| + |
CDK3 | up-regulates activity 
phosphorylation
|
ESR1 |
0.258 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273189 |
Ser104 |
FPPLNSVsPSPLMLL |
|
|
| pmid |
sentence |
| 26202215 |
CDK3 was shown to be overexpressed in breast cancer and phosphorylate ERα at Ser104/116 and Ser118. Furthermore, we found that Mir-873 inhibits ER activity and cell growth via targeting CDK3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273188 |
Ser106 |
PLNSVSPsPLMLLHP |
|
|
| pmid |
sentence |
| 26202215 |
CDK3 was shown to be overexpressed in breast cancer and phosphorylate ERα at Ser104/116 and Ser118. Furthermore, we found that Mir-873 inhibits ER activity and cell growth via targeting CDK3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273187 |
Ser118 |
LHPPPQLsPFLQPHG |
|
|
| pmid |
sentence |
| 26202215 |
CDK3 was shown to be overexpressed in breast cancer and phosphorylate ERα at Ser104/116 and Ser118. Furthermore, we found that Mir-873 inhibits ER activity and cell growth via targeting CDK3 |
|
| Publications: |
3 |
| + |
CDK3 | down-regulates quantity by destabilization 
phosphorylation
|
NOTCH1 |
0.242 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273169 |
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-273168 |
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-273167 |
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 |
| + |
CDK3 | up-regulates activity
phosphorylation
|
NFATC4 |
0.366 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278511 |
Ser259 |
APGPTPAsPRPASPC |
Homo sapiens |
|
| pmid |
sentence |
| 27893713 |
CDK3 enhances the transactivation and transcription activity of NFAT3.|NFAT3 can be phosphorylated by CDK3 at Ser259, which is critical for its transactivation activity and cell transformation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK3 |
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4.0
CDK3
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