CLK2 Protein, Human (Active, GST)

CLK2 protein, a dual specificity kinase, exhibits activity on both serine/threonine and tyrosine-containing substrates. Notably, it phosphorylates serine- and arginine-rich (SR) proteins within the spliceosomal complex, playing a role in the intricate network of regulatory mechanisms governing RNA splicing. This kinase's influence can lead to the redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Beyond its role in RNA processing, CLK2 serves as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes through phosphorylation. Additionally, it phosphorylates PPP2R5B, promoting the assembly of the PP2A phosphatase with the PPP2R5B-AKT1 complex, ultimately leading to the dephosphorylation of AKT1. CLK2 further exhibits a diverse substrate specificity by phosphorylating PTPN1, SRSF1, and SRSF3. Notably, it regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and phosphorylates PAGE4, attenuating its ability to potentiate the transcriptional activator activity of JUN.