CLK2

CDC-like kinase 2

Identifiers

CLK2; MGC61500; hCLK2

External IDs

OMIM: 602989 MGI: 1098669 HomoloGene: 33303 GeneCards: CLK2 Gene

2.7.12.1

Gene Ontology
Molecular function	• nucleotide binding • protein serine/threonine kinase activity • protein tyrosine kinase activity • ATP binding
Cellular component	• nucleus
Biological process	• protein amino acid phosphorylation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
155.23 – 155.25 Mb

Chr 3:
88.97 – 88.98 Mb

PubMed search

[1]

[2]

Dual specificity protein kinase CLK2 is an enzyme that in humans is encoded by the CLK2 gene.^[1]^[2]^[3]

This gene encodes a member of the CLK family of dual specificity protein kinases. CLK family members have shown to interact with, and phosphorylate, serine- and arginine-rich (SR) proteins of the spliceosomal complex, which is a part of the regulatory mechanism that enables the SR proteins to control RNA splicing. This protein kinase is involved in the regulation of several cellular processes and may serve as a link between cell cycle progression, apoptosis, and telomere length regulation.^[3]

References

^ Hanes J, von der Kammer H, Klaudiny J, Scheit KH (Jan 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.
^ 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: CLK2 CDC-like kinase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1196.

Lee K, Du C, Horn M, Rabinow L (1996). "Activity and autophosphorylation of LAMMER protein kinases.". J. Biol. Chem. 271 (44): 27299–303. doi:10.1074/jbc.271.44.27299. PMID 8910305.
Winfield SL, Tayebi N, Martin BM, et al. (1997). "Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease.". Genome Res. 7 (10): 1020–6. doi:10.1101/gr.7.10.1020. PMC 310674. PMID 9331372. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=310674.
Duncan PI, Stojdl DF, Marius RM, et al. (1998). "The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing.". Exp. Cell Res. 241 (2): 300–8. doi:10.1006/excr.1998.4083. PMID 9637771.
Tsujikawa M, Kurahashi H, Tanaka T, et al. (1998). "Homozygosity mapping of a gene responsible for gelatinous drop-like corneal dystrophy to chromosome 1p.". Am. J. Hum. Genet. 63 (4): 1073–7. doi:10.1086/302071. PMC 1377503. PMID 9758629. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1377503.
Nayler O, Schnorrer F, Stamm S, Ullrich A (1999). "The cellular localization of the murine serine/arginine-rich protein kinase CLK2 is regulated by serine 141 autophosphorylation.". J. Biol. Chem. 273 (51): 34341–8. doi:10.1074/jbc.273.51.34341. PMID 9852100.
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.
Nothwang HG, Kim HG, Aoki J, et al. (2001). "Functional hemizygosity of PAFAH1B3 due to a PAFAH1B3-CLK2 fusion gene in a female with mental retardation, ataxia and atrophy of the brain.". Hum. Mol. Genet. 10 (8): 797–806. doi:10.1093/hmg/10.8.797. PMID 11285245.
Ravichandran LV, Chen H, Li Y, Quon MJ (2002). "Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor.". Mol. Endocrinol. 15 (10): 1768–80. doi:10.1210/me.15.10.1768. PMID 11579209.
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.
Jiang N, Bénard CY, Kébir H, et al. (2003). "Human CLK2 links cell cycle progression, apoptosis, and telomere length regulation.". J. Biol. Chem. 278 (24): 21678–84. doi:10.1074/jbc.M300286200. PMID 12670948.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
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.
Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129.
Collis SJ, Barber LJ, Clark AJ, et al. (2007). "HCLK2 is essential for the mammalian S-phase checkpoint and impacts on Chk1 stability.". Nat. Cell Biol. 9 (4): 391–401. doi:10.1038/ncb1555. PMID 17384638.

CLK2

References

Further reading