SRp55
SRp55 is a serine/arginine-rich (SR) splicing factor that belongs to the SR protein family. Members of this family are involved in the regulation of pre-mRNA splicing, in particular alternative splicing. SRp55 proteins typically migrate around 55 kilodaltons and contain one or more RNA recognition motifs (RRMs) for binding RNA, together with an arginine-serine-rich (RS) domain that mediates protein interactions and regulation by phosphorylation.
Function: SRp55 participates in recognizing exonic splicing enhancers and modulating splice site selection, promoting exon inclusion
Structure and regulation: The RS domain is a major regulatory module; its phosphorylation state, controlled by
SRp55 typically resides in the nucleus but can shuttle to the cytoplasm under certain conditions.
Interactions and localization: It interacts with core spliceosome components and other SR proteins; localization and activity
Clinical and research notes: Misregulation of SRp55 has been reported in studies of cancer and other diseases,
Because of its central role in splicing, SRp55 is a common subject of studies on RNA processing