| + |
CDK9 | up-regulates 
phosphorylation
|
POLR2A |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203508 |
Ser1616 |
TPQSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203512 |
Ser1623 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203516 |
Ser1644 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203520 |
Ser1651 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203524 |
Ser1665 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203528 |
Ser1672 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203532 |
Ser1693 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203536 |
Ser1714 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203540 |
Ser1721 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203544 |
Ser1735 |
SPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203552 |
Ser1763 |
TPTSPSYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203556 |
Ser1784 |
TPTSPNYsPTSPSYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203560 |
Ser1861 |
TPTSPKYsPTSPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203564 |
Ser1868 |
SPTSPKYsPTSPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203568 |
Ser1875 |
SPTSPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203576 |
Ser1882 |
SPTSPTYsPTTPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203580 |
Ser1889 |
SPTTPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203584 |
Ser1896 |
SPTSPTYsPTSPVYT |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203588 |
Ser1910 |
TPTSPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203592 |
Ser1917 |
SPTSPTYsPTSPKYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself. Cellular kinase cdk9 phosphorylates serine-2 in the c-terminal domain (ctd) of rnap ii |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203596 |
Ser1924 |
SPTSPKYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203600 |
Ser1931 |
SPTSPTYsPTSPKGS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203604 |
Ser1941 |
SPKGSTYsPTSPGYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203608 |
Ser1948 |
SPTSPGYsPTSPTYS |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Publications: |
24 |
Organism: |
Homo Sapiens |
| + |
PP1 | up-regulates
dephosphorylation
|
CDK9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264671 |
Ser175 |
FGLARAFsLAKNSQP |
Homo sapiens |
|
| pmid |
sentence |
| 21533037 |
Protein phosphatase-1 activates cdk9 by dephosphorylating ser175 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP1CC | up-regulates
dephosphorylation
|
CDK9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173450 |
Ser175 |
FGLARAFsLAKNSQP |
Homo sapiens |
|
| pmid |
sentence |
| 21533037 |
Protein phosphatase-1 activates cdk9 by dephosphorylating ser175 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173454 |
Thr186 |
NSQPNRYtNRVVTLW |
Homo sapiens |
|
| pmid |
sentence |
| 21533037 |
Pp1 is an activator of cdk9. Pp1 dephosphorylates cdk9 thr186. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK9 | down-regulates 
phosphorylation
|
SMAD1 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161565 |
Ser187 |
NSHPFPHsPNSSYPN |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161658 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
|
| pmid |
sentence |
| 19914168 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161569 |
Ser195 |
PNSSYPNsPGSSSST |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161577 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161666 |
Ser214 |
PTSSDPGsPFQMPAD |
Homo sapiens |
|
| pmid |
sentence |
| 19914168 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
CDK9 | up-regulates activity
phosphorylation
|
POLR2A |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203572 |
Ser1878 |
SPKYSPTsPTYSPTT |
Homo sapiens |
|
| pmid |
sentence |
| 24385927 |
Cyclin-dependent kinase 9 (cdk9) promotes elongation by rna polymerase ii (rnapii), mrna processing, and co-transcriptional histone modification. Cdk9 phosphorylates multiple targets, including the conserved rnapii elongation factor spt5 and rnapii itself |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK9 | down-regulates quantity by destabilization
phosphorylation
|
SMAD1 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161573 |
Ser206 |
SSSTYPHsPTSSDPG |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Phosphorylation of the linker region of smad1, a receptor-activated smad (r-smad), at serine 206 (s206) and s214 induced by bmp and mediated by cdk8/9 is critical for binding of the e3 ubiquitin ligase smurf1. Binding of smurf1 leads to polyubiquitination of smad1 and its degradation by the proteasome;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK9 | down-regulates activity
phosphorylation
|
SMAD3 |
0.607 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161581 |
Ser208 |
DAGSPNLsPNPMSPA |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Similarly, tgf-?-Induced and cdk8/9-mediated phosphorylation of smad3 at threonine 179 (t179) is important for binding of the nedd4l e3 ubiquitin ligase, which accelerates smad3 turnover;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161589 |
Thr179 |
PQSNIPEtPPPGYLS |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Similarly, tgf-?-Induced and cdk8/9-mediated phosphorylation of smad3 at threonine 179 (t179) is important for binding of the nedd4l e3 ubiquitin ligase, which accelerates smad3 turnover;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK9 | down-regulates
phosphorylation
|
RCHY1 |
0.473 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201923 |
Ser211 |
VAQTPMPsEYQNMTV |
Homo sapiens |
|
| pmid |
sentence |
| 23603988 |
We showed that cdk9 phosphorylates pirh2 on ser-211 and thr-217 residues through their physical interaction. Phosphorylation of pirh2 renders it inactive and may contribute to p53-inhibition of transcriptional elongation of the hiv-1 ltr. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201927 |
Thr217 |
PSEYQNMtVDILCND |
Homo sapiens |
|
| pmid |
sentence |
| 23603988 |
We showed that cdk9 phosphorylates pirh2 on ser-211 and thr-217 residues through their physical interaction. Phosphorylation of pirh2 renders it inactive and may contribute to p53-inhibition of transcriptional elongation of the hiv-1 ltr. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK9 | down-regulates
phosphorylation
|
SMAD3 |
0.607 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161585 |
Ser213 |
NLSPNPMsPAHNNLD |
Homo sapiens |
|
| pmid |
sentence |
| 19914161 |
Similarly, tgf-?-Induced and cdk8/9-mediated phosphorylation of smad3 at threonine 179 (t179) is important for binding of the nedd4l e3 ubiquitin ligase, which accelerates smad3 turnover;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161678 |
Ser213 |
NLSPNPMsPAHNNLD |
Homo sapiens |
|
| pmid |
sentence |
| 19914168 |
Similarly, tgf-?-Induced and cdk8/9-mediated phosphorylation of smad3 at threonine 179 (t179) is important for binding of the nedd4l e3 ubiquitin ligase, which accelerates smad3 turnover;cdk8 and cyclint-cdk9 showed a preference for s206 and s214 but also phosphorylated s186 and s195 in the case of smad1;and t179, s208 and s213 in the case of smad3. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK9 | up-regulates activity
phosphorylation
|
TP53 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145311 |
Ser315 |
LPNNTSSsPQPKKKP |
Homo sapiens |
|
| pmid |
sentence |
| 24173284 |
The N-terminus of E2F1 can interact directly with a region towards the C-terminus of p53, resulting in increased nuclear retention of p53 and p53-mediated transcription and apoptosis. This is inhibited by competition between p53 and cyclin A at the binding site within E2F19,10. The interaction between p53 and E2F1 is enhanced by phosphorylation of p53 on Ser315, a residue within the E2F1 binding region that is phosphorylated by cell cycle kinases such as cdk1, cdk2, cdk9 and Aurora kinase A |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK9 |
phosphorylation
|
TP53 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145315 |
Ser33 |
LPENNVLsPLPSQAM |
Homo sapiens |
|
| pmid |
sentence |
| 16552184 |
Here, we report for the first time that cyclin dependent kinase 9, whose well-known substrate is rna polymerase ii, can also phosphorylate p53. Specifically, ser33 on the n-terminus and, ser315 and ser392 on the c-terminus of p53 were found to be phosphorylated. The precise biological role of this phosphorylation remains to be elucidated. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK9 | up-regulates quantity by stabilization
phosphorylation
|
TP53 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201931 |
Ser392 |
FKTEGPDsD |
Homo sapiens |
|
| pmid |
sentence |
| 23603988 |
We recently demonstrated that through their physical interaction, cdk9 phosphorylates p53 on ser-392, leading to p53 stability and accumulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK9 | up-regulates
phosphorylation
|
TP53 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201935 |
Ser392 |
FKTEGPDsD |
Homo sapiens |
|
| pmid |
sentence |
| 23603988 |
We recently demonstrated that through their physical interaction, cdk9 phosphorylates p53 on ser-392, leading to p53 stability and accumulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK9 | up-regulates activity
phosphorylation
|
NCOA2 |
0.248 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256096 |
Ser469 |
NYALKMNsPSQSSPG |
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 29170386 |
Interestingly, GRIP1 is phosphorylated at an N-terminal serine cluster by cyclin-dependent kinase-9 (CDK9), which is recruited into GC-induced GR:GRIP1:CDK9 hetero-complexes, producing distinct GRE-specific GRIP1 phospho-isoforms. Phosphorylation potentiates GRIP1 coactivator but, remarkably, not its corepressor properties. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256097 |
Ser487 |
GQPTSMLsPRHRMSP |
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 29170386 |
Interestingly, GRIP1 is phosphorylated at an N-terminal serine cluster by cyclin-dependent kinase-9 (CDK9), which is recruited into GC-induced GR:GRIP1:CDK9 hetero-complexes, producing distinct GRE-specific GRIP1 phospho-isoforms. Phosphorylation potentiates GRIP1 coactivator but, remarkably, not its corepressor properties. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256098 |
Ser493 |
LSPRHRMsSPGVAGS |
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 29170386 |
Interestingly, GRIP1 is phosphorylated at an N-terminal serine cluster by cyclin-dependent kinase-9 (CDK9), which is recruited into GC-induced GR:GRIP1:CDK9 hetero-complexes, producing distinct GRE-specific GRIP1 phospho-isoforms. Phosphorylation potentiates GRIP1 coactivator but, remarkably, not its corepressor properties. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256099 |
Ser499 |
MSPGVAGsPRIPPSQ |
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 29170386 |
Interestingly, GRIP1 is phosphorylated at an N-terminal serine cluster by cyclin-dependent kinase-9 (CDK9), which is recruited into GC-induced GR:GRIP1:CDK9 hetero-complexes, producing distinct GRE-specific GRIP1 phospho-isoforms. Phosphorylation potentiates GRIP1 coactivator but, remarkably, not its corepressor properties. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PPM1A | down-regulates activity
dephosphorylation
|
CDK9 |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248490 |
Thr186 |
NSQPNRYtNRVVTLW |
Homo sapiens |
|
| pmid |
sentence |
| 18829461 |
Taken together, our data indicate that PPM1A and to some extent PPM1B are important negative regulators of P-TEFb function |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPM1B |
dephosphorylation
|
CDK9 |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181396 |
Thr186 |
NSQPNRYtNRVVTLW |
Homo sapiens |
|
| pmid |
sentence |
| 18829461 |
Taken together, our data indicate that PPM1A and to some extent PPM1B are important negative regulators of P-TEFb function |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK9 | up-regulates activity
phosphorylation
|
XRN2 |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277194 |
Thr439 |
FTPSGILtPHALGSR |
in vitro |
|
| pmid |
sentence |
| 26728557 |
Among the RNA processing factors phosphorylated by Cdk9 was the 5'-to-3' "torpedo" exoribonuclease Xrn2, required in transcription termination by Pol II, which we validated as a bona fide P-TEFb substrate in vivo and in vitro. Phosphorylation by Cdk9 or phosphomimetic substitution of its target residue, Thr439, enhanced enzymatic activity of Xrn2 on synthetic substrates in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CDK9 | up-regulates
phosphorylation
|
SUPT5H |
0.769 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143919 |
Thr768 |
MTSTYGRtPMYGSQT |
Homo sapiens |
|
| pmid |
sentence |
| 16427012 |
We describe an evolutionarily conserved repetitive heptapeptide motif (consensus = g-s-r/q-t-p) in the c-terminal region (ctr) of hspt5, which, like the c-terminal domain (ctd) of rna pol ii, is highly phosphorylated by p-tefb. Thr-4 residues of the ctr repeats are functionally important phosphorylation sites. In vitro, thr-4 phosphorylation is critical for the elongation activation activity of dsif |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143923 |
Thr775 |
TPMYGSQtPMYGSGS |
Homo sapiens |
|
| pmid |
sentence |
| 16427012 |
We describe an evolutionarily conserved repetitive heptapeptide motif (consensus = g-s-r/q-t-p) in the c-terminal region (ctr) of hspt5, which, like the c-terminal domain (ctd) of rna pol ii, is highly phosphorylated by p-tefb. Thr-4 residues of the ctr repeats are functionally important phosphorylation sites. In vitro, thr-4 phosphorylation is critical for the elongation activation activity of dsif |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143927 |
Thr784 |
MYGSGSRtPMYGSQT |
Homo sapiens |
|
| pmid |
sentence |
| 16427012 |
We describe an evolutionarily conserved repetitive heptapeptide motif (consensus = g-s-r/q-t-p) in the c-terminal region (ctr) of hspt5, which, like the c-terminal domain (ctd) of rna pol ii, is highly phosphorylated by p-tefb. Thr-4 residues of the ctr repeats are functionally important phosphorylation sites. In vitro, thr-4 phosphorylation is critical for the elongation activation activity of dsif |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143931 |
Thr791 |
TPMYGSQtPLQDGSR |
Homo sapiens |
|
| pmid |
sentence |
| 16427012 |
We describe an evolutionarily conserved repetitive heptapeptide motif (consensus = g-s-r/q-t-p) in the c-terminal region (ctr) of hspt5, which, like the c-terminal domain (ctd) of rna pol ii, is highly phosphorylated by p-tefb. Thr-4 residues of the ctr repeats are functionally important phosphorylation sites. In vitro, thr-4 phosphorylation is critical for the elongation activation activity of dsif |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143935 |
Thr799 |
PLQDGSRtPHYGSQT |
Homo sapiens |
|
| pmid |
sentence |
| 16427012 |
We describe an evolutionarily conserved repetitive heptapeptide motif (consensus = g-s-r/q-t-p) in the c-terminal region (ctr) of hspt5, which, like the c-terminal domain (ctd) of rna pol ii, is highly phosphorylated by p-tefb. Thr-4 residues of the ctr repeats are functionally important phosphorylation sites. In vitro, thr-4 phosphorylation is critical for the elongation activation activity of dsif |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143939 |
Thr806 |
TPHYGSQtPLHDGSR |
Homo sapiens |
|
| pmid |
sentence |
| 16427012 |
We describe an evolutionarily conserved repetitive heptapeptide motif (consensus = g-s-r/q-t-p) in the c-terminal region (ctr) of hspt5, which, like the c-terminal domain (ctd) of rna pol ii, is highly phosphorylated by p-tefb. Thr-4 residues of the ctr repeats are functionally important phosphorylation sites. In vitro, thr-4 phosphorylation is critical for the elongation activation activity of dsif |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143943 |
Thr814 |
PLHDGSRtPAQSGAW |
Homo sapiens |
|
| pmid |
sentence |
| 16427012 |
We describe an evolutionarily conserved repetitive heptapeptide motif (consensus = g-s-r/q-t-p) in the c-terminal region (ctr) of hspt5, which, like the c-terminal domain (ctd) of rna pol ii, is highly phosphorylated by p-tefb. Thr-4 residues of the ctr repeats are functionally important phosphorylation sites. In vitro, thr-4 phosphorylation is critical for the elongation activation activity of dsif |
|
| Publications: |
7 |
Organism: |
Homo Sapiens |
| + |
ALK | up-regulates activity
phosphorylation
|
CDK9 |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277607 |
Tyr19 |
FCDEVSKyEKLAKIG |
in vitro |
|
| pmid |
sentence |
| 36253486 |
We report that anaplastic lymphoma kinase (ALK) directly phosphorylates CDK9 at tyrosine-19 to promote homologous recombination (HR) repair and PARP inhibitor resistance. Phospho-CDK9-Tyr19 increases its kinase activity and nuclear localization to stabilize positive transcriptional elongation factor b and activate polymerase II-dependent transcription of HR-repair genes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CDK9 | form complex 
binding
|
P-TEFb |
0.964 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267740 |
|
|
in vitro |
|
| pmid |
sentence |
| 34955012 |
Cyclin-dependent-kinases (CDKs) are members of the serine/threonine kinase family and are highly regulated by cyclins, a family of regulatory subunits that bind to CDKs. CDK9 represents one of the most studied examples of these transcriptional CDKs. CDK9 forms a heterodimeric complex with its regulatory subunit cyclins T1, T2 and K to form the positive transcription elongation factor b (P-TEFb). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CDK9 | up-regulates quantity by expression 
transcriptional regulation
|
HES1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-130703 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15546612 |
Cycc:cdk8 and cyct1:cdk9/p-tefb are recruited with notch and associated coactivators (mam, skip) to the hes1 promoter in signaling cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
4-(2-methyl-3-propan-2-yl-4-imidazolyl)-N-(4-methylsulfonylphenyl)-2-pyrimidinamine | down-regulates
chemical inhibition
|
CDK9 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190182 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
alvocidib hydrochloride | down-regulates
chemical inhibition
|
CDK9 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192480 |
|
|
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
|
CDK9 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206139 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
alvocidib | down-regulates
chemical inhibition
|
CDK9 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192449 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
4-(2,6-dichlorobenzamido)-N-(piperidin-4-yl)-pyrazole-3-carboxamide | down-regulates activity
chemical inhibition
|
CDK9 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262217 |
|
|
in vitro |
|
| pmid |
sentence |
| 29901072 |
AT7519, a pyrazole 3-carboxyamide compound, was developed by Astex and acts as an inhibitor of CDK1, CDK2, CDK4, CDK6 and CDK9. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
Dinaciclib | down-regulates
chemical inhibition
|
CDK9 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191331 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PHA-767491 | down-regulates
chemical inhibition
|
CDK9 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206115 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-SKP2 | down-regulates quantity by destabilization
polyubiquitination
|
CDK9 |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272666 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11689688 |
Here we report that CDK9 is ubiquitinated and degraded by the proteasome whereas cyclin T1 is stable. SCF(SKP2) was recruited to CDK9/cyclin T1 via cyclin T1 in an interaction requiring its PEST domain. CDK9 ubiquitination was modulated by cyclin T1 and p45(SKP2). |
|
| 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
|
CDK9 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207090 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDK9
- 
- 