| + |
CDK7 | up-regulates 
phosphorylation
|
ESR1 |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81170 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 10949034 |
Activation of estrogen receptor alpha by s118 phosphorylation involves a ligand-dependent interaction with tfiih and participation of cdk7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates quantity by stabilization
phosphorylation
|
POU5F1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264404 |
Ser12 |
LASDFAFsPPPGGGG |
Homo sapiens |
Embryonic Stem Cell |
| pmid |
sentence |
| 31306665 |
Here, we combined molecular and cellular biology with CRISPR/Cas9-mediated genome engineering to pinpoint the function of serine 12 of OCT4 in ESCs. Using chemical inhibitors and an antibody specific to OCT4 phosphorylated on S12, we identified cyclin-dependent kinase (CDK) 7 as upstream kinase. |Phosphorylation of OCT4 on S12 has been previously implicated to stabilize OCT4 by binding to PIN1, thereby preventing ubiquitinylation by WWP2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates activity
phosphorylation
|
MCM2 |
0.298 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259850 |
Ser139 |
RRGLLYDsDEEDEER |
Homo sapiens |
|
| pmid |
sentence |
| 16899510 |
Taken together, these results indicate that Cdc7/Dbf4 phosphorylation of MCM2 is essential for the initiation of DNA replication in mammalian cells. | Because MCM2 was phosphorylated in vivo at Ser27, Ser41, and Ser139, which were phosphorylated by Cdc7/Dbf4 in vitro, the results suggested that Ser27, Ser41, and Ser139 are in vivo Cdc7/Dbf4 phosphorylation sites in MCM2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259848 |
Ser27 |
GNDPLTSsPGRSSRR |
Homo sapiens |
|
| pmid |
sentence |
| 16899510 |
Taken together, these results indicate that Cdc7/Dbf4 phosphorylation of MCM2 is essential for the initiation of DNA replication in mammalian cells. | Because MCM2 was phosphorylated in vivo at Ser27, Ser41, and Ser139, which were phosphorylated by Cdc7/Dbf4 in vitro, the results suggested that Ser27, Ser41, and Ser139 are in vivo Cdc7/Dbf4 phosphorylation sites in MCM2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259849 |
Ser41 |
RTDALTSsPGRDLPP |
Homo sapiens |
|
| pmid |
sentence |
| 16899510 |
Taken together, these results indicate that Cdc7/Dbf4 phosphorylation of MCM2 is essential for the initiation of DNA replication in mammalian cells. | Because MCM2 was phosphorylated in vivo at Ser27, Ser41, and Ser139, which were phosphorylated by Cdc7/Dbf4 in vitro, the results suggested that Ser27, Ser41, and Ser139 are in vivo Cdc7/Dbf4 phosphorylation sites in MCM2. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates activity
phosphorylation
|
CDK5 |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278923 |
Ser159 |
GIPVRCYsAEVVTLW |
Homo sapiens |
|
| pmid |
sentence |
| 14586172 |
In addition, the Cdk7 substrate, CTD of RNAPII, causes a dose-dependent decline in Cdk5 activation by Cdk7.|Likewise, Cdk7 or cyclin H immunoprecipitate from mouse brain specifically phosphorylates wt Cdk5 at Ser159 and enhances Cdk5 and p25 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | down-regulates 
phosphorylation
|
POLR2A |
0.787 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119992 |
Ser1619 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119996 |
Ser1626 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120000 |
Ser1647 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120004 |
Ser1654 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120008 |
Ser1668 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120012 |
Ser1675 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120016 |
Ser1696 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120020 |
Ser1717 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120024 |
Ser1724 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120028 |
Ser1738 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120032 |
Ser1766 |
SPSYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120036 |
Ser1787 |
SPNYSPTsPSYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120040 |
Ser1864 |
SPKYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120044 |
Ser1871 |
SPKYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120048 |
Ser1882 |
SPTSPTYsPTTPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120052 |
Ser1892 |
TPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120056 |
Ser1899 |
SPTYSPTsPVYTPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120060 |
Ser1913 |
SPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120064 |
Ser1920 |
SPTYSPTsPKYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120068 |
Ser1927 |
SPKYSPTsPTYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120072 |
Ser1934 |
SPTYSPTsPKGSTYS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120076 |
Ser1944 |
GSTYSPTsPGYSPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120080 |
Ser1951 |
SPGYSPTsPTYSLTS |
Homo sapiens |
|
| pmid |
sentence |
| 14662762 |
Although there is some inconsistency in the literature, it is generally thought that cdk7, a component of the transcription factor (tf) iih, is a major ser-5 kinase, whereas cdk9, a component of positive transcription elongation factor (p-tef) b, is a major ser-2 kinase within cells. These results suggest that subsequent to h2o2 treatment, the ser-5-phosphorylated form, but not the ser-2-phosphorylated form or the unphosphorylated form, is targeted for rapid proteasomal degradation through its ubiquitination. |
|
| Publications: |
23 |
Organism: |
Homo Sapiens |
| + |
CDK2 |
phosphorylation
|
CDK7 |
0.572 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84832 |
Ser164 |
GLAKSFGsPNRAYTH |
Homo sapiens |
|
| pmid |
sentence |
| 11113184 |
Cdk2 phosphorylates serine-164 in the cdk7 t loop. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinA2/CDK2 | up-regulates activity
phosphorylation
|
CDK7 |
0.644 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270807 |
Ser164 |
GLAKSFGsPNRAYTH |
in vitro |
|
| pmid |
sentence |
| 11113184 |
Activating phosphorylation of CDK7 by CDC2 and CDK2. The ability of pure CDK2-cyclin A to activate CDK7 in T170-dependent fashion (Fig. (Fig.3C,3C, lane 2) strongly suggested a direct phosphorylation mechanism. Tryptic phosphopeptide mapping confirmed that both CDK2-cyclin A (Fig. (Fig.4A)4A) and CDC2-cyclin B (Fig. (Fig.4D)4D) phosphorylated CDK7 on both S164 and T170. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270806 |
Thr170 |
GSPNRAYtHQVVTRW |
in vitro |
|
| pmid |
sentence |
| 11113184 |
Activating phosphorylation of CDK7 by CDC2 and CDK2. The ability of pure CDK2-cyclin A to activate CDK7 in T170-dependent fashion (Fig. (Fig.3C,3C, lane 2) strongly suggested a direct phosphorylation mechanism. Tryptic phosphopeptide mapping confirmed that both CDK2-cyclin A (Fig. (Fig.4A)4A) and CDC2-cyclin B (Fig. (Fig.4D)4D) phosphorylated CDK7 on both S164 and T170. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CDK7 | up-regulates
phosphorylation
|
NR5A1 |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157952 |
Ser203 |
EYPEPYAsPPQPGLP |
Homo sapiens |
|
| pmid |
sentence |
| 17901130 |
In conclusion, our results indicate that cdk7, as part of the cak complex and tfiih, phosphorylates sf1 at s203 followed by increased transcriptional activity of sf1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 |
phosphorylation
|
PCGF6 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250769 |
Ser30 |
LPPPPPVsPPALTPA |
in vitro |
|
| pmid |
sentence |
| 12167161 |
In addition, we find that serine 32 of MBLR is specifically phosphorylated during mitosis, most likely by CDK7, a component of the basal transcriptional machinery. | These results indicate that, at least in vitro, MBLR is a substrate for CDK7 phosphorylation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CDK7 |
phosphorylation
|
TP53 |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-53311 |
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 |
| + |
CDK7 | up-regulates
phosphorylation
|
TP53 |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-51280 |
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-51284 |
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-51288 |
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-51292 |
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 |
| + |
CDK7 | down-regulates
phosphorylation
|
E2F1 |
0.497 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-69776 |
Ser403 |
PEEFISLsPPHEALD |
Homo sapiens |
|
| pmid |
sentence |
| 10428966 |
These results suggest that tfiih-mediated phosphorylation of e2f-1 plays a role in triggering e2f-1 degradation during s phase. here we show that the e2f-1 activation domain interacts with a kinase activity which phosphorylates two sites, ser403 and thr433, within the activation domain. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-69780 |
Thr433 |
DCDFGDLtPLDF |
Homo sapiens |
|
| pmid |
sentence |
| 10428966 |
These results suggest that tfiih-mediated phosphorylation of e2f-1 plays a role in triggering e2f-1 degradation during s phase. here we show that the e2f-1 activation domain interacts with a kinase activity which phosphorylates two sites, ser403 and thr433, within the activation domain. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK7 | down-regulates
phosphorylation
|
AR |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170599 |
Ser516 |
VSRVPYPsPTCVKSE |
Homo sapiens |
|
| pmid |
sentence |
| 21157430 |
Here, we show that the transcription factor tfiih, via its cdk7 kinase, phosphorylates the androgen receptor (ar) at position ar/s515. Strikingly, this phosphorylation is a key step for an accurate transactivation that includes the cyclic recruitment of the transcription machinery, the mdm2 e3 ligase, the subsequent ubiquitination of ar at the promoter of target genes and its degradation by the proteasome machinery |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates
phosphorylation
|
RARA |
0.544 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-49693 |
Ser77 |
EIVPSPPsPPPLPRI |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9230306 |
However, only the coexpression of cdk7 stimulated ser-77 phosphorylation in vivo and enhanced transactivation by rar alpha, but not by a s77a rar mutant. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 |
phosphorylation
|
RARA |
0.544 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-116582 |
Ser77 |
EIVPSPPsPPPLPRI |
Homo sapiens |
|
| pmid |
sentence |
| 11955452 |
Thus, we demonstrate that the cdk7 kinase of tfiih phosphorylates the nuclear receptor, then allowing ligand-dependent control of the activation of the hormone-responsive genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates activity
phosphorylation
|
RARG |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259853 |
Ser77 |
SEEMVPSsPSPPPPP |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 10748061 |
RARg Is Phosphorylated by cdk7 in Its B and F Regions | Mutation into alanine of Ser-77 and Ser-79 located in the A/B region reduced the transcriptional activity of hRARg1 (Fig. 9A), confirming that these phosphorylation sites are required for optimal transcription. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277896 |
Ser79 |
EMVPSSPsPPPPPRV |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 10748061 |
That phosphorylation of serines 77 and 79 by cdk7 could be responsible for efficient transcription was further supported by the observation that overexpressed cdk7 significantly enhanced transcription by hRARγ1WT but not by hRARγ1S77A/S79A (Fig. 9 B). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259852 |
Ser79 |
EMVPSSPsPPPPPRV |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 10748061 |
RARg Is Phosphorylated by cdk7 in Its B and F Regions | Mutation into alanine of Ser-77 and Ser-79 located in the A/B region reduced the transcriptional activity of hRARg1 (Fig. 9A), confirming that these phosphorylation sites are required for optimal transcription. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277897 |
Ser79 |
EMVPSSPsPPPPPRV |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 10748061 |
That phosphorylation of serines 77 and 79 by cdk7 could be responsible for efficient transcription was further supported by the observation that overexpressed cdk7 significantly enhanced transcription by hRARγ1WT but not by hRARγ1S77A/S79A (Fig. 9 B). |
|
| Publications: |
4 |
Organism: |
Chlorocebus Aethiops |
| + |
CDK7 | down-regulates quantity by destabilization
phosphorylation
|
ERCC3 |
0.896 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277433 |
Ser90 |
HIFLEAFsPVYKYAQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 30762924 |
These results led us to propose a model that spironolactone may trigger the phosphorylation of XPB at Ser90 by CDK7, which promotes the recognition and polyubiquitination of XPB by SCFFBXL18 for proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates activity
phosphorylation
|
CDK2 |
0.572 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250768 |
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 |
| + |
CDK7 | up-regulates
phosphorylation
|
CDK1 |
0.581 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-38307 |
Thr161 |
GIPIRVYtHEVVTLW |
Homo sapiens |
|
| pmid |
sentence |
| 8344251 |
The mo15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (cdks) through phosphorylation of thr161 and its homologues |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCI | up-regulates activity
phosphorylation
|
CDK7 |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280088 |
Thr170 |
GSPNRAYtHQVVTRW |
Homo sapiens |
|
| pmid |
sentence |
| 31784510 |
PKC\u03b9 activates CDK7 to promote glucose consumption.|PKC\u03b9 phosphorylates Thr170 on CDK7 in vitro, can associate with CDK7 in cells, and is activated downstream of PI3K signaling xref , xref \u2013 xref . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK2 | up-regulates
phosphorylation
|
CDK7 |
0.572 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85013 |
Thr170 |
GSPNRAYtHQVVTRW |
Homo sapiens |
|
| pmid |
sentence |
| 11113184 |
Threonine-170 of cdk7 is phosphorylated in vitro by cdk2. Full activation of cdk7 requires phorylation of a conserved threonine residue at position 170 in its own t loop. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates
phosphorylation
|
CDK4 |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36549 |
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 |
| + |
CDK7 | up-regulates activity
phosphorylation
|
CDK9 |
0.549 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279455 |
Thr186 |
NSQPNRYtNRVVTLW |
Homo sapiens |
|
| pmid |
sentence |
| 23064645 |
Cdk7 activates Cdk9 in vitro .|Cdk7 phosphorylates wild-type Cdk9 on Thr186, resulting in increased activity towards a recombinant GST-Spt5 substrate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates activity
phosphorylation
|
XRN2 |
0.247 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259851 |
Thr439 |
FTPSGILtPHALGSR |
Homo sapiens |
|
| pmid |
sentence |
| 26728557 |
CDKs and Xrn2 phosphorylation promote transcription termination. | Cdk7 phosphorylated Xrn2-Thr439 but was less efficient than Cdk9. | |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates activity
phosphorylation
|
CDK11B |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245871 |
Thr595 |
GSPLKAYtPVVVTLW |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 16327805 |
We conclude that CDK7 phsphorylates Cdk11, dependent on the conserved Thr219 residue in the CDK11 T loop, and it is therefore likely to be a genuine Cdk11 activating kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates activity
phosphorylation
|
CDK12 |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275509 |
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 |
| + |
PHA-767491 | down-regulates
chemical inhibition
|
CDK7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206112 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | form complex 
binding
|
CAK complex |
0.959 |
| 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 |
| + |
BS-181 hydrochloride | down-regulates
chemical inhibition
|
CDK7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190783 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
alvocidib | down-regulates
chemical inhibition
|
CDK7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192446 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-[6,6-dimethyl-5-[(1-methyl-4-piperidinyl)-oxomethyl]-1,4-dihydropyrrolo[3,4-c]pyrazol-3-yl]-3-methylbutanamide | down-regulates
chemical inhibition
|
CDK7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206136 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-(5-{[(5-tert-butyl-1,3-oxazol-2-yl)methyl]sulfanyl}-1,3-thiazol-2-yl)piperidine-4-carboxamide | down-regulates
chemical inhibition
|
CDK7 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207087 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | down-regulates activity
phosphorylation
|
MBD4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279686 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31466944 |
The mechanistic basis for the phase-separation of MED1 is not well understood, and we hypothesize that this may be due to the phosphorylation of MED1 by CDK7 in response to growth stimuli or nuclear translocation of steroid hormone receptors, such as AR.|Together, we demonstrate that CDK7 inhibition selectively targets MED1 mediated, AR dependent oncogenic transcriptional amplification, thus representing a potential new approach for the treatment of CRPC. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
CDK7
- 
- 