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Cyclin-dependent kinase 7 (EC 2.7.11.22) (EC 2.7.11.23) (39 kDa protein kinase) (p39 Mo15) (CDK-activating kinase 1) (Cell division protein kinase 7) (Serine/threonine-protein kinase 1) (TFIIH basal transcription factor complex kinase subunit)

 CDK7_HUMAN              Reviewed;         346 AA.
P50613; Q9BS60; Q9UE19;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 198.
RecName: Full=Cyclin-dependent kinase 7;
EC=2.7.11.22;
EC=2.7.11.23;
AltName: Full=39 kDa protein kinase;
Short=p39 Mo15;
AltName: Full=CDK-activating kinase 1;
AltName: Full=Cell division protein kinase 7;
AltName: Full=Serine/threonine-protein kinase 1;
AltName: Full=TFIIH basal transcription factor complex kinase subunit;
Name=CDK7; Synonyms=CAK, CAK1, CDKN7, MO15, STK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=7929589; DOI=10.1083/jcb.127.2.467;
Tassan J.-P., Schultz S.J., Bartek J., Nigg E.A.;
"Cell cycle analysis of the activity, subcellular localization, and
subunit composition of human CAK (CDK-activating kinase).";
J. Cell Biol. 127:467-478(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary gland;
PubMed=8208544;
Levedakou E.N., He M., Baptist E.W., Craven R.J., Cance W.G.,
Welcsh P.L., Simmons A., Naylor S.L., Leach R.J., Lewis T.B.,
Bowcock A., Liu E.T.;
"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.";
Oncogene 9:1977-1988(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7936635;
Darbon J.-M., Devault A., Taviaux S., Fesquet D., Martinez A.-M.,
Galas S., Cavadore J.-C., Doree M., Blanchard J.-M.;
"Cloning, expression and subcellular localization of the human homolog
of p40MO15 catalytic subunit of cdk-activating kinase.";
Oncogene 9:3127-3138(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=8208556;
Wu L., Yee A., Liu L., Carbonaro-Hall D., Venkatesan N., Tolo T.,
Hall F.L.;
"Molecular cloning of the human CAK1 gene encoding a cyclin-dependent
kinase-activating kinase.";
Oncogene 9:2089-2096(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung, and Thymus;
Kobelt D., Karn T., Hock B., Holtrich U., Braeuninger A., Wolf G.,
Strebhardt K., Ruebsamen-Waigmann H.;
"Human and Xenopus MO15 mRNA are highly conserved but show different
patterns of expression in adult tissues.";
Oncol. Rep. 1:1269-1275(1994).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-163 AND MET-285.
NIEHS SNPs program;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
MUTAGENESIS OF THR-170.
PubMed=8069918; DOI=10.1016/0092-8674(94)90535-5;
Fisher R.P., Morgan D.O.;
"A novel cyclin associates with MO15/CDK7 to form the CDK-activating
kinase.";
Cell 78:713-724(1994).
[9]
FUNCTION AS TP53 KINASE.
PubMed=9372954; DOI=10.1128/MCB.17.12.7220;
Ko L.J., Shieh S.-Y., Chen X., Jayaraman L., Tamai K., Taya Y.,
Prives C., Pan Z.-Q.;
"p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent
manner.";
Mol. Cell. Biol. 17:7220-7229(1997).
[10]
PHOSPHORYLATION AT SER-164 AND THR-170, AND MUTAGENESIS OF SER-164 AND
THR-170.
PubMed=9832506; DOI=10.1101/gad.12.22.3541;
Akoulitchev S., Reinberg D.;
"The molecular mechanism of mitotic inhibition of TFIIH is mediated by
phosphorylation of CDK7.";
Genes Dev. 12:3541-3550(1998).
[11]
IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
Kershnar E., Wu S.-Y., Chiang C.-M.;
"Immunoaffinity purification and functional characterization of human
transcription factor IIH and RNA polymerase II from clonal cell lines
that conditionally express epitope-tagged subunits of the multiprotein
complexes.";
J. Biol. Chem. 273:34444-34453(1998).
[12]
FUNCTION AS CDK2 KINASE, IDENTIFICATION IN COMPLEX WITH TP53, AND
ENZYME REGULATION.
PubMed=9840937; DOI=10.1038/sj.onc.1202504;
Schneider E., Montenarh M., Wagner P.;
"Regulation of CAK kinase activity by p53.";
Oncogene 17:2733-2741(1998).
[13]
FUNCTION.
PubMed=10024882; DOI=10.1016/S1097-2765(00)80177-X;
Tirode F., Busso D., Coin F., Egly J.-M.;
"Reconstitution of the transcription factor TFIIH: assignment of
functions for the three enzymatic subunits, XPB, XPD, and cdk7.";
Mol. Cell 3:87-95(1999).
[14]
INTERACTION WITH PUF60.
PubMed=10882074; DOI=10.1016/S1097-2765(00)80428-1;
Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M.,
Levens D.;
"The FBP interacting repressor targets TFIIH to inhibit activated
transcription.";
Mol. Cell 5:331-341(2000).
[15]
PHOSPHORYLATION AT SER-164 AND THR-170 BY CDK2, AND FUNCTION AS CDK2
KINASE.
PubMed=11113184; DOI=10.1128/MCB.21.1.88-99.2001;
Garrett S., Barton W.A., Knights R., Jin P., Morgan D.O., Fisher R.P.;
"Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed
by substrate specificity determinants outside the T loop.";
Mol. Cell. Biol. 21:88-99(2001).
[16]
INTERACTION WITH PRKCI, AND SUBCELLULAR LOCATION.
PubMed=15695176; DOI=10.1016/j.tice.2004.10.004;
Bicaku E., Patel R., Acevedo-Duncan M.;
"Cyclin-dependent kinase activating kinase/Cdk7 co-localizes with PKC-
iota in human glioma cells.";
Tissue Cell 37:53-58(2005).
[17]
FUNCTION AS SPT5/SUPT5H AND CDK KINASE, MUTAGENESIS OF PHE-91, AND
IDENTIFICATION IN CAK COMPLEX.
PubMed=16327805; DOI=10.1038/nsmb1028;
Larochelle S., Batliner J., Gamble M.J., Barboza N.M., Kraybill B.C.,
Blethrow J.D., Shokat K.M., Fisher R.P.;
"Dichotomous but stringent substrate selection by the dual-function
Cdk7 complex revealed by chemical genetics.";
Nat. Struct. Mol. Biol. 13:55-62(2006).
[18]
FUNCTION IN CELL CYCLE REGULATION.
PubMed=17386261; DOI=10.1016/j.molcel.2007.02.003;
Larochelle S., Merrick K.A., Terret M.-E., Wohlbold L., Barboza N.M.,
Zhang C., Shokat K.M., Jallepalli P.V., Fisher R.P.;
"Requirements for Cdk7 in the assembly of Cdk1/cyclin B and activation
of Cdk2 revealed by chemical genetics in human cells.";
Mol. Cell 25:839-850(2007).
[19]
FUNCTION AS CDK2 KINASE, AND INTERACTION WITH CDK2.
PubMed=17373709; DOI=10.1002/prot.21370;
Lolli G., Johnson L.N.;
"Recognition of Cdk2 by Cdk7.";
Proteins 67:1048-1059(2007).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-164 AND SER-321,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[22]
FUNCTION AS SF1/NR5A1 KINASE, AND INTERACTION WITH SF1/NR5A1.
PubMed=17901130; DOI=10.1210/me.2006-0478;
Lewis A.E., Rusten M., Hoivik E.A., Vikse E.L., Hansson M.L.,
Wallberg A.E., Bakke M.;
"Phosphorylation of steroidogenic factor 1 is mediated by cyclin-
dependent kinase 7.";
Mol. Endocrinol. 22:91-104(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND THR-170, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
FUNCTION AS POLR2A CTD KINASE.
PubMed=19450536; DOI=10.1016/j.molcel.2009.04.016;
Akhtar M.S., Heidemann M., Tietjen J.R., Zhang D.W., Chapman R.D.,
Eick D., Ansari A.Z.;
"TFIIH kinase places bivalent marks on the carboxy-terminal domain of
RNA polymerase II.";
Mol. Cell 34:387-393(2009).
[25]
FUNCTION AS SF1/NR5A1 KINASE.
PubMed=19015234; DOI=10.1128/MCB.00295-08;
Yang W.-H., Heaton J.H., Brevig H., Mukherjee S., Iniguez-Lluhi J.A.,
Hammer G.D.;
"SUMOylation inhibits SF-1 activity by reducing CDK7-mediated serine
203 phosphorylation.";
Mol. Cell. Biol. 29:613-625(2009).
[26]
FUNCTION AS POLR2A CTD KINASE.
PubMed=19667075; DOI=10.1128/MCB.00637-09;
Glover-Cutter K., Larochelle S., Erickson B., Zhang C., Shokat K.,
Fisher R.P., Bentley D.L.;
"TFIIH-associated Cdk7 kinase functions in phosphorylation of C-
terminal domain Ser7 residues, promoter-proximal pausing, and
termination by RNA polymerase II.";
Mol. Cell. Biol. 29:5455-5464(2009).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[28]
FUNCTION AS POLR2A CTD KINASE.
PubMed=19136461; DOI=10.1093/nar/gkn1061;
Lolli G.;
"Binding to DNA of the RNA-polymerase II C-terminal domain allows
discrimination between Cdk7 and Cdk9 phosphorylation.";
Nucleic Acids Res. 37:1260-1268(2009).
[29]
FUNCTION IN DNA-BOUND PEPTIDES TRANSCRIPTION INHIBITION, SUBCELLULAR
LOCATION, AND INDUCTION.
PubMed=19071173; DOI=10.1016/j.peptides.2008.11.008;
Lv X., Wang J., Dong Z., Lv F., Qin Y.;
"DNA-Bound peptides control the mRNA transcription through CDK7.";
Peptides 30:681-688(2009).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[31]
FUNCTION AS CDK1 AND CDK2 KINASE.
PubMed=20360007; DOI=10.1074/jbc.M109.096552;
Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.;
"Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B
at the G2/M transition.";
J. Biol. Chem. 285:16978-16990(2010).
[32]
ENZYME REGULATION.
PubMed=19911397; DOI=10.1002/jcb.22400;
Rogalinska M., Blonski J.Z., Komina O., Goralski P., Zolnierczyk J.D.,
Piekarski H., Robak T., Kilianska Z.M., Wesierska-Gadek J.;
"R-roscovitine (Seliciclib) affects CLL cells more strongly than
combinations of fludarabine or cladribine with cyclophosphamide:
Inhibition of CDK7 sensitizes leukemic cells to caspase-dependent
apoptosis.";
J. Cell. Biochem. 109:217-235(2010).
[33]
REVIEW ON CELL CYCLE REGULATION.
PubMed=15876871;
Lolli G., Johnson L.N.;
"CAK-Cyclin-dependent Activating Kinase: a key kinase in cell cycle
control and a target for drugs?";
Cell Cycle 4:572-577(2005).
[34]
REVIEW ON INHIBITORS, AND GENE FAMILY.
PubMed=19238148; DOI=10.1038/nrc2602;
Malumbres M., Barbacid M.;
"Cell cycle, CDKs and cancer: a changing paradigm.";
Nat. Rev. Cancer 9:153-166(2009).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170 AND SER-321, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[37]
REVIEW ON TRANSCRIPTION REGULATION.
PubMed=21592869; DOI=10.1016/j.dnarep.2011.04.021;
Egly J.M., Coin F.;
"A history of TFIIH: Two decades of molecular biology on a pivotal
transcription/repair factor.";
DNA Repair 10:714-721(2011).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[39]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND THR-170, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[42]
X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) IN COMPLEX WITH ATP, ACTIVE
SITE, AND PHOSPHORYLATION AT THR-170.
PubMed=15530371; DOI=10.1016/j.str.2004.08.013;
Lolli G., Lowe E.D., Brown N.R., Johnson L.N.;
"The crystal structure of human CDK7 and its protein recognition
properties.";
Structure 12:2067-2079(2004).
[43]
VARIANT [LARGE SCALE ANALYSIS] MET-285.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Serine/threonine kinase involved in cell cycle control
and in RNA polymerase II-mediated RNA transcription. Cyclin-
dependent kinases (CDKs) are activated by the binding to a cyclin
and mediate the progression through the cell cycle. Each different
complex controls a specific transition between 2 subsequent phases
in the cell cycle. Required for both activation and complex
formation of CDK1/cyclin-B during G2-M transition, and for
activation of CDK2/cyclins during G1-S transition (but not complex
formation). CDK7 is the catalytic subunit of the CDK-activating
kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1,
POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. CAK
activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6
by threonine phosphorylation, thus regulating cell cycle
progression. CAK complexed to the core-TFIIH basal transcription
factor activates RNA polymerase II by serine phosphorylation of
the repetitive C-terminal domain (CTD) of its large subunit
(POLR2A), allowing its escape from the promoter and elongation of
the transcripts. Phosphorylation of POLR2A in complex with DNA
promotes transcription initiation by triggering dissociation from
DNA. Its expression and activity are constant throughout the cell
cycle. Upon DNA damage, triggers p53/TP53 activation by
phosphorylation, but is inactivated in turn by p53/TP53; this
feedback loop may lead to an arrest of the cell cycle and of the
transcription, helping in cell recovery, or to apoptosis. Required
for DNA-bound peptides-mediated transcription and cellular growth
inhibition. {ECO:0000269|PubMed:10024882,
ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:16327805,
ECO:0000269|PubMed:17373709, ECO:0000269|PubMed:17386261,
ECO:0000269|PubMed:17901130, ECO:0000269|PubMed:19015234,
ECO:0000269|PubMed:19071173, ECO:0000269|PubMed:19136461,
ECO:0000269|PubMed:19450536, ECO:0000269|PubMed:19667075,
ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:9372954,
ECO:0000269|PubMed:9840937}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
[DNA-directed RNA polymerase] phosphate.
-!- ENZYME REGULATION: Inactivated by phosphorylation. Repressed by
roscovitine (seliciclib, CYC202), R547 (Ro-4584820) and SNS-032
(BMS-387032). The association of p53/TP53 to the CAK complex in
response to DNA damage reduces kinase activity toward CDK2 and RNA
polymerase II repetitive C-terminal domain (CTD), thus stopping
cell cycle progression. The inactivation by roscovitine promotes
caspase-mediated apoptosis in leukemic cells.
{ECO:0000269|PubMed:19911397, ECO:0000269|PubMed:9840937}.
-!- SUBUNIT: Associates primarily with cyclin-H (CCNH) and MAT1 to
form the CAK complex. CAK can further associate with the core-
TFIIH to form the TFIIH basal transcription factor; this complex
is sensitive to UV light. The CAK complex binds to p53/TP53 in
response to DNA damage. Interacts with CDK2, SF1/NR5A1, PUF60 and
PRKCI. {ECO:0000269|PubMed:10882074, ECO:0000269|PubMed:15530371,
ECO:0000269|PubMed:15695176, ECO:0000269|PubMed:16327805,
ECO:0000269|PubMed:17373709, ECO:0000269|PubMed:17901130,
ECO:0000269|PubMed:9840937, ECO:0000269|PubMed:9852112}.
-!- INTERACTION:
P24941:CDK2; NbExp=3; IntAct=EBI-1245958, EBI-375096;
P11802:CDK4; NbExp=2; IntAct=EBI-1245958, EBI-295644;
Q01094:E2F1; NbExp=2; IntAct=EBI-1245958, EBI-448924;
O00267:SUPT5H; NbExp=3; IntAct=EBI-1245958, EBI-710464;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear
region. Note=Colocalizes with PRKCI in the cytoplasm and nucleus.
Translocates from the nucleus to cytoplasm and perinuclear region
in response to DNA-bound peptides.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- INDUCTION: Repressed by DNA-bound peptides.
{ECO:0000269|PubMed:19071173}.
-!- PTM: Phosphorylation of Ser-164 during mitosis inactivates the
enzyme. Phosphorylation of Thr-170 is required for activity.
Phosphorylated at Ser-164 and Thr-170 by CDK2.
{ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:15530371,
ECO:0000269|PubMed:9832506}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/cdk7/";
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EMBL; X79193; CAA55785.1; -; mRNA.
EMBL; L20320; AAA36657.1; -; mRNA.
EMBL; X77743; CAA54793.1; -; mRNA.
EMBL; X77303; CAA54508.1; -; mRNA.
EMBL; Y13120; CAA73587.1; -; mRNA.
EMBL; AY130859; AAM77799.1; -; Genomic_DNA.
EMBL; BC000834; AAH00834.1; -; mRNA.
EMBL; BC005298; AAH05298.1; -; mRNA.
CCDS; CCDS3999.1; -.
PIR; A54820; A54820.
PIR; I37215; I37215.
RefSeq; NP_001310998.1; NM_001324069.1.
RefSeq; NP_001310999.1; NM_001324070.1.
RefSeq; NP_001311000.1; NM_001324071.1.
RefSeq; NP_001311006.1; NM_001324077.1.
RefSeq; NP_001790.1; NM_001799.3.
UniGene; Hs.184298; -.
PDB; 1LG3; Model; -; A=1-307.
PDB; 1PA8; Model; -; A=181-346.
PDB; 1UA2; X-ray; 3.02 A; A/B/C/D=1-346.
PDB; 2HIC; Model; -; B=13-311.
PDBsum; 1LG3; -.
PDBsum; 1PA8; -.
PDBsum; 1UA2; -.
PDBsum; 2HIC; -.
ProteinModelPortal; P50613; -.
SMR; P50613; -.
BioGrid; 107457; 86.
CORUM; P50613; -.
DIP; DIP-5995N; -.
IntAct; P50613; 30.
MINT; MINT-3018528; -.
STRING; 9606.ENSP00000256443; -.
BindingDB; P50613; -.
ChEMBL; CHEMBL3055; -.
DrugBank; DB03496; Flavopiridol.
DrugBank; DB02482; Phosphonothreonine.
GuidetoPHARMACOLOGY; 1979; -.
iPTMnet; P50613; -.
PhosphoSitePlus; P50613; -.
BioMuta; CDK7; -.
DMDM; 1705722; -.
EPD; P50613; -.
MaxQB; P50613; -.
PaxDb; P50613; -.
PeptideAtlas; P50613; -.
PRIDE; P50613; -.
DNASU; 1022; -.
Ensembl; ENST00000256443; ENSP00000256443; ENSG00000134058.
Ensembl; ENST00000615305; ENSP00000479116; ENSG00000277273.
GeneID; 1022; -.
KEGG; hsa:1022; -.
UCSC; uc003jvs.5; human.
CTD; 1022; -.
DisGeNET; 1022; -.
EuPathDB; HostDB:ENSG00000134058.10; -.
GeneCards; CDK7; -.
HGNC; HGNC:1778; CDK7.
HPA; CAB004364; -.
HPA; HPA007932; -.
MIM; 601955; gene.
neXtProt; NX_P50613; -.
OpenTargets; ENSG00000134058; -.
PharmGKB; PA26314; -.
eggNOG; KOG0659; Eukaryota.
eggNOG; ENOG410XQDH; LUCA.
GeneTree; ENSGT00830000128262; -.
HOGENOM; HOG000233024; -.
HOVERGEN; HBG014652; -.
InParanoid; P50613; -.
KO; K02202; -.
OMA; ADIKAWM; -.
OrthoDB; EOG091G0CI9; -.
PhylomeDB; P50613; -.
TreeFam; TF101024; -.
BRENDA; 2.7.11.22; 2681.
BRENDA; 2.7.11.23; 2681.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
Reactome; R-HSA-167161; HIV Transcription Initiation.
Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
Reactome; R-HSA-167172; Transcription of the HIV genome.
Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-HSA-72086; mRNA Capping.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
SignaLink; P50613; -.
SIGNOR; P50613; -.
EvolutionaryTrace; P50613; -.
GeneWiki; Cyclin-dependent_kinase_7; -.
GenomeRNAi; 1022; -.
PRO; PR:P50613; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000134058; -.
CleanEx; HS_CDK7; -.
ExpressionAtlas; P50613; baseline and differential.
Genevisible; P50613; HS.
GO; GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; IMP:CAFA.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005675; C:holo TFIIH complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070985; C:TFIIK complex; IBA:GO_Central.
GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
GO; GO:0007050; P:cell cycle arrest; TAS:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:CAFA.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
GO; GO:0042795; P:snRNA transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
Complete proteome; Cytoplasm; DNA damage; DNA repair; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 346 Cyclin-dependent kinase 7.
/FTId=PRO_0000085791.
DOMAIN 12 295 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 18 26 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:15530371}.
ACT_SITE 137 137 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027,
ECO:0000269|PubMed:15530371}.
BINDING 41 41 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:15530371}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 164 164 Phosphoserine; by CDK1 and CDK2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11113184,
ECO:0000269|PubMed:9832506}.
MOD_RES 170 170 Phosphothreonine; by CDK2.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11113184,
ECO:0000269|PubMed:15530371,
ECO:0000269|PubMed:9832506}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
VARIANT 163 163 G -> A. {ECO:0000269|Ref.6}.
/FTId=VAR_023118.
VARIANT 285 285 T -> M (in dbSNP:rs34584424).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.6}.
/FTId=VAR_023119.
MUTAGEN 41 41 K->A: Total loss of activity.
MUTAGEN 91 91 F->G: Enhanced capacity to bind ATP
analogs. {ECO:0000269|PubMed:16327805}.
MUTAGEN 164 164 S->A: No mitotic repression of
transcriptional activity of the
reconstituted TFIIH complex.
{ECO:0000269|PubMed:9832506}.
MUTAGEN 170 170 T->A: Total loss of activity. Total loss
of transcriptional activity of the
reconstituted TFIIH complex.
{ECO:0000269|PubMed:8069918,
ECO:0000269|PubMed:9832506}.
CONFLICT 130 130 Q -> R (in Ref. 7; AAH05298).
{ECO:0000305}.
CONFLICT 249 249 F -> C (in Ref. 5; CAA73587).
{ECO:0000305}.
CONFLICT 321 321 S -> A (in Ref. 5; CAA73587).
{ECO:0000305}.
STRAND 14 21 {ECO:0000244|PDB:1UA2}.
STRAND 24 30 {ECO:0000244|PDB:1UA2}.
STRAND 36 42 {ECO:0000244|PDB:1UA2}.
HELIX 58 68 {ECO:0000244|PDB:1UA2}.
STRAND 77 81 {ECO:0000244|PDB:1UA2}.
STRAND 88 92 {ECO:0000244|PDB:1UA2}.
STRAND 95 97 {ECO:0000244|PDB:1UA2}.
HELIX 98 102 {ECO:0000244|PDB:1UA2}.
HELIX 113 130 {ECO:0000244|PDB:1UA2}.
HELIX 140 142 {ECO:0000244|PDB:1UA2}.
STRAND 143 145 {ECO:0000244|PDB:1UA2}.
STRAND 151 153 {ECO:0000244|PDB:1UA2}.
HELIX 157 159 {ECO:0000244|PDB:1UA2}.
TURN 161 163 {ECO:0000244|PDB:1UA2}.
HELIX 181 184 {ECO:0000244|PDB:1UA2}.
HELIX 192 208 {ECO:0000244|PDB:1UA2}.
HELIX 218 229 {ECO:0000244|PDB:1UA2}.
TURN 234 236 {ECO:0000244|PDB:1UA2}.
STRAND 237 239 {ECO:0000244|PDB:1UA2}.
HELIX 257 260 {ECO:0000244|PDB:1UA2}.
HELIX 266 276 {ECO:0000244|PDB:1UA2}.
TURN 280 282 {ECO:0000244|PDB:1UA2}.
HELIX 286 290 {ECO:0000244|PDB:1UA2}.
HELIX 293 295 {ECO:0000244|PDB:1UA2}.
STRAND 297 299 {ECO:0000244|PDB:1UA2}.
STRAND 304 307 {ECO:0000244|PDB:1UA2}.
SEQUENCE 346 AA; 39038 MW; 0A94BFA7DD416CEB CRC64;
MALDVKSRAK RYEKLDFLGE GQFATVYKAR DKNTNQIVAI KKIKLGHRSE AKDGINRTAL
REIKLLQELS HPNIIGLLDA FGHKSNISLV FDFMETDLEV IIKDNSLVLT PSHIKAYMLM
TLQGLEYLHQ HWILHRDLKP NNLLLDENGV LKLADFGLAK SFGSPNRAYT HQVVTRWYRA
PELLFGARMY GVGVDMWAVG CILAELLLRV PFLPGDSDLD QLTRIFETLG TPTEEQWPDM
CSLPDYVTFK SFPGIPLHHI FSAAGDDLLD LIQGLFLFNP CARITATQAL KMKYFSNRPG
PTPGCQLPRP NCPVETLKEQ SNPALAIKRK RTEALEQGGL PKKLIF


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