterPro; IPR020810; Enolase_C.
InterPro; IPR020809; Enolase_CS.
InterPro; IPR020811; Enolase_N.
PANTHER; PTHR11902; PTHR11902; 1.
Pfam; PF00113; Enolase_C; 1.
Pfam; PF03952; Enolase_N; 1.
PIRSF; PIRSF001400; Enolase; 1.
PRINTS; PR00148; ENOLASE.
SMART; SM01192; Enolase_C; 1.
SMART; SM01193; Enolase_N; 1.
SUPFAM; SSF51604; SSF51604; 1.
SUPFAM; SSF54826; SSF54826; 1.
TIGRFAMs; TIGR01060; eno; 1.
PROSITE; PS00164; ENOLASE; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing;
Glycolysis; Hydroxylation; Isopeptide bond; Lyase; Magnesium; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:P06733"
CHAIN 2..434
/note="Alpha-enolase"
/id="PRO_0000134098"
REGION 370..373
/note="Substrate binding"
/evidence="ECO:0000250|UniProtKB:P00924"
REGION 405..434
/note="Required for interaction with PLG"
/evidence="ECO:0000250"
ACT_SITE 210
/note="Proton donor"
/evidence="ECO:0000250|UniProtKB:P00924"
ACT_SITE 343
/note="Proton acceptor"
/evidence="ECO:0000250|UniProtKB:P00924"
METAL 40
/note="Magnesium 1"
/evidence="ECO:0000250|UniProtKB:P06733"
METAL 245
/note="Magnesium 2"
/evidence="ECO:0000250|UniProtKB:P06733"
METAL 293
/note="Magnesium 2"
/evidence="ECO:0000250|UniProtKB:P06733"
METAL 318
/note="Magnesium 2"
/evidence="ECO:0000250|UniProtKB:P06733"
BINDING 158
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 167
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 293
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 318
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
BINDING 394
/note="Substrate"
/evidence="ECO:0000250|UniProtKB:P00924"
MOD_RES 2
/note="N-acetylserine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 44
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:18034455"
MOD_RES 60
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 60
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 71
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 89
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 89
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 92
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 126
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 193
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 199
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 202
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 228
/note="N6-(2-hydroxyisobutyryl)lysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 228
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 228
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 233
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 233
/note="N6-malonyllysine; alternate"
/evidence="ECO:0000250"
MOD_RES 254
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 256
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 263
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 281
/note="N6-(2-hydroxyisobutyryl)lysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 281
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 287
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 291
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 335
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 343
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 406
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:23806337"
MOD_RES 420
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
MOD_RES 420
/note="N6-malonyllysine; alternate"
/evidence="ECO:0000250"
MOD_RES 420
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000244|PubMed:23806337"
CROSSLNK 202
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P06733"
CONFLICT 359
/note="L -> P (in Ref. 1; CAA36605)"
/evidence="ECO:0000305"
SEQUENCE 434 AA; 47141 MW; DBEF6270A70DE3A6 CRC64;
MSILRIHARE IFDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DNDKTRFMGK
GVSQAVEHIN KTIAPALVSK KVNVVEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK
AGAVEKGVPL YRHIADLAGN PEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFRE
AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKTA IAKAGYTDQV
VIGMDVAASE FYRSGKYDLD FKSPDDPSRY ITPDQLADLY KSFVQNYPVV SIEDPFDQDD
WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AASEKSCNCL LLKVNQIGSV TESLQACKLA
QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQI LRIEEELGSK
AKFAGRSFRN PLAK


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U0537h CLIA 2-phospho-D-glycerate hydro-lyase,ENO2,Enolase 2,Gamma-enolase,Homo sapiens,Human,Neural enolase,Neuron-specific enolase,NSE 96T
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Pathways :
WP253: Glycolysis
WP1946: Cori Cycle
WP296: TCA Cycle - biocyc
WP1003: Ovarian Infertility Genes
WP2064: Neural Crest Differentiation
WP929: TNF-alpha NF-kB Signaling Pathway
WP1531: Vitamin D synthesis
WP1584: Type II diabetes mellitus
WP390: Serine-isocitrate lyase pathway
WP108: Selenium metabolism/Selenoproteins
WP2100: AhR pathway
WP1163: TNF-alpha NF-kB Signaling Pathway
WP2199: Seed Development
WP1640: Cysteine and methionine metabolism
WP457: TNF-alpha NF-kB Signaling Pathway
WP1705: Sulfur metabolism
WP548: neural crest development
WP1225: estrogen signalling
WP244: Alpha 6 Beta 4 signaling pathway
WP1358: Selenium metabolism Selenoproteins
WP262: EBV LMP1 signaling
WP1835: Interferon alpha/beta signaling
WP668: Octadecanoid Pathway
WP1963: The effect of Glucocorticoids on target gene expression
WP885: Ovarian Infertility Genes

Related Genes :
[Eno1 Eno-1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[Eno1 Eno-1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[ENO1 ENO1L1 MBPB1 MPB1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (C-myc promoter-binding protein) (Enolase 1) (MBP-1) (MPB-1) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase) (Plasminogen-binding protein)
[ENO1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (HAP47) (Non-neural enolase) (NNE) (Phosphopyruvate hydratase)
[ENO2] Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)
[Eno2 Eno-2] Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)
[Eno2 Eno-2] Gamma-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 2) (Neural enolase) (Neuron-specific enolase) (NSE)
[ENO1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[ENO1 QccE-14518] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[Eno3 Eno-3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[Eno3 Eno-3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[ENO2 LOS2 At2g36530 F1O11.16] Bifunctional enolase 2/transcriptional activator (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 2) (2-phosphoglycerate dehydratase 2) (LOW EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 1)
[ENO1 CAALFM_C108500CA CaO19.395 CaO19.8025] Enolase 1 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[ENO1] Alpha-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 1) (Non-neural enolase) (NNE) (Fragments)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[eno MSMEG_5415 MSMEI_5267] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[ENO3] Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)
[eno OR1_00408] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BON65_01250 BON66_15955 BON86_06490 BON95_14610 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP047_03567 BvCmsSINP011_04162 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 C9Z23_21970 C9Z37_00915 C9Z43_06360 C9Z78_05610 CDC27_10055 CDL37_00765 CI694_25210 COD46_23180 CQP61_17160 CRD98_26150 D2188_01360 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DEN89_24995 DEO04_05510 DL800_09215 DQE83_22775 DTL43_21780 DU321_04440 DXT73_20690 E2134_24005 E2135_17195 E2855_02503 E2863_02392 E5P22_21380 E5S46_06650 EC95NR1_00961 ED648_25045 ELT20_21515 ELV08_24970 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 ExPECSC038_01920 EXX71_02385 EXX78_21815 EYD11_09165 F7F11_20115 F7F29_22635 FNJ83_13175 FQ915_04255 FQR64_09390 FWK02_18105 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PGD_01271 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[eno CBP06_04475 E4195_23395 EQ845_16830] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR214_00082] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR37_00362] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno OR16_24200] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[emp-7 NCU10042] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (Embden-meyerhof pathway protein 7)
[eno Loa_02648] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno1 eno ACTI_28410] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno E4195_02605] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)
[eno BJD20_17165 CW311_11095] Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase)

Bibliography :
[26695425] Urinary biomarkers for the non-invasive diagnosis of endometriosis.
[24283984] Evaluation of elevated urinary enolase I levels in patients with endometriosis.
[15912209] Molecular evolution of enolase.
[9851734] Endothelial cell hypoxic stress proteins.
[9510436] Postnatal developmental changes in NSE and NNE mRNA expression in the rat pineal gland: in situ hybridization histochemistry.
[7499243] Non-neuronal enolase is an endothelial hypoxic stress protein.
[7877724] Repeated electroconvulsive shock selectively increases the expression of the neuron specific enolase in piriform cortex.
[8037719] Synthetic peptide corresponding to 30 amino acids of the C-terminal of neuron-specific enolase promotes survival of neocortical neurons in culture.
[8264236] Detection of neuron-specific gamma-enolase messenger ribonucleic acid in normal human leukocytes by polymerase chain reaction amplification with nested primers.
[7691181] Characterisation of an epitope specific to the neuron-specific isoform of human enolase recognised by a monoclonal antibody raised against a synthetic peptide corresponding to the C-terminus of beta/A4-protein.