Silent mating type information regulation 2 homolog
Silent mating type information regulation 2 S.cerevisiae homolog 7
SIR2 like protein 7
Sir2 related protein type 7
SIR2, S.CEREVISIAE, HOMOLOG-LIKE 7
SIR2-like protein 7
Sirtuin type 7
NAD-dependent protein deacetylase that specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays selectivity for a single histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors. SIRT7 thereby acts as a transcription repressor. Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells. These data suggest that SIRT7 may play a key role in oncogenic transformation by suppresses expression of tumor suppressor genes by locus-specific deacetylation of H3K18Ac at promoter regions. Also required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis: promotes the association of RNA polymerase I with the rDNA promoter region and coding region. Stimulates transcription activity of the RNA polymerase I complex. May also deacetylate p53/TP53 and promotes cell survival, however such data need additional confirmation.
Belongs to the sirtuin family. Class IV subfamily. Contains 1 deacetylase sirtuin-type domain.
Phosphorylated during mitosis.
Cytoplasm. Nucleus, nucleolus. Located close to the nuclear membrane when in the cytoplasm. Associated with chromatin. Associated with rDNA promoter and transcribed region. Associated with nucleolar organizer regions during mitosis.
ab95246 at 4 µg analysed on a 10% gel by SDS PAGE followed by coomassie staining (lane 1). ab95246 is >75% pure and has a molecular weight of 46 kDa. Lane 2 contains the protein molecular weight markers.
Recombinant Human SIRT7 protein (ab95246) 使用論文
has not yet been referenced specifically in any publications.