ACSS2

From Wikipedia, the free encyclopedia

Acyl-CoA synthetase short-chain family member 2

Identifiers

ACSS2; ACS; ACAS2; ACSA; AceCS; DKFZp762G026; MYH7B; dJ1161H23.1

External IDs

OMIM: 605832 MGI: 1890410 HomoloGene: 6469

Gene ontology
Molecular Function:	• catalytic activity • acetate-CoA ligase activity • protein binding • AMP binding • ligase activity
Cellular Component:	• cytoplasm
Biological Process:	• metabolic process • lipid biosynthetic process

Orthologs

Human

Mouse

Refseq

NM_139274 (mRNA)
NP_644803 (protein)

NM_019811 (mRNA)
NP_062785 (protein)

Location

Chr 20: 32.93 - 32.98 Mb

Chr 2: 155.21 - 155.28 Mb

Pubmed search

[1]

[2]

Acyl-CoA synthetase short-chain family member 2, also known as ACSS2, is a human gene.^[1]

This gene encodes a cytosolic enzyme that catalyzes the activation of acetate for use in lipid synthesis and energy generation. The protein acts as a monomer and produces acetyl-CoA from acetate in a reaction that requires ATP. Expression of this gene is regulated by sterol regulatory element-binding proteins, transcription factors that activate genes required for the synthesis of cholesterol and unsaturated fatty acids. Two transcript variants encoding different isoforms have been found for this gene.^[1]

[edit] References

^ ^a ^b Entrez Gene: ACSS2 acyl-CoA synthetase short-chain family member 2.

[edit] Further reading

Schwer B, Bunkenborg J, Verdin RO, et al. (2006). "Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2.". Proc. Natl. Acad. Sci. U.S.A. 103 (27): 10224-9. doi:10.1073/pnas.0603968103. PMID 16788062.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55-65. doi:10.1101/gr.4039406. PMID 16344560.
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.
Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315-23. doi:10.1101/gr.2122004. PMID 15231747.
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.
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.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865-71. doi:10.1038/414865a. PMID 11780052.
Luong A, Hannah VC, Brown MS, Goldstein JL (2000). "Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins.". J. Biol. Chem. 275 (34): 26458-66. doi:10.1074/jbc.M004160200. PMID 10843999.