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Identification
HMDB Protein ID HMDBP01085
Secondary Accession Numbers
  • 6374
  • HMDBP06629
Name Beta-enolase
Synonyms
  1. 2-phospho-D-glycerate hydro-lyase
  2. Enolase 3
  3. MSE
  4. Muscle-specific enolase
  5. Skeletal muscle enolase
Gene Name ENO3
Protein Type Unknown
Biological Properties
General Function Involved in magnesium ion binding
Specific Function Appears to have a function in striated muscle development and regeneration.
Pathways
  • glycolysis
  • Glycolysis / Gluconeogenesis
  • HIF-1 signaling pathway
  • RNA degradation
Reactions
2-Phospho-D-glyceric acid → Phosphoenolpyruvic acid + Water details
GO Classification
Biological Process
small molecule metabolic process
skeletal muscle tissue regeneration
glycolysis
response to drug
gluconeogenesis
aging
Cellular Component
cytosol
phosphopyruvate hydratase complex
Component
macromolecular complex
protein complex
phosphopyruvate hydratase complex
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
magnesium ion binding
lyase activity
carbon-oxygen lyase activity
hydro-lyase activity
phosphopyruvate hydratase activity
Molecular Function
magnesium ion binding
phosphopyruvate hydratase activity
Process
metabolic process
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
hexose metabolic process
glucose metabolic process
glucose catabolic process
glycolysis
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 17
Locus 17pter-p11
SNPs ENO3
Gene Sequence
>1305 bp
ATGGCCATGCAGAAAATCTTTGCCCGGGAAATCTTGGACTCCAGGGGCAACCCCACGGTG
GAGGTGGACCTGCACACGGCCAAGGGCCGATTCCGAGCAGCTGTGCCCAGTGGGGCTTCC
ACGGGTATCTATGAGGCTCTGGAACTAAGAGACGGAGACAAAGGCCGCTACCTGGGGAAA
GGAGTCCTGAAGGCTGTGGAGAACATCAACAATACTCTGGGCCCTGCTCTGCTGCAAAAG
AAACTAAGCGTTGTTGATCAAGAAAAAGTTGACAAATTTATGATTGAGCTAGATGGGACC
GAGAATAAGTCCAAGTTTGGGGCCAATGCCATCCTGGGCGTGTCCTTGGCCGTGTGTAAG
GCGGGAGCAGCTGAGAAGGGGGTCCCCCTGTACCGCCACATCGCAGATCTCGCTGGGAAC
CCTGACCTCATACTCCCAGTGCCAGCCTTCAATGTGATCAACGGGGGCTCCCATGCTGGA
AACAACTTGGCCATGCAGGAGTTCATGATTCTGCCTGTGGGAGCCAGCTCCTTCAAGGAA
GCCATGCGCATTGGCGCCGAGGTCTACCACCACCTCAAGGGGGTCATCAAGGCCAAGTAT
GGGAAGGATGCCACCAATGTGGGTGATGAAGGTGGCTTCGCACCCAACATCCTGGAGAAC
AATGAGGCCCTGGAGCTGCTGAAGACGGCCATCCAGGCGGCTGGTTACCCAGACAAGGTG
GTGATCGGCATGGATGTGGCAGCATCTGAGTTCTATCGCAATGGGAAGTACGATCTTGAC
TTCAAGTCGCCTGATGATCCCGCACGGCACATCACTGGGGAGAAGCTCGGAGAGCTGTAT
AAGAGCTTTATCAAGAACTATCCTGTGGTCTCCATCGAAGACCCCTTTGACCAGGATGAC
TGGGCCACTTGGACCTCCTTCCTCTCGGGGGTGAACATCCAGATTGTGGGGGATGACTTG
ACAGTCACCAACCCCAAGAGGATTGCCCAGGCCGTTGAGAAGAAGGCCTGCAACTGTCTG
CTGCTGAAGGTCAACCAGATCGGCTCGGTGACCGAATCGATCCAGGCGTGCAAACTGGCT
CAGTCTAATGGCTGGGGGGTGATGGTGAGCCACCGCTCAGGGGAGACTGAGGACACATTC
ATTGCTGACCTTGTGGTGGGGCTCTGCACAGGACAGATCAAGACTGGCGCCCCCTGCCGC
TCGGAGCGTCTGGCCAAATACAACCAACTCATGAGGATCGAGGAGGCTCTTGGGGACAAG
GCAATCTTTGCTGGACGCAAGTTCCGTAACCCGAAGGCCAAGTGA
Protein Properties
Number of Residues 434
Molecular Weight 42248.03
Theoretical pI 7.97
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Beta-enolase
MAMQKIFAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKGRYLGK
GVLKAVENINSTLGPALLQKKLSVADQEKVDKFMIELDGTENKSKFGANAILGVSLAVCK
AGAAEKGVPLYRHIADLAGNPDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKE
AMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKV
VIGMDVAASEFYRNGKYDLDFKSPDDPARHITGEKLGELYKSFIKNYPVVSIEDPFDQDD
WATWTSFLSGVNIQIVGDDLTVTNPKRIAQAVEKKACNCLLLKVNQIGSVTESIQACKLA
QSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEALGDK
AIFAGRKFRNPKAK
GenBank ID Protein 31170
UniProtKB/Swiss-Prot ID P13929
UniProtKB/Swiss-Prot Entry Name ENOB_HUMAN
PDB IDs
GenBank Gene ID X16504
GeneCard ID ENO3
GenAtlas ID ENO3
HGNC ID HGNC:3354
References
General References
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  3. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed:16625196 ]
  4. Peshavaria M, Hinks LJ, Day IN: Structure of human muscle (beta) enolase mRNA and protein deduced from a genomic clone. Nucleic Acids Res. 1989 Nov 11;17(21):8862. [PubMed:2587223 ]
  5. Cali L, Feo S, Oliva D, Giallongo A: Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE). Nucleic Acids Res. 1990 Apr 11;18(7):1893. [PubMed:2336366 ]
  6. Peshavaria M, Day IN: Molecular structure of the human muscle-specific enolase gene (ENO3). Biochem J. 1991 Apr 15;275 ( Pt 2):427-33. [PubMed:1840492 ]
  7. Giallongo A, Venturella S, Oliva D, Barbieri G, Rubino P, Feo S: Structural features of the human gene for muscle-specific enolase. Differential splicing in the 5'-untranslated sequence generates two forms of mRNA. Eur J Biochem. 1993 Jun 1;214(2):367-74. [PubMed:8513787 ]
  8. Li TB, Liu XH, Feng S, Hu Y, Yang WX, Han Y, Wang YG, Gong LM: Characterization of MR-1, a novel myofibrillogenesis regulator in human muscle. Acta Biochim Biophys Sin (Shanghai). 2004 Jun;36(6):412-8. [PubMed:15188056 ]
  9. Comi GP, Fortunato F, Lucchiari S, Bordoni A, Prelle A, Jann S, Keller A, Ciscato P, Galbiati S, Chiveri L, Torrente Y, Scarlato G, Bresolin N: Beta-enolase deficiency, a new metabolic myopathy of distal glycolysis. Ann Neurol. 2001 Aug;50(2):202-7. [PubMed:11506403 ]