In addition, CLK1 overexpression promoted exon 17 inclusion splicing and increased the expression of PKCβII through phosphorylation of SR proteins in response to insulin stumilization.5 It was reported that CLK1 phosphorylated SRSF5 on Ser 250, thereby, affecting alternative splicing of METTL14 and Cyclin L2 to promote cell metastasis and viability in pancreatic cancer.44 Inhibition of the CLKs enzymatic activities preferentially inhibited the phosphorylation of SRSF10 at Ser 129, 131, and 133 eliciting p53-dependent apoptosis in human colorectal cancer cells. This evidence concerns the gene CLK1 and familial pancreatic carcinoma.