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{{Redirect|CLK-1|the ship designated CLK-1|USS Norfolk (DL-1)}}
{{PBB_Controls
{{Infobox_gene}}
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'''Dual specificity protein kinase CLK1''' is an [[enzyme]] that in humans is encoded by the ''CLK1'' [[gene]].<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 = Hum Genet | volume = 103 | issue = 4 | pages = 523–4 | date = Dec 1998 | pmid = 9856501 | pmc = | doi = 10.1007/s004390050861 }}</ref><ref name="entrez"/>
| require_manual_inspection = no
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_CLK1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1z57.
| PDB = {{PDB2|1z57}}
| Name = CDC-like kinase 1
| HGNCid = 2068
| Symbol = CLK1
| AltSymbols =; CLK; CLK/STY; STY
| OMIM = 601951
| ECnumber = 
| Homologene = 48263
| MGIid = 
| GeneAtlas_image1 = PBB_GE_CLK1_214683_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:0004715 |text = non-membrane spanning 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:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0018105 |text = peptidyl-serine phosphorylation}} {{GNF_GO|id=GO:0018107 |text = peptidyl-threonine phosphorylation}} {{GNF_GO|id=GO:0018108 |text = peptidyl-tyrosine phosphorylation}} {{GNF_GO|id=GO:0046777 |text = protein amino acid autophosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1195
    | Hs_Ensembl = ENSG00000013441
    | Hs_RefseqProtein = NP_001019817
    | Hs_RefseqmRNA = NM_001024646
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 201425978
    | Hs_GenLoc_end = 201437667
    | Hs_Uniprot = P49759
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''CDC-like kinase 1''', also known as '''CLK1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CLK1 CDC-like kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1195| 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 CDC2-like (or LAMMER) family of [[dual specificity protein kinase]]s. 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.<ref name="entrez">{{cite web | title = Entrez Gene: CLK1 CDC-like kinase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1195| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the CDC2-like (or LAMMER) family of dual specificity protein kinases. In the 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.<ref name="entrez">{{cite web | title = Entrez Gene: CLK1 CDC-like kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1195| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
CLK1 has been shown to [[Protein-protein interaction|interact]] with [[ASF/SF2]].<ref name=pmid8798720>{{cite journal | vauthors = Colwill K, Feng LL, Yeakley JM, Gish GD, Cáceres JF, Pawson T, Fu XD | title = SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors | language =  | journal = J. Biol. Chem. | volume = 271 | issue = 40 | pages = 24569–75 | date = Oct 1996 | pmid = 8798720 | doi = 10.1074/jbc.271.40.24569 }}</ref><ref name=pmid12565863>{{cite journal | vauthors = Umehara H, Nishii Y, Morishima M, Kakehi Y, Kioka N, Amachi T, Koizumi J, Hagiwara M, Ueda K | title = Effect of cisplatin treatment on speckled distribution of a serine/arginine-rich nuclear protein CROP/Luc7A | language =  | journal = Biochem. Biophys. Res. Commun. | volume = 301 | issue = 2 | pages = 324–9 | date = Feb 2003 | pmid = 12565863 | doi = 10.1016/S0006-291X(02)03017-6 }}</ref>
 
== References ==
{{reflist}}
 
==External links==
* {{UCSC gene info|CLK1}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Johnson KW, Smith KA | title = Molecular cloning of a novel human cdc2/CDC28-like protein kinase. | journal = J. Biol. Chem. | volume = 266 | issue = 6 | pages = 3402–7 | year = 1991 | pmid = 1704889 | doi =  }}
| citations =
* {{cite journal | vauthors = Ben-David Y, Letwin K, Tannock L, Bernstein A, Pawson T | title = A mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulators | journal = EMBO J. | volume = 10 | issue = 2 | pages = 317–25 | year = 1991 | pmid = 1825055 | pmc = 452648 | doi =  }}
*{{cite journal | author=Johnson KW, Smith KA |title=Molecular cloning of a novel human cdc2/CDC28-like protein kinase. |journal=J. Biol. Chem. |volume=266 |issue= 6 |pages= 3402-7 |year= 1991 |pmid= 1704889 |doi=  }}
* {{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 = J. Mol. Biol. | volume = 244 | issue = 5 | pages = 665–72 | year = 1995 | pmid = 7990150 | doi = 10.1006/jmbi.1994.1763 }}
*{{cite journal | author=Ben-David Y, Letwin K, Tannock L, ''et al.'' |title=A mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulators. |journal=EMBO J. |volume=10 |issue= 2 |pages= 317-25 |year= 1991 |pmid= 1825055 |doi=  }}
* {{cite journal | vauthors = Colwill K, Pawson T, Andrews B, Prasad J, Manley JL, Bell JC, Duncan PI | title = The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution | journal = EMBO J. | volume = 15 | issue = 2 | pages = 265–75 | year = 1996 | pmid = 8617202 | pmc = 449941 | doi =  }}
*{{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 = Colwill K, Feng LL, Yeakley JM, Gish GD, Cáceres JF, Pawson T, Fu XD | title = SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors | journal = J. Biol. Chem. | volume = 271 | issue = 40 | pages = 24569–75 | year = 1996 | pmid = 8798720 | doi = 10.1074/jbc.271.40.24569 }}
*{{cite journal | author=Colwill K, Pawson T, Andrews B, ''et al.'' |title=The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution. |journal=EMBO J. |volume=15 |issue= 2 |pages= 265-75 |year= 1996 |pmid= 8617202 |doi=  }}
* {{cite journal | vauthors = Nestel FP, Colwill K, Harper S, Pawson T, Anderson SK | title = RS cyclophilins: identification of an NK-TR1-related cyclophilin | journal = Gene | volume = 180 | issue = 1–2 | pages = 151–5 | year = 1997 | pmid = 8973360 | doi = 10.1016/S0378-1119(96)00436-2 }}
*{{cite journal | author=Colwill K, Feng LL, Yeakley JM, ''et al.'' |title=SRPK1 and Clk/Sty protein kinases show distinct substrate specificities for serine/arginine-rich splicing factors. |journal=J. Biol. Chem. |volume=271 |issue= 40 |pages= 24569-75 |year= 1996 |pmid= 8798720 |doi= }}
* {{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 = J. Biol. Chem. | volume = 274 | issue = 38 | pages = 26697–704 | year = 1999 | pmid = 10480872 | doi = 10.1074/jbc.274.38.26697 }}
*{{cite journal | author=Nestel FP, Colwill K, Harper S, ''et al.'' |title=RS cyclophilins: identification of an NK-TR1-related cyclophilin. |journal=Gene |volume=180 |issue= 1-2 |pages= 151-5 |year= 1997 |pmid= 8973360 |doi= }}
* {{cite journal | vauthors = Menegay HJ, Myers MP, Moeslein FM, Landreth GE | title = Biochemical characterization and localization of the dual specificity kinase CLK1 | journal = J. Cell Sci. | volume = 113 | issue = 18 | pages = 3241–53 | year = 2000 | pmid = 10954422 | doi =  }}
*{{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 = Kojima T, Zama T, Wada K, Onogi H, Hagiwara M | title = Cloning of human PRP4 reveals interaction with Clk1 | journal = J. Biol. Chem. | volume = 276 | issue = 34 | pages = 32247–56 | year = 2001 | pmid = 11418604 | doi = 10.1074/jbc.M103790200 }}
*{{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 = Hartmann AM, Rujescu D, Giannakouros T, Nikolakaki E, Goedert M, Mandelkow EM, Gao QS, Andreadis A, Stamm S | title = Regulation of alternative splicing of human tau exon 10 by phosphorylation of splicing factors | journal = Mol. Cell. Neurosci. | volume = 18 | issue = 1 | pages = 80–90 | year = 2001 | pmid = 11461155 | doi = 10.1006/mcne.2001.1000 }}
*{{cite journal | author=Menegay HJ, Myers MP, Moeslein FM, Landreth GE |title=Biochemical characterization and localization of the dual specificity kinase CLK1. |journal=J. Cell. Sci. |volume=113 ( Pt 18) |issue= |pages= 3241-53 |year= 2000 |pmid= 10954422 |doi= }}
* {{cite journal | vauthors = Lai MC, Lin RI, Tarn WY | title = Differential effects of hyperphosphorylation on splicing factor SRp55 | journal = Biochem. J. | volume = 371 | issue = Pt 3 | pages = 937–45 | year = 2003 | pmid = 12549978 | pmc = 1223332 | doi = 10.1042/BJ20021827 }}
*{{cite journal | author=Kojima T, Zama T, Wada K, ''et al.'' |title=Cloning of human PRP4 reveals interaction with Clk1. |journal=J. Biol. Chem. |volume=276 |issue= 34 |pages= 32247-56 |year= 2001 |pmid= 11418604 |doi= 10.1074/jbc.M103790200 }}
* {{cite journal | vauthors = Umehara H, Nishii Y, Morishima M, Kakehi Y, Kioka N, Amachi T, Koizumi J, Hagiwara M, Ueda K | title = Effect of cisplatin treatment on speckled distribution of a serine/arginine-rich nuclear protein CROP/Luc7A | journal = Biochem. Biophys. Res. Commun. | volume = 301 | issue = 2 | pages = 324–9 | year = 2003 | pmid = 12565863 | doi = 10.1016/S0006-291X(02)03017-6 }}
*{{cite journal | author=Hartmann AM, Rujescu D, Giannakouros T, ''et al.'' |title=Regulation of alternative splicing of human tau exon 10 by phosphorylation of splicing factors. |journal=Mol. Cell. Neurosci. |volume=18 |issue= 1 |pages= 80-90 |year= 2001 |pmid= 11461155 |doi= 10.1006/mcne.2001.1000 }}
* {{cite journal | vauthors = Kantham L, Kerr-Bayles L, Godde N, Quick M, Webb R, Sunderland T, Bond J, Walder K, Augert G, Collier G | title = Beacon interacts with cdc2/cdc28-like kinases | journal = Biochem. Biophys. Res. Commun. | volume = 304 | issue = 1 | pages = 125–9 | year = 2003 | pmid = 12705895 | doi = 10.1016/S0006-291X(03)00549-7 }}
*{{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 = Prasad J, Manley JL | title = Regulation and Substrate Specificity of the SR Protein Kinase Clk/Sty | journal = Mol. Cell. Biol. | volume = 23 | issue = 12 | pages = 4139–49 | year = 2003 | pmid = 12773558 | pmc = 156123 | doi = 10.1128/MCB.23.12.4139-4149.2003 }}
*{{cite journal | author=Lai MC, Lin RI, Tarn WY |title=Differential effects of hyperphosphorylation on splicing factor SRp55. |journal=Biochem. J. |volume=371 |issue= Pt 3 |pages= 937-45 |year= 2003 |pmid= 12549978 |doi= 10.1042/BJ20021827 }}
* {{cite journal | vauthors = 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 | pmc = 395752 | doi = 10.1186/gb-2004-5-2-r8 }}
*{{cite journal | author=Umehara H, Nishii Y, Morishima M, ''et al.'' |title=Effect of cisplatin treatment on speckled distribution of a serine/arginine-rich nuclear protein CROP/Luc7A. |journal=Biochem. Biophys. Res. Commun. |volume=301 |issue= 2 |pages= 324-9 |year= 2003 |pmid= 12565863 |doi= }}
* {{cite journal | vauthors = 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 | title = Manipulation of alternative splicing by a newly developed inhibitor of Clks | journal = J. Biol. Chem. | volume = 279 | issue = 23 | pages = 24246–54 | year = 2004 | pmid = 15010457 | doi = 10.1074/jbc.M314298200 }}
*{{cite journal | author=Kantham L, Kerr-Bayles L, Godde N, ''et al.'' |title=Beacon interacts with cdc2/cdc28-like kinases. |journal=Biochem. Biophys. Res. Commun. |volume=304 |issue= 1 |pages= 125-9 |year= 2003 |pmid= 12705895 |doi= }}
* {{cite journal | vauthors = 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 | 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=Prasad J, Manley JL |title=Regulation and substrate specificity of the SR protein kinase Clk/Sty. |journal=Mol. Cell. Biol. |volume=23 |issue= 12 |pages= 4139-49 |year= 2003 |pmid= 12773558 |doi= }}
* {{cite journal | vauthors = Velazquez-Dones A, Hagopian JC, Ma CT, Zhong XY, Zhou H, Ghosh G, Fu XD, Adams JA | title = Mass spectrometric and kinetic analysis of ASF/SF2 phosphorylation by SRPK1 and Clk/Sty | journal = J. Biol. Chem. | volume = 280 | issue = 50 | pages = 41761–8 | year = 2006 | pmid = 16223727 | doi = 10.1074/jbc.M504156200 }}
*{{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=Muraki M, Ohkawara B, Hosoya T, ''et al.'' |title=Manipulation of alternative splicing by a newly developed inhibitor of Clks. |journal=J. Biol. Chem. |volume=279 |issue= 23 |pages= 24246-54 |year= 2004 |pmid= 15010457 |doi= 10.1074/jbc.M314298200 }}
*{{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=Velazquez-Dones A, Hagopian JC, Ma CT, ''et al.'' |title=Mass spectrometric and kinetic analysis of ASF/SF2 phosphorylation by SRPK1 and Clk/Sty. |journal=J. Biol. Chem. |volume=280 |issue= 50 |pages= 41761-8 |year= 2006 |pmid= 16223727 |doi= 10.1074/jbc.M504156200 }}
}}
{{refend}}
{{refend}}


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{{PDB Gallery|geneid=1195}}
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Latest revision as of 19:35, 8 November 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

Dual specificity protein kinase CLK1 is an enzyme that in humans is encoded by the CLK1 gene.[1][2]

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.[2]

Interactions

CLK1 has been shown to interact with ASF/SF2.[3][4]

References

  1. 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.
  2. 2.0 2.1 "Entrez Gene: CLK1 CDC-like kinase 1".
  3. 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.
  4. 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

Further reading