SIRT3

From Wikipedia, the free encyclopedia

Sirtuin (silent mating type information regulation 2 homolog) 3 (S. cerevisiae)

Identifiers

SIRT3; SIR2L3

External IDs

OMIM: 604481 MGI: 1927665 HomoloGene: 81827

Gene ontology
Molecular Function:	• DNA binding • NAD+ ADP-ribosyltransferase activity • zinc ion binding • hydrolase activity • metal ion binding
Cellular Component:	• chromatin silencing complex • cytoplasm • mitochondrion • membrane
Biological Process:	• chromatin silencing • regulation of transcription, DNA-dependent • protein amino acid ADP-ribosylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001017524 (mRNA)
NP_001017524 (protein)

NM_022433 (mRNA)
NP_071878 (protein)

Location

Chr 11: 0.21 - 0.23 Mb

Chr 7: 140.71 - 140.73 Mb

Pubmed search

[1]

[2]

Sirtuin (silent mating type information regulation 2 homolog) 3 (S. cerevisiae), also known as SIRT3, is a human gene.^[1]

This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family.^[1]

[edit] References

^ ^a ^b Entrez Gene: SIRT3 sirtuin (silent mating type information regulation 2 homolog) 3 (S. cerevisiae).

[edit] Further reading

Scher MB, Vaquero A, Reinberg D (2007). "SirT3 is a nuclear NAD+-dependent histone deacetylase that translocates to the mitochondria upon cellular stress.". Genes Dev. 21 (8): 920–8. doi:10.1101/gad.1527307. PMID 17437997.
Bellizzi D, Dato S, Cavalcante P, et al. (2007). "Characterization of a bidirectional promoter shared between two human genes related to aging: SIRT3 and PSMD13.". Genomics 89 (1): 143–50. doi:10.1016/j.ygeno.2006.09.004. PMID 17059877.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Bellizzi D, Rose G, Cavalcante P, et al. (2005). "A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages.". Genomics 85 (2): 258–63. doi:10.1016/j.ygeno.2004.11.003. PMID 15676284.
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.
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.
Onyango P, Celic I, McCaffery JM, et al. (2002). "SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria.". Proc. Natl. Acad. Sci. U.S.A. 99 (21): 13653–8. doi:10.1073/pnas.222538099. PMID 12374852.
Schwer B, North BJ, Frye RA, et al. (2002). "The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase.". J. Cell Biol. 158 (4): 647–57. doi:10.1083/jcb.200205057. PMID 12186850.
Yang YH, Chen YH, Zhang CY, et al. (2001). "Cloning and characterization of two mouse genes with homology to the yeast Sir2 gene.". Genomics 69 (3): 355–69. doi:10.1006/geno.2000.6360. PMID 11056054.
Frye RA (2000). "Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins.". Biochem. Biophys. Res. Commun. 273 (2): 793–8. doi:10.1006/bbrc.2000.3000. PMID 10873683.
Frye RA (1999). "Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity.". Biochem. Biophys. Res. Commun. 260 (1): 273–9. doi:10.1006/bbrc.1999.0897. PMID 10381378.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.