Dual specificity protein kinase CLK1 (CLK1)

Dual specificity protein kinase CLK1 is an enzyme encoded by the CLK1 gene in humans. It belongs to the LAMMER family of kinases and exhibits dual specificity, phosphorylating both serine/threonine and tyrosine residues. CLK1 is primarily localized in the nucleus, where it phosphorylates serine/arginine-rich (SR) proteins involved in spliceosomal complex assembly and alternative mRNA splicing. These actions regulate the activity and localization of splicing factors, thus influencing pre-mRNA processing and splice site selection. CLK1 activity is regulated by phosphorylation events at various residues and by the conformation of its N-terminal domain[1][2][3][6]. CLK1 plays important roles in gene expression regulation and has been implicated in diseases such as cancer and neurodegenerative disorders due to its central role in alternative splicing control[2][6]. Experimental inhibitors such as hymenialdisine have been identified, and understanding CLK1 structure-function relationships is a focus for targeted drug development[2][5].

Other names

CDC-like kinase 1CDC2-like kinase 1LAMMER kinaseCLK (less specific)

Inhibition of kinase activity (ATP-competitive inhibition); Modulation of alternative splicing by inhibiting SR protein phosphorylation