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Validated All-in-One™ qPCR Primer for SIRT2(NM_030593.3) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Two transcript variants result from alternative splicing of this gene. [provided by RefSeq].
Gene References into function
- Enzymatic analysis of recombinant SIRT2 in comparison to a yeast homolog of Sir2 protein (Hst2p) shows a striking preference of SIRT2 for acetylated tubulin peptide as a substrate relative to acetylated histone H3 peptide.
- SIRT2 is phosphorylated late in G(2), during M, and into the period of cytokinesis. CDC14B may provoke exit from mitosis coincident with the loss of SIRT2 via ubiquitination and subsequent degradation by the 26S proteasome.
- To inhibit myogenesis, Sir2 requires its NAD(+)-dependent deacetylase activity. Cells with reduced Sir2 levels are less sensitive to the inhibition imposed by an elevated [NAD(+)]/[NADH] ratio.
- SIRT2 gene expression is down-regulated in gliomas.
- Results show for the first time that SIRT2 interacts with the homeobox transcription factor, HOXA10.
- SIRT2 can discriminate among various monoacetylated histone H3 and H4 peptide substrates of NAD+-dependent histone/protein deacetylase, as well as display differences in catalytic efficiency.
- Sir2 and calorie restriction act in parallel pathways to promote longevity in yeast
- the absence of SIRT2, a potential tumor suppressor, could play a key role in the regulation of the cell-cycle within a multistep pathway that leads to full cellular transformation and, finally, the development of cellular malignancy
- a SIR2 reaction metabolite modulates TRPM2 ion channel
- SirT2 and its yeast counterpart Hst2 have a strong preference for histone H4K16Ac in their deacetylation activity in vitro and in vivo.
- Expressed SIRT2 blocks the entry to chromosome condensation and subsequent hyperploid cell formation in glioma cell lines.
- Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin
- Human silent information regulator 2 NAD (+)-dependent protein deacetylase, SIRT2, protect against alpha-synuclein-mediated toxicity in cellular models of Parkinson's disease. [SIRT2]
- reviewe emerging role of SIR2 as regulators of metabolism
- Therefore, our results suggest that the interaction between Sirt2 and 14-3-3 beta/gamma is a novel mechanism for the negative regulation of p53 beside the well-characterized Mdm2-mediated repression.
- Collectively, our findings identify a posttranslational mechanism that controls SIRT2 function, and they provide evidence for a novel regulatory circuitry involving Cdks, SIRT2, and microtubules.
- These observations demonstrate that p300 can inactivate Sirt2 by acetylation and that p300 may regulate the activity of p53 indirectly through Sirt2 in addition to its direct modification of p53.
- p300 undergoes a dynamic cycle of autoacetylation and deacetylation regulated by SIRT2.