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P50613

- CDK7_HUMAN

UniProt

P50613 - CDK7_HUMAN

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Protein

Cyclin-dependent kinase 7

Gene
CDK7, CAK, CAK1, CDKN7, MO15, STK1
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 411ATP
Active sitei137 – 1371Proton acceptor1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 269ATP

GO - Molecular functioni

  1. androgen receptor binding Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
  4. DNA-dependent ATPase activity Source: UniProtKB
  5. protein binding Source: IntAct
  6. protein C-terminus binding Source: UniProtKB
  7. protein kinase activity Source: ProtInc
  8. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB
  9. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: Reactome
  2. androgen receptor signaling pathway Source: UniProtKB
  3. ATP catabolic process Source: GOC
  4. cell cycle arrest Source: UniProtKB
  5. cell division Source: UniProtKB-KW
  6. cell proliferation Source: ProtInc
  7. DNA repair Source: Reactome
  8. G1/S transition of mitotic cell cycle Source: Reactome
  9. G2/M transition of mitotic cell cycle Source: Reactome
  10. gene expression Source: Reactome
  11. mitotic cell cycle Source: Reactome
  12. nucleotide-excision repair Source: Reactome
  13. nucleotide-excision repair, DNA damage removal Source: Reactome
  14. positive regulation of transcription, DNA-templated Source: UniProtKB
  15. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  16. positive regulation of viral transcription Source: Reactome
  17. regulation of cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
  18. termination of RNA polymerase I transcription Source: Reactome
  19. transcription-coupled nucleotide-excision repair Source: Reactome
  20. transcription elongation from RNA polymerase II promoter Source: Reactome
  21. transcription elongation from RNA polymerase I promoter Source: Reactome
  22. transcription from RNA polymerase II promoter Source: UniProtKB
  23. transcription from RNA polymerase I promoter Source: Reactome
  24. transcription initiation from RNA polymerase II promoter Source: Reactome
  25. transcription initiation from RNA polymerase I promoter Source: Reactome
  26. viral process Source: Reactome
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.
ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
REACT_1470. mRNA Capping.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
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_200856. NoRC negatively regulates rRNA expression.
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_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: Chromosome 5

Organism-specific databases

HGNCiHGNC:1778. CDK7.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. holo TFIIH complex Source: UniProtKB
  3. mitochondrion Source: HPA
  4. nucleoplasm Source: Reactome
  5. nucleus Source: HPA
  6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
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.

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.3 Publications

Gene expression databases

BgeeiP50613.
CleanExiHS_CDK7.
GenevestigatoriP50613.

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.7 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi107457. 68 interactions.
DIPiDIP-5995N.
IntActiP50613. 23 interactions.
MINTiMINT-3018528.
STRINGi9606.ENSP00000256443.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP50613.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 295284Protein kinaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiP50613.
KOiK02202.
OMAiCHRNWIL.
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_dom.
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

MALDVKSRAK RYEKLDFLGE GQFATVYKAR DKNTNQIVAI KKIKLGHRSE    50
AKDGINRTAL REIKLLQELS HPNIIGLLDA FGHKSNISLV FDFMETDLEV 100
IIKDNSLVLT PSHIKAYMLM TLQGLEYLHQ HWILHRDLKP NNLLLDENGV 150
LKLADFGLAK SFGSPNRAYT HQVVTRWYRA PELLFGARMY GVGVDMWAVG 200
CILAELLLRV PFLPGDSDLD QLTRIFETLG TPTEEQWPDM CSLPDYVTFK 250
SFPGIPLHHI FSAAGDDLLD LIQGLFLFNP CARITATQAL KMKYFSNRPG 300
PTPGCQLPRP NCPVETLKEQ SNPALAIKRK RTEALEQGGL PKKLIF 346
Length:346
Mass (Da):39,038
Last modified:October 1, 1996 - v1
Checksum:i0A94BFA7DD416CEB
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301Q → R in AAH05298. 1 Publication
Sequence conflicti249 – 2491F → C in CAA73587. 1 Publication
Sequence conflicti321 – 3211S → A in CAA73587. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000571640; ENSP00000460075; ENSG00000262841.
GeneIDi1022.
KEGGihsa:1022.
UCSCiuc003jvs.4. human.

Polymorphism databases

DMDMi1705722.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3999.1.
PIRi A54820.
I37215.
RefSeqi NP_001790.1. NM_001799.3.
UniGenei Hs.184298.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LG3 model - A 1-307 [» ]
1PA8 model - A 181-346 [» ]
1UA2 X-ray 3.02 A/B/C/D 1-346 [» ]
2HIC model - B 13-311 [» ]
ProteinModelPortali P50613.
SMRi P50613. Positions 13-311.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107457. 68 interactions.
DIPi DIP-5995N.
IntActi P50613. 23 interactions.
MINTi MINT-3018528.
STRINGi 9606.ENSP00000256443.

Chemistry

BindingDBi P50613.
ChEMBLi CHEMBL3055.
GuidetoPHARMACOLOGYi 1979.

PTM databases

PhosphoSitei P50613.

Polymorphism databases

DMDMi 1705722.

Proteomic databases

MaxQBi P50613.
PaxDbi P50613.
PeptideAtlasi P50613.
PRIDEi P50613.

Protocols and materials databases

DNASUi 1022.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256443 ; ENSP00000256443 ; ENSG00000134058 .
ENST00000571640 ; ENSP00000460075 ; ENSG00000262841 .
GeneIDi 1022.
KEGGi hsa:1022.
UCSCi uc003jvs.4. human.

Organism-specific databases

CTDi 1022.
GeneCardsi GC05P068530.
HGNCi HGNC:1778. CDK7.
HPAi CAB004364.
HPA007932.
MIMi 601955. gene.
neXtProti NX_P50613.
PharmGKBi PA26314.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233024.
HOVERGENi HBG014652.
InParanoidi P50613.
KOi K02202.
OMAi CHRNWIL.
PhylomeDBi P50613.
TreeFami TF101024.

Enzyme and pathway databases

BRENDAi 2.7.11.22. 2681.
Reactomei REACT_1074. RNA Polymerase I Transcription Termination.
REACT_1470. mRNA Capping.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
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_200856. NoRC negatively regulates rRNA expression.
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_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.
SignaLinki P50613.

Miscellaneous databases

EvolutionaryTracei P50613.
GeneWikii Cyclin-dependent_kinase_7.
GenomeRNAii 1022.
NextBioi 4295.
PROi P50613.
SOURCEi Search...

Gene expression databases

Bgeei P50613.
CleanExi HS_CDK7.
Genevestigatori P50613.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
    , 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: September 3, 2014
This is version 168 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

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