P51952 (CDK7_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified November 13, 2013. Version 117. History...
Names and origin
|Protein names||Recommended name:|
Cyclin-dependent kinase 7
39 protein kinase
Short name=P39 Mo15
CDK-activating kinase 1
Cell division protein kinase 7
TFIIH basal transcription factor complex kinase subunit
|Organism||Rattus norvegicus (Rat) [Reference proteome]|
|Taxonomic identifier||10116 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus|
|Sequence length||329 AA.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
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-terminus 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 By similarity.
ATP + a protein = ADP + a phosphoprotein.
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
Phosphorylation at Thr-162 is required for enzymatic activity. 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-terminus domain (CTD), thus stopping cell cycle progression By similarity.
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 By similarity.
Nucleus By similarity. Cytoplasm By similarity. Cytoplasm › perinuclear region By similarity. Note: Colocalizes with PRKCI in the cytoplasm and nucleus. Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides By similarity.
Phosphorylation of Ser-156 during mitosis inactivates the enzyme. Phosphorylation of Thr-162 is required for activity. Phosphorylated at Ser-156 and Thr-162 by CDK2 By similarity.
Contains 1 protein kinase domain.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||‹1 – ›329||›329||Cyclin-dependent kinase 7||PRO_0000085793|
|Domain||4 – 287||284||Protein kinase|
|Nucleotide binding||10 – 18||9||ATP By similarity|
|Active site||129||1||Proton acceptor By similarity|
|Binding site||33||1||ATP By similarity|
Amino acid modifications
|Modified residue||156||1||Phosphoserine; by CDK1 and CDK2 By similarity|
|Modified residue||162||1||Phosphothreonine; by CDK2 By similarity|
|Modified residue||313||1||Phosphoserine By similarity|
|X83579 mRNA. Translation: CAA58562.1. Sequence problems.|
3D structure databases
|SMR||P51952. Positions 5-303. |
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
|UCSC||RGD:621124. rat. |
|RGD||621124. Cdk7. |
Gene expression databases
Family and domain databases
|InterPro||IPR011009. Kinase-like_dom. |
|Pfam||PF00069. Pkinase. 1 hit. |
|SMART||SM00220. S_TKc. 1 hit. |
|SUPFAM||SSF56112. SSF56112. 1 hit. |
|PROSITE||PS00107. PROTEIN_KINASE_ATP. 1 hit. |
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
|Accession||Primary (citable) accession number: P51952|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families