SIRT2

Sirtuin (silent mating type information regulation 2 homolog) 2 (S. cerevisiae)
File:PBB Protein SIRT2 image.jpg PDB rendering based on 1j8f.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1j8f​
Identifiers
Symbols	SIRT2 ; SIR2L; SIR2L2
External IDs	Template:OMIM5 Template:MGI HomoloGene: 40823
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE SIRT2 220605 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Sirtuin (silent mating type information regulation 2 homolog) 2 (S. cerevisiae), also known as SIRT2, is a human gene.

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. Two transcript variants result from alternative splicing of this gene.

Further reading

• 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.
• Andersson B, Wentland MA, Ricafrente JY; et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yu W, Andersson B, Worley KC; et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. PMID 9110174.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.
• Afshar G, Murnane JP (1999). "Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2". Gene. 234 (1): 161–8. PMID 10393250.
• 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.
• Hu RM, Han ZG, Song HD; et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. doi:10.1073/pnas.160270997. PMID 10931946.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Finnin MS, Donigian JR, Pavletich NP (2001). "Structure of the histone deacetylase SIRT2". Nat. Struct. Biol. 8 (7): 621–5. doi:10.1038/89668. PMID 11427894.CS1 maint: Multiple names: authors list (link)
• Grozinger CM, Chao ED, Blackwell HE; et al. (2001). "Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening". J. Biol. Chem. 276 (42): 38837–43. doi:10.1074/jbc.M106779200. PMID 11483616.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Borra MT, O'Neill FJ, Jackson MD; et al. (2002). "Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases". J. Biol. Chem. 277 (15): 12632–41. doi:10.1074/jbc.M111830200. PMID 11812793.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• De Smet C, Nishimori H, Furnari FB; et al. (2002). "A novel seven transmembrane receptor induced during the early steps of astrocyte differentiation identified by differential expression". J. Neurochem. 81 (3): 575–88. PMID 12065666.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• North BJ, Marshall BL, Borra MT; et al. (2003). "The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase". Mol. Cell. 11 (2): 437–44. PMID 12620231.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Dryden SC, Nahhas FA, Nowak JE; et al. (2003). "Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle". Mol. Cell. Biol. 23 (9): 3173–85. PMID 12697818.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fulco M, Schiltz RL, Iezzi S; et al. (2003). "Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state". Mol. Cell. 12 (1): 51–62. PMID 12887892.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hiratsuka M, Inoue T, Toda T; et al. (2003). "Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene". Biochem. Biophys. Res. Commun. 309 (3): 558–66. PMID 12963026.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• van der Horst A, Tertoolen LG, de Vries-Smits LM; et al. (2004). "FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1)". J. Biol. Chem. 279 (28): 28873–9. doi:10.1074/jbc.M401138200. PMID 15126506.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bae NS, Swanson MJ, Vassilev A, Howard BH (2005). "Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10". J. Biochem. 135 (6): 695–700. doi:10.1093/jb/mvh084. PMID 15213244.CS1 maint: Multiple names: authors list (link)