P06733 (ENOA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-enolase
EC=4.2.1.11

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

Gene names

Name:	ENO1
Synonyms:	ENO1L1, MBPB1, MPB1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 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. Ref.23 Ref.27
Subcellular location	Cytoplasm. Cell membrane. Cytoplasm › myofibril › sarcomere › M line. Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M line. 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. Up-regulated in response to enterovirus 71 (EV71) infection (at protein level). Ref.19 Ref.31
Post-translational modification	ISGylated. Ref.29 Ref.32
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. 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. 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.
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. Ref.18
Sequence caution	The sequence AAA35698.1 differs from that shown. Reason: Frameshift at several positions. The sequence AAA35698.1 differs from that shown. Reason: 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 Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Traceable author statement. Source: Reactome glycolysis Traceable author statement. Source: Reactome negative regulation of cell growth Inferred from direct assay Ref.20. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.3. Source: ProtInc response to virus Inferred from expression pattern Ref.31. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	M band Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB nucleus Inferred by curator Ref.20. Source: UniProtKB phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphopyruvate hydratase activity Traceable author statement Ref.1. Source: ProtInc sequence-specific DNA binding transcription factor activity Traceable author statement Ref.3. Source: ProtInc transcription corepressor activity Traceable author statement Ref.3. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACHE	P22303	2	EBI-353877,EBI-1637793
TTN	Q8WZ42	3	EBI-353877,EBI-681210

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 Ref.35

Modified residue

5

1

N6-acetyllysine Ref.35

Modified residue

44

1

Phosphotyrosine Ref.30

Modified residue

64

1

N6-acetyllysine Ref.35

Modified residue

71

1

N6-acetyllysine Ref.35

Modified residue

89

1

N6-acetyllysine Ref.35

Modified residue

126

1

N6-acetyllysine Ref.35

Modified residue

193

1

N6-acetyllysine Ref.35

Modified residue

199

1

N6-acetyllysine Ref.35

Modified residue

228

1

N6-acetyllysine Ref.35

Modified residue

233

1

N6-acetyllysine Ref.35

Modified residue

233

1

N6-malonyllysine; alternate Ref.38

Modified residue

254

1

Phosphoserine Ref.33

Modified residue

256

1

N6-acetyllysine Ref.35

Modified residue

263

1

Phosphoserine Ref.33

Modified residue

272

1

Phosphoserine Ref.34

Modified residue

281

1

N6-acetyllysine Ref.35

Modified residue

285

1

N6-acetyllysine Ref.35

Modified residue

287

1

Phosphotyrosine Ref.30

Modified residue

420

1

N6-acetyllysine Ref.35

Modified residue

420

1

N6-malonyllysine; alternate Ref.38

Natural variations

Alternative sequence

1 – 93

93

Missing in isoform MBP-1.

VSP_018725

Natural variant

177

1

N → K. Ref.9
Corresponds to variant rs11544513 [ dbSNP | Ensembl ].

VAR_025172

Natural variant

325

1

P → Q.
Corresponds to variant rs11544514 [ dbSNP | Ensembl ].

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

1

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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 [UniParc]. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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(1994) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS AN AUTOANTIGEN IN HASHIMOTO ENCEPHALOPATHY.
[29]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." 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. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ISGYLATION.
[30]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44 AND TYR-287, MASS SPECTROMETRY.
[31]	"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection." Leong W.F., Chow V.T. Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, MASS SPECTROMETRY.
[32]	"HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets." Wong J.J., Pung Y.F., Sze N.S., Chin K.C. Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ISGYLATION.
[33]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 AND SER-263, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[34]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[35]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-5; LYS-64; LYS-71; LYS-89; LYS-126; LYS-193; LYS-199; LYS-228; LYS-233; LYS-256; LYS-281; LYS-285 AND LYS-420, MASS SPECTROMETRY.
[36]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[37]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]	"The first identification of lysine malonylation substrates and its regulatory enzyme." Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y. Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract] Cited for: MALONYLATION AT LYS-233 AND LYS-420.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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_001188412.1. NM_001201483.1.
NP_001419.1. NM_001428.3.

UniGene

Hs.517145.
Hs.701472.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P06733.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06733. 56 interactions.

MINT

MINT-155303.

PTM databases

PhosphoSite

P06733.

Polymorphism databases

DMDM

119339.

2D gel databases

DOSAC-COBS-2DPAGE

P06733.

OGP

P06733.

REPRODUCTION-2DPAGE

IPI00465248.
P06733.

SWISS-2DPAGE

P06733.

UCD-2DPAGE

P06733.

Proteomic databases

PaxDb

P06733.

PeptideAtlas

P06733.

PRIDE

P06733.

Protocols and materials databases

DNASU

2023.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000234590; ENSP00000234590; ENSG00000074800.

GeneID

2023.

KEGG

hsa:2023.

UCSC

uc001api.2. human.

Organism-specific databases

CTD

2023.

GeneCards

GC01M008921.

HGNC

HGNC:3350. ENO1.

HPA

CAB018614.

MIM

172430. gene.

neXtProt

NX_P06733.

PharmGKB

PA27786.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0148.

HOVERGEN

HBG000067.

InParanoid

P06733.

KO

K01689.

OMA

NVNVVEQ.

OrthoDB

EOG4T783B.

PhylomeDB

P06733.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000074800-MONOMER.

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P06733.

UniPathway

UPA00109; UER00187.

Gene expression databases

ArrayExpress

P06733.

Bgee

P06733.

Genevestigator

P06733.

GermOnline

ENSG00000074800. Homo sapiens.

Family and domain databases

InterPro

IPR000941. Enolase.
IPR020810. Enolase_C.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
[Graphical view]

PANTHER

PTHR11902. PTHR11902. 1 hit.

Pfam

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

PIRSF

PIRSF001400. Enolase. 1 hit.

PRINTS

PR00148. ENOLASE.

TIGRFAMs

TIGR01060. eno. 1 hit.

PROSITE

PS00164. ENOLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL3298.

ChiTaRS

ENO1. human.

EvolutionaryTrace

P06733.

GenomeRNAi

2023.

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:	May 29, 2013
This is version 171 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.