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Q96EB6

- SIR1_HUMAN

UniProt

Q96EB6 - SIR1_HUMAN

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Protein
NAD-dependent protein deacetylase sirtuin-1
Gene
SIRT1, SIR2L1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metobolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD+/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD+/NADP+ ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. Deacetylates H2A and 'Lys-26' of HIST1H1E. Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting. Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability. Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis. Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation. Involved in HES1- and HEY2-mediated transcriptional repression. In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62'. Deacetylates MEF2D. Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3. Represses HNF1A-mediated transcription. Required for the repression of ESRRG by CREBZF. Modulates AP-1 transcription factor activity. Deacetylates NR1H3 AND NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteosomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed. Involved in lipid metabolism. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2. Deacetylates ACSS2 leading to its activation, and HMGCS1. Involved in liver and muscle metabolism. Through deacteylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletel muscle under low-glucose conditions and is involved in glucose homeostasis. Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression. Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and faciliting recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2. Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1. Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear. In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability. Deacteylates MECOM/EVI1. Isoform 2 is shown to deacetylate 'Lys-382' of p53/TP53, however with lower activity than isoform 1. In combination, the two isoforms exert an additive effect. Isoform 2 regulates p53/TP53 expression and cellular stress response and is in turn repressed by p53/TP53 presenting a SIRT1 isoform-dependent auto-regulatory loop. In case of HIV-1 infection, interacts with and deacetylates the viral Tat protein. The viral Tat protein inhibits SIRT1 deacetylation activity toward RELA/NF-kappa-B p65, thereby potentiates its transcriptional activity and SIRT1 is proposed to contribute to T-cell hyperactivation during infection. Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization. During the neurogenic transition, repress selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation.50 Publications
SirtT1 75 kDa fragment: catalytically inactive 75SirT1 may be involved in regulation of apoptosis. May be involved in protecting chondrocytes from apoptotic death by associating with cytochrome C and interfering with apoptosome assembly.50 Publications

Catalytic activityi

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.1 Publication

Cofactori

Binds 1 zinc ion per subunit By similarity.

Enzyme regulationi

Inhibited by nicotinamide. Activated by resveratrol (3,5,4'-trihydroxy-trans-stilbene), butein (3,4,2',4'-tetrahydroxychalcone), piceatannol (3,5,3',4'-tetrahydroxy-trans-stilbene), Isoliquiritigenin (4,2',4'-trihydroxychalcone), fisetin (3,7,3',4'-tetrahydroxyflavone) and quercetin (3,5,7,3',4'-pentahydroxyflavone). MAPK8/JNK1 and RPS19BP1/AROS act as positive regulators of deacetylation activity. Negatively regulated by CCAR2.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei363 – 3631Proton acceptor
Metal bindingi371 – 3711Zinc By similarity
Metal bindingi374 – 3741Zinc By similarity
Metal bindingi395 – 3951Zinc By similarity
Metal bindingi398 – 3981Zinc By similarity
Binding sitei482 – 4821NAD; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi261 – 28020NAD By similarity
Add
BLAST
Nucleotide bindingi345 – 3484NAD By similarity
Nucleotide bindingi440 – 4423NAD By similarity
Nucleotide bindingi465 – 4673NAD By similarity

GO - Molecular functioni

  1. HLH domain binding Source: BHF-UCL
  2. NAD+ binding Source: InterPro
  3. NAD-dependent histone deacetylase activity Source: BHF-UCL
  4. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB
  5. NAD-dependent protein deacetylase activity Source: UniProtKB
  6. bHLH transcription factor binding Source: UniProtKB
  7. deacetylase activity Source: UniProtKB
  8. enzyme binding Source: UniProt
  9. histone binding Source: BHF-UCL
  10. histone deacetylase activity Source: BHF-UCL
  11. identical protein binding Source: BHF-UCL
  12. keratin filament binding Source: UniProt
  13. metal ion binding Source: UniProtKB-KW
  14. mitogen-activated protein kinase binding Source: BHF-UCL
  15. p53 binding Source: BHF-UCL
  16. protein C-terminus binding Source: UniProtKB
  17. protein binding Source: UniProtKB
  18. protein deacetylase activity Source: UniProtKB
  19. transcription corepressor activity Source: BHF-UCL
  20. transcription factor binding Source: UniProt
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: BHF-UCL
  2. DNA replication Source: BHF-UCL
  3. DNA synthesis involved in DNA repair Source: UniProtKB
  4. angiogenesis Source: UniProtKB
  5. cell aging Source: BHF-UCL
  6. cellular glucose homeostasis Source: UniProtKB
  7. cellular response to DNA damage stimulus Source: UniProtKB
  8. cellular response to hydrogen peroxide Source: BHF-UCL
  9. cellular response to hypoxia Source: UniProtKB
  10. cellular response to ionizing radiation Source: UniProtKB
  11. cellular response to starvation Source: BHF-UCL
  12. cellular response to tumor necrosis factor Source: UniProtKB
  13. cellular triglyceride homeostasis Source: UniProtKB
  14. cholesterol homeostasis Source: UniProtKB
  15. chromatin organization Source: UniProt
  16. chromatin silencing Source: ProtInc
  17. chromatin silencing at rDNA Source: UniProtKB
  18. establishment of chromatin silencing Source: BHF-UCL
  19. fatty acid homeostasis Source: UniProtKB
  20. histone H3 deacetylation Source: BHF-UCL
  21. histone deacetylation Source: UniProtKB
  22. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  23. maintenance of chromatin silencing Source: BHF-UCL
  24. methylation-dependent chromatin silencing Source: UniProtKB
  25. muscle organ development Source: UniProtKB-KW
  26. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
  27. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  28. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  29. negative regulation of TOR signaling Source: UniProtKB
  30. negative regulation of androgen receptor signaling pathway Source: BHF-UCL
  31. negative regulation of apoptotic process Source: UniProtKB
  32. negative regulation of cAMP-dependent protein kinase activity Source: UniProtKB
  33. negative regulation of cell growth Source: BHF-UCL
  34. negative regulation of cellular response to testosterone stimulus Source: BHF-UCL
  35. negative regulation of cellular senescence Source: UniProtKB
  36. negative regulation of fat cell differentiation Source: BHF-UCL
  37. negative regulation of helicase activity Source: UniProtKB
  38. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
  39. negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress Source: BHF-UCL
  40. negative regulation of peptidyl-lysine acetylation Source: UniProtKB
  41. negative regulation of phosphorylation Source: UniProtKB
  42. negative regulation of prostaglandin biosynthetic process Source: UniProtKB
  43. negative regulation of protein kinase B signaling Source: UniProtKB
  44. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  45. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  46. negative regulation of transcription, DNA-templated Source: BHF-UCL
  47. negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  48. ovulation from ovarian follicle Source: Ensembl
  49. peptidyl-lysine acetylation Source: UniProtKB
  50. peptidyl-lysine deacetylation Source: BHF-UCL
  51. positive regulation of DNA repair Source: UniProtKB
  52. positive regulation of MHC class II biosynthetic process Source: UniProtKB
  53. positive regulation of adaptive immune response Source: UniProtKB
  54. positive regulation of apoptotic process Source: UniProtKB
  55. positive regulation of cAMP-dependent protein kinase activity Source: UniProtKB
  56. positive regulation of cell proliferation Source: UniProtKB
  57. positive regulation of cellular senescence Source: UniProtKB
  58. positive regulation of cholesterol efflux Source: UniProtKB
  59. positive regulation of chromatin silencing Source: BHF-UCL
  60. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  61. positive regulation of histone H3-K9 methylation Source: UniProt
  62. positive regulation of insulin receptor signaling pathway Source: UniProtKB
  63. positive regulation of macroautophagy Source: UniProtKB
  64. positive regulation of macrophage apoptotic process Source: UniProtKB
  65. positive regulation of protein phosphorylation Source: UniProtKB
  66. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  67. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  68. protein deacetylation Source: UniProtKB
  69. protein destabilization Source: UniProtKB
  70. protein ubiquitination Source: UniProtKB
  71. pyrimidine dimer repair by nucleotide-excision repair Source: UniProtKB
  72. rRNA processing Source: UniProtKB-KW
  73. regulation of bile acid biosynthetic process Source: UniProtKB
  74. regulation of cell proliferation Source: BHF-UCL
  75. regulation of endodeoxyribonuclease activity Source: UniProtKB
  76. regulation of glucose metabolic process Source: UniProtKB
  77. regulation of mitotic cell cycle Source: UniProtKB
  78. regulation of peroxisome proliferator activated receptor signaling pathway Source: BHF-UCL
  79. regulation of protein import into nucleus, translocation Source: UniProtKB
  80. regulation of smooth muscle cell apoptotic process Source: UniProtKB
  81. response to hydrogen peroxide Source: UniProtKB
  82. response to insulin Source: UniProtKB
  83. response to oxidative stress Source: UniProtKB
  84. single strand break repair Source: UniProtKB
  85. spermatogenesis Source: Ensembl
  86. transcription, DNA-templated Source: UniProtKB-KW
  87. triglyceride mobilization Source: BHF-UCL
  88. viral process Source: UniProtKB-KW
  89. white fat cell differentiation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase

Keywords - Biological processi

Apoptosis, Differentiation, Host-virus interaction, Myogenesis, rRNA processing, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiREACT_200780. Regulation of HSF1-mediated heat shock response.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
SignaLinkiQ96EB6.

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent protein deacetylase sirtuin-1 (EC:3.5.1.-)
Short name:
hSIRT1
Alternative name(s):
Regulatory protein SIR2 homolog 1
SIR2-like protein 1
Short name:
hSIR2
Cleaved into the following chain:
SirtT1 75 kDa fragment
Short name:
75SirT1
Gene namesi
Name:SIRT1
Synonyms:SIR2L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:14929. SIRT1.

Subcellular locationi

NucleusPML body. Cytoplasm
Note: Recruited to the nuclear bodies via its interaction with PML. Colocalized with APEX1 in the nucleus. May be found in nucleolus, nuclear euchromatin, heterochromatin and inner membrane. Shuttles between nucleus and cytoplasm.7 Publications
Chain SirtT1 75 kDa fragment : Cytoplasm. Mitochondrion 7 Publications

GO - Cellular componenti

  1. PML body Source: BHF-UCL
  2. chromatin silencing complex Source: UniProtKB
  3. cytoplasm Source: BHF-UCL
  4. mitochondrion Source: HPA
  5. nuclear chromatin Source: BHF-UCL
  6. nuclear envelope Source: BHF-UCL
  7. nuclear euchromatin Source: UniProtKB
  8. nuclear heterochromatin Source: UniProtKB
  9. nuclear inner membrane Source: UniProtKB
  10. nucleolus Source: BHF-UCL
  11. nucleoplasm Source: UniProtKB
  12. nucleus Source: UniProtKB
  13. rDNA heterochromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271S → A: Greatly diminishes phosphorylation by MAPK8; when associated with A-47 and A-530. 1 Publication
Mutagenesisi47 – 471S → A: Blocks residue phosphorylation, restores deacetylation activity and inhibits DNA damage-induced apoptosis. 2 Publications
Mutagenesisi47 – 471S → A: Greatly diminishes phosphorylation by MAPK8; when associated with A-27 and A-530. 2 Publications
Mutagenesisi233 – 2331K → R: Impairs in vitro methylation by SETD7; when associated with R-235, R-236 and R-238. 1 Publication
Mutagenesisi235 – 2351K → R: Impairs in vitro methylation by SETD7; when associated with R-233, R-236 and R-238. 1 Publication
Mutagenesisi236 – 2361K → R: Impairs in vitro methylation by SETD7; when associated with R-233, R-235 and R-238. 1 Publication
Mutagenesisi238 – 2381K → R: Impairs in vitro methylation by SETD7; when associated with R-233, R-235a and R-236. 1 Publication
Mutagenesisi363 – 3631H → Y: Loss of function. Reduces the interaction with CCAR2 and APEX1. Increases acetylation of APEX1. 7 Publications
Mutagenesisi474 – 4741F → A: Abolishes phosphorylation at Ser-47, restores deacetylation activity and inhibits DNA damage-induced apoptosis. 1 Publication
Mutagenesisi530 – 5301T → A: Greatly diminishes phosphorylation by MAPK8; when associated with A-27 and A-47. 2 Publications
Mutagenesisi530 – 5301T → A: Reduces in vitro phosphorylation by CDK1. Impairs cell proliferation and cell cycle progression; when associated with A-540. 2 Publications
Mutagenesisi540 – 5401S → A: Reduces in vitro phosphorylation by CDK1. Impairs cell proliferation and cell cycle progression; when associated with A-530. 1 Publication
Mutagenesisi659 – 6591S → A: Reduces in vitro phosphorylation by CaMK2; when associated with S-661. Greatly reduces in vivo phosphorylation; when associated with A-661. 1 Publication
Mutagenesisi661 – 6611S → A: Reduces in vitro phosphorylation by CaMK2; when associated with S-659. Greatly reduces in vivo phosphorylation; when associated with A-659. 1 Publication
Mutagenesisi684 – 6841S → A: No effect on phosphorylation (in vitro and in vivo). 1 Publication

Organism-specific databases

PharmGKBiPA37935.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 747746NAD-dependent protein deacetylase sirtuin-1
PRO_0000110256Add
BLAST
Chaini2 – 533532SirtT1 75 kDa fragment
PRO_0000415289Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei14 – 141Phosphoserine3 Publications
Modified residuei26 – 261Phosphoserine1 Publication
Modified residuei27 – 271Phosphoserine; by MAPK83 Publications
Modified residuei47 – 471Phosphoserine; by MAPK87 Publications
Modified residuei159 – 1591Phosphoserine Inferred
Modified residuei162 – 1621Phosphoserine Inferred
Modified residuei172 – 1721Phosphoserine1 Publication
Modified residuei173 – 1731Phosphoserine1 Publication
Modified residuei395 – 3951S-nitrosocysteine By similarity
Modified residuei398 – 3981S-nitrosocysteine By similarity
Modified residuei530 – 5301Phosphothreonine; by DYRK1A, DYRK3 and MAPK83 Publications
Modified residuei535 – 5351Phosphoserine1 Publication
Modified residuei544 – 5441Phosphothreonine Inferred
Modified residuei545 – 5451Phosphoserine Inferred
Modified residuei659 – 6591Phosphoserine; by CaMK2 By similarity
Modified residuei661 – 6611Phosphoserine; by CaMK2 Inferred
Modified residuei719 – 7191Phosphothreonine4 Publications
Modified residuei747 – 7471Phosphoserine1 Publication

Post-translational modificationi

Methylated on multiple lysine residues; methylation is enhanced after DNA damage and is dispensable for deacetylase activity toward p53/TP53.
Phosphorylated. Phosphorylated by STK4/MST1, resulting in inhibition of SIRT1-mediated p53/TP53 deacetylation. Phosphorylation by MAPK8/JNK1 at Ser-27, Ser-47, and Thr-530 leads to increased nuclear localization and enzymatic activity. Phosphorylation at Thr-530 by DYRK1A and DYRK3 activates deacetylase activity and promotes cell survival. Phosphorylation by mammalian target of rapamycin complex 1 (mTORC1) at Ser-47 inhibits deacetylation activity. Phosphorylated by CaMK2, leading to increased p53/TP53 and NF-kappa-B p65/RELA deacetylation activity By similarity. Phosphorylation at Ser-27 implicating MAPK9 is linked to protein stability. There is some ambiguity for some phosphosites: Ser-159/Ser-162 and Thr-544/Ser-545.6 Publications
Proteolytically cleaved by cathepsin B upon TNF-alpha treatment to yield catalytic inactive but stable SirtT1 75 kDa fragment (75SirT1).1 Publication
S-nitrosylated by GAPDH, leading to inhibit the NAD-dependent protein deacetylase activity By similarity.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiQ96EB6.
PaxDbiQ96EB6.
PeptideAtlasiQ96EB6.
PRIDEiQ96EB6.

PTM databases

PhosphoSiteiQ96EB6.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Inductioni

Up-regulated by methyl methanesulfonate (MMS). In H293T cells by presence of rat calorie restriction (CR) serum.7 Publications

Gene expression databases

ArrayExpressiQ96EB6.
BgeeiQ96EB6.
CleanExiHS_SIRT1.
GenevestigatoriQ96EB6.

Organism-specific databases

HPAiCAB003855.
HPA006295.
HPA052351.

Interactioni

Subunit structurei

Found in a complex with PCAF and MYOD1. Interacts with FOXO1; the interaction deacetylates FOXO1, resulting in its nuclear retention and promotion of its transcriptional activity Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8. Interacts with HES1, HEY2 and PML. Interacts with RPS19BP1/AROS. Interacts with CCAR2 (via N-terminus); the interaction disrupts the interaction between SIRT1 and p53/TP53. Interacts with SETD7; the interaction induces the dissociation of SIRT1 from p53/TP53 and increases p53/TP53 activity. Interacts with MYCN, NR1I2, CREBZF, TSC2, TLE1, FOS, JUN, NR0B2, PPARG, NCOR, IRS1, IRS2 and NMNAT1. Interacts with HNF1A; the interaction occurs under nutrient restriction. Interacts with SUZ12; the interaction mediates the association with the PRC4 histone methylation complex which is specific as an association with PCR2 and PCR3 complex variants is not found. Interacts with HIV-1 tat. Interacts with BCL6; leads to a epigenetic repression of specific target genes.24 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACACAQ130853EBI-1802965,EBI-717681
AKT1P317495EBI-1802965,EBI-296087
APEX1P276956EBI-1802965,EBI-1048805
CCAR2Q8N1639EBI-1802965,EBI-355410
CIITAP330764EBI-1802965,EBI-1538819
CREBZFQ9NS373EBI-1802965,EBI-632965
CSNK2A1P684004EBI-1802965,EBI-347804
CSNK2BP678705EBI-1802965,EBI-348169
DNMT1P2635811EBI-1802965,EBI-719459
E2F1Q010943EBI-1802965,EBI-448924
EP300Q094722EBI-1802965,EBI-447295
FHL2Q141922EBI-1802965,EBI-701903
FOXO1Q127783EBI-1802965,EBI-1108782
Foxo1Q9R1E02EBI-1802965,EBI-1371343From a different organism.
FOXO3O435245EBI-1802965,EBI-1644164
FOXO4P981773EBI-1802965,EBI-4481939
HCFC1P516102EBI-1802965,EBI-396176
HES1Q144694EBI-1802965,EBI-2832522
HEY2Q9UBP53EBI-1802965,EBI-750630
IRS2Q9Y4H22EBI-1802965,EBI-1049582
KAT2BQ928313EBI-1802965,EBI-477430
MECOMQ031122EBI-1802965,EBI-1384862
MTORP423452EBI-1802965,EBI-359260
MYCP011064EBI-1802965,EBI-447544
MYCNP041983EBI-1802965,EBI-878369
NBNO609345EBI-1802965,EBI-494844
Ncor1Q609742EBI-1802965,EBI-349004From a different organism.
NHLH2Q025772EBI-1802965,EBI-5378683
NMNAT1Q9HAN93EBI-1802965,EBI-3917542
NR0B2Q154666EBI-1802965,EBI-3910729
Nr1h2Q606442EBI-1802965,EBI-5276809From a different organism.
Nr1h3Q9Z0Y92EBI-1802965,EBI-5276764From a different organism.
PIK3R1P279863EBI-1802965,EBI-79464
PpargP372383EBI-1802965,EBI-5260705From a different organism.
PpargP37238-12EBI-1802965,EBI-6267861From a different organism.
RARAP102763EBI-1802965,EBI-413374
RELAQ042064EBI-1802965,EBI-73886
RPS19BP1Q86WX311EBI-1802965,EBI-4479407
RPTORQ8N1223EBI-1802965,EBI-1567928
RRP8O431593EBI-1802965,EBI-2008793
SNW1Q135737EBI-1802965,EBI-632715
SREBF1P36956-32EBI-1802965,EBI-948338
Suv39h1O548644EBI-1802965,EBI-302230From a different organism.
tatP046083EBI-1802965,EBI-6164389From a different organism.
TLE1Q047244EBI-1802965,EBI-711424
TP53P0463713EBI-1802965,EBI-366083
TP73O153504EBI-1802965,EBI-389606
TSC2P498152EBI-1802965,EBI-396587
WRNQ141919EBI-1802965,EBI-368417
XPAP230258EBI-1802965,EBI-295222
XRCC6P129567EBI-1802965,EBI-353208

Protein-protein interaction databases

BioGridi116983. 269 interactions.
DIPiDIP-29757N.
IntActiQ96EB6. 112 interactions.
MINTiMINT-3052322.
STRINGi9606.ENSP00000212015.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi243 – 25210
Beta strandi254 – 2607
Helixi262 – 2687
Beta strandi273 – 2753
Turni276 – 2783
Helixi279 – 2868
Beta strandi290 – 2923
Helixi293 – 2975
Helixi299 – 3046
Helixi307 – 3126
Helixi313 – 3164
Beta strandi318 – 3203
Helixi325 – 33511
Beta strandi339 – 3446
Helixi350 – 3545
Beta strandi358 – 3614
Beta strandi364 – 3718
Turni372 – 3743
Beta strandi377 – 3793
Helixi380 – 3823
Helixi384 – 3885
Beta strandi396 – 3983
Beta strandi406 – 4116
Helixi420 – 42910
Turni430 – 4323
Beta strandi435 – 4406
Helixi448 – 4503
Helixi451 – 4544
Beta strandi461 – 4677
Beta strandi475 – 4806
Helixi482 – 49312
Helixi495 – 5006
Beta strandi643 – 6453
Turni646 – 6483
Beta strandi649 – 6513
Helixi656 – 6583

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I5IX-ray2.50A/B241-516[»]
4IF6X-ray2.25A234-510[»]
B641-665[»]
4IG9X-ray2.64A/C/E/G234-510[»]
B/D/F/H641-665[»]
4KXQX-ray1.85A234-510[»]
B641-663[»]
ProteinModelPortaliQ96EB6.
SMRiQ96EB6. Positions 234-510.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini244 – 498255Deacetylase sirtuin-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 268267Interaction with HIST1H1E
Add
BLAST
Regioni143 – 541399Interaction with CCAR2
Add
BLAST
Regioni538 – 5403Phosphorylated at one of three serine residues

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 398Nuclear localization signal By similarity
Motifi138 – 1458Nuclear export signal By similarity
Motifi223 – 2308Nuclear localization signal By similarity
Motifi425 – 4317Nuclear export signal By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi54 – 9845Ala-rich
Add
BLAST
Compositional biasi122 – 1276Poly-Asp
Compositional biasi128 – 1347Poly-Glu

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0846.
HOGENOMiHOG000038016.
HOVERGENiHBG054192.
InParanoidiQ96EB6.
KOiK11411.
OMAiNYPSNKS.
OrthoDBiEOG7WX09C.
PhylomeDBiQ96EB6.
TreeFamiTF105896.

Family and domain databases

Gene3Di3.30.1600.10. 2 hits.
3.40.50.1220. 3 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 1 hit.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96EB6-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MADEAALALQ PGGSPSAAGA DREAASSPAG EPLRKRPRRD GPGLERSPGE    50
PGGAAPEREV PAAARGCPGA AAAALWREAE AEAAAAGGEQ EAQATAAAGE 100
GDNGPGLQGP SREPPLADNL YDEDDDDEGE EEEEAAAAAI GYRDNLLFGD 150
EIITNGFHSC ESDEEDRASH ASSSDWTPRP RIGPYTFVQQ HLMIGTDPRT 200
ILKDLLPETI PPPELDDMTL WQIVINILSE PPKRKKRKDI NTIEDAVKLL 250
QECKKIIVLT GAGVSVSCGI PDFRSRDGIY ARLAVDFPDL PDPQAMFDIE 300
YFRKDPRPFF KFAKEIYPGQ FQPSLCHKFI ALSDKEGKLL RNYTQNIDTL 350
EQVAGIQRII QCHGSFATAS CLICKYKVDC EAVRGDIFNQ VVPRCPRCPA 400
DEPLAIMKPE IVFFGENLPE QFHRAMKYDK DEVDLLIVIG SSLKVRPVAL 450
IPSSIPHEVP QILINREPLP HLHFDVELLG DCDVIINELC HRLGGEYAKL 500
CCNPVKLSEI TEKPPRTQKE LAYLSELPPT PLHVSEDSSS PERTSPPDSS 550
VIVTLLDQAA KSNDDLDVSE SKGCMEEKPQ EVQTSRNVES IAEQMENPDL 600
KNVGSSTGEK NERTSVAGTV RKCWPNRVAK EQISRRLDGN QYLFLPPNRY 650
IFHGAEVYSD SEDDVLSSSS CGSNSDSGTC QSPSLEEPME DESEIEEFYN 700
GLEDEPDVPE RAGGAGFGTD GDDQEAINEA ISVKQEVTDM NYPSNKS 747
Length:747
Mass (Da):81,681
Last modified:October 31, 2003 - v2
Checksum:i2D3BEA6D73DA229F
GO
Isoform 2 (identifier: Q96EB6-2) [UniParc]FASTAAdd to Basket

Also known as: delta-exon8

The sequence of this isoform differs from the canonical sequence as follows:
     454-639: Missing.

Show »
Length:561
Mass (Da):61,066
Checksum:iBFD54C8E408F23BD
GO

Sequence cautioni

The sequence AAH12499.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31D → E.1 Publication
Corresponds to variant rs35671182 [ dbSNP | Ensembl ].
VAR_025148
Natural varianti484 – 4841V → D.
Corresponds to variant rs1063111 [ dbSNP | Ensembl ].
VAR_051976

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei454 – 639186Missing in isoform 2.
VSP_042189Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti386 – 3894DIFN → ALFS in AAH12499. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF083106 mRNA. Translation: AAD40849.2.
AF235040 mRNA. Translation: AAG38486.1.
DQ278604 Genomic DNA. Translation: ABB72675.1.
AL133551 Genomic DNA. Translation: CAI16036.1.
BC012499 mRNA. Translation: AAH12499.1. Different initiation.
CCDSiCCDS7273.1. [Q96EB6-1]
RefSeqiNP_001135970.1. NM_001142498.1.
NP_036370.2. NM_012238.4. [Q96EB6-1]
UniGeneiHs.369779.

Genome annotation databases

EnsembliENST00000212015; ENSP00000212015; ENSG00000096717. [Q96EB6-1]
GeneIDi23411.
KEGGihsa:23411.
UCSCiuc001jnd.3. human. [Q96EB6-1]

Polymorphism databases

DMDMi38258633.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF083106 mRNA. Translation: AAD40849.2 .
AF235040 mRNA. Translation: AAG38486.1 .
DQ278604 Genomic DNA. Translation: ABB72675.1 .
AL133551 Genomic DNA. Translation: CAI16036.1 .
BC012499 mRNA. Translation: AAH12499.1 . Different initiation.
CCDSi CCDS7273.1. [Q96EB6-1 ]
RefSeqi NP_001135970.1. NM_001142498.1.
NP_036370.2. NM_012238.4. [Q96EB6-1 ]
UniGenei Hs.369779.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4I5I X-ray 2.50 A/B 241-516 [» ]
4IF6 X-ray 2.25 A 234-510 [» ]
B 641-665 [» ]
4IG9 X-ray 2.64 A/C/E/G 234-510 [» ]
B/D/F/H 641-665 [» ]
4KXQ X-ray 1.85 A 234-510 [» ]
B 641-663 [» ]
ProteinModelPortali Q96EB6.
SMRi Q96EB6. Positions 234-510.
ModBasei Search...

Protein-protein interaction databases

BioGridi 116983. 269 interactions.
DIPi DIP-29757N.
IntActi Q96EB6. 112 interactions.
MINTi MINT-3052322.
STRINGi 9606.ENSP00000212015.

Chemistry

BindingDBi Q96EB6.
ChEMBLi CHEMBL4506.

PTM databases

PhosphoSitei Q96EB6.

Polymorphism databases

DMDMi 38258633.

Proteomic databases

MaxQBi Q96EB6.
PaxDbi Q96EB6.
PeptideAtlasi Q96EB6.
PRIDEi Q96EB6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000212015 ; ENSP00000212015 ; ENSG00000096717 . [Q96EB6-1 ]
GeneIDi 23411.
KEGGi hsa:23411.
UCSCi uc001jnd.3. human. [Q96EB6-1 ]

Organism-specific databases

CTDi 23411.
GeneCardsi GC10P069644.
HGNCi HGNC:14929. SIRT1.
HPAi CAB003855.
HPA006295.
HPA052351.
MIMi 604479. gene.
neXtProti NX_Q96EB6.
PharmGKBi PA37935.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0846.
HOGENOMi HOG000038016.
HOVERGENi HBG054192.
InParanoidi Q96EB6.
KOi K11411.
OMAi NYPSNKS.
OrthoDBi EOG7WX09C.
PhylomeDBi Q96EB6.
TreeFami TF105896.

Enzyme and pathway databases

Reactomei REACT_200780. Regulation of HSF1-mediated heat shock response.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
SignaLinki Q96EB6.

Miscellaneous databases

GeneWikii Sirtuin_1.
GenomeRNAii 23411.
NextBioi 45603.
PROi Q96EB6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96EB6.
Bgeei Q96EB6.
CleanExi HS_SIRT1.
Genevestigatori Q96EB6.

Family and domain databases

Gene3Di 3.30.1600.10. 2 hits.
3.40.50.1220. 3 hits.
InterProi IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR026590. Ssirtuin_cat_dom.
[Graphical view ]
PANTHERi PTHR11085. PTHR11085. 1 hit.
Pfami PF02146. SIR2. 1 hit.
[Graphical view ]
SUPFAMi SSF52467. SSF52467. 1 hit.
PROSITEi PS50305. SIRTUIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Frye R.A.
    Biochem. Biophys. Res. Commun. 260:273-279(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1- and HEY2-mediated transcriptional repression."
    Takata T., Ishikawa F.
    Biochem. Biophys. Res. Commun. 301:250-257(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH HES1 AND HEY2, MUTAGENESIS OF HIS-363.
  3. NIEHS SNPs program
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-3.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-747.
    Tissue: Prostate.
  6. Cited for: FUNCTION IN DEACETYLATION OF TP53, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-363.
  7. "Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence."
    Langley E., Pearson M., Faretta M., Bauer U.-M., Frye R.A., Minucci S., Pelicci P.G., Kouzarides T.
    EMBO J. 21:2383-2396(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH PML, MUTAGENESIS OF HIS-363.
  8. "Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1."
    Bitterman K.J., Anderson R.M., Cohen H.Y., Latorre-Esteves M., Sinclair D.A.
    J. Biol. Chem. 277:45099-45107(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. Cited for: ENZYME REGULATION.
  10. "Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase."
    Frye R.A., Mayo M.W.
    EMBO J. 23:2369-2380(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: FUNCTION IN DEACETYLATION OF FOXO3, FUNCTION IN REGULATION OF FOXO3.
  12. "FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1)."
    van der Horst A., Tertoolen L.G.J., de Vries-Smits L.M.M., Frye R.A., Medema R.H., Burgering B.M.T.
    J. Biol. Chem. 279:28873-28879(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF MLLT7.
  13. "Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin."
    Vaquero A., Scher M., Lee D., Erdjument-Bromage H., Tempst P., Reinberg D.
    Mol. Cell 16:93-105(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. Cited for: FUNCTION IN DEACETYLATION OF FOXO3, FUNCTION IN REGULATION OF FOXO3.
  15. "Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase."
    Cohen H.Y., Miller C., Bitterman K.J., Wall N.R., Hekking B., Kessler B., Howitz K.T., Gorospe M., de Cabo R., Sinclair D.A.
    Science 305:390-392(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF XRCC6, INDUCTION BY CR.
  16. "Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation."
    Yang Y., Hou H., Haller E.M., Nicosia S.V., Bai W.
    EMBO J. 24:1021-1032(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FHL2, FUNCTION IN DEACETYLATION OF FOXO1, FUNCTION IN REGULATION OF FOXO1.
  17. "Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins."
    Michishita E., Park J.Y., Burneskis J.M., Barrett J.C., Horikawa I.
    Mol. Biol. Cell 16:4623-4635(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  18. "Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications."
    Zhao X., Sternsdorf T., Bolger T.A., Evans R.M., Yao T.-P.
    Mol. Cell. Biol. 25:8456-8464(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF MEF2D, INTERACTION WITH HDAC4.
  19. Cited for: INTERACTION WITH HIV-1 TAT.
  20. "Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation."
    Kuzmichev A., Margueron R., Vaquero A., Preissner T.S., Scher M., Kirmizis A., Ouyang X., Brockdorff N., Abate-Shen C., Farnham P.J., Reinberg D.
    Proc. Natl. Acad. Sci. U.S.A. 102:1859-1864(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH THE PRC4 COMPLEX, INTERACTION WITH SUZ12.
  21. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Interactions between E2F1 and SirT1 regulate apoptotic response to DNA damage."
    Wang C., Chen L., Hou X., Li Z., Kabra N., Ma Y., Nemoto S., Finkel T., Gu W., Cress W.D., Chen J.
    Nat. Cell Biol. 8:1025-1031(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH E2F1.
  23. "Deacetylation of the retinoblastoma tumour suppressor protein by SIRT1."
    Wong S., Weber J.D.
    Biochem. J. 407:451-460(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF RB1.
  24. "Sirt1 interacts with transducin-like enhancer of split-1 to inhibit nuclear factor kappaB-mediated transcription."
    Ghosh H.S., Spencer J.V., Ng B., McBurney M.W., Robbins P.D.
    Biochem. J. 408:105-111(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TLE1.
  25. "SIRT1 promotes DNA repair activity and deacetylation of Ku70."
    Jeong J., Juhn K., Lee H., Kim S.H., Min B.H., Lee K.M., Cho M.H., Park G.H., Lee K.H.
    Exp. Mol. Med. 39:8-13(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF XRCC6, FUNCTION IN DNA REPAIR.
  26. "SIRT1 interacts with p73 and suppresses p73-dependent transcriptional activity."
    Dai J.M., Wang Z.Y., Sun D.C., Lin R.X., Wang S.Q.
    J. Cell. Physiol. 210:161-166(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF TP73, FUNCTION IN REGULATION OF TP73.
  27. "Sirtuin 1 is required for antagonist-induced transcriptional repression of androgen-responsive genes by the androgen receptor."
    Dai Y., Ngo D., Forman L.W., Qin D.C., Jacob J., Faller D.V.
    Mol. Endocrinol. 21:1807-1821(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AR-DEPENDENT REPRESSION.
  28. "Active regulator of SIRT1 cooperates with SIRT1 and facilitates suppression of p53 activity."
    Kim E.-J., Kho J.-H., Kang M.-R., Um S.-J.
    Mol. Cell 28:277-290(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPS19BP1.
  29. Erratum
    Kim E.-J., Kho J.-H., Kang M.-R., Um S.-J.
    Mol. Cell 28:513-513(2007)
  30. "SIRT1 deacetylates and positively regulates the nuclear receptor LXR."
    Li X., Zhang S., Blander G., Tse J.G., Krieger M., Guarente L.
    Mol. Cell 28:91-106(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF NR1H3 AND NR1H2.
  31. "SIRT1 regulates the function of the Nijmegen breakage syndrome protein."
    Yuan Z., Zhang X., Sengupta N., Lane W.S., Seto E.
    Mol. Cell 27:149-162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF NBN, FUNCTION IN DNA REPAIR.
  32. "An acetylation/deacetylation-SUMOylation switch through a phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1 regulates transcriptional repression activity."
    Stankovic-Valentin N., Deltour S., Seeler J., Pinte S., Vergoten G., Guerardel C., Dejean A., Leprince D.
    Mol. Cell. Biol. 27:2661-2675(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF HIC1.
  33. "SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation."
    Vaquero A., Scher M., Erdjument-Bromage H., Tempst P., Serrano L., Reinberg D.
    Nature 450:440-444(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-363.
  34. Cited for: IDENTIFICATION IN THE ENOSC COMPLEX, FUNCTION, MUTAGENESIS OF HIS-363.
  35. "JNK2-dependent regulation of SIRT1 protein stability."
    Ford J., Ahmed S., Allison S., Jiang M., Milner J.
    Cell Cycle 7:3091-3097(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-27 AND SER-47.
  36. "Human immunodeficiency virus type 1 Tat protein inhibits the SIRT1 deacetylase and induces T cell hyperactivation."
    Kwon H.S., Brent M.M., Getachew R., Jayakumar P., Chen L.F., Schnolzer M., McBurney M.W., Marmorstein R., Greene W.C., Ott M.
    Cell Host Microbe 3:158-167(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT, FUNCTION IN T-CELL ACTIVATION.
  37. "Regulation of WRN protein cellular localization and enzymatic activities by SIRT1-mediated deacetylation."
    Li K., Casta A., Wang R., Lozada E., Fan W., Kane S., Ge Q., Gu W., Orren D., Luo J.
    J. Biol. Chem. 283:7590-7598(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF WRN, FUNCTION IN DNA DAMAGE.
  38. "SIRT1 modulation of the acetylation status, cytosolic localization, and activity of LKB1. Possible role in AMP-activated protein kinase activation."
    Lan F., Cacicedo J.M., Ruderman N., Ido Y.
    J. Biol. Chem. 283:27628-27635(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF STK11.
  39. "DBC1 is a negative regulator of SIRT1."
    Kim J.-E., Chen J., Lou Z.
    Nature 451:583-586(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCAR2, ENZYME REGULATION, MUTAGENESIS OF HIS-363, IDENTIFICATION BY MASS SPECTROMETRY.
  40. "Negative regulation of the deacetylase SIRT1 by DBC1."
    Zhao W., Kruse J.-P., Tang Y., Jung S.Y., Qin J., Gu W.
    Nature 451:587-590(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCAR2, ENZYME REGULATION.
  41. Cited for: PHOSPHORYLATION AT SER-14; SER-26; SER-27; SER-47; SER-159; SER-162; SER-172; SER-173; THR-530; THR-544; SER-545; THR-719 AND SER-747, MUTAGENESIS OF THR-530 AND SER-540.
  42. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-719, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  43. "A role for the NAD-dependent deacetylase Sirt1 in the regulation of autophagy."
    Lee I.H., Cao L., Mostoslavsky R., Lombard D.B., Liu J., Bruns N.E., Tsokos M., Alt F.W., Finkel T.
    Proc. Natl. Acad. Sci. U.S.A. 105:3374-3379(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF ATG5; ATG7 AND MAP1LC3B, FUNCTION IN AUTOPHAGY.
  44. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  45. "Carboxy-terminal phosphorylation of SIRT1 by protein kinase CK2."
    Zschoernig B., Mahlknecht U.
    Biochem. Biophys. Res. Commun. 381:372-377(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-659 AND SER-661, MUTAGENESIS OF SER-659; SER-661 AND SER-684.
  46. "Investigating the ADP-ribosyltransferase activity of sirtuins with NAD analogues and 32P-NAD."
    Du J., Jiang H., Lin H.
    Biochemistry 48:2878-2890(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  47. "Hepatocyte-specific deletion of SIRT1 alters fatty acid metabolism and results in hepatic steatosis and inflammation."
    Purushotham A., Schug T.T., Xu Q., Surapureddi S., Guo X., Li X.
    Cell Metab. 9:327-338(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPARA.
  48. "Transcriptional corepressor SMILE recruits SIRT1 to inhibit nuclear receptor estrogen receptor-related receptor gamma transactivation."
    Xie Y.B., Park J.H., Kim D.K., Hwang J.H., Oh S., Park S.B., Shong M., Lee I.K., Choi H.S.
    J. Biol. Chem. 284:28762-28774(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CREBZF.
  49. "A c-Myc-SIRT1 feedback loop regulates cell growth and transformation."
    Yuan J., Minter-Dykhouse K., Lou Z.
    J. Cell Biol. 185:203-211(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF MYC, FUNCTION IN REGULATION OF MYC.
  50. "hSirT1-dependent regulation of the PCAF-E2F1-p73 apoptotic pathway in response to DNA damage."
    Pediconi N., Guerrieri F., Vossio S., Bruno T., Belloni L., Schinzari V., Scisciani C., Fanciulli M., Levrero M.
    Mol. Cell. Biol. 29:1989-1998(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF PCAF, FUNCTION IN DNA REPAIR.
  51. "JNK1 phosphorylates SIRT1 and promotes its enzymatic activity."
    Nasrin N., Kaushik V.K., Fortier E., Wall D., Pearson K.J., de Cabo R., Bordone L.
    PLoS ONE 4:E8414-E8414(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-27; SER-47 AND THR-530, MUTAGENESIS OF SER-27; SER-47 AND THR-530, SUBCELLULAR LOCATION.
  52. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-530; SER-535 AND THR-719, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  53. "SIRT1 promotes proliferation and prevents senescence through targeting LKB1 in primary porcine aortic endothelial cells."
    Zu Y., Liu L., Lee M.Y., Xu C., Liang Y., Man R.Y., Vanhoutte P.M., Wang Y.
    Circ. Res. 106:1384-1393(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF STK11.
  54. Cited for: FUNCTION IN DNA REPAIR HOMOLOGOUS RECOMBINATION.
  55. "SIRT1 suppresses activator protein-1 transcriptional activity and cyclooxygenase-2 expression in macrophages."
    Zhang R., Chen H.Z., Liu J.J., Jia Y.Y., Zhang Z.Q., Yang R.F., Zhang Y., Xu J., Wei Y.S., Liu D.P., Liang C.C.
    J. Biol. Chem. 285:7097-7110(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FOS AND JUN.
  56. "SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60."
    Wang J., Chen J.
    J. Biol. Chem. 285:11458-11464(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF KAT5.
  57. "SIRT1 deacetylates and inhibits SREBP-1C activity in regulation of hepatic lipid metabolism."
    Ponugoti B., Kim D.H., Xiao Z., Smith Z., Miao J., Zang M., Wu S.Y., Chiang C.M., Veenstra T.D., Kemper J.K.
    J. Biol. Chem. 285:33959-33970(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF SREBF1.
  58. "Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha."
    Lim J.H., Lee Y.M., Chun Y.S., Chen J., Kim J.E., Park J.W.
    Mol. Cell 38:864-878(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF HIF1A, FUNCTION IN REGULATION OF HIF1A.
  59. "SIRT1 regulates UV-induced DNA repair through deacetylating XPA."
    Fan W., Luo J.
    Mol. Cell 39:247-258(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF XPA.
  60. Cited for: FUNCTION IN DEACETYLATION OF APEX1, FUNCTION IN DNA REPAIR, MUTAGENESIS OF HIS-363, INDUCTION, SUBCELLULAR LOCATION.
  61. "Transcriptional corepressor SHP recruits SIRT1 histone deacetylase to inhibit LRH-1 transactivation."
    Chanda D., Xie Y.B., Choi H.S.
    Nucleic Acids Res. 38:4607-4619(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NR0B2.
  62. "SIRT1 negatively regulates the mammalian target of rapamycin."
    Ghosh H.S., McBurney M., Robbins P.D.
    PLoS ONE 5:E9199-E9199(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TSC2.
  63. "SIRT1 undergoes alternative splicing in a novel auto-regulatory loop with p53."
    Lynch C.J., Shah Z.H., Allison S.J., Ahmed S.U., Ford J., Warnock L.J., Li H., Serrano M., Milner J.
    PLoS ONE 5:E13502-E13502(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION (ISOFORM 2), INDUCTION (ISOFORM 2), INTERACTION WITH TP53 AND RPS19BP1.
  64. "Regulation of global genome nucleotide excision repair by SIRT1 through xeroderma pigmentosum C."
    Ming M., Shea C.R., Guo X., Li X., Soltani K., Han W., He Y.Y.
    Proc. Natl. Acad. Sci. U.S.A. 107:22623-22628(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA REPAIR, SUPPRESSION OF XPC.
  65. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  66. "SIRT1 and SIRT3 deacetylate homologous substrates: AceCS1,2 and HMGCS1,2."
    Hirschey M.D., Shimazu T., Capra J.A., Pollard K.S., Verdin E.
    Aging (Albany NY) 3:635-642(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF HMGCS1.
  67. "Tumor necrosis factor alpha-mediated cleavage and inactivation of SirT1 in human osteoarthritic chondrocytes."
    Dvir-Ginzberg M., Gagarina V., Lee E.J., Booth R., Gabay O., Hall D.J.
    Arthritis Rheum. 63:2363-2373(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROCESSING.
  68. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  69. "EVI1 up-regulates the stress responsive gene SIRT1 which triggers deacetylation and degradation of EVI1."
    Pradhan A.K., Kuila N., Singh S., Chakraborty S.
    Biochim. Biophys. Acta 1809:269-275(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF MECOM.
  70. "Energy sensing factors PGC-1alpha and SIRT1 modulate PXR expression and function."
    Buler M., Aatsinki S.M., Skoumal R., Hakkola J.
    Biochem. Pharmacol. 82:2008-2015(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR1I2.
  71. Cited for: FUNCTION IN DEACETYLATION OF MYC, FUNCTION IN REGULATION OF MYC.
  72. "MST1 promotes apoptosis through regulating Sirt1-dependent p53 deacetylation."
    Yuan F., Xie Q., Wu J., Bai Y., Mao B., Dong Y., Bi W., Ji G., Tao W., Wang Y., Yuan Z.
    J. Biol. Chem. 286:6940-6945(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY STK4/MST1.
  73. "Cancer cell survival following DNA damage-mediated premature senescence is regulated by mammalian target of rapamycin (mTOR)-dependent Inhibition of sirtuin 1."
    Back J.H., Rezvani H.R., Zhu Y., Guyonnet-Duperat V., Athar M., Ratner D., Kim A.L.
    J. Biol. Chem. 286:19100-19108(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, PHOSPHORYLATION AT SER-47, MUTAGENESIS OF SER-47 AND PHE-474.
  74. "Stabilization of Suv39H1 by SirT1 is part of oxidative stress response and ensures genome protection."
    Bosch-Presegue L., Raurell-Vila H., Marazuela-Duque A., Kane-Goldsmith N., Valle A., Oliver J., Serrano L., Vaquero A.
    Mol. Cell 42:210-223(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN STABILIZATION OF SUV39H1.
  75. "SIRT1 deacetylates the DNA methyltransferase 1 (DNMT1) protein and alters its activities."
    Peng L., Yuan Z., Ling H., Fukasawa K., Robertson K., Olashaw N., Koomen J., Chen J., Lane W.S., Seto E.
    Mol. Cell. Biol. 31:4720-4734(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF DNMT1, FUNCTION IN REGULATION OF DNMT1.
  76. "SIRT1 promotes N-Myc oncogenesis through a positive feedback loop involving the effects of MKP3 and ERK on N-Myc protein stability."
    Marshall G.M., Liu P.Y., Gherardi S., Scarlett C.J., Bedalov A., Xu N., Iraci N., Valli E., Ling D., Thomas W., van Bekkum M., Sekyere E., Jankowski K., Trahair T., Mackenzie K.L., Haber M., Norris M.D., Biankin A.V., Perini G., Liu T.
    PLoS Genet. 7:E1002135-E1002135(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF MYCN, INTERACTION WITH MYCN.
  77. "The evolutionarily conserved longevity determinants HCF-1 and SIR-2.1/SIRT1 collaborate to regulate DAF-16/FOXO."
    Rizki G., Iwata T.N., Li J., Riedel C.G., Picard C.L., Jan M., Murphy C.T., Lee S.S.
    PLoS Genet. 7:E1002235-E1002235(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCFC1.
  78. "Methyltransferase Set7/9 regulates p53 activity by interacting with Sirtuin 1 (SIRT1)."
    Liu X., Wang D., Zhao Y., Tu B., Zheng Z., Wang L., Wang H., Gu W., Roeder R.G., Zhu W.G.
    Proc. Natl. Acad. Sci. U.S.A. 108:1925-1930(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SETD7, MUTAGENESIS OF LYS-233; LYS-235; LYS-236 AND LYS-238.
  79. "The deacetylase SIRT1 promotes membrane localization and activation of Akt and PDK1 during tumorigenesis and cardiac hypertrophy."
    Sundaresan N.R., Pillai V.B., Wolfgeher D., Samant S., Vasudevan P., Parekh V., Raghuraman H., Cunningham J.M., Gupta M., Gupta M.P.
    Sci. Signal. 4:RA46-RA46(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF AKT1, FUNCTION IN REGULATION OF AKT1.
  80. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-47 AND THR-719, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  81. "75kDa SirT1 blocks TNFalpha-mediated apoptosis in human osteoarthritic chondrocytes."
    Oppenheimer H., Gabay O., Meir H., Haze A., Kandel L., Liebergall M., Gagarina V., Lee E.J., Dvir-Ginzberg M.
    Arthritis Rheum. 64:718-728(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (SIRTT1 75 KDA FRAGMENT), SUBCELLULAR LOCATION (75SIRT1).
  82. Cited for: FUNCTION IN DEACETYLATION OF CIITA.
  83. Cited for: FUNCTION IN DEACETYLATION OF PML.
  84. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  85. "Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation."
    Wang F., Chan C.H., Chen K., Guan X., Lin H.K., Tong Q.
    Oncogene 31:1546-1557(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEACETYLATION OF FOXO3, FUNCTION IN REGULATION OF FOXO3.
  86. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  87. "Deleted in breast cancer 1 (DBC1) deficiency results in apoptosis of breast cancer cells through impaired responses to UV-induced DNA damage."
    Kim W., Kim J.E.
    Cancer Lett. 333:180-186(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCAR2.

Entry informationi

Entry nameiSIR1_HUMAN
AccessioniPrimary (citable) accession number: Q96EB6
Secondary accession number(s): Q2XNF6
, Q5JVQ0, Q9GZR9, Q9Y6F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 31, 2003
Last modified: September 3, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Red wine, which contains resveratrol, may participate in activation of sirtuin proteins, and may therefore participate in an extended lifespan as it has been observed in yeast.
Calf histone H1 is used as substrate in the in vitro deacetylation assay (1 Publication). As, in vivo, interaction occurs between SIRT1 with HIST1H1E, deacetylation has been validated only for HIST1H1E.
The reported ADP-ribosyltransferase activity of sirtuins is likely some inefficient side reaction of the deacetylase activity and may not be physiologically relevant (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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