EC Number   |
General Information |
Reference |
|---|
   2.3.1.B41 | evolution |
SIRT6 belongs to the mammalian homologues of Sir2 histone NAD+-dependent deacylase family |
756407 |
| 2.3.1.B41 | evolution |
sirtuin 6 (SIRT6) is a member of the sirtuin family of nicotinamide adenine dinucleotide?dependent protein deacetylases |
757294 |
| 2.3.1.B41 | evolution |
sirtuin6 belongs to the Sirtuin family |
757644 |
| 2.3.1.B41 | evolution |
sirtuin6 is a member of the sirtuin family which function as NAD+-dependent deacetylases |
757530 |
| 2.3.1.B41 | evolution |
sirtuins are an evolutionarily conserved family of proteins originally defined as the class III histone deacetylases (HDACs). The sirtuin family of proteins share a conserved central catalytic domain and the ability to couple the cleavage of NAD+ to the removal of an acyl group from the epsilon-amino group of lysines. Each family member (SIRT1-7) contains variable N-terminal and C-terminal domains and has diverse subcellular localization and function |
757236 |
| 2.3.1.B41 | evolution |
sirtuins, silent mating-type information regulation 2 (SIRTs), are a family of nicotinamide adenine dinucleotide (NAD+)-dependent histone deacetylases with important roles in regulating energy metabolism and senescence. SIRT6 reduces the upregulation of genes involved in inflammation, vascular remodeling, oxidative stress, and angiogenesis, including interleukin 1-beta |
755918 |
| 2.3.1.B41 | evolution |
there are seven evolutionarily conserved mammalian sirtuins (SIRT1-7) distributed to different compartments of the cell. They possess different deacylation activities to post-translationally modulate functions of their targets influencing major cellular pathways. SIRT6 is associated with chromatin and possesses histone deacetylase as well as mono-ADP-ribosylase activities, for both of which it needs NAD+ as a co-substrate |
758395 |
| 2.3.1.B41 | malfunction |
an inactivating mutation in the histone deacetylase SIRT6 causes human perinatal lethality. The homozygous inactivating mutation D63H in the histone deacetylase SIRT6 results in severe congenital anomalies and perinatal lethality in four affected fetuses. Human induced pluripotent stem cells (iPSCs) derived from D63H homozygous fetuses fail to differentiate into embryoid bodies (EBs), functional cardiomyocytes, and neural progenitor cells due to a failure to repress pluripotent genes. SIRT6 knockout ESCs cultured to form EBs are significantly smaller than their wild-type counterparts. SIRT6 D63H mutant mESCs fail to differentiate into functional cardiomyocyte foci. SIRT6 D63H mutant cardiomyocytes fail to suppress HAND1 expression while exhibiting significantly reduced FBN1 levels when compared with SIRT6 knockout cells |
756879 |
| 2.3.1.B41 | malfunction |
analysis of effects of inhibition of SIRT6 on differentiation and lipid synthesis, and related molecular mechanisms, overview. Overexpression of SIRT6 significantly inhibits the mRNA expression of key adipogenesis genes such as CCAAT enhancer binding protein alpha (CEBPalpha), FABP4, FASN, peroxisome proliferator-activated receptor gamma (PPARgamma), and stearoyl-CoA desaturase (SCD), and promotes the expression of lipolysis genes including lipoprotein lipase (LPL), while interference of SIRT6 obtains the opposite results. The lipolysis drug Cl316,243 interfering with SIRT6 significantly promotes the expression of CEBPalpha, FABP4, FASN, PPARgamma, and SCD, and inhibited the expression of LPL, while overexpression of SIRT6 results in the opposite results |
755904 |
| 2.3.1.B41 | malfunction |
diabetic mice exhibit reduced Sirt6 expression and AMP kinase (AMPK) dephosphorylation accompanied by mitochondrial morphological abnormalities. Hyperglycemia-induced Sirt6 levels are decreased in vivo. Hyperglycemia promotes podocyte mitochondrial dysfunction in mice with diabetic nephropathy (DN) |
-, 756973 |
