SRSF12

SRSF12, or serine/arginine-rich splicing factor 12, is a protein encoded by the SRSF12 gene in humans. It belongs to the serine/arginine-rich (SR) family of splicing factors, a group of nuclear proteins that regulate pre-mRNA splicing and other aspects of RNA metabolism.

Like other SR proteins, SRSF12 is characterized by RNA-binding activity and an arginine/serine-rich (RS) region that mediates protein–protein interactions within the spliceosome. The RS domain helps recruit and coordinate components of the splicing machinery, while the RNA-binding domains enable recognition of specific RNA motifs.

SRSF12 localizes primarily to the nucleus and is expressed across multiple tissues, though expression levels can vary depending on cellular context. Functionally, it participates in the regulation of constitutive and alternative splicing by influencing splice site selection and exon inclusion or skipping. Through its RS domain, SRSF12 interacts with other splicing factors and contributes to the assembly and regulation of the spliceosome.

Regulation of SRSF12 activity occurs largely through phosphorylation. SR protein kinases, such as SRPKs and CLKs, modulate its phosphorylation state, affecting RNA binding, protein interactions, and subnuclear localization, which in turn influences splicing outcomes.

In terms of clinical relevance, there are no well-defined disease-specific roles universally attributed to SRSF12, but as with other SR proteins, altered expression or function can impact splicing programs in development and disease. Ongoing research aims to clarify the specific targets and regulatory networks involving SRSF12.