DegronMD - Q96EB6(SIRT1)

FUNCTION: 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, metabolism, apoptosis and autophagy (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:17290224, 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:20955178, PubMed:21149730, PubMed:21245319, PubMed:21471201, PubMed:21504832, PubMed:21555002, PubMed:21698133, PubMed:21701047, PubMed:21775285, PubMed:21807113, PubMed:21841822, PubMed:21890893, PubMed:21947282, PubMed:22274616, PubMed:24415752, PubMed:24824780, PubMed:29765047, PubMed:30409912). Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression (PubMed:15469825). Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively (PubMed:15152190, PubMed:14980222, PubMed:14976264). Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction (PubMed:15205477). 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) (By similarity). 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 (PubMed:18485871). 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 (PubMed:18485871, PubMed:21504832). Deacetylates 'Lys-266' of SUV39H1, leading to its activation (PubMed:21504832). Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1 (PubMed:19188449). Deacetylates H2A and 'Lys-26' of H1-4 (PubMed:15469825). 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 (PubMed:20375098). Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting (By similarity). Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1 (PubMed:15469825, PubMed:18004385). Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2 (PubMed:18004385, PubMed:21504832). 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 (PubMed:18004385, PubMed:21504832). Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence (PubMed:11672523, PubMed:12006491). Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I (By similarity). Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability (PubMed:19364925, PubMed:21807113). 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 (PubMed:14980222, PubMed:14976264, PubMed:21841822). Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis (PubMed:15126506). Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing (PubMed:21947282). Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha (PubMed:15152190). Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1 (PubMed:17620057, PubMed:17283066, PubMed:20100829, PubMed:20620956). Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver (PubMed:15692560). Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation (PubMed:16892051). Involved in HES1- and HEY2-mediated transcriptional repression (PubMed:12535671). In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62' (PubMed:21698133). Deacetylates MEF2D (PubMed:16166628). Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3 (PubMed:17505061). Represses HNF1A-mediated transcription (By similarity). Required for the repression of ESRRG by CREBZF (PubMed:19690166). 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 (PubMed:17936707). Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis (PubMed:20817729, PubMed:29765047). Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2 (By similarity). Deacetylates p300/EP300 and PRMT1 (By similarity). Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation (PubMed:21701047). Involved in liver and muscle metabolism. Through deacetylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletal muscle under low-glucose conditions and is involved in glucose homeostasis (PubMed:23142079). 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 (PubMed:17290224, PubMed:20817729). Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and facilitating 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 (PubMed:15205477, PubMed:17334224, PubMed:16998810, PubMed:17612497, PubMed:20670893, PubMed:21149730). Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN (PubMed:15205477, PubMed:17334224, PubMed:20097625). Promotes DNA double-strand breaks by mediating deacetylation of SIRT6 (PubMed:32538779). 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 (PubMed:18203716). Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1 (PubMed:19934257). Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER) (PubMed:32034146). 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 (PubMed:18296641). Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation (PubMed:21775285). 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 (PubMed:18687677, PubMed:20203304). 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 (PubMed:21890893). Deacetylates MECOM/EVI1 (PubMed:21555002). Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization (PubMed:22274616). During the neurogenic transition, represses 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 (PubMed:18662546). Deacetylates ARNTL/BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator (By similarity). Deacetylates PER2, facilitating its ubiquitination and degradation by the proteosome (By similarity). Protects cardiomyocytes against palmitate-induced apoptosis (By similarity). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (PubMed:20955178). Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis (PubMed:30193097). 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). In addition to protein deacetylase activity, also acts as protein-lysine deacylase by mediating protein depropionylation and decrotonylation (PubMed:28497810). Mediates depropionylation of Osterix (SP7) (By similarity). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase (PubMed:28497810). Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity (By similarity). Involved in the regulation of centrosome duplication. Deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly (PubMed:31722219). Deacetylates NDC80/HEC1 (PubMed:30409912). {ECO:0000250|UniProtKB:Q923E4, ECO:0000269|PubMed:11672523, ECO:0000269|PubMed:12006491, ECO:0000269|PubMed:12535671, ECO:0000269|PubMed:14976264, ECO:0000269|PubMed:14980222, ECO:0000269|PubMed:15126506, ECO:0000269|PubMed:15152190, ECO:0000269|PubMed:15205477, ECO:0000269|PubMed:15469825, ECO:0000269|PubMed:15692560, ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:16166628, ECO:0000269|PubMed:16892051, ECO:0000269|PubMed:16998810, ECO:0000269|PubMed:17283066, ECO:0000269|PubMed:17290224, ECO:0000269|PubMed:17334224, ECO:0000269|PubMed:17505061, ECO:0000269|PubMed:17612497, ECO:0000269|PubMed:17620057, ECO:0000269|PubMed:17936707, ECO:0000269|PubMed:18203716, ECO:0000269|PubMed:18296641, ECO:0000269|PubMed:18485871, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:18687677, ECO:0000269|PubMed:19188449, ECO:0000269|PubMed:19220062, ECO:0000269|PubMed:19364925, ECO:0000269|PubMed:19690166, ECO:0000269|PubMed:19934257, ECO:0000269|PubMed:20097625, ECO:0000269|PubMed:20100829, ECO:0000269|PubMed:20203304, ECO:0000269|PubMed:20375098, ECO:0000269|PubMed:20620956, ECO:0000269|PubMed:20670893, ECO:0000269|PubMed:20817729, ECO:0000269|PubMed:20955178, ECO:0000269|PubMed:21149730, ECO:0000269|PubMed:21245319, ECO:0000269|PubMed:21471201, ECO:0000269|PubMed:21504832, ECO:0000269|PubMed:21555002, ECO:0000269|PubMed:21698133, ECO:0000269|PubMed:21701047, ECO:0000269|PubMed:21775285, ECO:0000269|PubMed:21807113, ECO:0000269|PubMed:21841822, ECO:0000269|PubMed:21890893, ECO:0000269|PubMed:21947282, ECO:0000269|PubMed:22274616, ECO:0000269|PubMed:23142079, ECO:0000269|PubMed:24415752, ECO:0000269|PubMed:24824780, ECO:0000269|PubMed:28497810, ECO:0000269|PubMed:29765047, ECO:0000269|PubMed:30193097, ECO:0000269|PubMed:30409912, ECO:0000269|PubMed:31722219, ECO:0000269|PubMed:32034146, ECO:0000269|PubMed:32538779}.; FUNCTION: [Isoform 2]: Deacetylates '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. {ECO:0000269|PubMed:20975832}.; FUNCTION: [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. {ECO:0000269|PubMed:21987377}.; FUNCTION: (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. {ECO:0000269|PubMed:18329615}. View more >>

GO - Biological processes (BP): angiogenesis [GO:0001525]; behavioral response to starvation [GO:0042595]; cell aging [GO:0007569]; cellular glucose homeostasis [GO:0001678]; cellular response to DNA damage stimulus [GO:0006974]; cellular response to glucose starvation [GO:0042149]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular response to ionizing radiation [GO:0071479]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to starvation [GO:0009267]; cellular response to tumor necrosis factor [GO:0071356]; cellular triglyceride homeostasis [GO:0035356]; cholesterol homeostasis [GO:0042632]; chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; DNA methylation-dependent heterochromatin assembly [GO:0006346]; DNA synthesis involved in DNA repair [GO:0000731]; energy homeostasis [GO:0097009]; fatty acid homeostasis [GO:0055089]; heterochromatin assembly [GO:0031507]; histone deacetylation [GO:0016575]; histone H3 deacetylation [GO:0070932]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; leptin-mediated signaling pathway [GO:0033210]; macrophage differentiation [GO:0030225]; muscle organ development [GO:0007517]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cAMP-dependent protein kinase activity [GO:2000480]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell growth [GO:0030308]; negative regulation of cellular response to testosterone stimulus [GO:2000655]; negative regulation of cellular senescence [GO:2000773]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043518]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of helicase activity [GO:0051097]; negative regulation of histone H3-K14 acetylation [GO:0071441]; negative regulation of histone H3-K9 trimethylation [GO:1900113]; negative regulation of histone H4-K16 acetylation [GO:2000619]; negative regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043124]; negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:1902166]; negative regulation of neuron death [GO:1901215]; negative regulation of NF-kappaB transcription factor activity [GO:0032088]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of peptidyl-lysine acetylation [GO:2000757]; negative regulation of phosphorylation [GO:0042326]; negative regulation of prostaglandin biosynthetic process [GO:0031393]; negative regulation of protein acetylation [GO:1901984]; negative regulation of protein kinase B signaling [GO:0051898]; negative regulation of TOR signaling [GO:0032007]; negative regulation of transcription, DNA-templated [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; ovulation from ovarian follicle [GO:0001542]; peptidyl-lysine acetylation [GO:0018394]; peptidyl-lysine deacetylation [GO:0034983]; positive regulation of adaptive immune response [GO:0002821]; positive regulation of adipose tissue development [GO:1904179]; positive regulation of angiogenesis [GO:0045766]; positive regulation of apoptotic process [GO:0043065]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cAMP-dependent protein kinase activity [GO:2000481]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cellular senescence [GO:2000774]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of DNA repair [GO:0045739]; positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902237]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of histone deacetylation [GO:0031065]; positive regulation of histone H3-K9 methylation [GO:0051574]; positive regulation of histone methylation [GO:0031062]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of macroautophagy [GO:0016239]; positive regulation of macrophage apoptotic process [GO:2000111]; positive regulation of macrophage cytokine production [GO:0060907]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of phosphatidylinositol 3-kinase signaling [GO:0014068]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of smooth muscle cell differentiation [GO:0051152]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deacetylation [GO:0006476]; protein depropionylation [GO:0106230]; protein destabilization [GO:0031648]; protein ubiquitination [GO:0016567]; pyrimidine dimer repair by nucleotide-excision repair [GO:0000720]; rDNA heterochromatin assembly [GO:0000183]; regulation of apoptotic process [GO:0042981]; regulation of bile acid biosynthetic process [GO:0070857]; regulation of brown fat cell differentiation [GO:0090335]; regulation of cell population proliferation [GO:0042127]; regulation of cellular response to heat [GO:1900034]; regulation of centrosome duplication [GO:0010824]; regulation of endodeoxyribonuclease activity [GO:0032071]; regulation of glucose metabolic process [GO:0010906]; regulation of lipid storage [GO:0010883]; regulation of mitotic cell cycle [GO:0007346]; regulation of peroxisome proliferator activated receptor signaling pathway [GO:0035358]; regulation of protein serine/threonine kinase activity [GO:0071900]; regulation of smooth muscle cell apoptotic process [GO:0034391]; regulation of transcription by glucose [GO:0046015]; response to hydrogen peroxide [GO:0042542]; response to insulin [GO:0032868]; response to leptin [GO:0044321]; response to oxidative stress [GO:0006979]; single strand break repair [GO:0000012]; spermatogenesis [GO:0007283]; stress-induced premature senescence [GO:0090400]; transforming growth factor beta receptor signaling pathway [GO:0007179]; triglyceride mobilization [GO:0006642]; UV-damage excision repair [GO:0070914]; white fat cell differentiation [GO:0050872] View more >>

GO - Molecular function (MF): View more >>

GO - Cellular component (CC): View more >>

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Open in full screen with detailed sequence annotations

Mutation	Sample	Cancer	Dataset	Degron hit	Class	Location	Type	Impact score
p.A617V	TCGA-AA-3672	COAD	TCGA	VGSST	DEG_SPOP_SBC_1	603:607	Mutation rewiring degron network	0.0556
p.V665I	TCGA-AX-A0J1	UCEC	TCGA	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation altering degron motif	0.7076
p.V665I	TCGA-FI-A2D0	UCEC	TCGA	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation altering degron motif	0.7076
p.A655T	TCGA-AX-A2HD	UCEC	TCGA	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation rewiring degron network	0.0556
p.S675N	TCGA-AZ-4315	COAD	TCGA	DSGTCQS	DEG_SCF_TRCP1_1	676:682	Mutation rewiring degron network	0.3056
p.S675N	TCGA-AZ-4315	COAD	TCGA	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation rewiring degron network	0.1667
p.S669G	TCGA-D7-6521	STAD	TCGA	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation altering degron motif	0.8104
p.Q681H	TCGA-E2-A1LG	BRCA	TCGA	DSGTCQS	DEG_SCF_TRCP1_1	676:682	Mutation altering degron motif	0.647
p.E609A	TCGA-XF-A9T0	BLCA	TCGA	VGSST	DEG_SPOP_SBC_1	603:607	Mutation rewiring degron network	0.2778
p.S668F	SIDM02042	Pancreatic Carcinoma	GDSC	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation altering degron motif	0.7982
p.S668F	SIDM00895	B-Cell Non-Hodgkin's Lymphoma	GDSC	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation altering degron motif	0.7982
p.S668F	ACH-002215	Lymphoma	CCLE	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation altering degron motif	0.7982
p.S668F	BC-3	haematopoietic and lymphoid tissue	COSMIC	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation altering degron motif	0.7982
p.E687K	SIDM00118	Colorectal Carcinoma	GDSC	DSGTCQS	DEG_SCF_TRCP1_1	676:682	Mutation rewiring degron network	0.1944
p.E687K	ACH-001081	Colon/Colorectal Cancer	CCLE	DSGTCQS	DEG_SCF_TRCP1_1	676:682	Mutation rewiring degron network	0.1944
p.E687K	HCC2998	large intestine	COSMIC	DSGTCQS	DEG_SCF_TRCP1_1	676:682	Mutation rewiring degron network	0.1944
p.S673G	SIDM01608	Endometrial Carcinoma	GDSC	DSGTCQS	DEG_SCF_TRCP1_1	676:682	Mutation rewiring degron network	0.25
p.S673G	SIDM01608	Endometrial Carcinoma	GDSC	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation rewiring degron network	0.2222
p.S673G	ACH-000990	Endometrial/Uterine Cancer	CCLE	DSGTCQS	DEG_SCF_TRCP1_1	676:682	Mutation rewiring degron network	0.25
p.S673G	ACH-000990	Endometrial/Uterine Cancer	CCLE	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation rewiring degron network	0.2222
p.E662D	SIDM01617	Endometrial Carcinoma	GDSC	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation rewiring degron network	0.25
p.E662D	ACH-000994	Endometrial/Uterine Cancer	CCLE	VLSSS	DEG_SPOP_SBC_1	665:669	Mutation rewiring degron network	0.25

DegronMD: protein-targeted degradation, mutation and drug response to degrons

SIRT1

UniProt ID: Q96EB6

Entrez ID: 23411

Protein name: NAD-dependent protein deacetylase sirtuin-1 (hSIRT1) (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 1) (SIR2-like protein 1) (hSIR2) [Cleaved into: SirtT1 75 kDa fragment (75SirT1)]

External links: UniprotKB HGNC RefSeq COSMIC

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Kaplan plot for SIRT1 in