Reviewed, UniProtKB/Swiss-Prot P06733 (ENOA_HUMAN)

Names and origin

Protein names

Recommended name:
    Alpha-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Non-neural enolase
      Short name=NNE
    Enolase 1
    Phosphopyruvate hydratase
    C-myc promoter-binding protein
    MBP-1
    MPB-1
    Plasminogen-binding protein

Gene names

Name:	ENO1
Synonyms:	ENO1L1, MBPB1, MPB1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Multifunctional enzyme that, as well as its role in glycolysis, plays a part 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. Ref.3 Ref.18 Ref.20 Ref.21 Ref.22 MBP1 binds to the c-myc promoter and acts as a transcriptional repressor. May be a tumor suppressor. Ref.3 Ref.18 Ref.20 Ref.21 Ref.22
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H2O. Ref.18
Cofactor	Magnesium. Required for catalysis and for stabilizing the dimer.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subunit structure	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.
Subcellular location	Cytoplasm. Cell membrane. Cytoplasm › myofibril › sarcomere › M-band. Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M-band. Ref.21 Isoform MBP-1: Nucleus. Ref.21
Tissue specificity	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.
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.
Induction	Induced in diffuse large cell lymphoma (DLCL) after treatment with the natural biological agent, Bryo1. Ref.19
Involvement in disease	ENO1 is identified as an autoantigen in Hashimoto encephalopathy (HE) a rare autoimmune disease associated with Hashimoto thyroiditis (HT). HT is a disorder in which destructive processes overcome the potential capacity of thyroid replacement leading to hypothyroidism. Antibodies against alpha-enolase are present in sera from patients with cancer-associated retinopathy syndrome (CAR), a progressive blinding disease which occurs in the presence of systemic tumor growth, primarily small-cell carcinoma of the lung and other malignancies. Ref.24
Miscellaneous	Used as a diagnostic marker for many tumors and, in the heterodimeric form, alpha/gamma, as a marker for hypoxic brain injury after cardiac arrest. Also marker for endometriosis.
Sequence similarities	Belongs to the enolase family.
biophysicochemical properties	pH dependence: Enolase activity is lost above pH 9.0. Immunoglobulin production stimulating activity is retained at pH 13.0.
Sequence caution	The sequence AAA35698.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAA35698.1 differs from that shown. Reason: Miscellaneous discrepancy. Sequencing errors.

Ontologies

Keywords
Biological process	Glycolysis Plasminogen activation Transcription Transcription regulation
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative initiation Polymorphism
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	Lyase Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell growth Ref.20 Inferred from direct assay. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Ref.3 Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	M band Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Ref.20 Inferred by curator. Source: UniProtKB phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Ref.1 Traceable author statement. Source: ProtInc serine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW transcription corepressor activity Ref.3 Traceable author statement. Source: ProtInc transcription factor activity Ref.3 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform alpha-enolase (identifier: P06733-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform MBP-1 (identifier: P06733-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: Missing.

Note: It is uncertain whether the alternative initiation site is at Met-94 or at Met-97.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.13 Ref.14

Chain

2 – 434

433

Alpha-enolase

PRO_0000134097

Regions

Region

31 – 38

8

Epitope recognized by CAR and healthy patient antibodies

Region

56 – 63

8

Epitope recognized by CAR antibodies

Region

97 – 237

141

Required for repression of c-myc promoter activity

Region

370 – 373

4

Substrate binding By similarity

Region

405 – 434

30

Required for interaction with PLG By similarity

Sites

Active site

210

1

Proton donor By similarity

Active site

343

1

Proton acceptor By similarity

Metal binding

245

1

Magnesium By similarity

Metal binding

293

1

Magnesium By similarity

Metal binding

318

1

Magnesium By similarity

Binding site

158

1

Substrate By similarity

Binding site

167

1

Substrate By similarity

Binding site

293

1

Substrate By similarity

Binding site

318

1

Substrate By similarity

Binding site

394

1

Substrate By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.14

Modified residue

44

1

Phosphotyrosine Ref.29 Ref.31

Modified residue

57

1

Phosphotyrosine Ref.33

Modified residue

63

1

Phosphoserine Ref.33

Modified residue

71

1

N6-acetyllysine Ref.30

Modified residue

72

1

Phosphothreonine Ref.32

Modified residue

254

1

Phosphoserine Ref.34

Modified residue

263

1

Phosphoserine Ref.34

Modified residue

287

1

Phosphotyrosine Ref.29 Ref.31

Natural variations

Alternative sequence

1 – 93

93

Missing in isoform MBP-1.

VSP_018725

Natural variant

177

1

N → K Ref.9

VAR_025172

Natural variant

325

1

P → Q: dbSNP rs11544514.

VAR_048936

Experimental info

Mutagenesis

94

1

M → I: MBP1 protein production. No MBP1 protein production; when associated with I-97. Ref.25

Mutagenesis

97

1

M → I: MBP1 protein production. No MBP1 protein production; when associated with I-94. Ref.25

Mutagenesis

384

1

L → A: Loss of transcriptional repression and cell growth inhibition; when associated with A-388. Ref.20

Mutagenesis

388

1

L → A: Loss of transcriptional repression and cell growth inhibition; when associated with A-384. Ref.20

Sequence conflict

55

1

T → A in CAD97642. Ref.8

Sequence conflict

78

1

V → A in BAD96237. Ref.7

Sequence conflict

187

1

E → G in CAD97642. Ref.8

Sequence conflict

199

1

K → R in BAD96912. Ref.7

Sequence conflict

252

1

F → S in CAA59331. Ref.4

Sequence conflict

310

1

S → I in CAD97642. Ref.8

Secondary structure

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434

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Beta strand

18 – 26

9

Beta strand

29 – 34

6

Helix

57 – 59

3

Helix

63 – 71

9

Helix

73 – 79

7

Helix

87 – 98

12

Turn

104 – 106

3

Helix

108 – 125

18

Helix

130 – 138

9

Beta strand

147 – 154

8

Helix

156 – 158

3

Beta strand

159 – 162

4

Beta strand

167 – 171

5

Helix

178 – 200

23

Helix

202 – 204

3

Helix

220 – 233

14

Turn

237 – 239

3

Beta strand

241 – 245

5

Helix

248 – 250

3

Turn

259 – 262

4

Helix

267 – 269

3

Helix

273 – 286

14

Beta strand

289 – 293

5

Helix

301 – 311

11

Beta strand

313 – 318

6

Turn

319 – 323

5

Helix

325 – 334

10

Beta strand

338 – 342

5

Helix

344 – 347

4

Helix

350 – 362

13

Beta strand

366 – 370

5

Helix

380 – 387

8

Beta strand

391 – 394

4

Helix

401 – 417

17

Helix

418 – 420

3

Helix

425 – 427

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform alpha-enolase [UniParc]. Last modified January 23, 2007. Version 2. Checksum: A0ED663FCC15ADA5	FASTA	434	47,169
	10 20 30 40 50 60 MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK 70 80 90 100 110 120 GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK 130 140 150 160 170 180 AGAVEKGVPL YRHIADLAGN SEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAANFRE 190 200 210 220 230 240 AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV 250 260 270 280 290 300 VIGMDVAASE FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD 310 320 330 340 350 360 WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV TESLQACKLA 370 380 390 400 410 420 QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK 430 AKFAGRNFRN PLAK
	Isoform MBP-1. Checksum: 96D437CF21772928	FASTA	341	36,928
	10 20 30 40 50 60 MIEMDGTENK SKFGANAILG VSLAVCKAGA VEKGVPLYRH IADLAGNSEV ILPVPAFNVI 70 80 90 100 110 120 NGGSHAGNKL AMQEFMILPV GAANFREAMR IGAEVYHNLK NVIKEKYGKD ATNVGDEGGF 130 140 150 160 170 180 APNILENKEG LELLKTAIGK AGYTDKVVIG MDVAASEFFR SGKYDLDFKS PDDPSRYISP 190 200 210 220 230 240 DQLADLYKSF IKDYPVVSIE DPFDQDDWGA WQKFTASAGI QVVGDDLTVT NPKRIAKAVN 250 260 270 280 290 300 EKSCNCLLLK VNQIGSVTES LQACKLAQAN GWGVMVSHRS GETEDTFIAD LVVGLCTGQI 310 320 330 340 KTGAPCRSER LAKYNQLLRI EEELGSKAKF AGRNFRNPLA K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and nucleotide sequence of a full-length cDNA for human alpha enolase." Giallongo A., Feo S., Moore R., Croce C.M., Showe L.C. Proc. Natl. Acad. Sci. U.S.A. 83:6741-6745(1986) [PubMed: 3529090] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-ENOLASE).
[2]	"Structure of the human gene for alpha-enolase." Giallongo A., Oliva D., Cali L., Barba G., Barbieri G., Feo S. Eur. J. Biochem. 190:567-573(1990) [PubMed: 2373081] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-ENOLASE). Tissue: T-cell.
[3]	"Cloning and characterization of a human c-myc promoter-binding protein." Ray R., Miller D.M. Mol. Cell. Biol. 11:2154-2161(1991) [PubMed: 2005901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MBP-1), FUNCTION. Tissue: Cervix carcinoma.
[4]	"Autoreactive epitopes within the human alpha-enolase and their recognition by sera from patients with endometriosis." Walter M., Berg H., Leidenberger F.A., Schweppe K.W., Northemann W. J. Autoimmun. 8:931-945(1995) [PubMed: 8824716] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-ENOLASE), MARKER FOR ENDOMETRIOSIS. Tissue: Endometrium.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE). Tissue: Umbilical cord blood.
[7]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE). Tissue: Adipose tissue and Kidney proximal tubule.
[8]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE). Tissue: Retina and Stomach.
[9]	NIEHS SNPs program Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-177.
[10]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE). Tissue: Brain, Eye, Lung, Ovary, Placenta and Skin.
[13]	"A two-dimensional gel database of human colon carcinoma proteins." Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J. Electrophoresis 18:605-613(1997) [PubMed: 9150948] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-9 (ISOFORM ALPHA-ENOLASE). Tissue: Colon carcinoma.
[14]	Bienvenut W.V., Lilla S., Zebisch A., Kolch W. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-28; 65-80; 121-162; 234-253; 270-281; 331-394 AND 407-420, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[15]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 16-28; 33-50; 93-103; 106-120; 163-179; 184-193; 203-221; 240-253; 257-262; 270-281; 286-326; 336-394 AND 407-412, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[16]	"Molecular cloning and expression analysis of five novel genes in chromosome 1p36." Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A. Genomics 50:187-198(1998) [PubMed: 9653645] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 166-434.
[17]	"Large-scale concatenation cDNA sequencing." Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A. Genome Res. 7:353-358(1997) [PubMed: 9110174] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-434. Tissue: Brain.
[18]	"Purification and characterization of immunoglobulin production stimulating factor-II beta derived from Namalwa cells." Sugahara T., Nakajima H., Shirahata S., Murakami H. Cytotechnology 10:137-146(1992) [PubMed: 1369209] [Abstract] Cited for: PROTEIN SEQUENCE OF 203-228, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Lymphoma.
[19]	"Induced expression of alpha-enolase in differentiated diffuse large cell lymphoma." Mohamad R.M., Hamdan M.Y., Maki A., Al-Katib A. Enzyme Protein 48:37-44(1995) [PubMed: 7787969] [Abstract] Cited for: PROTEIN SEQUENCE OF 270-281 AND 307-321, INDUCTION IN DIFFUSE LARGE CELL LYMPHOMA.
[20]	"Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation." Ghosh A.K., Steele R., Ray R.B. Mol. Cell. Biol. 19:2880-2886(1999) [PubMed: 10082554] [Abstract] Cited for: FUNCTION OF MBP1, IDENTIFICATION OF REPRESSOR DOMAINS, MUTAGENESIS OF LEU-384 AND LEU-388.
[21]	"ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1)." Feo S., Arcuri D., Piddini E., Passantino R., Giallongo A. FEBS Lett. 473:47-52(2000) [PubMed: 10802057] [Abstract] Cited for: FUNCTION AS A C-MYC TRANSCRIPTIONAL REPRESSOR, SUBCELLULAR LOCATION.
[22]	"Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against alpha-enolase." Lopez-Alemany R., Longstaff C., Hawley S., Mirshahi M., Fabregas P., Jardi M., Merton E., Miles L.A., Felez J. Am. J. Hematol. 72:234-242(2003) [PubMed: 12666133] [Abstract] Cited for: FUNCTION IN PLASMINOGEN ACTIVATION.
[23]	"Identification of an epitope of alpha-enolase (a candidate plasminogen receptor) by phage display." Arza B., Felez J., Lopez-Alemany R., Miles L.A., Munoz-Canoves P. Thromb. Haemost. 78:1097-1103(1997) [PubMed: 9308760] [Abstract] Cited for: INTERACTION WITH PLG.
[24]	"Anti-enolase-alpha autoantibodies in cancer-associated retinopathy: epitope mapping and cytotoxicity on retinal cells." Adamus G., Amundson D., Seigel G.M., Machnicki M. J. Autoimmun. 11:671-677(1998) [PubMed: 9878089] [Abstract] Cited for: EPITOPE MAPPING, ASSOCIATION WITH CAR.
[25]	"Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene." Subramanian A., Miller D.M. J. Biol. Chem. 275:5958-5965(2000) [PubMed: 10681589] [Abstract] Cited for: IDENTIFICATION OF MBP1 AS AN ALPHA-ENOLASE ALTERNATIVE INITIATION PRODUCT, MUTAGENESIS OF MET-94 AND MET-97.
[26]	"Multifunctional alpha-enolase: its role in diseases." Pancholi V. Cell. Mol. Life Sci. 58:902-920(2001) [PubMed: 11497239] [Abstract] Cited for: REVIEW.
[27]	"A novel 16-kilodalton cellular protein physically interacts with and antagonizes the functional activity of c-myc promoter-binding protein 1." Ghosh A.K., Majumder M., Steele R., White R.A., Ray R.B. Mol. Cell. Biol. 21:655-662(2001) [PubMed: 11134351] [Abstract] Cited for: INTERACTION OF MBP1 WITH SEDL.
[28]	"Proteomic analysis of human brain identifies alpha-enolase as a novel autoantigen in Hashimoto's encephalopathy." Ochi H., Horiuchi I., Araki N., Toda T., Araki T., Sato K., Murai H., Osoegawa M., Yamada T., Okamura K., Ogino T., Mizumoto K., Yamashita H., Saya H., Kira J. FEBS Lett. 528:197-202(2002) [PubMed: 12297304] [Abstract] Cited for: IDENTIFICATION AS AN AUTOANTIGEN IN HASHIMOTO ENCEPHALOPATHY.
[29]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44 AND TYR-287, MASS SPECTROMETRY.
[30]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71, MASS SPECTROMETRY. Tissue: Epithelium.
[31]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44 AND TYR-287, MASS SPECTROMETRY.
[32]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, MASS SPECTROMETRY. Tissue: Epithelium.
[33]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-57 AND SER-63, MASS SPECTROMETRY.
[34]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 AND SER-263, MASS SPECTROMETRY.
[35]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

M14328 mRNA. Translation: AAA52387.1.
X16288, X16289, X16290 Genomic DNA. Translation: CAA34360.1.
M55914 mRNA. Translation: AAA35698.1. Frameshift.
X84907 mRNA. Translation: CAA59331.1.
BT007163 mRNA. Translation: AAP35827.1.
AK315417 mRNA. Translation: BAG37806.1.
AL833741 mRNA. Translation: CAH56247.1.
BX537400 mRNA. Translation: CAD97642.1.
AK222517 mRNA. Translation: BAD96237.1.
AK223192 mRNA. Translation: BAD96912.1.
DQ056744 Genomic DNA. Translation: AAY43128.1.
AL139415 Genomic DNA. Translation: CAC42425.1.
CH471130 Genomic DNA. Translation: EAW71604.1.
BC001810 mRNA. Translation: AAH01810.1.
BC004458 mRNA. Translation: AAH04458.1.
BC009912 mRNA. Translation: AAH09912.1.
BC011130 mRNA. Translation: AAH11130.1.
BC015641 mRNA. Translation: AAH15641.1.
BC021166 mRNA. Translation: AAH21166.2.
BC022545 mRNA. Translation: AAH22545.1.
BC027725 mRNA. Translation: AAH27725.1.
BC050642 mRNA. Translation: AAH50642.1.
U88968 mRNA. Translation: AAC39935.1.
AF035286 mRNA. Translation: AAB88178.1.

IPI

IPI00465248.
IPI00759806.

PIR

A39579.
A29170. S11696.

RefSeq

NP_001419.1.

UniGene

Hs.517145

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PSN	X-ray	2.20	A/B/C/D	1-434	[»]
3B97	X-ray	2.20	A/B/C/D	2-434	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P06733. 6 interactions.

PTM databases

PhosphoSite

P06733.

2-D gel databases

SWISS-2DPAGE

P06733.

Aarhus/Ghent-2DPAGE

1325. IEF.
5406. NEPHGE.

Cornea-2DPAGE

P06733.

DOSAC-COBS-2DPAGE

P06733.

OGP

P06733.

REPRODUCTION-2DPAGE

IPI00465248.
P06733.

Proteomic databases

PeptideAtlas

P06733.

PRIDE

P06733.

Genome annotation databases

Ensembl

ENSG00000074800. Homo sapiens. [Contig view]

GeneID

2023.

KEGG

hsa:2023.

Organism-specific databases

GeneCards

GC01M008855.

H-InvDB

HIX0000101.

HGNC

HGNC:3350. ENO1.

HPA

CAB018614.

MIM

172430. gene.

Orphanet

299. Enolase deficiency.

PharmGKB

PA27786.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P06733.

OMA

P06733. SDSSKWL.

Enzyme and pathway databases

BRENDA

4.2.1.11. 247.

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_474. Metabolism of carbohydrates.

Gene expression databases

ArrayExpress

P06733.

Bgee

P06733.

GermOnline

ENSG00000074800. Homo sapiens.

Family and domain databases

InterPro

IPR000941. Enolase.
[Graphical view]

PANTHER

PTHR11902. Enolase. 1 hit.

Pfam

PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]

PIRSF

PIRSF001400. Enolase. 1 hit.

PRINTS

PR00148. ENOLASE.

ProDom

PD000902. Enolase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01060. eno. 1 hit.

PROSITE

PS00164. ENOLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

8197.

PMAP-CutDB

P06733.

SOURCE

Search...

Entry information

Entry name

ENOA_HUMAN

Accession

Primary (citable) accession number: P06733
Secondary accession number(s): B2RD59 , P22712, Q16704, Q4TUS4, Q53FT9, Q53HR3, Q658M5, Q6GMP2, Q71V37, Q7Z3V6, Q8WU71, Q9UCH6, Q9UM55

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)