| + |
CAK complex |
phosphorylation
|
TP53 |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269326 |
Ser33 |
LPENNVLsPLPSQAM |
Homo sapiens |
|
| pmid |
sentence |
| 9372954 |
We have mapped a major site of phosphorylation by cak to ser-33 of p53 and have demonstrated as well that p53 is phosphorylated at this site in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAK complex | up-regulates 
phosphorylation
|
TP53 |
0.446 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269327 |
Ser371 |
AHSSHLKsKKGQSTS |
Homo sapiens |
|
| pmid |
sentence |
| 9315650 |
The cdk7-cych-p36 complex of transcription factor iih phosphorylates p53, enhancing its sequence-specific dna binding activity in vitro. serines 371, 376, 378, and 392 may be the potential sites for this kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269328 |
Ser376 |
LKSKKGQsTSRHKKL |
Homo sapiens |
|
| pmid |
sentence |
| 9315650 |
The cdk7-cych-p36 complex of transcription factor iih phosphorylates p53, enhancing its sequence-specific dna binding activity in vitro. serines 371, 376, 378, and 392 may be the potential sites for this kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269325 |
Ser378 |
SKKGQSTsRHKKLMF |
Homo sapiens |
|
| pmid |
sentence |
| 9315650 |
The cdk7-cych-p36 complex of transcription factor iih phosphorylates p53, enhancing its sequence-specific dna binding activity in vitro. serines 371, 376, 378, and 392 may be the potential sites for this kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269324 |
Ser392 |
FKTEGPDsD |
Homo sapiens |
|
| pmid |
sentence |
| 9315650 |
The cdk7-cych-p36 complex of transcription factor iih phosphorylates p53, enhancing its sequence-specific dna binding activity in vitro. serines 371, 376, 378, and 392 may be the potential sites for this kinase. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CAK complex | up-regulates activity
phosphorylation
|
RARG |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275969 |
Ser77 |
SEEMVPSsPSPPPPP |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 10748061 |
Retinoic acid receptor gamma (RARgamma) is phosphorylated in COS-1 cells at two conserved serine residues located in the N-terminal region (serines 77 and 79 in RARgamma1 and serines 66 and 68 in RARgamma2) that contains the activation function AF-1. These serines are phosphorylated in vitro by cdk7, a cyclin-dependent kinase associated to cyclin H and MAT1 in the CAK complex (cdk7.cyclin H. MAT1), that is found either free or as a component of the transcription/DNA repair factor TFIIH. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275968 |
Ser79 |
EMVPSSPsPPPPPRV |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 10748061 |
Retinoic acid receptor gamma (RARgamma) is phosphorylated in COS-1 cells at two conserved serine residues located in the N-terminal region (serines 77 and 79 in RARgamma1 and serines 66 and 68 in RARgamma2) that contains the activation function AF-1. These serines are phosphorylated in vitro by cdk7, a cyclin-dependent kinase associated to cyclin H and MAT1 in the CAK complex (cdk7.cyclin H. MAT1), that is found either free or as a component of the transcription/DNA repair factor TFIIH. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
CAK complex | up-regulates activity
phosphorylation
|
CDK2 |
0.611 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269330 |
Thr160 |
GVPVRTYtHEVVTLW |
in vitro |
|
| pmid |
sentence |
| 10085115 |
Phosphorylation of monomeric human CDK2 by CAK1 is more efficient than phosphorylation of the binary CDK2-cyclin A complex. Phosphorylated CDK2 exhibits histone H1 kinase activity corresponding to approximately 0.3% of that observed with the fully activated phosphorylated CDK2-cyclin A complex. Fluorescence measurements have shown that Thr160 phosphorylation increases the affinity of CDK2 for both histone substrate and ATP and decreases its affinity for ADP. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CAK complex | up-regulates
phosphorylation
|
CDK4 |
0.56 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269329 |
Thr172 |
YSYQMALtPVVVTLW |
Homo sapiens |
|
| pmid |
sentence |
| 8139570 |
Phosphorylation of cdk4 on threonine 172 by a cdk-activating kinase (cak). therefore, formation of the cyclin d-cdk4 complex and phosphorylation of the bound catalytic subunit are independently regulated, and in addition to the requirement for cak activity, serum stimulation is required to promote assembly of the complexes in mammalian cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAK complex | up-regulates activity
phosphorylation
|
CDK12 |
0.519 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275510 |
Thr893 |
SEESRPYtNKVITLW |
|
|
| pmid |
sentence |
| 24662513 |
Although Cdk12/CycK kinase complex lacking T-loop phosphorylation showed some basal activity towards a CTD substrate prephosphorylated at position Ser7, its activity was significantly increased upon coexpression with the CAK from S. cerevisiae (Supplementary Fig. 9a). Mutation of T893 to E to mimic phosphorylation showed no effect on basal kinase activity. Quantitative phosphorylation of a single residue occurred upon coexpression with Cak1, as determined by ESI mass spectrometry (Supplementary Fig. 9b). |
|
| Publications: |
1 |
| + |
CDK7 | form complex 
binding
|
CAK complex |
0.958 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269319 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAK complex | form complex
binding
|
TFIIH |
0.85 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269318 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair.|The TFIIH core complex is composed of the seven subunits XPB, XPD, p62, p52, p44, p34, and p8, and is the form of TFIIH active in DNA repair|and additionally the CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCNH | form complex
binding
|
CAK complex |
0.96 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269321 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MNAT1 | form complex
binding
|
CAK complex |
0.946 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269320 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30860024 |
CdK activating kinase (CAK) complex, which harbors the kinase activity of CDK7 as well as the Cyclin H and MAT1 subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CAK complex
CPX-578