Splicing factor U2AF 65 kDa subunit (U2AF2)

Splicing factor U2AF 65 kDa subunit (U2AF2) is a key RNA-binding protein essential for pre-mRNA splicing in eukaryotes[1][2]. U2AF2 forms a heterodimer with U2AF1 and is required for the recognition of the polypyrimidine (Py) tract at the 3′ splice site of introns during spliceosome assembly[1][2]. The protein contains three RNA recognition motifs (RRMs) and an arginine/serine-rich (RS) domain, binding to uridine-rich sequences and establishing protein–protein interactions with other splicing factors such as SF1 and UAP56[1]. U2AF2’s activity is critical for spliceosome fidelity—it proofreads and selects strong Py-tracts while disfavoring weak, non-bona fide splice sites; dysregulation of its assembly or RNA binding results in alternative splicing errors[2][3]. Mutations in U2AF2 have been implicated in various cancers, developmental syndromes, retinal disease, cystic fibrosis, and autoimmune conditions[2]. While U2AF2 is not a conventional drug target or receptor, understanding its function is vital for research into RNA biology and the molecular basis of pre-mRNA splicing diseases[1][2][3].

Other names

U2AF65hU2AF65U2AF^65^U2 auxiliary factor 65 kDa subunitU2 snRNP auxiliary factor large subunitSplicing factor U2AF 65 kD subunitU2 small nuclear ribonucleoprotein auxiliary factor (65kD)DEVDFBU2 (RNU2) small nuclear RNA auxiliary factor 2