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Protein Page:
CDK7 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CDK7 a protein kinase of the CDK family. Forms a trimeric complex with cyclin H and MAT1, which functions as a Cdk-activating kinase (CAK). Activates the cyclin-associated kinases CDK1, -2, -4 and -6. An essential component of the transcription factor TFIIH, that is involved in transcription initiation and DNA repair. Serves as a direct link between the regulation of transcription and the cell cycle. Phosphorylates and activates RNA polymerase II, allowing its escape from the promoter and elongation of the transcripts. Involved in cell cycle control and in RNA transcription by RNA polymerase II. Its expression and activity are constant throughout the cell cycle. Note: This description may include information from UniProtKB.
Protein type: Kinase, protein; Cell cycle regulation; EC 2.7.11.22; Protein kinase, Ser/Thr (non-receptor); Protein kinase, CMGC; EC 2.7.11.23; Nuclear receptor co-regulator; CMGC group; CDK family; CDK/CDK7 subfamily; CDK7 subfamily
Chromosomal Location of Human Ortholog: 5q12.1
Cellular Component: cytoplasm; holo TFIIH complex; mitochondrion; nucleoplasm; nucleus
Molecular Function: DNA-dependent ATPase activity; kinase activity; protein binding; protein C-terminus binding; protein kinase activity; protein serine/threonine kinase activity; RNA polymerase subunit kinase activity
Biological Process: cell cycle arrest; cell proliferation; G1/S transition of mitotic cell cycle; G2/M transition of mitotic cell cycle; mRNA capping; nucleotide-excision repair, preincision complex assembly; positive regulation of transcription from RNA polymerase II promoter; regulation of cyclin-dependent protein kinase activity; RNA elongation from RNA polymerase I promoter; RNA elongation from RNA polymerase II promoter; snRNA transcription from RNA polymerase II promoter; termination of RNA polymerase I transcription; transcription from RNA polymerase II promoter; transcription initiation from RNA polymerase I promoter; transcription initiation from RNA polymerase II promoter; transcription-coupled nucleotide-excision repair
Reference #:  P50613 (UniProtKB)
Alt. Names/Synonyms: 39 kDa protein kinase; CAK; CAK1; CDK-activating kinase; CDK7; CDKN7; Cell division protein kinase 7; cyclin-dependent kinase 7; cyclin-dependent kinase 7 (MO15 homolog, Xenopus laevis, cdk-activating kinase); homolog of Xenopus MO15 Cdk-activating kinase; kinase subunit of CAK; MO15; p39 Mo15; p39MO15; serine/threonine kinase stk1; serine/threonine protein kinase 1; serine/threonine protein kinase MO15; STK1; TFIIH basal transcription factor complex kinase subunit
Gene Symbols: CDK7
Molecular weight: 39,038 Da
Basal Isoelectric point: 8.66  Predict pI for various phosphorylation states
CST Pathways:  G2/M DNA Damage Checkpoint  |  Protein Acetylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CDK7

Protein Structure Not Found.
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Substrate Sequence Logo
Sequence Logo

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Sites Implicated In
cell cycle regulation: S164‑p
transcription, altered: S164‑p, T170‑p
enzymatic activity, induced: T170‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 3 S7‑p _MALDVKsRAKRYEK
0 1 T110‑p KDNSLVLtPSHIKAY
0 1 K139‑ub WILHRDLkPNNLLLD
0 1 K160‑ub LADFGLAksFGsPNR
1 6 S161‑p ADFGLAksFGsPNRA
3 58 S164‑p GLAksFGsPNRAytH
0 4 Y169‑p FGsPNRAytHQVVtR
5 140 T170‑p GsPNRAytHQVVtRW
0 1 T175‑p AytHQVVtRWYRAPE
0 1 S217‑p VPFLPGDsDLDQLTR
0 1 T287‑p PCARITAtQALkMKY
0 1 K291‑ub ITAtQALkMKYFSNR
0 6 S321‑p VETLKEQsNPALAIk
0 1 K328‑ub sNPALAIkRKRtEAL
0 1 T332‑p LAIkRKRtEALEQGG
  mouse

 
S7 _MAVDVKSRAKRYEK
T110 KDNSLVLTPSHIKAY
K139 WILHRDLKPNNLLLD
K160 LADFGLAKsFGsPNR
S161‑p ADFGLAKsFGsPNRA
S164‑p GLAKsFGsPNRAytH
Y169‑p FGsPNRAytHQVVTR
T170‑p GsPNRAytHQVVTRW
T175 AytHQVVTRWYRAPE
S217 VPFLPGDSDLDQLTR
S287 PCTRTTASQALKTKY
K291 TTASQALKTKYFSNR
A321 VEALKEPANPTVATK
K328 ANPTVATKRKRAEAL
A332 VATKRKRAEALEQGI
  rat

 
- gap
T102 KDNSLVLTPSHIKAY
K131 WILHRDLKPNNLLLD
K152 LADFGLAKSFGsPNW
S153 ADFGLAKSFGsPNWA
S156‑p GLAKSFGsPNWAYtH
Y161 FGsPNWAYtHQVVTR
T162‑p GsPNWAYtHQVVTRW
T167 AYtHQVVTRWYRAPE
S209 VPFLPGDSDLDQLTR
S279 PCTRITASQALRTKY
R283 ITASQALRTKYFSNR
S313 VEALKEQSNPAMATK
K320 SNPAMATKRKRAEAL
A324 MATKRKRAEALEQ__
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