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P50613 (CDK7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase 7

EC=2.7.11.22
EC=2.7.11.23
Alternative name(s):
39 kDa protein kinase
Short name=p39 Mo15
CDK-activating kinase 1
Cell division protein kinase 7
Serine/threonine-protein kinase 1
TFIIH basal transcription factor complex kinase subunit
Gene names
Name:CDK7
Synonyms:CAK, CAK1, CDKN7, MO15, STK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.9 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.22 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.31

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

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. Ref.12 Ref.32

Subunit structure

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. Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.19 Ref.22

Subcellular location

Nucleus. Cytoplasm. Cytoplasmperinuclear 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. Ref.16 Ref.29

Tissue specificity

Ubiquitous.

Induction

Repressed by DNA-bound peptides. Ref.12 Ref.29 Ref.32

Post-translational modification

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. Ref.10 Ref.15 Ref.40

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

ATP catabolic process

Inferred from direct assay Ref.11. Source: GOC

DNA repair

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

androgen receptor signaling pathway

Non-traceable author statement PubMed 15572661. Source: UniProtKB

cell cycle arrest

Traceable author statement Ref.33. Source: UniProtKB

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Traceable author statement PubMed 7533895. Source: ProtInc

gene expression

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleotide-excision repair

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 8692841. Source: UniProtKB

positive regulation of transcription, DNA-templated

Non-traceable author statement PubMed 15572661. Source: UniProtKB

positive regulation of viral transcription

Traceable author statement. Source: Reactome

regulation of cyclin-dependent protein serine/threonine kinase activity

Traceable author statement PubMed 7533895. Source: ProtInc

termination of RNA polymerase I transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.11. Source: UniProtKB

transcription initiation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

holo TFIIH complex

Inferred from direct assay Ref.11. Source: UniProtKB

mitochondrion

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent ATPase activity

Inferred from direct assay Ref.11. Source: UniProtKB

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from direct assay PubMed 12721286Ref.11. Source: UniProtKB

androgen receptor binding

Non-traceable author statement PubMed 15572661. Source: UniProtKB

cyclin-dependent protein serine/threonine kinase activity

Traceable author statement Ref.2. Source: ProtInc

protein C-terminus binding

Inferred from physical interaction PubMed 10801852. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 23397142. Source: IntAct

protein kinase activity

Traceable author statement PubMed 7533895. Source: ProtInc

transcription coactivator activity

Non-traceable author statement PubMed 15572661. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

E2F1Q010942EBI-1245958,EBI-448924

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.39
Chain2 – 346345Cyclin-dependent kinase 7
PRO_0000085791

Regions

Domain12 – 295284Protein kinase
Nucleotide binding18 – 269ATP

Sites

Active site1371Proton acceptor Ref.40
Binding site411ATP

Amino acid modifications

Modified residue21N-acetylalanine Ref.39
Modified residue71Phosphoserine Ref.21
Modified residue1641Phosphoserine; by CDK1 and CDK2 Ref.10 Ref.15 Ref.21 Ref.23
Modified residue1701Phosphothreonine; by CDK2 Ref.10 Ref.15 Ref.23 Ref.30 Ref.35 Ref.38 Ref.40
Modified residue3211Phosphoserine Ref.21 Ref.35

Natural variations

Natural variant1631G → A. Ref.6
VAR_023118
Natural variant2851T → M. Ref.6 Ref.41
Corresponds to variant rs34584424 [ dbSNP | Ensembl ].
VAR_023119

Experimental info

Mutagenesis411K → A: Total loss of activity.
Mutagenesis911F → G: Enhanced capacity to bind ATP analogs. Ref.17
Mutagenesis1641S → A: No mitotic repression of transcriptional activity of the reconstituted TFIIH complex. Ref.10
Mutagenesis1701T → A: Total loss of activity. Total loss of transcriptional activity of the reconstituted TFIIH complex. Ref.8 Ref.10
Sequence conflict1301Q → R in AAH05298. Ref.7
Sequence conflict2491F → C in CAA73587. Ref.5
Sequence conflict3211S → A in CAA73587. Ref.5

Secondary structure

.................................................. 346
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50613 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 0A94BFA7DD416CEB

FASTA34639,038
        10         20         30         40         50         60 
MALDVKSRAK RYEKLDFLGE GQFATVYKAR DKNTNQIVAI KKIKLGHRSE AKDGINRTAL 

        70         80         90        100        110        120 
REIKLLQELS HPNIIGLLDA FGHKSNISLV FDFMETDLEV IIKDNSLVLT PSHIKAYMLM 

       130        140        150        160        170        180 
TLQGLEYLHQ HWILHRDLKP NNLLLDENGV LKLADFGLAK SFGSPNRAYT HQVVTRWYRA 

       190        200        210        220        230        240 
PELLFGARMY GVGVDMWAVG CILAELLLRV PFLPGDSDLD QLTRIFETLG TPTEEQWPDM 

       250        260        270        280        290        300 
CSLPDYVTFK SFPGIPLHHI FSAAGDDLLD LIQGLFLFNP CARITATQAL KMKYFSNRPG 

       310        320        330        340 
PTPGCQLPRP NCPVETLKEQ SNPALAIKRK RTEALEQGGL PKKLIF 

« Hide

References

« Hide 'large scale' references
[1]"Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase)."
Tassan J.-P., Schultz S.J., Bartek J., Nigg E.A.
J. Cell Biol. 127:467-478(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"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."
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.
Oncogene 9:1977-1988(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.
[3]"Cloning, expression and subcellular localization of the human homolog of p40MO15 catalytic subunit of cdk-activating kinase."
Darbon J.-M., Devault A., Taviaux S., Fesquet D., Martinez A.-M., Galas S., Cavadore J.-C., Doree M., Blanchard J.-M.
Oncogene 9:3127-3138(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Molecular cloning of the human CAK1 gene encoding a cyclin-dependent kinase-activating kinase."
Wu L., Yee A., Liu L., Carbonaro-Hall D., Venkatesan N., Tolo T., Hall F.L.
Oncogene 9:2089-2096(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[5]"Human and Xenopus MO15 mRNA are highly conserved but show different patterns of expression in adult tissues."
Kobelt D., Karn T., Hock B., Holtrich U., Braeuninger A., Wolf G., Strebhardt K., Ruebsamen-Waigmann H.
Oncol. Rep. 1:1269-1275(1994)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung and Thymus.
[6]NIEHS SNPs program
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-163 AND MET-285.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cervix and Urinary bladder.
[8]"A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase."
Fisher R.P., Morgan D.O.
Cell 78:713-724(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF THR-170.
[9]"p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner."
Ko L.J., Shieh S.-Y., Chen X., Jayaraman L., Tamai K., Taya Y., Prives C., Pan Z.-Q.
Mol. Cell. Biol. 17:7220-7229(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS TP53 KINASE.
[10]"The molecular mechanism of mitotic inhibition of TFIIH is mediated by phosphorylation of CDK7."
Akoulitchev S., Reinberg D.
Genes Dev. 12:3541-3550(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-164 AND THR-170, MUTAGENESIS OF SER-164 AND THR-170.
[11]"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."
Kershnar E., Wu S.-Y., Chiang C.-M.
J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
[12]"Regulation of CAK kinase activity by p53."
Schneider E., Montenarh M., Wagner P.
Oncogene 17:2733-2741(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CDK2 KINASE, IDENTIFICATION IN COMPLEX WITH TP53, ENZYME REGULATION.
[13]"Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7."
Tirode F., Busso D., Coin F., Egly J.-M.
Mol. Cell 3:87-95(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"The FBP interacting repressor targets TFIIH to inhibit activated transcription."
Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D.
Mol. Cell 5:331-341(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PUF60.
[15]"Reciprocal activation by cyclin-dependent kinases 2 and 7 is directed by substrate specificity determinants outside the T loop."
Garrett S., Barton W.A., Knights R., Jin P., Morgan D.O., Fisher R.P.
Mol. Cell. Biol. 21:88-99(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-164 AND THR-170 BY CDK2, FUNCTION AS CDK2 KINASE.
[16]"Cyclin-dependent kinase activating kinase/Cdk7 co-localizes with PKC-iota in human glioma cells."
Bicaku E., Patel R., Acevedo-Duncan M.
Tissue Cell 37:53-58(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKCI, SUBCELLULAR LOCATION.
[17]"Dichotomous but stringent substrate selection by the dual-function Cdk7 complex revealed by chemical genetics."
Larochelle S., Batliner J., Gamble M.J., Barboza N.M., Kraybill B.C., Blethrow J.D., Shokat K.M., Fisher R.P.
Nat. Struct. Mol. Biol. 13:55-62(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS SPT5/SUPT5H AND CDK KINASE, MUTAGENESIS OF PHE-91, IDENTIFICATION IN CAK COMPLEX.
[18]"Requirements for Cdk7 in the assembly of Cdk1/cyclin B and activation of Cdk2 revealed by chemical genetics in human cells."
Larochelle S., Merrick K.A., Terret M.-E., Wohlbold L., Barboza N.M., Zhang C., Shokat K.M., Jallepalli P.V., Fisher R.P.
Mol. Cell 25:839-850(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL CYCLE REGULATION.
[19]"Recognition of Cdk2 by Cdk7."
Lolli G., Johnson L.N.
Proteins 67:1048-1059(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CDK2 KINASE, INTERACTION WITH CDK2.
[20]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-164 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Phosphorylation of steroidogenic factor 1 is mediated by cyclin-dependent kinase 7."
Lewis A.E., Rusten M., Hoivik E.A., Vikse E.L., Hansson M.L., Wallberg A.E., Bakke M.
Mol. Endocrinol. 22:91-104(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS SF1/NR5A1 KINASE, INTERACTION WITH SF1/NR5A1.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND THR-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"TFIIH kinase places bivalent marks on the carboxy-terminal domain of RNA polymerase II."
Akhtar M.S., Heidemann M., Tietjen J.R., Zhang D.W., Chapman R.D., Eick D., Ansari A.Z.
Mol. Cell 34:387-393(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS POLR2A CTD KINASE.
[25]"SUMOylation inhibits SF-1 activity by reducing CDK7-mediated serine 203 phosphorylation."
Yang W.-H., Heaton J.H., Brevig H., Mukherjee S., Iniguez-Lluhi J.A., Hammer G.D.
Mol. Cell. Biol. 29:613-625(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS SF1/NR5A1 KINASE.
[26]"TFIIH-associated Cdk7 kinase functions in phosphorylation of C-terminal domain Ser7 residues, promoter-proximal pausing, and termination by RNA polymerase II."
Glover-Cutter K., Larochelle S., Erickson B., Zhang C., Shokat K., Fisher R.P., Bentley D.L.
Mol. Cell. Biol. 29:5455-5464(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS POLR2A CTD KINASE.
[27]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Binding to DNA of the RNA-polymerase II C-terminal domain allows discrimination between Cdk7 and Cdk9 phosphorylation."
Lolli G.
Nucleic Acids Res. 37:1260-1268(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS POLR2A CTD KINASE.
[29]"DNA-Bound peptides control the mRNA transcription through CDK7."
Lv X., Wang J., Dong Z., Lv F., Qin Y.
Peptides 30:681-688(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA-BOUND PEPTIDES TRANSCRIPTION INHIBITION, SUBCELLULAR LOCATION, INDUCTION.
[30]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[31]"Cdc25 phosphatases are required for timely assembly of CDK1-cyclin B at the G2/M transition."
Timofeev O., Cizmecioglu O., Settele F., Kempf T., Hoffmann I.
J. Biol. Chem. 285:16978-16990(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CDK1 AND CDK2 KINASE.
[32]"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."
Rogalinska M., Blonski J.Z., Komina O., Goralski P., Zolnierczyk J.D., Piekarski H., Robak T., Kilianska Z.M., Wesierska-Gadek J.
J. Cell. Biochem. 109:217-235(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[33]"CAK-Cyclin-dependent Activating Kinase: a key kinase in cell cycle control and a target for drugs?"
Lolli G., Johnson L.N.
Cell Cycle 4:572-577(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON CELL CYCLE REGULATION.
[34]"Cell cycle, CDKs and cancer: a changing paradigm."
Malumbres M., Barbacid M.
Nat. Rev. Cancer 9:153-166(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON INHIBITORS, GENE FAMILY.
[35]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170 AND SER-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[36]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"A history of TFIIH: Two decades of molecular biology on a pivotal transcription/repair factor."
Egly J.M., Coin F.
DNA Repair 10:714-721(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON TRANSCRIPTION REGULATION.
[38]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[40]"The crystal structure of human CDK7 and its protein recognition properties."
Lolli G., Lowe E.D., Brown N.R., Johnson L.N.
Structure 12:2067-2079(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) IN COMPLEX WITH ATP, ACTIVE SITE, PHOSPHORYLATION AT THR-170.
[41]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-285.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X79193 mRNA. Translation: CAA55785.1.
L20320 mRNA. Translation: AAA36657.1.
X77743 mRNA. Translation: CAA54793.1.
X77303 mRNA. Translation: CAA54508.1.
Y13120 mRNA. Translation: CAA73587.1.
AY130859 Genomic DNA. Translation: AAM77799.1.
BC000834 mRNA. Translation: AAH00834.1.
BC005298 mRNA. Translation: AAH05298.1.
CCDSCCDS3999.1.
PIRA54820.
I37215.
RefSeqNP_001790.1. NM_001799.3.
UniGeneHs.184298.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LG3model-A1-307[»]
1PA8model-A181-346[»]
1UA2X-ray3.02A/B/C/D1-346[»]
2HICmodel-B13-311[»]
ProteinModelPortalP50613.
SMRP50613. Positions 13-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107457. 68 interactions.
DIPDIP-5995N.
IntActP50613. 23 interactions.
MINTMINT-3018528.
STRING9606.ENSP00000256443.

Chemistry

BindingDBP50613.
ChEMBLCHEMBL3055.
GuidetoPHARMACOLOGY1979.

PTM databases

PhosphoSiteP50613.

Polymorphism databases

DMDM1705722.

Proteomic databases

MaxQBP50613.
PaxDbP50613.
PeptideAtlasP50613.
PRIDEP50613.

Protocols and materials databases

DNASU1022.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256443; ENSP00000256443; ENSG00000134058.
ENST00000571640; ENSP00000460075; ENSG00000262841.
GeneID1022.
KEGGhsa:1022.
UCSCuc003jvs.4. human.

Organism-specific databases

CTD1022.
GeneCardsGC05P068530.
HGNCHGNC:1778. CDK7.
HPACAB004364.
HPA007932.
MIM601955. gene.
neXtProtNX_P50613.
PharmGKBPA26314.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidP50613.
KOK02202.
OMACHRNWIL.
PhylomeDBP50613.
TreeFamTF101024.

Enzyme and pathway databases

BRENDA2.7.11.22. 2681.
ReactomeREACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_1788. Transcription.
REACT_216. DNA Repair.
REACT_71. Gene Expression.
SignaLinkP50613.

Gene expression databases

BgeeP50613.
CleanExHS_CDK7.
GenevestigatorP50613.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP50613.
GeneWikiCyclin-dependent_kinase_7.
GenomeRNAi1022.
NextBio4295.
PROP50613.
SOURCESearch...

Entry information

Entry nameCDK7_HUMAN
AccessionPrimary (citable) accession number: P50613
Secondary accession number(s): Q9BS60, Q9UE19
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM