SIRT1 Antibody (OAAJ06507)

Catalog No: OAAJ06507

Size:100 uL

Western blot analysis of extracts of various cell lines, using SIRT1 antibody.

Product Info

• Predicted Species Reactivity: Human, Mouse, Rat
• Product Format: Liquid
• Clonality: Polyclonal
• Host: Rabbit
• Application: WB, IHC
• Reconstitution and Storage: Store at +4C. For long term storage, aliquot and store at -20C. Avoid freeze/thaw cycles.
• Immunogen: C term -peptideof human SIRT1
• Purification: Immunogen affinity chromatography
• Concentration: 1 mg/mL

Target Info

• Gene Symbol: SIRT1
• Alias Symbols: SIR2, SIR2L1, SIR2alpha
• NCBI Gene Id: 23411
• Protein Name: NAD-dependent protein deacetylase sirtuin-1
• Description of Target: 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. 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. Regulates the circadian expression of several core clock genes, including ARNTL/BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling. Deacetylates ARNTL/BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator. Deacetylates PER2, facilitating its ubiquitination and degradation by the proteosome. Protects cardiomyocytes against palmitate-induced apoptosis (PubMed:11672523, PubMed:12006491, PubMed:14976264, PubMed:14980222, PubMed:15126506, PubMed:15152190, PubMed:15205477, PubMed:15469825, PubMed:15692560, PubMed:16079181, PubMed:16166628, PubMed:16892051, PubMed:16998810, PubMed:17283066, PubMed:17334224, PubMed:17505061, PubMed:17612497, PubMed:17620057, PubMed:17936707, PubMed:18203716, PubMed:18296641, PubMed:18662546, PubMed:18687677, PubMed:19188449, PubMed:19220062, PubMed:19364925, PubMed:19690166, PubMed:19934257, PubMed:20097625, PubMed:20100829, PubMed:20203304, PubMed:20375098, PubMed:20620956, PubMed:20670893, PubMed:20817729, PubMed:21149730, PubMed:21245319, PubMed:21471201, PubMed:21504832, PubMed:21555002, PubMed:21698133, PubMed:21701047, PubMed:21775285, PubMed:21807113, PubMed:21841822, PubMed:21890893, PubMed:21909281, PubMed:21947282, PubMed:22274616). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (PubMed:20955178). Involved in the CCAR2-mediated regulation of PCK1 and NR1D1 (PubMed:24415752). Deacetylates CTNB1 at 'Lys-49' (PubMed:24824780). In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling (By similarity).By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More…</a></p> Manual assertion inferred from sequence similarity toiUniProtKB:Q923E4 (SIR1_MOUSE)53 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.6"hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase." Vaziri H., Dessain S.K., Ng Eaton E., Imai S., Frye R.A., Pandita T.K., Guarente L., Weinberg R.A. Cell 107:149-159(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEACETYLATION OF TP53, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-363.Ref.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.Ref.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.Ref.11"Mammalian SIRT1 represses forkhead transcription factors." Motta M.C., Divecha N., Lemieux M., Kamel C., Chen D., Gu W., Bultsma Y., McBurney M., Guarente L. Cell 116:551-563(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEACETYLATION OF FOXO3, FUNCTION IN REGULATION OF FOXO3.Ref.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.Ref.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.Ref.14"Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase." Brunet A., Sweeney L.B., Sturgill J.F., Chua K.F., Greer P.L., Lin Y., Tran H., Ross S.E., Mostoslavsky R., Cohen H.Y., Hu L.S., Cheng H.L., Jedrychowski M.P., Gygi S.P., Sinclair D.A., Alt F.W., Greenberg M.E. Science 303:2011-2015(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEACETYLATION OF FOXO3, FUNCTION IN REGULATION OF FOXO3.Ref.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.Ref.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.Ref.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.Ref.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.Ref.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.Ref.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.Ref.25"Distinct C/EBPalpha motifs regulate lipogenic and gluconeogenic gene expression in vivo." Pedersen T.A., Bereshchenko O., Garcia-Silva S., Ermakova O., Kurz E., Mandrup S., Porse B.T., Nerlov C. EMBO J. 26:1081-1093(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF HIS-363.Ref.26"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.Ref.27"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.Ref.28"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.Ref.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.Ref.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.Ref.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.Ref.34"SIRT1 regulates circadian clock gene expression through PER2 deacetylation." Asher G., Gatfield D., Stratmann M., Reinke H., Dibner C., Kreppel F., Mostoslavsky R., Alt F.W., Schibler U. Cell 134:317-328(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.Ref.38"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.Ref.39"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.Ref.44"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.Ref.47"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.Ref.49"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.Ref.50"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.Ref.51"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.Ref.54"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.Ref.55"Role of SIRT1 in homologous recombination." Uhl M., Csernok A., Aydin S., Kreienberg R., Wiesmuller L., Gatz S.A. DNA Repair 9:383-393(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DNA REPAIR HOMOLOGOUS RECOMBINATION.Ref.57"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.Ref.58"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.Ref.59"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.Ref.60"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.Ref.61"SIRT1 deacetylates APE1 and regulates cellular base excision repair." Yamamori T., DeRicco J., Naqvi A., Hoffman T.A., Mattagajasingh I., Kasuno K., Jung S.B., Kim C.S., Irani K. Nucleic Acids Res. 38:832-845(2010) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEACETYLATION OF APEX1, FUNCTION IN DNA REPAIR, MUTAGENESIS OF HIS-363, INDUCTION, SUBCELLULAR LOCATION.Ref.62"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.Ref.65"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.Ref.67"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.Ref.70"Regulation of unfolded protein response modulator XBP1s by acetylation and deacetylation." Wang F.M., Chen Y.J., Ouyang H.J. Biochem. J. 433:245-252(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEACETYLATION OF XBP1, INTERACTION WITH XBP1, SUBCELLULAR LOCATION.Ref.71"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.Ref.73"Sirt1 deacetylates c-Myc and promotes c-Myc/Max association." Mao B., Zhao G., Lv X., Chen H.Z., Xue Z., Yang B., Liu D.P., Liang C.C. Int. J. Biochem. Cell Biol. 43:1573-1581(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEACETYLATION OF MYC, FUNCTION IN REGULATION OF MYC.Ref.75"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.Ref.76"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.Ref.77"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.Ref.78"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.Ref.79"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.Ref.80"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.Ref.81"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.Ref.84"SIRT1 links CIITA deacetylation to MHC II activation." Wu X., Kong X., Chen D., Li H., Zhao Y., Xia M., Fang M., Li P., Fang F., Sun L., Tian W., Xu H., Yang Y., Qi X., Gao Y., Sha J., Chen Q., Xu Y. Nucleic Acids Res. 39:9549-9558(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEACETYLATION OF CIITA.Ref.85"PML regulates PER2 nuclear localization and circadian function." Miki T., Xu Z., Chen-Goodspeed M., Liu M., Van Oort-Jansen A., Rea M.A., Zhao Z., Lee C.C., Chang K.S. EMBO J. 31:1427-1439(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEACETYLATION OF PML.Ref.87"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.Ref.92"Deleted in breast cancer 1 (DBC1) protein regulates hepatic gluconeogenesis." Nin V., Chini C.C., Escande C., Capellini V., Chini E.N. J. Biol. Chem. 289:5518-5527(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION.Ref.96"MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in the cytoplasm." Pangon L., Mladenova D., Watkins L., Van Kralingen C., Currey N., Al-Sohaily S., Lecine P., Borg J.P., Kohonen-Corish M.R. Int. J. Cancer 136:55-64(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN DEACETYLATION OF CTNB1. Isoform 2: 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.1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.64"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. (Microbial infection) 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.1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.37"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 (MICROBIAL INFECTION). 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.1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment iniRef.83"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).
• Uniprot ID: Q96EB6
• Protein Accession #: NP_001135970
• Nucleotide Accession #: NM_001142498
• Molecular Weight: 82 kDa