CLK4

CLK4 is the most divergent of the CDC-like kinases and remains the least understood. It preserves the family signature of an RS-rich N-terminal segment followed by a dual-specificity catalytic domain capable of activation-loop tyrosine autophosphorylation and of serine phosphorylation of SR-type splicing factors. Expression is comparatively low and tissue-restricted, and its nuclear localization overlaps the speckle compartment used by CLK1, CLK2, and CLK3. Functional studies based on overexpression and inhibition place CLK4 in the control of pre-mRNA splicing and cell proliferation, although isoform-specific substrates are still being defined. Recombinant CLK4 completes CLK-family panels for splicing research and kinase-inhibitor selectivity assessment.