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Gene Ontology Classifications
Symbol
Name
ID
Sirt1
sirtuin 1
MGI:2135607

Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Sirt1. (This text reflects annotations as of Thursday, July 24, 2014.)
Summary from NCBI RefSeq


[Summary is not available for the mouse gene. This summary is for the human ortholog.] 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. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2008]
Summary text based on GO annotations supported by experimental evidence in mouse
Summary text based on GO annotations supported by experimental evidence in other organisms
Summary text based on GO annotations supported by structural data
Summary text for additional MGI annotations
References
  1. . () , :. (PubMed:)
  2. Asher G et al. (2008) SIRT1 regulates circadian clock gene expression through PER2 deacetylation. Cell, 134:317-28. (PubMed:18662546)
  3. Chanda D et al. (2010) Transcriptional corepressor SHP recruits SIRT1 histone deacetylase to inhibit LRH-1 transactivation. Nucleic Acids Res, 38:4607-19. (PubMed:20375098)
  4. Chen WY et al. (2005) Tumor suppressor HIC1 directly regulates SIRT1 to modulate p53-dependent DNA-damage responses. Cell, 123:437-48. (PubMed:16269335)
  5. Daitoku H et al. (2004) Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity. Proc Natl Acad Sci U S A, 101:10042-7. (PubMed:15220471)
  6. Gerhart-Hines Z et al. (2007) Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC-1alpha. EMBO J, 26:1913-23. (PubMed:17347648)
  7. Ghosh HS et al. (2010) SIRT1 negatively regulates the mammalian target of rapamycin. PLoS One, 5:e9199. (PubMed:20169165)
  8. Grimm AA et al. (2011) A nutrient-sensitive interaction between Sirt1 and HNF-1alpha regulates Crp expression. Aging Cell, 10:305-17. (PubMed:21176092)
  9. Guo X et al. (2010) DYRK1A and DYRK3 promote cell survival through phosphorylation and activation of SIRT1. J Biol Chem, 285:13223-32. (PubMed:20167603)
  10. Imai S et al. (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature, 403:795-800. (PubMed:10693811)
  11. Kang H et al. (2009) CK2 is the regulator of SIRT1 substrate-binding affinity, deacetylase activity and cellular response to DNA-damage. PLoS One, 4:e6611. (PubMed:19680552)
  12. Kornberg MD et al. (2010) GAPDH mediates nitrosylation of nuclear proteins. Nat Cell Biol, 12:1094-100. (PubMed:20972425)
  13. Kume S et al. (2007) SIRT1 inhibits transforming growth factor beta-induced apoptosis in glomerular mesangial cells via Smad7 deacetylation. J Biol Chem, 282:151-8. (PubMed:17098745)
  14. Lan F et al. (2008) SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation. J Biol Chem, 283:27628-35. (PubMed:18687677)
  15. Lee IH et al. (2008) A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy. Proc Natl Acad Sci U S A, 105:3374-9. (PubMed:18296641)
  16. Li X et al. (2007) SIRT1 deacetylates and positively regulates the nuclear receptor LXR. Mol Cell, 28:91-106. (PubMed:17936707)
  17. Libert S et al. (2011) SIRT1 Activates MAO-A in the Brain to Mediate Anxiety and Exploratory Drive. Cell, 147:1459-72. (PubMed:22169038)
  18. Luo J et al. (2001) Negative Control of p53 by Sir2alpha Promotes Cell Survival under Stress. Cell, 107:137-48. (PubMed:11672522)
  19. McBurney MW et al. (2003) The mammalian SIR2alpha protein has a role in embryogenesis and gametogenesis. Mol Cell Biol, 23:38-54. (PubMed:12482959)
  20. Ming M et al. (2010) Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C. Proc Natl Acad Sci U S A, 107:22623-8. (PubMed:21149730)
  21. Nakahata Y et al. (2008) The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control. Cell, 134:329-40. (PubMed:18662547)
  22. Nemoto S et al. (2005) SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1{alpha}. J Biol Chem, 280:16456-60. (PubMed:15716268)
  23. Parker JA et al. (2012) Integration of beta-Catenin, Sirtuin, and FOXO Signaling Protects from Mutant Huntingtin Toxicity. J Neurosci, 32:12630-40. (PubMed:22956852)
  24. Picard F et al. (2004) Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma. Nature, 429:771-6. (PubMed:15175761)
  25. Ponugoti B et al. (2010) SIRT1 deacetylates and inhibits SREBP-1C activity in regulation of hepatic lipid metabolism. J Biol Chem, 285:33959-70. (PubMed:20817729)
  26. Powell MJ et al. (2011) Disruption of a Sirt1-dependent autophagy checkpoint in the prostate results in prostatic intraepithelial neoplasia lesion formation. Cancer Res, 71:964-75. (PubMed:21189328)
  27. Qiang L et al. (2012) Brown remodeling of white adipose tissue by SirT1-dependent deacetylation of Ppargamma. Cell, 150:620-32. (PubMed:22863012)
  28. Rajamohan SB et al. (2009) SIRT1 promotes cell survival under stress by deacetylation-dependent deactivation of poly(ADP-ribose) polymerase 1. Mol Cell Biol, 29:4116-29. (PubMed:19470756)
  29. Revollo JR et al. (2004) The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells. J Biol Chem, 279:50754-63. (PubMed:15381699)
  30. Rodgers JT et al. (2005) Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature, 434:113-8. (PubMed:15744310)
  31. Satoh A et al. (2010) SIRT1 promotes the central adaptive response to diet restriction through activation of the dorsomedial and lateral nuclei of the hypothalamus. J Neurosci, 30:10220-32. (PubMed:20668205)
  32. Tanno M et al. (2007) Nucleocytoplasmic shuttling of the NAD+-dependent histone deacetylase SIRT1. J Biol Chem, 282:6823-32. (PubMed:17197703)
  33. Tiberi L et al. (2012) BCL6 controls neurogenesis through Sirt1-dependent epigenetic repression of selective Notch targets. Nat Neurosci, 15:1627-35. (PubMed:23160044)
  34. Vaquero A et al. (2007) SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation. Nature, 450:440-4. (PubMed:18004385)
  35. Vaziri H et al. (2001) hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell, 107:149-59. (PubMed:11672523)
  36. Wang C et al. (2006) Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage. Nat Cell Biol, 8:1025-31. (PubMed:16892051)
  37. Wong S et al. (2007) Deacetylation of the retinoblastoma tumour suppressor protein by SIRT1. Biochem J, 407:451-60. (PubMed:17620057)
  38. Yuan Z et al. (2007) SIRT1 regulates the function of the Nijmegen breakage syndrome protein. Mol Cell, 27:149-62. (PubMed:17612497)
  39. Zhang J. (2007) The direct involvement of SirT1 in insulin-induced insulin receptor substrate-2 tyrosine phosphorylation. J Biol Chem, 282:34356-64. (PubMed:17901049)
  40. Zhang R et al. (2010) SIRT1 suppresses activator protein-1 transcriptional activity and cyclooxygenase-2 expression in macrophages. J Biol Chem, 285:7097-110. (PubMed:20042607)
  41. Zhou Y et al. (2009) Reversible acetylation of the chromatin remodelling complex NoRC is required for non-coding RNA-dependent silencing. Nat Cell Biol, 11:1010-6. (PubMed:19578370)



Go Annotations in Tabular Form (Text View) (GO Graph)

 
 


Gene Ontology Evidence Code Abbreviations:

  EXP Inferred from experiment
  IC Inferred by curator
  IDA Inferred from direct assay
  IEA Inferred from electronic annotation
  IGI Inferred from genetic interaction
  IMP Inferred from mutant phenotype
  IPI Inferred from physical interaction
  ISS Inferred from sequence or structural similarity
  ISO Inferred from sequence orthology
  ISA Inferred from sequence alignment
  ISM Inferred from sequence model
  NAS Non-traceable author statement
  ND No biological data available
  RCA Reviewed computational analysis
  TAS Traceable author statement


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Mouse Genome Database (MGD), Gene Expression Database (GXD), Mouse Tumor Biology (MTB), Gene Ontology (GO), MouseCyc
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last database update
11/18/2014
MGI 5.20
The Jackson Laboratory