P13929 (ENOB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-enolase
EC=4.2.1.11

Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 3
Muscle-specific enolase
Short name=MSE
Skeletal muscle enolase

Gene names

Name:

ENO3

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	Appears to have a function in striated muscle development and regeneration.
Catalytic activity	2-phospho-D-glycerate = phosphoenolpyruvate + H2O.
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. Interacts with PNKD. Ref.9
Subcellular location	Cytoplasm. Note: Localized to the Z line. Some colocalization with CKM at M-band By similarity.
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.
Involvement in disease	Glycogen storage disease 13 (GSD13) [MIM:612932]: A metabolic disorder that results in exercise-induced myalgias, generalized muscle weakness and fatigability. It is characterized by increased serum creatine kinase and decreased enolase 3 activity. Dramatically reduced protein levels with focal sarcoplasmic accumulation of glycogen-beta particles are detected on ultrastructural analysis. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Glycogen storage disease
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	gluconeogenesis Traceable author statement. Source: Reactome glycolysis Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphopyruvate hydratase activity Traceable author statement Ref.4. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P13929-1)

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 2 (identifier: P13929-2)

The sequence of this isoform differs from the canonical sequence as follows:
     150-177: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P13929-3)

The sequence of this isoform differs from the canonical sequence as follows:
     61-104: GVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKS → A

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 434

433

Beta-enolase

PRO_0000134107

Regions

Region

370 – 373

4

Substrate binding 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

Natural variations

Alternative sequence

61 – 104

44

GVLKA…TENKS → A in isoform 3.

VSP_037752

Alternative sequence

150 – 177

28

Missing in isoform 2.

VSP_037753

Natural variant

71

1

N → S. Ref.4 Ref.5 Ref.8
Corresponds to variant rs238238 [ dbSNP | Ensembl ].

VAR_020618

Natural variant

85

1

V → A. Ref.2 Ref.4 Ref.5 Ref.8
Corresponds to variant rs238239 [ dbSNP | Ensembl ].

VAR_020619

Natural variant

156

1

G → D in GSD13; when associated with E-374. Ref.11

VAR_020620

Natural variant

374

1

G → E in GSD13; when associated with D-156. Ref.11

VAR_020621

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

Beta strand

43 – 45

3

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

150 – 154

5

Helix

156 – 158

3

Beta strand

159 – 162

4

Beta strand

167 – 171

5

Helix

178 – 200

23

Helix

220 – 234

15

Turn

237 – 239

3

Beta strand

241 – 245

5

Helix

248 – 251

4

Turn

259 – 262

4

Helix

267 – 269

3

Helix

273 – 286

14

Beta strand

289 – 293

5

Helix

301 – 309

9

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 – 388

9

Beta strand

391 – 394

4

Helix

401 – 417

17

Helix

418 – 420

3

Helix

425 – 427

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 28, 2012. Version 5. Checksum: 4D9D8DCF32CF153F	FASTA	434	46,987
	10 20 30 40 50 60 MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKGRYLGK 70 80 90 100 110 120 GVLKAVENIN NTLGPALLQK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK 130 140 150 160 170 180 AGAAEKGVPL YRHIADLAGN PDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE 190 200 210 220 230 240 AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV 250 260 270 280 290 300 VIGMDVAASE FYRNGKYDLD FKSPDDPARH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD 310 320 330 340 350 360 WATWTSFLSG VNIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA 370 380 390 400 410 420 QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK 430 AIFAGRKFRN PKAK
	Isoform 2 [UniParc]. Checksum: E0D4621669448D46	FASTA	406	44,115
	10 20 30 40 50 60 MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKGRYLGK 70 80 90 100 110 120 GVLKAVENIN NTLGPALLQK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK 130 140 150 160 170 180 AGAAEKGVPL YRHIADLAGN PDLILPVPAF KEAMRIGAEV YHHLKGVIKA KYGKDATNVG 190 200 210 220 230 240 DEGGFAPNIL ENNEALELLK TAIQAAGYPD KVVIGMDVAA SEFYRNGKYD LDFKSPDDPA 250 260 270 280 290 300 RHITGEKLGE LYKSFIKNYP VVSIEDPFDQ DDWATWTSFL SGVNIQIVGD DLTVTNPKRI 310 320 330 340 350 360 AQAVEKKACN CLLLKVNQIG SVTESIQACK LAQSNGWGVM VSHRSGETED TFIADLVVGL 370 380 390 400 CTGQIKTGAP CRSERLAKYN QLMRIEEALG DKAIFAGRKF RNPKAK
	Isoform 3 [UniParc]. Checksum: 0B6DB38924087E00	FASTA	391	42,248
	10 20 30 40 50 60 MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKGRYLGK 70 80 90 100 110 120 AKFGANAILG VSLAVCKAGA AEKGVPLYRH IADLAGNPDL ILPVPAFNVI NGGSHAGNKL 130 140 150 160 170 180 AMQEFMILPV GASSFKEAMR IGAEVYHHLK GVIKAKYGKD ATNVGDEGGF APNILENNEA 190 200 210 220 230 240 LELLKTAIQA AGYPDKVVIG MDVAASEFYR NGKYDLDFKS PDDPARHITG EKLGELYKSF 250 260 270 280 290 300 IKNYPVVSIE DPFDQDDWAT WTSFLSGVNI QIVGDDLTVT NPKRIAQAVE KKACNCLLLK 310 320 330 340 350 360 VNQIGSVTES IQACKLAQSN GWGVMVSHRS GETEDTFIAD LVVGLCTGQI KTGAPCRSER 370 380 390 LAKYNQLMRI EEALGDKAIF AGRKFRNPKA K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of human muscle (beta) enolase mRNA and protein deduced from a genomic clone." Peshavaria M., Hinks L.J., Day I.N.M. Nucleic Acids Res. 17:8862-8862(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE)." Cali L., Feo S., Oliva D., Giallongo A. Nucleic Acids Res. 18:1893-1893(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-85.
[3]	"Molecular structure of the human muscle-specific enolase gene (ENO3)." Peshavaria M., Day I.N.M. Biochem. J. 275:427-433(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]	"Structural features of the human gene for muscle-specific enolase. Differential splicing in the 5'-untranslated sequence generates two forms of mRNA." Giallongo A., Venturella S., Oliva D., Barbieri G., Rubino P., Feo S. Eur. J. Biochem. 214:367-374(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS SER-71 AND ALA-85.
[5]	"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] (ISOFORMS 2 AND 3), VARIANTS SER-71 AND ALA-85. Tissue: Skeletal muscle.
[6]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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 1), VARIANTS SER-71 AND ALA-85. Tissue: Muscle.
[9]	"Characterization of MR-1, a novel myofibrillogenesis regulator in human muscle." Li T.-B., Liu X.-H., Feng S., Hu Y., Yang W.-X., Han Y., Wang Y.-G., Gong L.-M. Acta Biochim. Biophys. Sin. 36:412-418(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PNKD.
[10]	"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].
[11]	"Beta-enolase deficiency, a new metabolic myopathy of distal glycolysis." Comi G.P., Fortunato F., Lucchiari S., Bordoni A., Prelle A., Jann S., Keller A., Ciscato P., Galbiati S., Chiveri L., Torrente Y., Scarlato G., Bresolin N. Ann. Neurol. 50:202-207(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD13 ASP-156 AND GLU-374.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16504 mRNA. Translation: CAA34513.1.
X51957 mRNA. Translation: CAA36216.1.
X55976 Genomic DNA. Translation: CAA39446.1.
X56832 Genomic DNA. Translation: CAA40163.1.
AK300662 mRNA. Translation: BAG62348.1.
AK300709 mRNA. Translation: BAG62388.1.
AC004771 Genomic DNA. No translation available.
AC109333 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90375.1.
CH471108 Genomic DNA. Translation: EAW90379.1.
CH471108 Genomic DNA. Translation: EAW90380.1.
BC017249 mRNA. Translation: AAH17249.1.

IPI

IPI00218474.
IPI00909949.
IPI00942494.

PIR

S06756.

RefSeq

NP_001180432.1. NM_001193503.1.
NP_001967.3. NM_001976.4.
NP_443739.3. NM_053013.3.

UniGene

Hs.224171.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XSX	X-ray	1.70	A/B	1-434	[»]

ProteinModelPortal

P13929.

SMR

P13929. Positions 1-434.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13929. 17 interactions.

STRING

9606.ENSP00000324105.

PTM databases

PhosphoSite

P13929.

Polymorphism databases

DMDM

254763441.

2D gel databases

UCD-2DPAGE

P13929.

Proteomic databases

PaxDb

P13929.

PRIDE

P13929.

Protocols and materials databases

DNASU

2027.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000323997; ENSP00000324105; ENSG00000108515.
ENST00000518175; ENSP00000431087; ENSG00000108515.
ENST00000519584; ENSP00000430636; ENSG00000108515.

GeneID

2027.

KEGG

hsa:2027.

UCSC

uc010vss.2. human.
uc010vst.2. human.

Organism-specific databases

CTD

2027.

GeneCards

GC17P004851.

H-InvDB

HIX0013457.

HGNC

HGNC:3354. ENO3.

HPA

HPA000793.

MIM

131370. gene.
612932. phenotype.

neXtProt

NX_P13929.

Orphanet

99849. Beta-enolase deficiency.

PharmGKB

PA27789.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0148.

HOGENOM

HOG000072174.

HOVERGEN

HBG000067.

InParanoid

P13929.

KO

K01689.

OMA

GELYKNF.

OrthoDB

EOG4T783B.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P13929.

UniPathway

UPA00109; UER00187.

Gene expression databases

ArrayExpress

P13929.

Bgee

P13929.

CleanEx

HS_ENO3.

Genevestigator

P13929.

GermOnline

ENSG00000108515. 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

CHEMBL2268.

GenomeRNAi

2027.

NextBio

8207.

SOURCE

Search...

Entry information

Entry name

ENOB_HUMAN

Accession

Primary (citable) accession number: P13929
Secondary accession number(s): B4DUI6 , B4DUM6, D3DTL2, E7ENK8, Q96AE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	November 28, 2012
Last modified:	May 1, 2013
This is version 144 of the entry and version 5 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.