InnateDB: Systems Biology of the Innate Immune Response

Mus musculus Protein: Cdk7

Summary

InnateDB Protein

IDBP-178512.6

Last Modified

2014-10-13 [Report errors or provide feedback]

Gene Symbol

Cdk7

Protein Name

cyclin-dependent kinase 7

Synonyms

AI323415; AI528512; C230069N13; Cdkn7; Crk4;

Species

Mus musculus

Ensembl Protein

ENSMUSP00000088845

InnateDB Gene

IDBG-178510 (Cdk7)

Protein Structure

UniProt Annotation

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.

Subcellular Localization

Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. 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). {ECO:0000250}.

Disease Associations

Tissue Specificity

Comments

Interactions

Number of Interactions

This gene and/or its encoded proteins are associated with 5 experimentally validated interaction(s) in this database.
They are also associated with 64 interaction(s) predicted by orthology.

Experimentally validated
Total	5 [view]
Protein-Protein	5 [view]
Protein-DNA	0
Protein-RNA	0
DNA-DNA	0
RNA-RNA	0
DNA-RNA	0

Predicted by orthology
Total	64 [view]

Gene Ontology

Molecular Function

Accession	GO Term
GO:0004672	protein kinase activity
GO:0004693	cyclin-dependent protein serine/threonine kinase activity
GO:0004713	protein tyrosine kinase activity
GO:0005515	protein binding
GO:0005524	ATP binding
GO:0008022	protein C-terminus binding
GO:0008094	DNA-dependent ATPase activity
GO:0008353	RNA polymerase II carboxy-terminal domain kinase activity
GO:0016301	kinase activity
GO:0016772	transferase activity, transferring phosphorus-containing groups

Biological Process

GO:0006200	ATP catabolic process
GO:0006281	DNA repair
GO:0006366	transcription from RNA polymerase II promoter
GO:0006468	protein phosphorylation
GO:0007049	cell cycle
GO:0045944	positive regulation of transcription from RNA polymerase II promoter
GO:0051301	cell division

Cellular Component

GO:0005634	nucleus
GO:0005675	holo TFIIH complex
GO:0005737	cytoplasm
GO:0005739	mitochondrion
GO:0048471	perinuclear region of cytoplasm

Protein Structure and Domains

PDB ID

MGI:102956

InterPro

IPR000719 Protein kinase domain
IPR001245 Serine-threonine/tyrosine-protein kinase catalytic domain
IPR002290 Serine/threonine- /dual specificity protein kinase, catalytic domain
IPR011009 Protein kinase-like domain
IPR020635 Tyrosine-protein kinase, catalytic domain

PFAM

PF00069
PF07714

PRINTS

PR00109

PIRSF

SMART

SM00220
SM00219

TIGRFAMs

Post-translational Modifications

Modification

Cross-References

SwissProt