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{{Infobox_gene}}
{{PBB_Controls
'''Dual specificity protein kinase CLK2''' is an [[enzyme]] that in humans is encoded by the ''CLK2'' [[gene]].<ref name="pmid7990150">{{cite journal | vauthors = Hanes J, von der Kammer H, Klaudiny J, Scheit KH | title = Characterization by cDNA cloning of two new human protein kinases. Evidence by sequence comparison of a new family of mammalian protein kinases | journal = Journal of Molecular Biology | volume = 244 | issue = 5 | pages = 665–72 | date = Dec 1994 | pmid = 7990150 | pmc =  | doi = 10.1006/jmbi.1994.1763 }}</ref><ref name="pmid9856501">{{cite journal | vauthors = Talmadge CB, Finkernagel S, Sumegi J, Sciorra L, Rabinow L | title = Chromosomal mapping of three human LAMMER protein-kinase-encoding genes | journal = Human Genetics | volume = 103 | issue = 4 | pages = 523–4 | date = Oct 1998 | pmid = 9856501 | pmc =  | doi = 10.1007/s004390050861 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CLK2 CDC-like kinase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1196| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = CDC-like kinase 2
| HGNCid = 2069
| Symbol = CLK2
| AltSymbols =; MGC61500; hCLK2
| OMIM = 602989
| ECnumber = 
| Homologene = 33303
| MGIid = 1098669
| GeneAtlas_image1 = PBB_GE_CLK2_203229_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1196
    | Hs_Ensembl = ENSG00000176444
    | Hs_RefseqProtein = XP_001128256
    | Hs_RefseqmRNA = XM_001128256
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 153499283
    | Hs_GenLoc_end = 153509931
    | Hs_Uniprot = P49760
    | Mm_EntrezGene = 12748
    | Mm_Ensembl = ENSMUSG00000068917
    | Mm_RefseqmRNA = NM_007712
    | Mm_RefseqProtein = NP_031738
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 89252962
    | Mm_GenLoc_end = 89262506
    | Mm_Uniprot = Q3UFP4
  }}
}}
'''CDC-like kinase 2''', also known as '''CLK2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CLK2 CDC-like kinase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1196| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a member of the CLK family of [[dual specificity protein kinase]]s. CLK family members have shown to interact with, and [[phosphorylate]], [[serine]]/[[arginine]]-rich (SR) proteins of the [[spliceosome|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.<ref name="entrez">{{cite web | title = Entrez Gene: CLK2 CDC-like kinase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1196| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: CLK2 CDC-like kinase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1196| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
==External links==
* {{UCSC gene info|CLK2}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Lee K, Du C, Horn M, Rabinow L | title = Activity and autophosphorylation of LAMMER protein kinases | journal = The Journal of Biological Chemistry | volume = 271 | issue = 44 | pages = 27299–303 | date = Nov 1996 | pmid = 8910305 | doi = 10.1074/jbc.271.44.27299 }}
| citations =
* {{cite journal | vauthors = Winfield SL, Tayebi N, Martin BM, Ginns EI, Sidransky E | title = Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease | journal = Genome Research | volume = 7 | issue = 10 | pages = 1020–6 | date = Oct 1997 | pmid = 9331372 | pmc = 310674 | doi = 10.1101/gr.7.10.1020 }}
*{{cite journal | author=Hanes J, von der Kammer H, Klaudiny J, Scheit KH |title=Characterization by cDNA cloning of two new human protein kinases. Evidence by sequence comparison of a new family of mammalian protein kinases. |journal=J. Mol. Biol. |volume=244 |issue= 5 |pages= 665-72 |year= 1995 |pmid= 7990150 |doi= 10.1006/jmbi.1994.1763 }}
* {{cite journal | vauthors = Duncan PI, Stojdl DF, Marius RM, Scheit KH, Bell JC | title = The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing | journal = Experimental Cell Research | volume = 241 | issue = 2 | pages = 300–8 | date = Jun 1998 | pmid = 9637771 | doi = 10.1006/excr.1998.4083 }}
*{{cite journal  | author=Lee K, Du C, Horn M, Rabinow L |title=Activity and autophosphorylation of LAMMER protein kinases. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27299-303 |year= 1996 |pmid= 8910305 |doi= }}
* {{cite journal | vauthors = Tsujikawa M, Kurahashi H, Tanaka T, Okada M, Yamamoto S, Maeda N, Watanabe H, Inoue Y, Kiridoshi A, Matsumoto K, Ohashi Y, Kinoshita S, Shimomura Y, Nakamura Y, Tano Y | title = Homozygosity mapping of a gene responsible for gelatinous drop-like corneal dystrophy to chromosome 1p | journal = American Journal of Human Genetics | volume = 63 | issue = 4 | pages = 1073–7 | date = Oct 1998 | pmid = 9758629 | pmc = 1377503 | doi = 10.1086/302071 }}
*{{cite journal | author=Winfield SL, Tayebi N, Martin BM, ''et al.'' |title=Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease. |journal=Genome Res. |volume=7 |issue= 10 |pages= 1020-6 |year= 1997 |pmid= 9331372 |doi= }}
* {{cite journal | vauthors = Nayler O, Schnorrer F, Stamm S, Ullrich A | title = The cellular localization of the murine serine/arginine-rich protein kinase CLK2 is regulated by serine 141 autophosphorylation | journal = The Journal of Biological Chemistry | volume = 273 | issue = 51 | pages = 34341–8 | date = Dec 1998 | pmid = 9852100 | doi = 10.1074/jbc.273.51.34341 }}
*{{cite journal | author=Duncan PI, Stojdl DF, Marius RM, ''et al.'' |title=The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing. |journal=Exp. Cell Res. |volume=241 |issue= 2 |pages= 300-8 |year= 1998 |pmid= 9637771 |doi= 10.1006/excr.1998.4083 }}
* {{cite journal | vauthors = Moeslein FM, Myers MP, Landreth GE | title = The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B | journal = The Journal of Biological Chemistry | volume = 274 | issue = 38 | pages = 26697–704 | date = Sep 1999 | pmid = 10480872 | doi = 10.1074/jbc.274.38.26697 }}
*{{cite journal | author=Tsujikawa M, Kurahashi H, Tanaka T, ''et al.'' |title=Homozygosity mapping of a gene responsible for gelatinous drop-like corneal dystrophy to chromosome 1p. |journal=Am. J. Hum. Genet. |volume=63 |issue= 4 |pages= 1073-7 |year= 1998 |pmid= 9758629 |doi= }}
* {{cite journal | vauthors = Nothwang HG, Kim HG, Aoki J, Geisterfer M, Kübart S, Wegner RD, van Moers A, Ashworth LK, Haaf T, Bell J, Arai H, Tommerup N, Ropers HH, Wirth J | title = Functional hemizygosity of PAFAH1B3 due to a PAFAH1B3-CLK2 fusion gene in a female with mental retardation, ataxia and atrophy of the brain | journal = Human Molecular Genetics | volume = 10 | issue = 8 | pages = 797–806 | date = Apr 2001 | pmid = 11285245 | doi = 10.1093/hmg/10.8.797 }}
*{{cite journal | author=Nayler O, Schnorrer F, Stamm S, Ullrich A |title=The cellular localization of the murine serine/arginine-rich protein kinase CLK2 is regulated by serine 141 autophosphorylation. |journal=J. Biol. Chem. |volume=273 |issue= 51 |pages= 34341-8 |year= 1999 |pmid= 9852100 |doi= }}
* {{cite journal | vauthors = Ravichandran LV, Chen H, Li Y, Quon MJ | title = Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor | journal = Molecular Endocrinology | volume = 15 | issue = 10 | pages = 1768–80 | date = Oct 2001 | pmid = 11579209 | doi = 10.1210/mend.15.10.0711 }}
*{{cite journal  | author=Talmadge CB, Finkernagel S, Sumegi J, ''et al.'' |title=Chromosomal mapping of three human LAMMER protein-kinase-encoding genes. |journal=Hum. Genet. |volume=103 |issue= 4 |pages= 523-4 |year= 1998 |pmid= 9856501 |doi=  }}
* {{cite journal | vauthors = Jiang N, Bénard CY, Kébir H, Shoubridge EA, Hekimi S | title = Human CLK2 links cell cycle progression, apoptosis, and telomere length regulation | journal = The Journal of Biological Chemistry | volume = 278 | issue = 24 | pages = 21678–84 | date = Jun 2003 | pmid = 12670948 | doi = 10.1074/jbc.M300286200 }}
*{{cite journal | author=Moeslein FM, Myers MP, Landreth GE |title=The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B. |journal=J. Biol. Chem. |volume=274 |issue= 38 |pages= 26697-704 |year= 1999 |pmid= 10480872 |doi= }}
* {{cite journal | vauthors = Hillman RT, Green RE, Brenner SE | title = An unappreciated role for RNA surveillance | journal = Genome Biology | volume = 5 | issue = 2 | pages = R8 | year = 2005 | pmid = 14759258 | pmc = 395752 | doi = 10.1186/gb-2004-5-2-r8 }}
*{{cite journal | author=Nothwang HG, Kim HG, Aoki J, ''et al.'' |title=Functional hemizygosity of PAFAH1B3 due to a PAFAH1B3-CLK2 fusion gene in a female with mental retardation, ataxia and atrophy of the brain. |journal=Hum. Mol. Genet. |volume=10 |issue= 8 |pages= 797-806 |year= 2001 |pmid= 11285245 |doi= }}
* {{cite journal | vauthors = Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T | title = Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization | journal = Current Biology | volume = 14 | issue = 16 | pages = 1436–50 | date = Aug 2004 | pmid = 15324660 | doi = 10.1016/j.cub.2004.07.051 }}
*{{cite journal | author=Ravichandran LV, Chen H, Li Y, Quon MJ |title=Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor. |journal=Mol. Endocrinol. |volume=15 |issue= 10 |pages= 1768-80 |year= 2002 |pmid= 11579209 |doi= }}
* {{cite journal | vauthors = Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S | title = Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes | journal = Genome Research | volume = 16 | issue = 1 | pages = 55–65 | date = Jan 2006 | pmid = 16344560 | pmc = 1356129 | doi = 10.1101/gr.4039406 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Collis SJ, Barber LJ, Clark AJ, Martin JS, Ward JD, Boulton SJ | title = HCLK2 is essential for the mammalian S-phase checkpoint and impacts on Chk1 stability | journal = Nature Cell Biology | volume = 9 | issue = 4 | pages = 391–401 | date = Apr 2007 | pmid = 17384638 | doi = 10.1038/ncb1555 }}
*{{cite journal | author=Jiang N, Bénard CY, Kébir H, ''et al.'' |title=Human CLK2 links cell cycle progression, apoptosis, and telomere length regulation. |journal=J. Biol. Chem. |volume=278 |issue= 24 |pages= 21678-84 |year= 2003 |pmid= 12670948 |doi= 10.1074/jbc.M300286200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8 }}
*{{cite journal | author=Jin J, Smith FD, Stark C, ''et al.'' |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436-50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal | author=Collis SJ, Barber LJ, Clark AJ, ''et al.'' |title=HCLK2 is essential for the mammalian S-phase checkpoint and impacts on Chk1 stability. |journal=Nat. Cell Biol. |volume=9 |issue= 4 |pages= 391-401 |year= 2007 |pmid= 17384638 |doi= 10.1038/ncb1555 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 09:49, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. ↑ Hanes J, von der Kammer H, Klaudiny J, Scheit KH (Dec 1994). "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. doi:10.1006/jmbi.1994.1763. PMID 7990150.
  2. ↑ Talmadge CB, Finkernagel S, Sumegi J, Sciorra L, Rabinow L (Oct 1998). "Chromosomal mapping of three human LAMMER protein-kinase-encoding genes". Human Genetics. 103 (4): 523–4. doi:10.1007/s004390050861. PMID 9856501.
  3. ↑ 3.0 3.1 "Entrez Gene: CLK2 CDC-like kinase 2".

External links

Further reading

Retrieved from "https://www.wikidoc.org/index.php?title=CLK2&oldid=1411063"