Q92879

Members of the CELF/BRUNOL protein family contain two N-terminal RNA recognition motif (RRM) domains, one C-terminal RRM domain, and a divergent segment of 160-230 aa between the second and third RRM domains. CELF1 plays a crucial role in the regulation of RNA splicing and translation, particularly in the context of myotonic dystrophy, a neuromuscular disorder characterized by a (CTG)n repeat expansion in the myotonin protein kinase gene (DMPK). CELF1 is primarily located in the nucleus, where CELF1 binds to CUG repeat sequences, influencing the expression of key regulatory proteins such as p21. Nuclear localization of CELF1 is vital for function, as nuclear positioning allows for precise modulation of mRNA processing and translation in response to cellular signals.