Cyclin-dependent kinase 7: Difference between revisions

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{{Infobox_gene}}
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{{GNF_Protein_box
| image = PBB_Protein_CDK7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ua2.
| PDB = {{PDB2|1ua2}}
| Name = Cyclin-dependent kinase 7 (MO15 homolog, Xenopus laevis, cdk-activating kinase)
| HGNCid = 1778
| Symbol = CDK7
| AltSymbols =; CAK1; CDKN7; STK1; p39MO15
| OMIM = 601955
| ECnumber = 
| Homologene = 1363
| MGIid = 102956
| GeneAtlas_image1 = PBB_GE_CDK7_211297_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004693 |text = cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0050681 |text = androgen receptor binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006367 |text = transcription initiation from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0051301 |text = cell division}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1022
    | Hs_Ensembl = ENSG00000134058
    | Hs_RefseqProtein = NP_001790
    | Hs_RefseqmRNA = NM_001799
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 68566456
    | Hs_GenLoc_end = 68609006
    | Hs_Uniprot = P50613
    | Mm_EntrezGene = 12572
    | Mm_Ensembl = ENSMUSG00000069089
    | Mm_RefseqmRNA = NM_009874
    | Mm_RefseqProtein = NP_034004
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 101803575
    | Mm_GenLoc_end = 101831184
    | Mm_Uniprot = Q3THG5
  }}
}}
__NOTOC__
__NOTOC__
'''Cyclin-dependent kinase 7 (MO15 homolog, Xenopus laevis, cdk-activating kinase)''', also known as '''CDK7''', is a human [[gene]].
'''Cell division protein kinase 7''' is an [[enzyme]] that in humans is encoded by the ''CDK7'' [[gene]].<ref name="pmid8069918">{{cite journal | vauthors = Fisher RP, Morgan DO | title = A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase | journal = Cell | volume = 78 | issue = 4 | pages = 713–24 | date = Aug 1994 | pmid = 8069918 | pmc =  | doi = 10.1016/0092-8674(94)90535-5 }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is a member of the [[Cyclin-dependent kinase|cyclin-dependent protein kinase]] (CDK) family. CDK family members are highly similar to the gene products of [[Saccharomyces cerevisiae]] [[cdc28]], and [[Schizosaccharomyces pombe]] [[cdc2]], and are known to be important regulators of cell cycle progression. This protein forms a trimeric complex with [[cyclin H]] and [[MAT1]], which functions as a Cdk-activating kinase (CAK). It is an essential component of the transcription factor [[TFIIH]], that is involved in transcription initiation and DNA repair. This protein is thought to serve as a direct link between the regulation of transcription and the cell cycle.<ref name="entrez">{{cite web | title = Entrez Gene: CDK7 cyclin-dependent kinase 7 (MO15 homolog, Xenopus laevis, cdk-activating kinase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1022| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the cyclin-dependent protein kinase (CDK) family. CDK family members are highly similar to the gene products of Saccharomyces cerevisiae cdc28, and Schizosaccharomyces pombe cdc2, and are known to be important regulators of cell cycle progression. This protein forms a trimeric complex with cyclin H and MAT1, which functions as a Cdk-activating kinase (CAK). It is an essential component of the transcription factor TFIIH, that is involved in transcription initiation and DNA repair. This protein is thought to serve as a direct link between the regulation of transcription and the cell cycle.<ref name="entrez">{{cite web | title = Entrez Gene: CDK7 cyclin-dependent kinase 7 (MO15 homolog, Xenopus laevis, cdk-activating kinase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1022| accessdate = }}</ref>
}}


==See also==
== Interactions ==
 
Cyclin-dependent kinase 7 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[Androgen receptor]],<ref name = pmid10734072>{{cite journal | vauthors = Lee DK, Duan HO, Chang C | title = From androgen receptor to the general transcription factor TFIIH. Identification of cdk activating kinase (CAK) as an androgen receptor NH(2)-terminal associated coactivator | journal = The Journal of Biological Chemistry | volume = 275 | issue = 13 | pages = 9308–13 | date = Mar 2000 | pmid = 10734072 | doi =  10.1074/jbc.275.13.9308}}</ref>
* [[Cyclin H]],<ref name = pmid8521393/><ref name = pmid8078587>{{cite journal | vauthors = Mäkelä TP, Tassan JP, Nigg EA, Frutiger S, Hughes GJ, Weinberg RA | title = A cyclin associated with the CDK-activating kinase MO15 | journal = Nature | volume = 371 | issue = 6494 | pages = 254–7 | date = Sep 1994 | pmid = 8078587 | doi = 10.1038/371254a0 }}</ref><ref name = pmid10958691>{{cite journal | vauthors = Garber ME, Mayall TP, Suess EM, Meisenhelder J, Thompson NE, Jones KA | title = CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA | journal = Molecular and Cellular Biology | volume = 20 | issue = 18 | pages = 6958–69 | date = Sep 2000 | pmid = 10958691 | pmc = 88771 | doi =  10.1128/mcb.20.18.6958-6969.2000}}</ref>
* [[GTF2H1]],<ref name = pmid9130708/><ref name = pmid8521393/><ref name = pmid7533895>{{cite journal | vauthors = Shiekhattar R, Mermelstein F, Fisher RP, Drapkin R, Dynlacht B, Wessling HC, Morgan DO, Reinberg D | title = Cdk-activating kinase complex is a component of human transcription factor TFIIH | journal = Nature | volume = 374 | issue = 6519 | pages = 283–7 | date = Mar 1995 | pmid = 7533895 | doi = 10.1038/374283a0 }}</ref>
* [[MNAT1]],<ref name = pmid8521393/><ref name = pmid12527756>{{cite journal | vauthors = Talukder AH, Mishra SK, Mandal M, Balasenthil S, Mehta S, Sahin AA, Barnes CJ, Kumar R | title = MTA1 interacts with MAT1, a cyclin-dependent kinase-activating kinase complex ring finger factor, and regulates estrogen receptor transactivation functions | journal = The Journal of Biological Chemistry | volume = 278 | issue = 13 | pages = 11676–85 | date = Mar 2003 | pmid = 12527756 | doi = 10.1074/jbc.M209570200 }}</ref>
* [[P53]],<ref name = pmid9372954>{{cite journal | vauthors = Ko LJ, Shieh SY, Chen X, Jayaraman L, Tamai K, Taya Y, Prives C, Pan ZQ | title = p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner | journal = Molecular and Cellular Biology | volume = 17 | issue = 12 | pages = 7220–9 | date = Dec 1997 | pmid = 9372954 | pmc = 232579 | doi =  10.1128/mcb.17.12.7220}}</ref><ref name = pmid9840937>{{cite journal | vauthors = Schneider E, Montenarh M, Wagner P | title = Regulation of CAK kinase activity by p53 | journal = Oncogene | volume = 17 | issue = 21 | pages = 2733–41 | date = Nov 1998 | pmid = 9840937 | doi = 10.1038/sj.onc.1202504 }}</ref>
* [[SUPT5H]],<ref name = pmid10958691/> and
* [[XPB]].<ref name = pmid15220921>{{cite journal | vauthors = Giglia-Mari G, Coin F, Ranish JA, Hoogstraten D, Theil A, Wijgers N, Jaspers NG, Raams A, Argentini M, van der Spek PJ, Botta E, Stefanini M, Egly JM, Aebersold R, Hoeijmakers JH, Vermeulen W | title = A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A | journal = Nature Genetics | volume = 36 | issue = 7 | pages = 714–9 | date = Jul 2004 | pmid = 15220921 | doi = 10.1038/ng1387 | author16 = Vermeulen Wim | author14 = Aebersold Ruedi | author15 = Hoeijmakers Jan H J | author13 = Egly Jean-Marc }}</ref><ref name = pmid9130708>{{cite journal | vauthors = Rossignol M, Kolb-Cheynel I, Egly JM | title = Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH | journal = The EMBO Journal | volume = 16 | issue = 7 | pages = 1628–37 | date = Apr 1997 | pmid = 9130708 | pmc = 1169767 | doi = 10.1093/emboj/16.7.1628 }}</ref><ref name = pmid8521393>{{cite journal | vauthors = Yee A, Nichols MA, Wu L, Hall FL, Kobayashi R, Xiong Y | title = Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor | journal = Cancer Research | volume = 55 | issue = 24 | pages = 6058–62 | date = Dec 1995 | pmid = 8521393 | doi =  }}</ref>
{{Div col end}}
 
== See also ==
* [[Cyclin-dependent kinase]]
* [[Cyclin-dependent kinase]]
* [[CDK7 pathway]]
== References ==
{{reflist}}


==References==
== Further reading ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Jeang KT | title = Tat, Tat-associated kinase, and transcription | journal = Journal of Biomedical Science | volume = 5 | issue = 1 | pages = 24–7 | year = 1998 | pmid = 9570510 | doi = 10.1007/BF02253352 }}
| citations =
* {{cite journal | vauthors = Yankulov K, Bentley D | title = Transcriptional control: Tat cofactors and transcriptional elongation | journal = Current Biology | volume = 8 | issue = 13 | pages = R447-9 | date = Jun 1998 | pmid = 9651670 | doi = 10.1016/S0960-9822(98)70289-1 }}
*{{cite journal | author=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24-7 |year= 1998 |pmid= 9570510 |doi= }}
* {{cite journal | vauthors = Shiekhattar R, Mermelstein F, Fisher RP, Drapkin R, Dynlacht B, Wessling HC, Morgan DO, Reinberg D | title = Cdk-activating kinase complex is a component of human transcription factor TFIIH | journal = Nature | volume = 374 | issue = 6519 | pages = 283–7 | date = Mar 1995 | pmid = 7533895 | doi = 10.1038/374283a0 }}
*{{cite journal | author=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447-9 |year= 1998 |pmid= 9651670 |doi= }}
* {{cite journal | vauthors = Aprelikova O, Xiong Y, Liu ET | title = Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase | journal = The Journal of Biological Chemistry | volume = 270 | issue = 31 | pages = 18195–7 | date = Aug 1995 | pmid = 7629134 | doi = 10.1074/jbc.270.31.18195 }}
*{{cite journal | author=Shiekhattar R, Mermelstein F, Fisher RP, ''et al.'' |title=Cdk-activating kinase complex is a component of human transcription factor TFIIH. |journal=Nature |volume=374 |issue= 6519 |pages= 283-7 |year= 1995 |pmid= 7533895 |doi= 10.1038/374283a0 }}
* {{cite journal | vauthors = Serizawa H, Mäkelä TP, Conaway JW, Conaway RC, Weinberg RA, Young RA | title = Association of Cdk-activating kinase subunits with transcription factor TFIIH | journal = Nature | volume = 374 | issue = 6519 | pages = 280–2 | date = Mar 1995 | pmid = 7885450 | doi = 10.1038/374280a0 }}
*{{cite journal | author=Aprelikova O, Xiong Y, Liu ET |title=Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase. |journal=J. Biol. Chem. |volume=270 |issue= 31 |pages= 18195-7 |year= 1995 |pmid= 7629134 |doi= }}
* {{cite journal | vauthors = Tassan JP, Schultz SJ, Bartek J, Nigg EA | title = Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase) | journal = The Journal of Cell Biology | volume = 127 | issue = 2 | pages = 467–78 | date = Oct 1994 | pmid = 7929589 | pmc = 2120215 | doi = 10.1083/jcb.127.2.467 }}
*{{cite journal | author=Serizawa H, Mäkelä TP, Conaway JW, ''et al.'' |title=Association of Cdk-activating kinase subunits with transcription factor TFIIH. |journal=Nature |volume=374 |issue= 6519 |pages= 280-2 |year= 1995 |pmid= 7885450 |doi= 10.1038/374280a0 }}
* {{cite journal | vauthors = Darbon JM, Devault A, Taviaux S, Fesquet D, Martinez AM, Galas S, Cavadore JC, Dorée M, Blanchard JM | title = Cloning, expression and subcellular localization of the human homolog of p40MO15 catalytic subunit of cdk-activating kinase | journal = Oncogene | volume = 9 | issue = 11 | pages = 3127–38 | date = Nov 1994 | pmid = 7936635 | doi =  }}
*{{cite journal | author=Tassan JP, Schultz SJ, Bartek J, Nigg EA |title=Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase). |journal=J. Cell Biol. |volume=127 |issue= 2 |pages= 467-78 |year= 1994 |pmid= 7929589 |doi= }}
* {{cite journal | vauthors = Williams RT, Wu L, Carbonaro-Hall DA, Hall FL | title = Identification, assay, and purification of a Cdc2-activating threonine-161 protein kinase from human cells | journal = Archives of Biochemistry and Biophysics | volume = 314 | issue = 1 | pages = 99–106 | date = Oct 1994 | pmid = 7944411 | doi = 10.1006/abbi.1994.1416 }}
*{{cite journal | author=Darbon JM, Devault A, Taviaux S, ''et al.'' |title=Cloning, expression and subcellular localization of the human homolog of p40MO15 catalytic subunit of cdk-activating kinase. |journal=Oncogene |volume=9 |issue= 11 |pages= 3127-38 |year= 1994 |pmid= 7936635 |doi=  }}
* {{cite journal | vauthors = Mäkelä TP, Tassan JP, Nigg EA, Frutiger S, Hughes GJ, Weinberg RA | title = A cyclin associated with the CDK-activating kinase MO15 | journal = Nature | volume = 371 | issue = 6494 | pages = 254–7 | date = Sep 1994 | pmid = 8078587 | doi = 10.1038/371254a0 }}
*{{cite journal | author=Williams RT, Wu L, Carbonaro-Hall DA, Hall FL |title=Identification, assay, and purification of a Cdc2-activating threonine-161 protein kinase from human cells. |journal=Arch. Biochem. Biophys. |volume=314 |issue= 1 |pages= 99-106 |year= 1994 |pmid= 7944411 |doi= }}
* {{cite journal | vauthors = Levedakou EN, He M, Baptist EW, Craven RJ, Cance WG, Welcsh PL, Simmons A, Naylor SL, Leach RJ, Lewis TB | title = Two novel human serine/threonine kinases with homologies to the cell cycle regulating Xenopus MO15, and NIMA kinases: cloning and characterization of their expression pattern | journal = Oncogene | volume = 9 | issue = 7 | pages = 1977–88 | date = Jul 1994 | pmid = 8208544 | doi = }}
*{{cite journal | author=Fisher RP, Morgan DO |title=A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase. |journal=Cell |volume=78 |issue= 4 |pages= 713-24 |year= 1994 |pmid= 8069918 |doi= }}
* {{cite journal | vauthors = Wu L, Yee A, Liu L, Carbonaro-Hall D, Venkatesan N, Tolo VT, Hall FL | title = Molecular cloning of the human CAK1 gene encoding a cyclin-dependent kinase-activating kinase | journal = Oncogene | volume = 9 | issue = 7 | pages = 2089–96 | date = Jul 1994 | pmid = 8208556 | doi =  }}
*{{cite journal | author=Mäkelä TP, Tassan JP, Nigg EA, ''et al.'' |title=A cyclin associated with the CDK-activating kinase MO15. |journal=Nature |volume=371 |issue= 6494 |pages= 254-7 |year= 1994 |pmid= 8078587 |doi= 10.1038/371254a0 }}
* {{cite journal | vauthors = Yee A, Nichols MA, Wu L, Hall FL, Kobayashi R, Xiong Y | title = Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor | journal = Cancer Research | volume = 55 | issue = 24 | pages = 6058–62 | date = Dec 1995 | pmid = 8521393 | doi =  }}
*{{cite journal | author=Levedakou EN, He M, Baptist EW, ''et al.'' |title=Two novel human serine/threonine kinases with homologies to the cell cycle regulating Xenopus MO15, and NIMA kinases: cloning and characterization of their expression pattern. |journal=Oncogene |volume=9 |issue= 7 |pages= 1977-88 |year= 1994 |pmid= 8208544 |doi=  }}
* {{cite journal | vauthors = Blau J, Xiao H, McCracken S, O'Hare P, Greenblatt J, Bentley D | title = Three functional classes of transcriptional activation domain | journal = Molecular and Cellular Biology | volume = 16 | issue = 5 | pages = 2044–55 | date = May 1996 | pmid = 8628270 | pmc = 231191 | doi =  }}
*{{cite journal | author=Wu L, Yee A, Liu L, ''et al.'' |title=Molecular cloning of the human CAK1 gene encoding a cyclin-dependent kinase-activating kinase. |journal=Oncogene |volume=9 |issue= 7 |pages= 2089-96 |year= 1994 |pmid= 8208556 |doi=  }}
* {{cite journal | vauthors = Bartkova J, Zemanova M, Bartek J | title = Expression of CDK7/CAK in normal and tumor cells of diverse histogenesis, cell-cycle position and differentiation | journal = International Journal of Cancer | volume = 66 | issue = 6 | pages = 732–7 | date = Jun 1996 | pmid = 8647641 | doi = 10.1002/(SICI)1097-0215(19960611)66:6<732::AID-IJC4>3.0.CO;2-0 }}
*{{cite journal | author=Yee A, Nichols MA, Wu L, ''et al.'' |title=Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor. |journal=Cancer Res. |volume=55 |issue= 24 |pages= 6058-62 |year= 1996 |pmid= 8521393 |doi=  }}
* {{cite journal | vauthors = Reardon JT, Ge H, Gibbs E, Sancar A, Hurwitz J, Pan ZQ | title = Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 13 | pages = 6482–7 | date = Jun 1996 | pmid = 8692841 | pmc = 39049 | doi = 10.1073/pnas.93.13.6482 }}
*{{cite journal | author=Blau J, Xiao H, McCracken S, ''et al.'' |title=Three functional classes of transcriptional activation domain. |journal=Mol. Cell. Biol. |volume=16 |issue= 5 |pages= 2044-55 |year= 1996 |pmid= 8628270 |doi= }}
* {{cite journal | vauthors = Drapkin R, Le Roy G, Cho H, Akoulitchev S, Reinberg D | title = Human cyclin-dependent kinase-activating kinase exists in three distinct complexes | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 13 | pages = 6488–93 | date = Jun 1996 | pmid = 8692842 | pmc = 39050 | doi = 10.1073/pnas.93.13.6488 }}
*{{cite journal  | author=Bartkova J, Zemanova M, Bartek J |title=Expression of CDK7/CAK in normal and tumor cells of diverse histogenesis, cell-cycle position and differentiation. |journal=Int. J. Cancer |volume=66 |issue= 6 |pages= 732-7 |year= 1996 |pmid= 8647641 |doi= 10.1002/(SICI)1097-0215(19960611)66:6<732::AID-IJC4>3.0.CO;2-0 }}
* {{cite journal | vauthors = Zhou Q, Sharp PA | title = Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat | journal = Science | volume = 274 | issue = 5287 | pages = 605–10 | date = Oct 1996 | pmid = 8849451 | doi = 10.1126/science.274.5287.605 }}
*{{cite journal | author=Reardon JT, Ge H, Gibbs E, ''et al.'' |title=Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6482-7 |year= 1996 |pmid= 8692841 |doi= }}
* {{cite journal | vauthors = Parada CA, Roeder RG | title = Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain | journal = Nature | volume = 384 | issue = 6607 | pages = 375–8 | date = Nov 1996 | pmid = 8934526 | doi = 10.1038/384375a0 }}
*{{cite journal | author=Drapkin R, Le Roy G, Cho H, ''et al.'' |title=Human cyclin-dependent kinase-activating kinase exists in three distinct complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6488-93 |year= 1996 |pmid= 8692842 |doi= }}
* {{cite journal | vauthors = García-Martínez LF, Ivanov D, Gaynor RB | title = Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes | journal = The Journal of Biological Chemistry | volume = 272 | issue = 11 | pages = 6951–8 | date = Mar 1997 | pmid = 9054383 | doi = 10.1074/jbc.272.11.6951 }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi= }}
*{{cite journal | author=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375-8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
*{{cite journal  | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951-8 |year= 1997 |pmid= 9054383 |doi=  }}
}}
{{refend}}
{{refend}}


==External links==
== External links ==
* {{MeshName|CDK7+protein,+human}}
* {{MeshName|CDK7+protein,+human}}
* {{UCSC genome browser|CDK7}}
* {{UCSC gene details|CDK7}}


{{Enzyme-stub}}
{{PDB Gallery|geneid=1022}}
{{Cell cycle proteins}}
{{Cell cycle proteins}}
{{Serine/threonine-specific protein kinases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}


{{DEFAULTSORT:Cyclin-dependent kinase 07}}
[[Category:Cell cycle]]
[[Category:Cell cycle]]
[[Category:Proteins]]
[[Category:EC 2.7.11]]

Latest revision as of 21:56, 25 November 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

Cell division protein kinase 7 is an enzyme that in humans is encoded by the CDK7 gene.[1]

The protein encoded by this gene is a member of the cyclin-dependent protein kinase (CDK) family. CDK family members are highly similar to the gene products of Saccharomyces cerevisiae cdc28, and Schizosaccharomyces pombe cdc2, and are known to be important regulators of cell cycle progression. This protein forms a trimeric complex with cyclin H and MAT1, which functions as a Cdk-activating kinase (CAK). It is an essential component of the transcription factor TFIIH, that is involved in transcription initiation and DNA repair. This protein is thought to serve as a direct link between the regulation of transcription and the cell cycle.[2]

Interactions

Cyclin-dependent kinase 7 has been shown to interact with:

See also

References

  1. ↑ Fisher RP, Morgan DO (Aug 1994). "A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase". Cell. 78 (4): 713–24. doi:10.1016/0092-8674(94)90535-5. PMID 8069918.
  2. ↑ "Entrez Gene: CDK7 cyclin-dependent kinase 7 (MO15 homolog, Xenopus laevis, cdk-activating kinase)".
  3. ↑ Lee DK, Duan HO, Chang C (Mar 2000). "From androgen receptor to the general transcription factor TFIIH. Identification of cdk activating kinase (CAK) as an androgen receptor NH(2)-terminal associated coactivator". The Journal of Biological Chemistry. 275 (13): 9308–13. doi:10.1074/jbc.275.13.9308. PMID 10734072.
  4. ↑ 4.0 4.1 4.2 4.3 Yee A, Nichols MA, Wu L, Hall FL, Kobayashi R, Xiong Y (Dec 1995). "Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor". Cancer Research. 55 (24): 6058–62. PMID 8521393.
  5. ↑ Mäkelä TP, Tassan JP, Nigg EA, Frutiger S, Hughes GJ, Weinberg RA (Sep 1994). "A cyclin associated with the CDK-activating kinase MO15". Nature. 371 (6494): 254–7. doi:10.1038/371254a0. PMID 8078587.
  6. ↑ 6.0 6.1 Garber ME, Mayall TP, Suess EM, Meisenhelder J, Thompson NE, Jones KA (Sep 2000). "CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA". Molecular and Cellular Biology. 20 (18): 6958–69. doi:10.1128/mcb.20.18.6958-6969.2000. PMC 88771. PMID 10958691.
  7. ↑ 7.0 7.1 Rossignol M, Kolb-Cheynel I, Egly JM (Apr 1997). "Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH". The EMBO Journal. 16 (7): 1628–37. doi:10.1093/emboj/16.7.1628. PMC 1169767. PMID 9130708.
  8. ↑ Shiekhattar R, Mermelstein F, Fisher RP, Drapkin R, Dynlacht B, Wessling HC, Morgan DO, Reinberg D (Mar 1995). "Cdk-activating kinase complex is a component of human transcription factor TFIIH". Nature. 374 (6519): 283–7. doi:10.1038/374283a0. PMID 7533895.
  9. ↑ Talukder AH, Mishra SK, Mandal M, Balasenthil S, Mehta S, Sahin AA, Barnes CJ, Kumar R (Mar 2003). "MTA1 interacts with MAT1, a cyclin-dependent kinase-activating kinase complex ring finger factor, and regulates estrogen receptor transactivation functions". The Journal of Biological Chemistry. 278 (13): 11676–85. doi:10.1074/jbc.M209570200. PMID 12527756.
  10. ↑ Ko LJ, Shieh SY, Chen X, Jayaraman L, Tamai K, Taya Y, Prives C, Pan ZQ (Dec 1997). "p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner". Molecular and Cellular Biology. 17 (12): 7220–9. doi:10.1128/mcb.17.12.7220. PMC 232579. PMID 9372954.
  11. ↑ Schneider E, Montenarh M, Wagner P (Nov 1998). "Regulation of CAK kinase activity by p53". Oncogene. 17 (21): 2733–41. doi:10.1038/sj.onc.1202504. PMID 9840937.
  12. ↑ Giglia-Mari G, Coin F, Ranish JA, Hoogstraten D, Theil A, Wijgers N, Jaspers NG, Raams A, Argentini M, van der Spek PJ, Botta E, Stefanini M, Egly JM, Aebersold R, Hoeijmakers JH, Vermeulen W (Jul 2004). "A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A". Nature Genetics. 36 (7): 714–9. doi:10.1038/ng1387. PMID 15220921.

Further reading

External links

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