ECHS1
From Wikipedia, the free encyclopedia
Enoyl Coenzyme A hydratase, short chain, 1, mitochondrial
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PDB rendering based on 1dub. | ||||||||||||||
Available structures: 1dub, 2dub, 2hw5 | ||||||||||||||
Identifiers | ||||||||||||||
Symbol(s) | ECHS1; SCEH | |||||||||||||
External IDs | OMIM: 602292 MGI: 2136460 HomoloGene: 3018 | |||||||||||||
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RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 1892 | 93747 | ||||||||||||
Ensembl | ENSG00000127884 | ENSMUSG00000025465 | ||||||||||||
Uniprot | P30084 | Q8BU95 | ||||||||||||
Refseq | NM_004092 (mRNA) NP_004083 (protein) |
NM_053119 (mRNA) NP_444349 (protein) |
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Location | Chr 10: 135.03 - 135.04 Mb | Chr 7: 139.96 - 139.97 Mb | ||||||||||||
Pubmed search | [1] | [2] |
Enoyl Coenzyme A hydratase, short chain, 1, mitochondrial, also known as ECHS1, is a human gene.[1]
The protein encoded by this gene functions in the second step of the mitochondrial fatty acid beta-oxidation pathway. It catalyzes the hydration of 2-trans-enoyl-coenzyme A (CoA) intermediates to L-3-hydroxyacyl-CoAs. The gene product is a member of the hydratase/isomerase superfamily. It localizes to the mitochondrial matrix. Transcript variants utilizing alternative transcription initiation sites have been described in the literature.[1]
[edit] References
[edit] Further reading
- Hochstrasser DF, Frutiger S, Paquet N, et al. (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison.". Electrophoresis 13 (12): 992–1001. PMID 1286669.
- Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. PMID 1602151.
- Li J, Norwood DL, Mao LF, Schulz H (1991). "Mitochondrial metabolism of valproic acid.". Biochemistry 30 (2): 388–94. PMID 1988037.
- Jackson S, Schaefer J, Middleton B, Turnbull DM (1995). "Characterisation of a novel enzyme of human fatty acid beta-oxidation: a matrix-associated, mitochondrial 2-enoyl-CoA hydratase.". Biochem. Biophys. Res. Commun. 214 (1): 247–53. PMID 7669045.
- Kanazawa M, Ohtake A, Abe H, et al. (1994). "Molecular cloning and sequence analysis of the cDNA for human mitochondrial short-chain enoyl-CoA hydratase.". Enzyme Protein 47 (1): 9–13. PMID 8012501.
- Janssen U, Davis EM, Le Beau MM, Stoffel W (1997). "Human mitochondrial enoyl-CoA hydratase gene (ECHS1): structural organization and assignment to chromosome 10q26.2-q26.3.". Genomics 40 (3): 470–5. doi: . PMID 9073515.
- Hubbard MJ, McHugh NJ (2001). "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping.". Electrophoresis 21 (17): 3785–96. doi: . PMID 11271497.
- Jiang LQ, Wen SJ, Wang HY, Chen LY (2003). "Screening the proteins that interact with calpain in a human heart cDNA library using a yeast two-hybrid system.". Hypertens. Res. 25 (4): 647–52. PMID 12358155.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi: . PMID 12477932.
- Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10.". Nature 429 (6990): 375–81. doi: . PMID 15164054.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi: . PMID 15489334.
- Bruneel A, Labas V, Mailloux A, et al. (2006). "Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis.". Proteomics 5 (15): 3876–84. doi: . PMID 16130169.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi: . PMID 17353931.
- Takahashi M, Watari E, Shinya E, et al. (2007). "Suppression of virus replication via down-modulation of mitochondrial short chain enoyl-CoA hydratase in human glioblastoma cells.". Antiviral Res. 75 (2): 152–8. doi: . PMID 17395278.