CLK1

This article is about the kinase protein enzyme. For other uses, see CLK-1 (disambiguation).

CLK1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1Z57, 2VAG, 5J1V, 5J1W
Identifiers
Aliases	CLK1, CLK, CLK/STY, STY, CDC like kinase 1
External IDs	OMIM: 601951 MGI: 107403 HomoloGene: 101535 GeneCards: CLK1
Gene location (Human) Chr. Chromosome 2 (human) Band 2q33.1 Start 200,853,009 bp End 200,864,691 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 C1.3|1 29.09 cM Start 58,449,348 bp End 58,463,225 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube tibial nerve anterior pituitary left lobe of thyroid gland canal of the cervix gastric mucosa right lung body of pancreas right lobe of thyroid gland ganglionic eminence Top expressed in pineal gland spleen lymph node left lung lobe superior cervical ganglion blood ciliary body iris thymus uterus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding protein serine/threonine/tyrosine kinase activity protein serine/threonine kinase activity protein kinase activity protein tyrosine kinase activity non-membrane spanning protein tyrosine kinase activity protein binding ATP binding kinase activity Cellular component cytoplasm nucleus Biological process protein autophosphorylation peptidyl-tyrosine phosphorylation regulation of RNA splicing protein phosphorylation cell population proliferation peptidyl-threonine phosphorylation peptidyl-serine phosphorylation phosphorylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1195 12747 Ensembl ENSG00000013441 ENSMUSG00000026034 UniProt P49759 P22518 RefSeq (mRNA) NM_001024646 NM_001162407 NM_004071 NM_001042634 NM_009905 RefSeq (protein) NP_001155879 NP_004062 NP_001036099 Location (UCSC) Chr 2: 200.85 – 200.86 Mb Chr 1: 58.45 – 58.46 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Dual specificity protein kinase CLK1 is an enzyme that in humans is encoded by the CLK1 gene.

Function

This gene encodes a member of the CDC2-like (or LAMMER) family of dual specificity protein kinases. In the cell 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.

Interactions

CLK1 has been shown to interact with ASF/SF2.

External links

• Human CLK1 genome location and CLK1 gene details page in the UCSC Genome Browser.

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. doi:10.1016/S0021-9258(19)67807-5. PMID 1704889.
• Ben-David Y, Letwin K, Tannock L, Bernstein A, Pawson T (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. doi:10.1002/j.1460-2075.1991.tb07952.x. PMC 452648. 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, Prasad J, Manley JL, Bell JC, Duncan PI (1996). "The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution". EMBO J. 15 (2): 265–75. doi:10.1002/j.1460-2075.1996.tb00357.x. PMC 449941. PMID 8617202.
• Colwill K, Feng LL, Yeakley JM, Gish GD, Cáceres JF, Pawson T, Fu XD (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, Pawson T, Anderson SK (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 (18): 3241–53. doi:10.1242/jcs.113.18.3241. PMID 10954422.
• Kojima T, Zama T, Wada K, Onogi H, Hagiwara M (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, Nikolakaki E, Goedert M, Mandelkow EM, Gao QS, Andreadis A, Stamm S (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. S2CID 18388526.
• 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.
• Umehara H, Nishii Y, Morishima M, Kakehi Y, Kioka N, Amachi T, Koizumi J, Hagiwara M, Ueda K (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, Quick M, Webb R, Sunderland T, Bond J, Walder K, Augert G, Collier G (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.
• 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.
• Muraki M, Ohkawara B, Hosoya T, Onogi H, Koizumi J, Koizumi T, Sumi K, Yomoda J, Murray MV, Kimura H, Furuichi K, Shibuya H, Krainer AR, Suzuki M, Hagiwara M (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, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Velazquez-Dones A, Hagopian JC, Ma CT, Zhong XY, Zhou H, Ghosh G, Fu XD, Adams JA (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.