Biology:CLK2
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Generic protein structure example |
Dual specificity protein kinase CLK2 is an enzyme that in humans is encoded by the CLK2 gene.[1][2][3]
Function
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/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
- ↑ "Characterization by cDNA cloning of two new human protein kinases. Evidence by sequence comparison of a new family of mammalian protein kinases". Journal of Molecular Biology 244 (5): 665–72. Dec 1994. doi:10.1006/jmbi.1994.1763. PMID 7990150.
- ↑ "Chromosomal mapping of three human LAMMER protein-kinase-encoding genes". Human Genetics 103 (4): 523–4. Oct 1998. doi:10.1007/s004390050861. PMID 9856501.
- ↑ 3.0 3.1 "Entrez Gene: CLK2 CDC-like kinase 2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1196.
External links
- Human CLK2 genome location and CLK2 gene details page in the UCSC Genome Browser.
- Overview of all the structural information available in the PDB for UniProt: P49760 (Dual specificity protein kinase CLK2) at the PDBe-KB.
Further reading
- "Activity and autophosphorylation of LAMMER protein kinases". The Journal of Biological Chemistry 271 (44): 27299–303. Nov 1996. doi:10.1074/jbc.271.44.27299. PMID 8910305.
- "Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease". Genome Research 7 (10): 1020–6. Oct 1997. doi:10.1101/gr.7.10.1020. PMID 9331372.
- "The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing". Experimental Cell Research 241 (2): 300–8. Jun 1998. doi:10.1006/excr.1998.4083. PMID 9637771.
- "Homozygosity mapping of a gene responsible for gelatinous drop-like corneal dystrophy to chromosome 1p". American Journal of Human Genetics 63 (4): 1073–7. Oct 1998. doi:10.1086/302071. PMID 9758629.
- "The cellular localization of the murine serine/arginine-rich protein kinase CLK2 is regulated by serine 141 autophosphorylation". The Journal of Biological Chemistry 273 (51): 34341–8. Dec 1998. doi:10.1074/jbc.273.51.34341. PMID 9852100.
- "The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B". The Journal of Biological Chemistry 274 (38): 26697–704. Sep 1999. doi:10.1074/jbc.274.38.26697. PMID 10480872.
- "Functional hemizygosity of PAFAH1B3 due to a PAFAH1B3-CLK2 fusion gene in a female with mental retardation, ataxia and atrophy of the brain". Human Molecular Genetics 10 (8): 797–806. Apr 2001. doi:10.1093/hmg/10.8.797. PMID 11285245.
- "Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor". Molecular Endocrinology 15 (10): 1768–80. Oct 2001. doi:10.1210/mend.15.10.0711. PMID 11579209.
- "Human CLK2 links cell cycle progression, apoptosis, and telomere length regulation". The Journal of Biological Chemistry 278 (24): 21678–84. Jun 2003. doi:10.1074/jbc.M300286200. PMID 12670948.
- "An unappreciated role for RNA surveillance". Genome Biology 5 (2): R8. 2005. doi:10.1186/gb-2004-5-2-r8. PMID 14759258.
- "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology 14 (16): 1436–50. Aug 2004. doi:10.1016/j.cub.2004.07.051. PMID 15324660. http://faculty.washington.edu/scottjdw/pdfs/jin_curr_biol_2004_p1436.pdf.
- "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research 16 (1): 55–65. Jan 2006. doi:10.1101/gr.4039406. PMID 16344560.
- "HCLK2 is essential for the mammalian S-phase checkpoint and impacts on Chk1 stability". Nature Cell Biology 9 (4): 391–401. Apr 2007. doi:10.1038/ncb1555. PMID 17384638. https://escholarship.org/uc/item/2h12m58f.