lmmol · Proteins

Cyclin-dependent kinase 7

UniProt P50613 Organism Homo sapiens Gene CAK, CAK1, CDK7, CDKN7, MO15, STK1 EC 2.7.11.22, 2.7.11.23

Also known as: CAK, CAK1, CDK7, CDKN7, MO15, STK1

Function

Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. As a cyclin-dependent kinase, CDK7 is activated by the binding to cyclin-H/CCNH and the CDK-activating kinase assembly factor MAT1. Catalytic subunit of the CDK-activating kinase (CAK) complex, a master regulator of CDK activity by catalyzing the activating threonine phosphorylation of CDKs. CAK activates major mediators of cell cycle control, including CDK1, CDK2, CDK4 and CDK6, and plays a key role in regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the CTD of POLR2A, allowing its escape from the promoter and elongation of the transcripts. Initiates transcription by RNA polymerase II by mediating phosphorylation of POLR2A at 'Ser-5' of the repetitive C-terminal domain (CTD) when POLR2A is in complex with DNA, promoting dissociation from DNA and initiation. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11. 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.

Classification

Family (Pfam)
PF00069 Pkinase
InterPro
CDK, CDK7, Kinase-like_dom_sf, Prot_kinase_dom, Protein_kinase_ATP_BS, Ser/Thr_kinase_AS
Functional cluster
Serine/Threonine Protein Kinases

Experimental structures · PDB · 53

A predicted model is available from AlphaFold.

Gene Ontology · 27

Drugs targeting this protein · 9

Related proteins · sequence + function similarity

Co-cited proteins · studied together in the literature

Literature · 45 cited papers

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