The formation of the spliceosome includes the assembly of Sm proteins in an ordered manner onto snRNAs. This process is mediated by the survival of a motor neuron (SMN) protein and is enhanced by modification of specific Arginine residues in the Sm proteins to symmetrical dimethylarginines (sDMAs). sDMA modification of Sm proteins is catalyzed by the methylosome, a complex comprised of the type II methyltransferase PRMT5, also designated JAK-binding protein 1), (JBP1), pICln, and two novel factors. PRMT5 binds the Sm proteins via their Arginine- and Glycine-rich (RG) domains, while pICln binds the Sm domains. PRMT5 is a distinct member of the protein-Arginine methyltransferase (PRMT) family, and predominantly localizes to the cytoplasm in a wide variety of tissues. PRMT5 also associates specifically with the transcription start site region of the cyclin E1 promoter, and, therefore, is involved in the control of transcription and proliferation. The gene encoding human PRMT5 maps to chromosome 14q11.