Two SR Protein-specific Kinases, SRPK1 and SRPK2, have been shown to phosphorylate specifically the RS motifs of the SR family of splicing factors. Phosphorylation of an SR protein (ASF/SF2) by either SRPk1 or 2 enhanced its interaction with another RS domain-containing protein, and overexpression of either kinase induced specific redistribution of splicing factors in the nucleus. SRPK1 is considered to be a constitutively active kinase predominantly active in testis. Inhibition of SRPK1 may render male germ cell and other tumors insensitive to cisplatin. GenBank NM_003137
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