Reviewed, UniProtKB/Swiss-Prot P13929 (ENOB_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-enolase
    EC=4.2.1.11
Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Muscle-specific enolase
      Short name=MSE
    Skeletal muscle enolase
    Enolase 3

Gene names

Name:

ENO3

Organism

Homo sapiens (Human) [Complete proteome]

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	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.8
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	Defects in ENO3 are the cause of glycogen storage disease type 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.
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	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphopyruvate hydratase activity Ref.4 Traceable author statement. 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: GVLKAVENINSTLGPALLQKKLSVADQEKVDKFMIELDGTENKS → 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	S → N: dbSNP rs238238. Ref.1 Ref.2 Ref.3		VAR_020618
	Natural variant	85	1	A → V: dbSNP rs238239. Ref.1 Ref.3		VAR_020619
	Natural variant	156	1	G → D in GSD13; when associated with E-374.		VAR_020620
	Natural variant	374	1	G → E in GSD13; when associated with D-156.		VAR_020621

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 28, 2009. Version 4. Checksum: 366B189FFEFE2644	FASTA	434	46,932
	10 20 30 40 50 60 MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKGRYLGK 70 80 90 100 110 120 GVLKAVENIN STLGPALLQK KLSVADQEKV 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. Checksum: E7DC957936D1E889	FASTA	406	44,059
	10 20 30 40 50 60 MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKGRYLGK 70 80 90 100 110 120 GVLKAVENIN STLGPALLQK KLSVADQEKV 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. 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: 2587223] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASN-71 AND VAL-85.
[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: 2336366] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-71.
[3]	"Molecular structure of the human muscle-specific enolase gene (ENO3)." Peshavaria M., Day I.N.M. Biochem. J. 275:427-433(1991) [PubMed: 1840492] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS ASN-71 AND VAL-85.
[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: 8513787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). 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: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 1). Tissue: Muscle.
[8]	"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: 15188056] [Abstract] Cited for: INTERACTION WITH PNKD.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"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: 11506403] [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. AC109333 Genomic DNA. No translation available. BC017249 mRNA. Translation: AAH17249.1.
IPI	IPI00218474. IPI00909949. IPI00942494.
PIR	S06756.
RefSeq	NP_001967.2. NP_443739.2.
UniGene	Hs.224171
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P13929.
PTM databases
PhosphoSite	P13929.
Proteomic databases
PRIDE	P13929.
Genome annotation databases
Ensembl	ENST00000323997; ENSP00000324105; ENSG00000108515; Homo sapiens. [Genome view] ENST00000381335; ENSP00000370739; ENSG00000108515; Homo sapiens. [Genome view]
GeneID	2027.
KEGG	hsa:2027.
UCSC	uc002gab.2. human.
Organism-specific databases
CTD	2027.
GeneCards	GC17P004795.
HGNC	HGNC:3354. ENO3.
HPA	HPA000793.
MIM	131370. gene. 612932. phenotype.
Orphanet	299. Enolase deficiency.
PharmGKB	PA27789.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08456.
HOGENOM	HBG726599.
HOVERGEN	P13929.
InParanoid	P13929.
OrthoDB	EOG9B5RQC.
PhylomeDB	P13929.
Enzyme and pathway databases
BRENDA	4.2.1.11. 247.
Reactome	REACT_1505. Integration of energy metabolism. REACT_15380. Diabetes pathways. REACT_474. Metabolism of carbohydrates.
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]
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 Resources
NextBio	8207.
SOURCE	Search...

Entry information

Entry name

ENOB_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	July 28, 2009
Last modified:	February 9, 2010
This is version 114 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.