CDK7
entrez
1022
canonical
uniprot
P50613
canonical
ensembl
ENSG00000134058
resolver
ensembl
ENSG00000277273
resolver
ensp
ENSP00000256443
resolver
ensp
ENSP00000422121
resolver
ensp
ENSP00000426561
resolver
ensp
ENSP00000478687
resolver
ensp
ENSP00000479116
resolver
ensp
ENSP00000479440
resolver
ensp
ENSP00000560385
resolver
enst
ENST00000256443
resolver
enst
ENST00000502604
resolver
enst
ENST00000510106
resolver
enst
ENST00000614858
resolver
enst
ENST00000615305
resolver
enst
ENST00000615854
resolver
genesymbol
CDK7
resolver
genesymbol_syn
CAK
resolver
genesymbol_syn
CAK1
resolver
genesymbol_syn
CDKN7
resolver
genesymbol_syn
MO15
resolver
genesymbol_syn
STK1
resolver
hgnc
HGNC:1778
resolver
uniprot
A0A0S2Z3F7
resolver
uniprot
A0A0S2Z3F9
resolver
uniprot
D6R9G1
resolver
uniprot
D6RFL0
resolver
uniprot
Q9BS60
resolver
uniprot
Q9UE19
resolver
uniprot_entry
A0A0S2Z3F7_HUMAN
resolver
uniprot_entry
A0A0S2Z3F9_HUMAN
resolver
uniprot_entry
CDK7_HUMAN
resolver
uniprot_entry
D6R9G1_HUMAN
resolver
uniprot_entry
D6RFL0_HUMAN
resolver
uniprot_sec
Q9BS60
resolver
uniprot_sec
Q9UE19
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phosphorylation (PubMed:41100585). Phosphorylated by CDKs, including CDK1 and CDK2, and reciprocally phosphorylating its activating kinase (PubMed:41100585). 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 (PubMed:9840937). The inactivation by roscovitine promotes caspase-mediated apoptosis in leukemic cells (PubMed:19911397). Specifically inactivated by THZ1 (PubMed:26257281). {ECO:0000269|PubMed:19911397, ECO:0000269|PubMed:26257281, ECO:0000269|PubMed:41100585, ECO:0000269|PubMed:9840937}.
uniprot
proteins
amino_acid_sequence
MALDVKSRAKRYEKLDFLGEGQFATVYKARDKNTNQIVAIKKIKLGHRSEAKDGINRTALREIKLLQELSHPNIIGLLDAFGHKSNISLVFDFMETDLEVIIKDNSLVLTPSHIKAYMLMTLQGLEYLHQHWILHRDLKPNNLLLDENGVLKLADFGLAKSFGSPNRAYTHQVVTRWYRAPELLFGARMYGVGVDMWAVGCILAELLLRVPFLPGDSDLDQLTRIFETLGTPTEEQWPDMCSLPDYVTFKSFPGIPLHHIFSAAGDDLLDLIQGLFLFNPCARITATQALKMKYFSNRPGPTPGCQLPRPNCPVETLKEQSNPALAIKRKRTEALEQGGLPKKLIF
uniprot
proteins
ec_number
2.7.11.22
uniprot
proteins
ec_number
2.7.11.23
uniprot
proteins
function
FUNCTION: Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription (PubMed:9852112, PubMed:19136461, PubMed:26257281, PubMed:28768201). As a cyclin-dependent kinase, CDK7 is activated by the binding to cyclin-H/CCNH and the CDK-activating kinase assembly factor MAT1 (PubMed:41100585). Catalytic subunit of the CDK-activating kinase (CAK) complex, a master regulator of CDK activity by catalyzing the activating threonine phosphorylation of CDKs (PubMed:41100585). CAK activates major mediators of cell cycle control, including CDK1, CDK2, CDK4 and CDK6, and plays a key role in regulating cell cycle progression (PubMed:41100585). 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 (PubMed:9852112). 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 (PubMed:19136461, PubMed:26257281, PubMed:28768201). Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11 (PubMed:9372954, PubMed:9840937, PubMed:19136461, PubMed:26257281, PubMed:28768201, PubMed:41100585, PubMed:41100585). 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. {ECO:0000269|PubMed:10024882, ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:16327805, ECO:0000269|PubMed:17373709, ECO:0000269|PubMed:17386261, ECO:0000269|PubMed:17901130, ECO:0000269|PubMed:19015234, ECO:0000269|PubMed:19071173, ECO:0000269|PubMed:19136461, ECO:0000269|PubMed:19450536, ECO:0000269|PubMed:19667075, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:26257281, ECO:0000269|PubMed:28768201, ECO:0000269|PubMed:41100585, ECO:0000269|PubMed:9372954, ECO:0000269|PubMed:9840937, ECO:0000269|PubMed:9852112}.
uniprot
proteins
mass_dalton
39038
uniprot
proteins
mutagenesis
MUTAGEN 41; /note="K->A: Total loss of activity."; MUTAGEN 41; /note="K->M: No effect on interaction with HINT1."; /evidence="ECO:0000269|PubMed:10958787"; MUTAGEN 91; /note="F->G: Enhanced capacity to bind ATP analogs."; /evidence="ECO:0000269|PubMed:16327805"; MUTAGEN 164; /note="S->A: No mitotic repression of transcriptional activity of the reconstituted TFIIH complex."; /evidence="ECO:0000269|PubMed:9832506"; MUTAGEN 170; /note="T->A: Total loss of activity. Total loss of transcriptional activity of the reconstituted TFIIH complex."; /evidence="ECO:0000269|PubMed:8069918, ECO:0000269|PubMed:9832506"; MUTAGEN 170; /note="T->E: No effect on interaction with HINT1."; /evidence="ECO:0000269|PubMed:10958787"; MUTAGEN 176; /note="R->A: Impairs phosphorylation of CDK2; when associated with A-217 and A-223."; /evidence="ECO:0000269|PubMed:41100585"; MUTAGEN 217; /note="S->A: Impairs phosphorylation of CDK2; when associated with A-176 and A-223."; /evidence="ECO:0000269|PubMed:41100585"; MUTAGEN 219; /note="L->R: Impairs phosphorylation of CDK2."; /evidence="ECO:0000269|PubMed:41100585"; MUTAGEN 223; /note="T->A: Impairs phosphorylation of CDK2; when associated with A-176 and A-217."; /evidence="ECO:0000269|PubMed:41100585
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:11113184, ECO:0000269|PubMed:15530371, ECO:0000269|PubMed:9832506}.
uniprot
proteins
protein_family
CDC2/CDKX subfamily
uniprot
proteins
protein_family
CMGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10024882
uniprot
proteins
pubmed
10882074
uniprot
proteins
pubmed
10958787
uniprot
proteins
pubmed
11113184
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15530371
uniprot
proteins
pubmed
15695176
uniprot
proteins
pubmed
15876871
uniprot
proteins
pubmed
16327805
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17373709
uniprot
proteins
pubmed
17386261
uniprot
proteins
pubmed
17901130
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19015234
uniprot
proteins
pubmed
19071173
uniprot
proteins
pubmed
19136461
uniprot
proteins
pubmed
19238148
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19450536
uniprot
proteins
pubmed
19667075
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19911397
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20360007
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21592869
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26257281
uniprot
proteins
pubmed
28768201
uniprot
proteins
pubmed
41100585
uniprot
proteins
pubmed
7929589
uniprot
proteins
pubmed
7936635
uniprot
proteins
pubmed
8069918
uniprot
proteins
pubmed
8208544
uniprot
proteins
pubmed
8208556
uniprot
proteins
pubmed
9372954
uniprot
proteins
pubmed
9832506
uniprot
proteins
pubmed
9840937
uniprot
proteins
pubmed
9852112
uniprot
proteins
sequence_length
346
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10958787, ECO:0000269|PubMed:15695176, ECO:0000269|PubMed:19071173}. Cytoplasm {ECO:0000269|PubMed:15695176}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19071173}. Note=Colocalizes with PRKCI in the cytoplasm and nucleus (PubMed:15695176). Translocates from the nucleus to cytoplasm and perinuclear region in response to DNA-bound peptides (PubMed:19071173). {ECO:0000269|PubMed:15695176, ECO:0000269|PubMed:19071173}.
uniprot
proteins