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Small nuclear ribonucleoprotein polypeptide A (SNRPA) is a core protein component of the U1 small nuclear ribonucleoprotein (snRNP) complex, which is essential for the recognition of the 5' splice site in precursor mRNAs during pre-mRNA splicing. SNRPA binds specifically to stem loop II of U1 snRNA, facilitating spliceosome assembly and regulation of RNA processing. The protein also autoregulates its own pre-mRNA by inhibiting polyadenylation via dimerization, thereby linking splicing and polyadenylation. In immune cells, SNRPA has been shown to modulate expression and alternative polyadenylation of specific mRNAs such as STAT5B, influencing Th1 differentiation. Germline mutations in SNRPA result in neurodevelopmental syndromes, and dysregulation of SNRPA has been implicated in various cancers by affecting cell survival and proliferation through RNA processing, including binding to G-quadruplex structures in oncogenic mRNAs. SNRPA interacts with factors such as CDC5L and has a role in nuclear retention of long noncoding RNAs. Despite its critical roles, SNRPA is not currently considered a direct therapeutic target and there are no drugs clinically targeting it.
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