SF3A1 is a core component of the 17S U2 small nuclear ribonucleoprotein (snRNP) complex within the spliceosome, a large ribonucleoprotein machine that removes introns from precursor mRNA. SF3A1 participates in early spliceosome assembly and directly promotes branch-site adenosine selection, a critical step in pre-mRNA splicing catalysis. The protein contains a ubiquitin-like domain and tandem SURP domains that mediate transient interactions with other splicing factors: the ubiquitin-like domain recognizes stem-loop 4 of U1 snRNA in a sequence-specific manner via an RGG motif, thereby bridging U1 and U2 snRNPs, while the SURP1 domain binds the splicing factor SF1 during early spliceosomal complex assembly. SF3A1 dysregulation has been implicated in multiple cancers. In pancreatic cancer, carriers of specific alleles at rs2074733 in SF3A1 showed reduced disease risk, with synergistic effects observed when combined with smoking or drinking 1. In metastatic castration-resistant prostate cancer, SF3A1 expression is driven by non-coding enhancers and promotes tumor growth in vivo 2. Recent evidence suggests SF3A1 could serve as a therapeutic target in prostate, colorectal, and hepatocellular carcinoma 3. Additionally, SF3A1 has been identified as a target for hydroxysafflor yellow A in alleviating myocardial ischemia/reperfusion injury through regulation of mitochondrial energy metabolism 4.