| + |
CDK3 | up-regulates activity 
phosphorylation
|
ESR1 |
0.263 |
| 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 |
0.245 |
| 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 |
phosphorylation
|
CABLES1 |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250679 |
Ser273 |
PGQGGSTsAFEQLQR |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 11733001 |
P70ik3-1 is phosphorylated by either cyclin A/cdk3 or cyclin E/cdk3 reconstituted in COS7 cells. Accordingly, we can conclude that in COS7 cells, Ser274 in p70ik3-1 is phosphorylated by endogenous kinases other than cdk5 (Fig. 4), at least one of which is cdk3 as shown in this work. Currently, however, the question of how ik3-1 function is modified by its cdk3-mediated phosphorylation of Ser274 remains to be adressed. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
CDK3 | down-regulates
phosphorylation
|
TFCP2 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184164 |
Ser309 |
SLGEGNGsPNHQPEP |
Homo sapiens |
|
| pmid |
sentence |
| 19237534 |
In vitro, lsf is phosphorylated by cyclin e/cyclin-dependent kinase 2 (cdk2), cyclin c/cdk2, and cyclin c/cdk3, predominantly on s309. Phosphorylation by cyclin c/cyclin-dependent kinase 2 following mitogenic stimulation of murine fibroblasts inhibits transcriptional activity of lsf during g1 progression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK3 | up-regulates activity
phosphorylation
|
MECOM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273431 |
Ser624 |
KMFKDKVsPLQNLAS |
|
|
| pmid |
sentence |
| 33082307 |
The motif harbouring S436 is a target of CDK2 and CDK3 kinases, which interacted with EVI1-WT. The methyltransferase DNMT3A bound preferentially to EVI1-WT compared with EVI1-S436A, and a hypomethylated cell population associated by EVI1-WT expression in murine haematopoietic progenitors is not maintained with EVI1-S436A. |
|
| Publications: |
1 |
| + |
CDK3 | up-regulates
phosphorylation
|
JUN |
0.455 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183009 |
Ser63 |
KNSDLLTsPDVGLLK |
Homo sapiens |
|
| pmid |
sentence |
| 19118012 |
Egf-induced cdk3 activation caused c-jun phosphorylation at ser63 and ser73, resulting in increased ap-1 transactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183013 |
Ser73 |
VGLLKLAsPELERLI |
Homo sapiens |
|
| pmid |
sentence |
| 19118012 |
Egf-induced cdk3 activation caused c-jun phosphorylation at ser63 and ser73, resulting in increased ap-1 transactivation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK3 | up-regulates
phosphorylation
|
ATF1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180920 |
Ser63 |
GILARRPsYRKILKD |
Homo sapiens |
Glioblastoma Cell |
| pmid |
sentence |
| 18794154 |
Cyclin-dependent kinase 3-mediated activating transcription factor 1 phosphorylation enhances cell transformationwe found that cdk3 phosphorylates activating transcription factor 1 (atf1) at serine 63 and enhances the transactivation and transcriptional activities of atf1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
CDK3 | down-regulates
phosphorylation
|
RB1 |
0.454 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124212 |
Ser811 |
IYISPLKsPYKISEG |
Homo sapiens |
|
| pmid |
sentence |
| 15084261 |
The active form of prb is underphosphorylated. Cdk3/cyclin-c-mediated phosphorylation at ser-807 and ser-811 is required for g0-g1 transition. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK3 | up-regulates
phosphorylation
|
LIN9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-204529 |
Thr96 |
KFTATMStPDKKASQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 24475316 |
In this report, we demonstrate that cyclin e1/cdk3 phosphorylates lin-9 on thr-96. Mutating thr-96 to alanine inhibits activation of cyclins a2 and b1 promoters, whereas a phosphomimetic asp mutant strongly activates their promoters and triggers accelerated entry into g2/m phase in 293t cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK3 | form complex 
binding
|
CyclinE1/CDK3 |
0.753 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273185 |
|
|
|
|
| pmid |
sentence |
| 37104883 |
Among them, CDK3 is critically important because it triggers the transitions of G0 to G1 and G1 to S phase through binding to cyclin C and cyclin E1, respectively. |
|
| Publications: |
1 |
| + |
4-(2,6-dichlorobenzamido)-N-(piperidin-4-yl)-pyrazole-3-carboxamide | down-regulates
chemical inhibition
|
CDK3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189987 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDKN1A | down-regulates
binding
|
CDK3 |
0.663 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-29954 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7626805 |
P21cip1 is a cyclin-dependent kinase (cdk) inhibitor that is transcriptionally activated by p53 in response to dna damage. We have explored the interaction of p21 with the currently known cdks. p21 effectively inhibits cdk2, cdk3, cdk4, and cdk6 kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK3 | form complex
binding
|
CyclinC/CDK3 |
0.681 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273157 |
|
|
Homo sapiens |
MOLT-16 Cell |
| pmid |
sentence |
| 25344755 |
Cyclin C was cloned as a growth-promoting G1 cyclin, and was also shown to regulate gene transcription. Here we report that in vivo cyclin C acts as a haploinsufficient tumor suppressor, by controlling Notch1 oncogene levels. Cyclin C activates an “orphan” CDK19 kinase, as well as CDK8 and CDK3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDK3
- 
- 