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U2 snRNP-associated SURP domain-containing protein (U2SURP) is a member of the serine/arginine-rich (SR) protein family that plays a critical role in RNA metabolism, specifically in the regulation of pre-mRNA splicing[1][2][3]. It is a component of the U2 small nuclear ribonucleoprotein (snRNP) complex, a central player in the spliceosome machinery responsible for the removal of introns from precursor mRNAs[2][6]. U2SURP binds RNA and interacts with other spliceosomal proteins including RBM17 and CHERP, forming a functional module that coordinates alternative splicing and regulates a specific network of transcripts[2]. It is predominantly localized in the nucleoplasm[3][5]. U2SURP is upregulated in certain cancers, such as triple-negative breast cancer, where it is linked to oncogenic phenotypes and poor prognosis through its effects on alternative splicing of cancer-relevant genes[1]. While U2SURP is not established as a direct therapeutic target (such as a receptor, enzyme, or transporter), its critical role in splicing regulation implicates it indirectly in diseases caused by splicing dysregulation[1][2][4].
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