SIRT2

From Wikipedia, the free encyclopedia

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

PDB rendering based on 1j8f.

Available structures: 1j8f

Identifiers

Symbol(s)

SIRT2; SIR2L; SIR2L2

External IDs

OMIM: 604480 MGI: 1927664 HomoloGene: 40823

Gene ontology
Molecular Function:	• DNA binding • transcription factor binding • zinc ion binding • hydrolase activity • NAD-dependent histone deacetylase activity • histone acetyltransferase binding • histone deacetylase binding • tubulin deacetylase activity • ubiquitin binding • metal ion binding
Cellular Component:	• chromatin silencing complex • cytoplasm • cytoskeleton • microtubule
Biological Process:	• chromatin silencing at rDNA • chromatin silencing • chromatin silencing at telomere • regulation of transcription, DNA-dependent • protein amino acid ADP-ribosylation • redox signal response • cell cycle • mitosis • regulation of exit from mitosis • negative regulation of transcription • histone deacetylation • regulation of phosphorylation • negative regulation of striated muscle development • cell division

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_012237 (mRNA)
NP_036369 (protein)

NM_022432 (mRNA)
NP_071877 (protein)

Location

Chr 19: 44.06 - 44.08 Mb

Chr 7: 28.48 - 28.5 Mb

Pubmed search

[1]

[2]

Sirtuin (silent mating type information regulation 2 homolog) 2 (S. cerevisiae), also known as SIRT2, 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. Two transcript variants result from alternative splicing of this gene.^[1]

[edit] References

^ ^a ^b Entrez Gene: SIRT2 sirtuin (silent mating type information regulation 2 homolog) 2 (S. cerevisiae).

[edit] 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.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353-8. PMID 9110174.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.