CDC42BPA: Difference between revisions

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{{Underlinked|date=May 2016}}
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{{Infobox_gene}}
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'''Serine/threonine-protein kinase MRCK alpha''' is an [[enzyme]] that in humans is encoded by the ''CDC42BPA'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CDC42BPA CDC42 binding protein kinase alpha (DMPK-like)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8476| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = CDC42 binding protein kinase alpha (DMPK-like)
| HGNCid = 1737
| Symbol = CDC42BPA
| AltSymbols =; DKFZp686L1738; DKFZp686P1738; FLJ23347; KIAA0451; MRCK; MRCKA; PK428
| OMIM = 603412
| ECnumber = 
| Homologene = 55765
| MGIid = 2441841
| GeneAtlas_image1 = PBB_GE_CDC42BPA_203794_at_tn.png
| GeneAtlas_image2 = PBB_GE_CDC42BPA_213595_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_CDC42BPA_214464_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005083 |text = small GTPase regulator activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005911 |text = intercellular junction}} {{GNF_GO|id=GO:0031252 |text = leading edge}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0031532 |text = actin cytoskeleton reorganization}} {{GNF_GO|id=GO:0051056 |text = regulation of small GTPase mediated signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8476
    | Hs_Ensembl = ENSG00000143776
    | Hs_RefseqProtein = NP_003598
    | Hs_RefseqmRNA = NM_003607
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 225244189
    | Hs_GenLoc_end = 225572798
    | Hs_Uniprot = Q5VT25
    | Mm_EntrezGene = 226751
    | Mm_Ensembl = ENSMUSG00000026490
    | Mm_RefseqmRNA = XM_900254
    | Mm_RefseqProtein = XP_905347
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 181836036
    | Mm_GenLoc_end = 181998838
    | Mm_Uniprot = 
  }}
}}
'''CDC42 binding protein kinase alpha (DMPK-like)''', also known as '''CDC42BPA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CDC42BPA CDC42 binding protein kinase alpha (DMPK-like)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8476| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene is a member of the Serine/Threonine protein kinase family. This kinase contains multiple functional domains. Its kinase domain is highly similar to that of the myotonic dystrophy protein kinase (DMPK). This kinase also contains a Rac interactive binding (CRIB) domain, and has been shown to bind CDC42. It may function as a CDC42 downstream effector mediating CDC42 induced peripheral actin formation, and promoting cytoskeletal reorganization. Multiple alternatively spliced transcript variants have been described, and the full-length nature of two of them has been reported.<ref name="entrez">{{cite web | title = Entrez Gene: CDC42BPA CDC42 binding protein kinase alpha (DMPK-like)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8476| accessdate = }}</ref>
| summary_text = The protein encoded by this gene is a member of the Serine/Threonine protein kinase family. This kinase contains multiple functional domains. Its kinase domain is highly similar to that of the myotonic dystrophy protein kinase (DMPK). This kinase also contains a Rac interactive binding (CRIB) domain, and has been shown to bind CDC42. It may function as a CDC42 downstream effector mediating CDC42 induced peripheral actin formation, and promoting cytoskeletal reorganization. Multiple alternatively spliced transcript variants have been described, and the full-length nature of two of them has been reported.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|CDC42BPA}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Zhao Y, Loyer P, Li H, ''et al.'' |title=Cloning and chromosomal location of a novel member of the myotonic dystrophy family of protein kinases. |journal=J. Biol. Chem. |volume=272 |issue= 15 |pages= 10013-20 |year= 1997 |pmid= 9092543 |doi=  }}
*{{cite journal  | vauthors=Zhao Y, Loyer P, Li H |title=Cloning and chromosomal location of a novel member of the myotonic dystrophy family of protein kinases. |journal=J. Biol. Chem. |volume=272 |issue= 15 |pages= 10013–20 |year= 1997 |pmid= 9092543 |doi=10.1074/jbc.272.15.10013 |display-authors=etal}}
*{{cite journal  | author=Leung T, Chen XQ, Tan I, ''et al.'' |title=Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization. |journal=Mol. Cell. Biol. |volume=18 |issue= 1 |pages= 130-40 |year= 1998 |pmid= 9418861 |doi=  }}
*{{cite journal  | vauthors=Leung T, Chen XQ, Tan I |title=Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization. |journal=Mol. Cell. Biol. |volume=18 |issue= 1 |pages= 130–40 |year= 1998 |pmid= 9418861 |doi=  10.1128/mcb.18.1.130| pmc=121465  |display-authors=etal}}
*{{cite journal  | author=Seki N, Ohira M, Nagase T, ''et al.'' |title=Characterization of cDNA clones in size-fractionated cDNA libraries from human brain. |journal=DNA Res. |volume=4 |issue= 5 |pages= 345-9 |year= 1998 |pmid= 9455484 |doi=  }}
*{{cite journal  | vauthors=Seki N, Ohira M, Nagase T |title=Characterization of cDNA clones in size-fractionated cDNA libraries from human brain. |journal=DNA Res. |volume=4 |issue= 5 |pages= 345–9 |year= 1998 |pmid= 9455484 |doi=10.1093/dnares/4.5.345 |display-authors=etal}}
*{{cite journal  | author=Moncrieff CL, Bailey ME, Morrison N, Johnson KJ |title=Cloning and chromosomal localization of human Cdc42-binding protein kinase beta. |journal=Genomics |volume=57 |issue= 2 |pages= 297-300 |year= 1999 |pmid= 10198171 |doi= 10.1006/geno.1999.5769 }}
*{{cite journal  | vauthors=Moncrieff CL, Bailey ME, Morrison N, Johnson KJ |title=Cloning and chromosomal localization of human Cdc42-binding protein kinase beta. |journal=Genomics |volume=57 |issue= 2 |pages= 297–300 |year= 1999 |pmid= 10198171 |doi= 10.1006/geno.1999.5769 }}
*{{cite journal  | author=Edwards DC, Sanders LC, Bokoch GM, Gill GN |title=Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. |journal=Nat. Cell Biol. |volume=1 |issue= 5 |pages= 253-9 |year= 1999 |pmid= 10559936 |doi= 10.1038/12963 }}
*{{cite journal  | vauthors=Edwards DC, Sanders LC, Bokoch GM, Gill GN |title=Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. |journal=Nat. Cell Biol. |volume=1 |issue= 5 |pages= 253–9 |year= 1999 |pmid= 10559936 |doi= 10.1038/12963 }}
*{{cite journal  | author=Ohashi K, Nagata K, Maekawa M, ''et al.'' |title=Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop. |journal=J. Biol. Chem. |volume=275 |issue= 5 |pages= 3577-82 |year= 2000 |pmid= 10652353 |doi=  }}
*{{cite journal  | vauthors=Ohashi K, Nagata K, Maekawa M |title=Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop. |journal=J. Biol. Chem. |volume=275 |issue= 5 |pages= 3577–82 |year= 2000 |pmid= 10652353 |doi=10.1074/jbc.275.5.3577 |display-authors=etal}}
*{{cite journal  | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi=  }}
*{{cite journal  | vauthors=Dias Neto E, Correa RG, Verjovski-Almeida S |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491–6 |year= 2000 |pmid= 10737800 |doi=10.1073/pnas.97.7.3491 | pmc=16267  |display-authors=etal}}
*{{cite journal  | author=Nakamura N, Oshiro N, Fukata Y, ''et al.'' |title=Phosphorylation of ERM proteins at filopodia induced by Cdc42. |journal=Genes Cells |volume=5 |issue= 7 |pages= 571-81 |year= 2000 |pmid= 10947843 |doi=  }}
*{{cite journal  | vauthors=Nakamura N, Oshiro N, Fukata Y |title=Phosphorylation of ERM proteins at filopodia induced by Cdc42. |journal=Genes Cells |volume=5 |issue= 7 |pages= 571–81 |year= 2000 |pmid= 10947843 |doi=10.1046/j.1365-2443.2000.00348.x |display-authors=etal}}
*{{cite journal  | author=Lam LT, Pham YC, Nguyen TM, Morris GE |title=Characterization of a monoclonal antibody panel shows that the myotonic dystrophy protein kinase, DMPK, is expressed almost exclusively in muscle and heart. |journal=Hum. Mol. Genet. |volume=9 |issue= 14 |pages= 2167-73 |year= 2000 |pmid= 10958655 |doi= }}
*{{cite journal  | vauthors=Lam LT, Pham YC, Nguyen TM, Morris GE |title=Characterization of a monoclonal antibody panel shows that the myotonic dystrophy protein kinase, DMPK, is expressed almost exclusively in muscle and heart. |journal=Hum. Mol. Genet. |volume=9 |issue= 14 |pages= 2167–73 |year= 2000 |pmid= 10958655 |doi=10.1093/hmg/9.14.2167  }}
*{{cite journal  | author=Tan I, Seow KT, Lim L, Leung T |title=Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha. |journal=Mol. Cell. Biol. |volume=21 |issue= 8 |pages= 2767-78 |year= 2001 |pmid= 11283256 |doi= 10.1128/MCB.21.8.2767-2778.2001 }}
*{{cite journal  | vauthors=Tan I, Seow KT, Lim L, Leung T |title=Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha. |journal=Mol. Cell. Biol. |volume=21 |issue= 8 |pages= 2767–78 |year= 2001 |pmid= 11283256 |doi= 10.1128/MCB.21.8.2767-2778.2001 | pmc=86907 }}
*{{cite journal  | author=Sumi T, Matsumoto K, Shibuya A, Nakamura T |title=Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha. |journal=J. Biol. Chem. |volume=276 |issue= 25 |pages= 23092-6 |year= 2001 |pmid= 11340065 |doi= 10.1074/jbc.C100196200 }}
*{{cite journal  | vauthors=Sumi T, Matsumoto K, Shibuya A, Nakamura T |title=Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha. |journal=J. Biol. Chem. |volume=276 |issue= 25 |pages= 23092–6 |year= 2001 |pmid= 11340065 |doi= 10.1074/jbc.C100196200 }}
*{{cite journal  | author=Lemercier C, Brocard MP, Puvion-Dutilleul F, ''et al.'' |title=Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor. |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 22045-52 |year= 2002 |pmid= 11929873 |doi= 10.1074/jbc.M201736200 }}
*{{cite journal  | vauthors=Lemercier C, Brocard MP, Puvion-Dutilleul F |title=Class II histone deacetylases are directly recruited by BCL6 transcriptional repressor. |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 22045–52 |year= 2002 |pmid= 11929873 |doi= 10.1074/jbc.M201736200 |display-authors=etal}}
*{{cite journal  | author=Dong JM, Leung T, Manser E, Lim L |title=Cdc42 antagonizes inductive action of cAMP on cell shape, via effects of the myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) on myosin light chain phosphorylation. |journal=Eur. J. Cell Biol. |volume=81 |issue= 4 |pages= 231-42 |year= 2003 |pmid= 12018391 |doi=  }}
*{{cite journal  | vauthors=Dong JM, Leung T, Manser E, Lim L |title=Cdc42 antagonizes inductive action of cAMP on cell shape, via effects of the myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) on myosin light chain phosphorylation. |journal=Eur. J. Cell Biol. |volume=81 |issue= 4 |pages= 231–42 |year= 2003 |pmid= 12018391 |doi=10.1078/0171-9335-00238 }}
*{{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=Strausberg RL, Feingold EA, Grouse LH |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 | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Tan I, Cheong A, Lim L, Leung T |title=Genomic organization of human myotonic dystrophy kinase-related Cdc42-binding kinase alpha reveals multiple alternative splicing and functional diversity. |journal=Gene |volume=304 |issue=  |pages= 107-15 |year= 2003 |pmid= 12568720 |doi=  }}
*{{cite journal  | vauthors=Tan I, Cheong A, Lim L, Leung T |title=Genomic organization of human myotonic dystrophy kinase-related Cdc42-binding kinase alpha reveals multiple alternative splicing and functional diversity. |journal=Gene |volume=304 |issue=  |pages= 107–15 |year= 2003 |pmid= 12568720 |doi=10.1016/S0378-1119(02)01185-X }}
*{{cite journal  | author=Wilkinson S, Paterson HF, Marshall CJ |title=Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion. |journal=Nat. Cell Biol. |volume=7 |issue= 3 |pages= 255-61 |year= 2005 |pmid= 15723050 |doi= 10.1038/ncb1230 }}
*{{cite journal  | vauthors=Wilkinson S, Paterson HF, Marshall CJ |title=Cdc42-MRCK and Rho-ROCK signalling cooperate in myosin phosphorylation and cell invasion. |journal=Nat. Cell Biol. |volume=7 |issue= 3 |pages= 255–61 |year= 2005 |pmid= 15723050 |doi= 10.1038/ncb1230 }}
*{{cite journal  | author=Cmejla R, Petrak J, Cmejlova J |title=A novel iron responsive element in the 3'UTR of human MRCKalpha. |journal=Biochem. Biophys. Res. Commun. |volume=341 |issue= 1 |pages= 158-66 |year= 2006 |pmid= 16412980 |doi= 10.1016/j.bbrc.2005.12.155 }}
*{{cite journal  | vauthors=Cmejla R, Petrak J, Cmejlova J |title=A novel iron responsive element in the 3'UTR of human MRCKalpha. |journal=Biochem. Biophys. Res. Commun. |volume=341 |issue= 1 |pages= 158–66 |year= 2006 |pmid= 16412980 |doi= 10.1016/j.bbrc.2005.12.155 }}
*{{cite journal  | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
*{{cite journal  | vauthors=Gregory SG, Barlow KF, McLay KE |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |display-authors=etal}}
*{{cite journal  | author=Lefort K, Mandinova A, Ostano P, ''et al.'' |title=Notch1 is a p53 target gene involved in human keratinocyte tumor suppression through negative regulation of ROCK1/2 and MRCKalpha kinases. |journal=Genes Dev. |volume=21 |issue= 5 |pages= 562-77 |year= 2007 |pmid= 17344417 |doi= 10.1101/gad.1484707 }}
*{{cite journal  | vauthors=Lefort K, Mandinova A, Ostano P |title=Notch1 is a p53 target gene involved in human keratinocyte tumor suppression through negative regulation of ROCK1/2 and MRCKalpha kinases. |journal=Genes Dev. |volume=21 |issue= 5 |pages= 562–77 |year= 2007 |pmid= 17344417 |doi= 10.1101/gad.1484707 | pmc=1820898 |display-authors=etal}}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{Serine/threonine-specific protein kinases}}
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Revision as of 09:26, 30 August 2017

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

n/a

n/a

RefSeq (protein)

n/a

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

Serine/threonine-protein kinase MRCK alpha is an enzyme that in humans is encoded by the CDC42BPA gene.[1]

The protein encoded by this gene is a member of the Serine/Threonine protein kinase family. This kinase contains multiple functional domains. Its kinase domain is highly similar to that of the myotonic dystrophy protein kinase (DMPK). This kinase also contains a Rac interactive binding (CRIB) domain, and has been shown to bind CDC42. It may function as a CDC42 downstream effector mediating CDC42 induced peripheral actin formation, and promoting cytoskeletal reorganization. Multiple alternatively spliced transcript variants have been described, and the full-length nature of two of them has been reported.[1]

References

  1. 1.0 1.1 "Entrez Gene: CDC42BPA CDC42 binding protein kinase alpha (DMPK-like)".

External links

Further reading