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WD repeat domain 33 (WDR33) is a highly conserved nuclear protein that acts as a central subunit of the cleavage and polyadenylation specificity factor (CPSF) complex, directly binding and recognizing the AAUAAA polyadenylation signal in pre-mRNA to facilitate 3′ end processing and mRNA maturation. The full-length protein contains multiple WD repeat domains and localizes to the nucleus, participating in the assembly of active RNA processing complexes. Alternative transcript variants generate non-canonical isoforms with additional roles, including modulation of the innate immune response via STING interaction. As a member of the WD repeat protein family, WDR33 forms stable protein-protein interaction platforms crucial for a variety of essential cellular processes, though it is not a direct therapeutic target or clinical biomarker at present.
Not applicable (no drugs known to target WDR33; it acts as part of a multiprotein complex mediating RNA 3′ end processing)
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