SIRT1(SIR2L1);

NAD-dependent deacetylase sirtuin-1(hSIRT1);

SIR2-like protein 1(hSIR2);

SIRT1 (Homo sapiens). 

Interacts with TAF1B. Found in a complex with PCAF and MYOD1 (By similarity). Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8. Interacts with MLLT7/FOXO4, HES1, HEY2, p53/TP53 and PML. Interacts with RPS19BP1/AROS. Interacts with KIAA1967/DBC1 (via N-terminus). Interacts with APEX1; the interaction is promoted in the context of genotoxic stress. Interacts with FOXO1 and this interaction requires the presence of KRIT1 (By similarity). Interacts with STK4/MST1.

NAD-dependent protein deacetylase, which regulates processes such as apoptosis and muscle differentiation by deacetylating key proteins. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Deacetylates 'Lys-26' of HIST1H1E. Involved in HES1- and HEY2-mediated transcriptional repression. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. May serve as a sensor of the cytosolic ratio of NAD(+)/NADH, which is essential in skeletal muscle cell differentiation. Deacetylates 'Lys-16' of histone H4 (in vitro). 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 H2A. In case of HIV-1 infection, interacts with and deacetylates the viral Tat protein. Deacetylates APEX1 at 'Lys-6' and 'Lys-7'. Stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1.

Nucleus PML body 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.

747

N/A

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hsa:23411

Hs.369779

Q96EB6

PF02146

604479

Q96EB6