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Protein

Cyclin-dependent kinase 7

Gene

CDK7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.14 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Enzyme regulationi

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411ATPPROSITE-ProRule annotation1 Publication
Active sitei137 – 1371Proton acceptorPROSITE-ProRule annotation1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 269ATPPROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
  • DNA-dependent ATPase activity Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein kinase activity Source: ProtInc
  • RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.22. 2681.
2.7.11.23. 2681.
ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
REACT_1470. mRNA Capping.
REACT_1574. Cyclin E associated events during G1/S transition.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1845. Formation of RNA Pol II elongation complex.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_257. Formation of incision complex in GG-NER.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_311. Dual incision reaction in GG-NER.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_821. Cyclin D associated events in G1.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
REACT_953. RNA Polymerase I Transcription Initiation.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.
SignaLinkiP50613.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CDK7
Synonyms:CAK, CAK1, CDKN7, MO15, STK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 5, Unplaced

Organism-specific databases

HGNCiHGNC:1778. CDK7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411K → A: Total loss of activity.
Mutagenesisi91 – 911F → G: Enhanced capacity to bind ATP analogs. 1 Publication
Mutagenesisi164 – 1641S → A: No mitotic repression of transcriptional activity of the reconstituted TFIIH complex. 1 Publication
Mutagenesisi170 – 1701T → A: Total loss of activity. Total loss of transcriptional activity of the reconstituted TFIIH complex. 2 Publications

Organism-specific databases

PharmGKBiPA26314.

Polymorphism and mutation databases

BioMutaiCDK7.
DMDMi1705722.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 346345Cyclin-dependent kinase 7PRO_0000085791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei7 – 71Phosphoserine1 Publication
Modified residuei164 – 1641Phosphoserine; by CDK1 and CDK24 Publications
Modified residuei170 – 1701Phosphothreonine; by CDK27 Publications
Modified residuei321 – 3211Phosphoserine2 Publications

Post-translational modificationi

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 CDK2.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP50613.
PaxDbiP50613.
PeptideAtlasiP50613.
PRIDEiP50613.

PTM databases

PhosphoSiteiP50613.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

Repressed by DNA-bound peptides.1 Publication

Gene expression databases

BgeeiP50613.
CleanExiHS_CDK7.
ExpressionAtlasiP50613. baseline.
GenevisibleiP50613. HS.

Organism-specific databases

HPAiCAB004364.
HPA007932.

Interactioni

Subunit structurei

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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
E2F1Q010942EBI-1245958,EBI-448924

Protein-protein interaction databases

BioGridi107457. 81 interactions.
DIPiDIP-5995N.
IntActiP50613. 23 interactions.
MINTiMINT-3018528.

Structurei

Secondary structure

1
346
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 218Combined sources
Beta strandi24 – 307Combined sources
Beta strandi36 – 427Combined sources
Helixi58 – 6811Combined sources
Beta strandi77 – 815Combined sources
Beta strandi88 – 925Combined sources
Beta strandi95 – 973Combined sources
Helixi98 – 1025Combined sources
Helixi113 – 13018Combined sources
Helixi140 – 1423Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi151 – 1533Combined sources
Helixi157 – 1593Combined sources
Turni161 – 1633Combined sources
Helixi181 – 1844Combined sources
Helixi192 – 20817Combined sources
Helixi218 – 22912Combined sources
Turni234 – 2363Combined sources
Beta strandi237 – 2393Combined sources
Helixi257 – 2604Combined sources
Helixi266 – 27611Combined sources
Turni280 – 2823Combined sources
Helixi286 – 2905Combined sources
Helixi293 – 2953Combined sources
Beta strandi297 – 2993Combined sources
Beta strandi304 – 3074Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LG3model-A1-307[»]
1PA8model-A181-346[»]
1UA2X-ray3.02A/B/C/D1-346[»]
2HICmodel-B13-311[»]
ProteinModelPortaliP50613.
SMRiP50613. Positions 13-311.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50613.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 295284Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119242.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP50613.
KOiK02202.
OMAiGPKLPMP.
PhylomeDBiP50613.
TreeFamiTF101024.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P50613-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALDVKSRAK RYEKLDFLGE GQFATVYKAR DKNTNQIVAI KKIKLGHRSE
60 70 80 90 100
AKDGINRTAL REIKLLQELS HPNIIGLLDA FGHKSNISLV FDFMETDLEV
110 120 130 140 150
IIKDNSLVLT PSHIKAYMLM TLQGLEYLHQ HWILHRDLKP NNLLLDENGV
160 170 180 190 200
LKLADFGLAK SFGSPNRAYT HQVVTRWYRA PELLFGARMY GVGVDMWAVG
210 220 230 240 250
CILAELLLRV PFLPGDSDLD QLTRIFETLG TPTEEQWPDM CSLPDYVTFK
260 270 280 290 300
SFPGIPLHHI FSAAGDDLLD LIQGLFLFNP CARITATQAL KMKYFSNRPG
310 320 330 340
PTPGCQLPRP NCPVETLKEQ SNPALAIKRK RTEALEQGGL PKKLIF
Length:346
Mass (Da):39,038
Last modified:October 1, 1996 - v1
Checksum:i0A94BFA7DD416CEB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301Q → R in AAH05298 (PubMed:15489334).Curated
Sequence conflicti249 – 2491F → C in CAA73587 (Ref. 5) Curated
Sequence conflicti321 – 3211S → A in CAA73587 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti163 – 1631G → A.1 Publication
VAR_023118
Natural varianti285 – 2851T → M.2 Publications
Corresponds to variant rs34584424 [ dbSNP | Ensembl ].
VAR_023119

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3999.1.
PIRiA54820.
I37215.
RefSeqiNP_001790.1. NM_001799.3.
UniGeneiHs.184298.

Genome annotation databases

EnsembliENST00000256443; ENSP00000256443; ENSG00000134058.
ENST00000615305; ENSP00000479116; ENSG00000277273.
GeneIDi1022.
KEGGihsa:1022.
UCSCiuc003jvs.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3999.1.
PIRiA54820.
I37215.
RefSeqiNP_001790.1. NM_001799.3.
UniGeneiHs.184298.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LG3model-A1-307[»]
1PA8model-A181-346[»]
1UA2X-ray3.02A/B/C/D1-346[»]
2HICmodel-B13-311[»]
ProteinModelPortaliP50613.
SMRiP50613. Positions 13-311.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107457. 81 interactions.
DIPiDIP-5995N.
IntActiP50613. 23 interactions.
MINTiMINT-3018528.

Chemistry

BindingDBiP50613.
ChEMBLiCHEMBL3055.
GuidetoPHARMACOLOGYi1979.

PTM databases

PhosphoSiteiP50613.

Polymorphism and mutation databases

BioMutaiCDK7.
DMDMi1705722.

Proteomic databases

MaxQBiP50613.
PaxDbiP50613.
PeptideAtlasiP50613.
PRIDEiP50613.

Protocols and materials databases

DNASUi1022.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256443; ENSP00000256443; ENSG00000134058.
ENST00000615305; ENSP00000479116; ENSG00000277273.
GeneIDi1022.
KEGGihsa:1022.
UCSCiuc003jvs.4. human.

Organism-specific databases

CTDi1022.
GeneCardsiGC05P068530.
HGNCiHGNC:1778. CDK7.
HPAiCAB004364.
HPA007932.
MIMi601955. gene.
neXtProtiNX_P50613.
PharmGKBiPA26314.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119242.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP50613.
KOiK02202.
OMAiGPKLPMP.
PhylomeDBiP50613.
TreeFamiTF101024.

Enzyme and pathway databases

BRENDAi2.7.11.22. 2681.
2.7.11.23. 2681.
ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
REACT_1470. mRNA Capping.
REACT_1574. Cyclin E associated events during G1/S transition.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1845. Formation of RNA Pol II elongation complex.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_257. Formation of incision complex in GG-NER.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_311. Dual incision reaction in GG-NER.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_821. Cyclin D associated events in G1.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
REACT_953. RNA Polymerase I Transcription Initiation.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.
SignaLinkiP50613.

Miscellaneous databases

EvolutionaryTraceiP50613.
GeneWikiiCyclin-dependent_kinase_7.
GenomeRNAii1022.
NextBioi4295.
PROiP50613.
SOURCEiSearch...

Gene expression databases

BgeeiP50613.
CleanExiHS_CDK7.
ExpressionAtlasiP50613. baseline.
GenevisibleiP50613. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  40. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  41. "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.
  42. "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.
    , 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.

Entry informationi

Entry nameiCDK7_HUMAN
AccessioniPrimary (citable) accession number: P50613
Secondary accession number(s): Q9BS60, Q9UE19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 176 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.