ACOT2

From Wikipedia, the free encyclopedia

Acyl-CoA thioesterase 2

Identifiers

ACOT2; PTE2; Mte1; ZAP128

External IDs

OMIM: 609972 MGI: 2159605 HomoloGene: 25661

Gene ontology
Molecular Function:	• carboxylesterase activity • palmitoyl-CoA hydrolase activity • hydrolase activity
Cellular Component:	• mitochondrion • peroxisome
Biological Process:	• very-long-chain fatty acid metabolic process • long-chain fatty acid metabolic process • lipid metabolic process • acyl-CoA metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_006821 (mRNA)
NP_006812 (protein)

NM_134188 (mRNA)
NP_598949 (protein)

Location

Chr 14: 73.11 - 73.11 Mb

n/a

Pubmed search

[1]

[2]

Acyl-CoA thioesterase 2, also known as ACOT2, is a human gene.^[1]

[edit] References

^ Entrez Gene: ACOT2 acyl-CoA thioesterase 2.

[edit] Further reading

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:10.1038/msb4100134. PMID 17353931.
Hunt MC, Rautanen A, Westin MA, et al. (2006). "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs.". FASEB J. 20 (11): 1855–64. doi:10.1096/fj.06-6042com. PMID 16940157.
Hunt MC, Yamada J, Maltais LJ, et al. (2005). "A revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases.". J. Lipid Res. 46 (9): 2029–32. doi:10.1194/jlr.E500003-JLR200. PMID 16103133.
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:10.1101/gr.2596504. PMID 15489334.
Westin MA, Alexson SE, Hunt MC (2004). "Molecular cloning and characterization of two mouse peroxisome proliferator-activated receptor alpha (PPARalpha)-regulated peroxisomal acyl-CoA thioesterases.". J. Biol. Chem. 279 (21): 21841–8. doi:10.1074/jbc.M313863200. PMID 15007068.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
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:10.1073/pnas.242603899. PMID 12477932.
Jones JM, Gould SJ (2000). "Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase.". Biochem. Biophys. Res. Commun. 275 (1): 233–40. doi:10.1006/bbrc.2000.3285. PMID 10944470.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Sherrington R, Rogaev EI, Liang Y, et al. (1995). "Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease.". Nature 375 (6534): 754–60. doi:10.1038/375754a0. PMID 7596406.