The protein encoded by this gene belongs to the CDC2-like protein kinase (CLK) family. This protein kinase can interact with and phosphorylate the serine- and arginine-rich (SR) proteins, which are known to play an important role in the formation of spliceosomes, and thus may be involved in the regulation of alternative splicing. Studies in the Israeli sand rat Psammomys obesus suggested that the ubiquitin-like 5 (UBL5/BEACON), a highly conserved ubiquitin-like protein, may interact with and regulate the activity of this kinase. Multiple alternatively spliced transcript variants have been observed, but the full-length natures of which have not yet been determined. [provided by RefSeq, Jul 2008].
Eisenreich, Zakrzewicz, Huber, Thierbach, Pepke, Goldin-Lang, Schultheiss, Pries, Rauch: "Regulation of pro-angiogenic tissue factor expression in hypoxia-induced human lung cancer cells." in: Oncology reports, Vol. 30, Issue 1, pp. 462-70, (2013) (PubMed).
McNally, Huang, Janis, Liu, Olejniczak, Reilly: "Structural analysis of UBL5, a novel ubiquitin-like modifier." in: Protein science : a publication of the Protein Society, Vol. 12, Issue 7, pp. 1562-6, (2003) (PubMed).
Katsu, Onogi, Wada, Kawaguchi, Hagiwara: "Novel SR-rich-related protein clasp specifically interacts with inactivated Clk4 and induces the exon EB inclusion of Clk." in: The Journal of biological chemistry, Vol. 277, Issue 46, pp. 44220-8, (2002) (PubMed).
Schultz, Jones, Bork, Sheer, Blencke, Steyrer, Wellbrock, Bevec, Ullrich, Wallasch: "Molecular characterization of a cDNA encoding functional human CLK4 kinase and localization to chromosome 5q35 [correction of 4q35]." in: Genomics, Vol. 71, Issue 3, pp. 368-70, (2001) (PubMed).