CLK1

CDC-like kinase 1

PDB rendering based on 1z57.

Available structures
PDB	1Z57, 2VAG

Identifiers

Symbols

CLK1; CLK; CLK/STY; STY

External IDs

OMIM: 601951 HomoloGene: 101535 GeneCards: CLK1 Gene

EC number

2.7.12.1

Gene Ontology
Molecular function	• nucleotide binding • protein serine/threonine kinase activity • non-membrane spanning protein tyrosine kinase activity • ATP binding
Cellular component	• nucleus
Biological process	• cell proliferation • peptidyl-serine phosphorylation • peptidyl-threonine phosphorylation • peptidyl-tyrosine phosphorylation • protein autophosphorylation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

NM_001162407.1

n/a

RefSeq (protein)

NP_001155879.1

NP_001036099.1

Location (UCSC)

Chr 2:
201.72 – 201.73 Mb

Chr 1:
58.47 – 58.48 Mb

PubMed search

[1]

[2]

Dual specificity protein kinase CLK1 is an enzyme that in humans is encoded by the CLK1 gene.^[1]^[2]

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.^[2]

Interactions

CLK1 has been shown to interact with ASF/SF2.^[3]^[4]

References

^ Talmadge CB, Finkernagel S, Sumegi J, Sciorra L, Rabinow L (Dec 1998). "Chromosomal mapping of three human LAMMER protein-kinase-encoding genes". Hum Genet 103 (4): 523–4. doi:10.1007/s004390050861. PMID 9856501.
^ ^a ^b "Entrez Gene: CLK1 CDC-like kinase 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1195.
^ Colwill, K; Feng L L, Yeakley J M, Gish G D, Cáceres J F, Pawson T, Fu X D (Oct. 1996). "SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors". J. Biol. Chem. (UNITED STATES) 271 (40): 24569–75. doi:10.1074/jbc.271.40.24569. ISSN 0021-9258. PMID 8798720.
^ Umehara, Hiroshi; Nishii Yoichi, Morishima Masaki, Kakehi Yoshiyuki, Kioka Noriyuki, Amachi Teruo, Koizumi Jun, Hagiwara Masatoshi, Ueda Kazumitsu (Feb. 2003). "Effect of cisplatin treatment on speckled distribution of a serine/arginine-rich nuclear protein CROP/Luc7A". Biochem. Biophys. Res. Commun. (United States) 301 (2): 324–9. doi:10.1016/S0006-291X(02)03017-6. ISSN 0006-291X. PMID 12565863.

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. PMC 452648. PMID 1825055. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=452648.
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. PMC 449941. PMID 8617202. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=449941.
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. doi:10.1074/jbc.271.40.24569. 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. doi:10.1016/S0378-1119(96)00436-2. PMID 8973360.
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. doi:10.1074/jbc.274.38.26697. 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. PMC 1223332. PMID 12549978. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223332.
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. doi:10.1016/S0006-291X(02)03017-6. 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. doi:10.1016/S0006-291X(03)00549-7. 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. doi:10.1128/MCB.23.12.4139-4149.2003. PMC 156123. PMID 12773558. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=156123.
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. PMC 395752. PMID 14759258. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=395752.
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.

PDB gallery

1z57: Crystal structure of human CLK1 in complex with 10Z-Hymenialdisine

CLK1

Interactions

References

Further reading