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SAP30-binding protein (SAP30BP) is a nuclear protein in humans that serves as an essential cofactor in RNA splicing and transcriptional repression. SAP30BP interacts tightly with CDK11 and cyclins L1/L2, functioning as a critical activator of CDK11 kinase activity and thereby regulating global pre-mRNA splicing[1]. It is also a key cofactor of RBM17 (SPF45), guiding its recruitment to active spliceosomes—particularly for the splicing of a subset of short introns with truncated polypyrimidine tracts, where it promotes assembly of the spliceosome independently of the canonical U2AF2–U2AF1 heterodimer[2][4]. Beyond splicing, SAP30BP can promote histone deacetylase activity, resulting in epigenetic modification through H3 deacetylation[3]. While not generally classified as a therapeutic target (receptor, enzyme, transporter), SAP30BP is essential for RNA processing and cell cycle regulation, which implicates it in diseases such as cancer, although no targeted drugs or biomarker applications are currently reported[1][2][3][4].
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