| + |
CDK19 |
phosphorylation
|
PAK1 |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185000 |
Ser174 |
TPAVPPVsEDEDDDD |
Homo sapiens |
|
| pmid |
sentence |
| 19520772 |
Here, we identified p21 activated kinase 1 (pak1) as a new cdk11(p58) substrate and we mapped a new phosphorylation site of ser174 on pak1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK19 | down-regulates quantity by destabilization 
phosphorylation
|
NOTCH1 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273136 |
Ser2513 |
EHPFLTPsPESPDQW |
in vitro |
|
| pmid |
sentence |
| 25344755 |
Mapping of cyclin C-dependent phosphosites on ICN1, using mass spectrometry revealed that several of them are located within the PEST-domain of Notch1, which controls ICN1 degradation38,39 (Fig. 5g and Supplementary Table 1). Three of them (T2512, S2514 and S2517) are localized within the consensus motif, “Cdc4 phosphodegron”, which is shared by most substrates of Fbw7 (Cdc4) ubiquitin ligase38. Two of these residues (S2514 and S2517) were previously shown by Fryer et al.20 to be phosphorylated by cyclin C-CDK8 in vitro, and all three were shown to play a role in controlling ICN1 stability via Fbw740. We verified that cyclin C-CDK8, C-CDK19 and C-CDK3 phosphorylate ICN1 on these three residues |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273135 |
Ser2516 |
FLTPSPEsPDQWSSS |
in vitro |
|
| pmid |
sentence |
| 25344755 |
Mapping of cyclin C-dependent phosphosites on ICN1, using mass spectrometry revealed that several of them are located within the PEST-domain of Notch1, which controls ICN1 degradation38,39 (Fig. 5g and Supplementary Table 1). Three of them (T2512, S2514 and S2517) are localized within the consensus motif, “Cdc4 phosphodegron”, which is shared by most substrates of Fbw7 (Cdc4) ubiquitin ligase38. Two of these residues (S2514 and S2517) were previously shown by Fryer et al.20 to be phosphorylated by cyclin C-CDK8 in vitro, and all three were shown to play a role in controlling ICN1 stability via Fbw740. We verified that cyclin C-CDK8, C-CDK19 and C-CDK3 phosphorylate ICN1 on these three residues |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273137 |
Thr2511 |
VPEHPFLtPSPESPD |
in vitro |
|
| pmid |
sentence |
| 25344755 |
Mapping of cyclin C-dependent phosphosites on ICN1, using mass spectrometry revealed that several of them are located within the PEST-domain of Notch1, which controls ICN1 degradation38,39 (Fig. 5g and Supplementary Table 1). Three of them (T2512, S2514 and S2517) are localized within the consensus motif, “Cdc4 phosphodegron”, which is shared by most substrates of Fbw7 (Cdc4) ubiquitin ligase38. Two of these residues (S2514 and S2517) were previously shown by Fryer et al.20 to be phosphorylated by cyclin C-CDK8 in vitro, and all three were shown to play a role in controlling ICN1 stability via Fbw740. We verified that cyclin C-CDK8, C-CDK19 and C-CDK3 phosphorylate ICN1 on these three residues |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CDK19 | form complex 
binding
|
CyclinC/CDK19 |
0.911 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273155 |
|
|
Homo sapiens |
MOLT-16 Cell |
| pmid |
sentence |
| 25344755 |
We found that in MOLT-16 cells cyclin C physically interacts with CDK19 (Fig. 5a) and activates its kinase activity (Fig. 5e and Supplementary Fig. 4f,g). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDK19
- 
- 