Cyclin-dependent kinase 7 (Protein name
), CDK7_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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Gene name:
CDK7(CAK;CAK1;CDKN7;MO15;STK1);
Protein name:
Cyclin-dependent kinase 7;
Alternative:
CDK-activating kinase 1;39 kDa protein kinase(p39 Mo15);Serine/threonine-protein kinase 1;Cell division protein kinase 7;TFIIH basal transcription factor complex kinase subunit;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
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.
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-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.
Subcellular Location:
Nucleus
Cytoplasm
Cytoplasm
perinuclear region
Colocalizes with PRKCI in the cytoplasm and nucleus. Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides.
NIEHS SNPs program
Submitted (2002-07) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANTS ALA-163 AND MET-285
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Cited for: PHOSPHORYLATION AT SER-164 AND THR-170;MUTAGENESIS OF SER-164 AND THR-170
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Cited for: IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR
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Cited for: FUNCTION AS CDK2 KINASE;IDENTIFICATION IN COMPLEX WITH TP53;ENZYME REGULATION
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Cited for: PHOSPHORYLATION AT SER-164 AND THR-170 BY CDK2;FUNCTION AS CDK2 KINASE
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Cited for: FUNCTION AS SPT5/SUPT5H AND CDK KINASE;MUTAGENESIS OF PHE-91;IDENTIFICATION IN CAK COMPLEX
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-164 AND SER-321;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION AS SF1/NR5A1 KINASE;INTERACTION WITH SF1/NR5A1
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND THR-170;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION IN DNA-BOUND PEPTIDES TRANSCRIPTION INHIBITION;SUBCELLULAR LOCATION;INDUCTION
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170 AND SER-321;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
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Cited for: X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) IN COMPLEX WITH ATP;ACTIVE SITE;PHOSPHORYLATION AT THR-170