Arginine and serine rich protein 1 (RSRP1)

Arginine and serine rich protein 1 (RSRP1) is a nuclear, RNA-binding protein that serves as a spliceosomal factor, participating in spliceosome assembly and alternative splicing regulation. RSRP1 is enriched in arginine and serine residues and mediates interactions with other spliceosome proteins, notably via serine phosphorylation within its RS domain, particularly at residues S107 and S109. Functionally, RSRP1 regulates the splicing of genes such as PARP6 and contributes to oncogenic phenotypes by facilitating alternative splicing events that promote NF-κB activation, thereby supporting glioblastoma cell invasion, apoptosis resistance, and mesenchymal transdifferentiation. Elevated RSRP1 expression is strongly associated with high-grade gliomas and the aggressive mesenchymal subtype, suggesting a role in tumor progression. While essential in RNA processing and cancer biology, RSRP1 is not currently considered a classic therapeutic target such as a receptor, enzyme, or transporter.

Other names

Arginine/serine-rich protein 1C1orf63HT033NPD014DJ465N24.2.1UPF0471 protein C1orf63D4Ucla2D4Wsu53eLOC101928189LOC105376881RGD1359529