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SIRT1 (NAD-dependent protein deacetylase sirtuin-1) is a protein that switches other genes on and off. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Pancreatic ductal adenocarcinoma.
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. 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.
CIViC holds 2 clinical evidence items and 0 assertions across 1 variant, naming Niacinamide.
In plain words · SIRT1 (NAD-dependent protein deacetylase sirtuin-1) is a protein that switches other genes on and off. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Pancreatic ductal adenocarcinoma.
SIRT1 (NAD-dependent protein deacetylase sirtuin-1) is a protein that switches other genes on and off. The public catalogues list it as a drug target and a biomarker, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Pancreatic ductal adenocarcinoma.
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.
No product in this corpus aims at SIRT1 yet. Transcription factors have no pocket to plug, so drugs either degrade them or block the partner protein they need to dock on DNA.
Broadly expressed or essential: HPA finds the RNA at low tissue specificity; a medicine acting on the wild-type protein would expose normal tissue too. HPA SIRT1: RNA low tissue specificity; high antibody staining in 3 normal tissues; highest cancer staining cervical cancer (7 of 11 high). Distribution: 1 cancer family in the corpus carries a prevalence row, label threshold or catalogue link for it (Pancreatic ductal adenocarcinoma); Open Targets associates it with 0 specific cancer types at or above 0.5. (Rule 7 of scripts/fetch-target-specificity.ts.)
Sources: Human Protein Atlas SIRT1 tissue; Open Targets ENSG00000096717 associations
First described 1999. Earliest sequence paper UniProt cites for the protein: Frye R.A., Biochem. Biophys. Res. Commun, 1999, "Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity". Source.
Sources: HGNC HGNC:14929 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt Q96EB6 (protein name, function text, keywords and locations (REST API)); CIViC gene SIRT1 (2 evidence items, 0 assertions, 1 variants; diseases: Pancreatic Ductal Carcinoma, Pancreatic Cancer (GraphQL API, CC0))
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. 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. Location: Nucleus, PML body; Cytoplasm; Nucleus; Nucleus, nucleoplasm (UniProt). Locus 10q21.3 (HGNC).
RNA: low tissue specificity, detected in all normal tissues.
Medium: Bone marrow, Placenta, Tonsil.
Medium only: breast cancer, colorectal cancer, lymphoma, prostate cancer.
Human Protein Atlas version 25.1, antibody staining at reliability approved, enhanced or supported; used under CC BY-SA 3.0. Staining counts are patients per level in the atlas cohort, not population prevalence.
Query for this target: (TITLE:"SIRT1" OR ABSTRACT:"SIRT1" OR TITLE:"sirtuin 1" OR ABSTRACT:"sirtuin 1" OR TITLE:"NAD-dependent protein deacetylase sirtuin-1" OR ABSTRACT:"NAD-dependent protein deacetylase sirtuin-1" OR TITLE:"SIR2L1" OR ABSTRACT:"SIR2L1") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about SIRT1, not a curated reading list.