CLK1

From Wikipedia, the free encyclopedia

CDC-like kinase 1

PDB rendering based on 1z57.

Available structures: 1z57

Identifiers

Symbol(s)

CLK1; CLK; CLK/STY; STY

External IDs

OMIM: 601951 HomoloGene: 48263

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • non-membrane spanning protein tyrosine kinase activity • ATP binding • transferase activity
Cellular Component:	• nucleus
Biological Process:	• regulation of progression through cell cycle • cell proliferation • peptidyl-serine phosphorylation • peptidyl-threonine phosphorylation • peptidyl-tyrosine phosphorylation • protein amino acid autophosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

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n/a

Refseq

NM_001024646 (mRNA)
NP_001019817 (protein)

n/a (mRNA)
n/a (protein)

Location

Chr 2: 201.43 - 201.44 Mb

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Pubmed search

[1]

n/a

CDC-like kinase 1, also known as CLK1, is a human gene.^[1]

This gene encodes a member of the CDC2-like (or LAMMER) family of dual specificity protein kinases. In the nucleus, the encoded protein phosphorylates serine/arginine-rich proteins involved in pre-mRNA processing, releasing them into the nucleoplasm. The choice of splice sites during pre-mRNA processing may be regulated by the concentration of transacting factors, including serine/arginine rich proteins. Therefore, the encoded protein may play an indirect role in governing splice site selection.^[1]

[edit] References

^ ^a ^b Entrez Gene: CLK1 CDC-like kinase 1.

[edit] Further reading

Johnson KW, Smith KA (1991). "Molecular cloning of a novel human cdc2/CDC28-like protein kinase.". J. Biol. Chem. 266 (6): 3402–7. PMID 1704889.
Ben-David Y, Letwin K, Tannock L, et al. (1991). "A mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulators.". EMBO J. 10 (2): 317–25. PMID 1825055.
Hanes J, von der Kammer H, Klaudiny J, Scheit KH (1995). "Characterization by cDNA cloning of two new human protein kinases. Evidence by sequence comparison of a new family of mammalian protein kinases.". J. Mol. Biol. 244 (5): 665–72. doi:10.1006/jmbi.1994.1763. PMID 7990150.
Colwill K, Pawson T, Andrews B, et al. (1996). "The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution.". EMBO J. 15 (2): 265–75. PMID 8617202.
Colwill K, Feng LL, Yeakley JM, et al. (1996). "SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors.". J. Biol. Chem. 271 (40): 24569–75. PMID 8798720.
Nestel FP, Colwill K, Harper S, et al. (1997). "RS cyclophilins: identification of an NK-TR1-related cyclophilin.". Gene 180 (1-2): 151–5. PMID 8973360.
Talmadge CB, Finkernagel S, Sumegi J, et al. (1998). "Chromosomal mapping of three human LAMMER protein-kinase-encoding genes.". Hum. Genet. 103 (4): 523–4. PMID 9856501.
Moeslein FM, Myers MP, Landreth GE (1999). "The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B.". J. Biol. Chem. 274 (38): 26697–704. PMID 10480872.
Menegay HJ, Myers MP, Moeslein FM, Landreth GE (2000). "Biochemical characterization and localization of the dual specificity kinase CLK1.". J. Cell. Sci. 113 ( Pt 18): 3241–53. PMID 10954422.
Kojima T, Zama T, Wada K, et al. (2001). "Cloning of human PRP4 reveals interaction with Clk1.". J. Biol. Chem. 276 (34): 32247–56. doi:10.1074/jbc.M103790200. PMID 11418604.
Hartmann AM, Rujescu D, Giannakouros T, et al. (2001). "Regulation of alternative splicing of human tau exon 10 by phosphorylation of splicing factors.". Mol. Cell. Neurosci. 18 (1): 80–90. doi:10.1006/mcne.2001.1000. PMID 11461155.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Lai MC, Lin RI, Tarn WY (2003). "Differential effects of hyperphosphorylation on splicing factor SRp55.". Biochem. J. 371 (Pt 3): 937–45. doi:10.1042/BJ20021827. PMID 12549978.
Umehara H, Nishii Y, Morishima M, et al. (2003). "Effect of cisplatin treatment on speckled distribution of a serine/arginine-rich nuclear protein CROP/Luc7A.". Biochem. Biophys. Res. Commun. 301 (2): 324–9. PMID 12565863.
Kantham L, Kerr-Bayles L, Godde N, et al. (2003). "Beacon interacts with cdc2/cdc28-like kinases.". Biochem. Biophys. Res. Commun. 304 (1): 125–9. PMID 12705895.
Prasad J, Manley JL (2003). "Regulation and substrate specificity of the SR protein kinase Clk/Sty.". Mol. Cell. Biol. 23 (12): 4139–49. PMID 12773558.
Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance.". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMID 14759258.
Muraki M, Ohkawara B, Hosoya T, et al. (2004). "Manipulation of alternative splicing by a newly developed inhibitor of Clks.". J. Biol. Chem. 279 (23): 24246–54. doi:10.1074/jbc.M314298200. PMID 15010457.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Velazquez-Dones A, Hagopian JC, Ma CT, et al. (2006). "Mass spectrometric and kinetic analysis of ASF/SF2 phosphorylation by SRPK1 and Clk/Sty.". J. Biol. Chem. 280 (50): 41761–8. doi:10.1074/jbc.M504156200. PMID 16223727.