Histone deacetylase complex subunit SAP30 (SAP30)

Histone deacetylase complex subunit SAP30 (SAP30) is a core component of the SIN3/HDAC histone deacetylase complex, acting as a scaffold that recruits the complex to specific genomic loci, thereby mediating transcriptional repression through histone deacetylation[1][2][3][4][5][6][7]. SAP30 interacts with key partners such as SIN3A, HDAC1, HDAC2, RbAp46/48, and others, influencing chromatin structure and gene expression. It can bind DNA and is regulated by nuclear phosphoinositides. In human cancers, including clear cell renal cell carcinoma, SAP30 is implicated in tumor proliferation and apoptosis—partly via repression of MT1G and p53 activity—making it a potential therapeutic and prognostic target[4]. No drugs are known to directly target SAP30, but it is essential for the function of HDAC complexes, which are therapeutically targeted in oncology and other diseases.

Other names

Sin3A-associated protein, 30 kDaSin3 corepressor complex subunit SAP3030 kDa Sin3-associated polypeptideSin3-associated polypeptide p30Sin3-associated polypeptide, 30 kDaSAP30

When part of an HDAC complex, inhibition by HDAC inhibitors leads to increased histone acetylation and de-represssion of gene expression; SAP30 mediates recruitment of HDAC activity to specific gene loci.