CLK1

Dual specificity protein kinase CLK1 is an enzyme that in humans is encoded by the CLK1 gene.[5][6]

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)[1] Band 2q33.1 Start 200,853,009 bp[1] End 200,864,744 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1 C1.3|1 29.09 cM Start 58,410,189 bp[2] End 58,424,066 bp[2]
RNA expression pattern 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 • GO:0001948 protein binding • ATP binding • kinase activity Cellular component • cytoplasm • cell nucleus Biological process • autophosphorylation • peptidyl-tyrosine phosphorylation • regulation of RNA splicing • protein phosphorylation • cellular 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: 58.41 – 58.42 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

Interactions

CLK1 has been shown to interact with ASF/SF2.[7][8]

References

1. GRCh38: Ensembl release 89: ENSG00000013441 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026034 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: CLK1 CDC-like kinase 1".
7. Colwill K, Feng LL, Yeakley JM, Gish GD, Cáceres JF, Pawson T, Fu XD (Oct 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.
8. Umehara H, Nishii Y, Morishima M, Kakehi Y, Kioka N, Amachi T, Koizumi J, Hagiwara M, Ueda K (Feb 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.

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. 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. 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. 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. 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.
• 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. doi:10.1038/nature04209. PMID 16189514.
• 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.