| + |
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 |
| + |
CyclinE1/CDK3 |
phosphorylation
|
CABLES1 |
0.489 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273183 |
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 |
| + |
CDK5 |
phosphorylation
|
CABLES1 |
0.73 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112418 |
Ser313 |
RCRTLSGsPRPKNFK |
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 |
| + |
AKT1 | down-regulates activity 
phosphorylation
|
CABLES1 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276756 |
Thr309 |
APLRRCRtLSGSPRP |
in vitro |
|
| pmid |
sentence |
| 25361894 |
Here, we report that Cables1 levels are controlled by a phosphorylation and 14-3-3-dependent mechanism. Mutagenic analyses identified two residues, T44 and T150, that are specifically critical for 14-3-3 binding and that serve as substrates for phosphorylation by the cell survival kinase Akt, which by binding directly to Cables1 recruits 14-3-3 to the complex.Ectopic expression of activated Akt (AKT1) prevented Cables1-induced apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276757 |
Thr415 |
AFGARRNtIDSTSSF |
in vitro |
|
| pmid |
sentence |
| 25361894 |
Here, we report that Cables1 levels are controlled by a phosphorylation and 14-3-3-dependent mechanism. Mutagenic analyses identified two residues, T44 and T150, that are specifically critical for 14-3-3 binding and that serve as substrates for phosphorylation by the cell survival kinase Akt, which by binding directly to Cables1 recruits 14-3-3 to the complex.Ectopic expression of activated Akt (AKT1) prevented Cables1-induced apoptosis. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CABLES1 | down-regulates activity
binding
|
CDK2 |
0.472 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276759 |
|
|
in vitro |
|
| pmid |
sentence |
| 25361894 |
Our study also showed that Cables1 increases the level of p21 and decreases the level of pRb, but does not affect the other cell cycle-related proteins we studied. Induction of apoptosis by Cables1, which occurs partially through inhibiting Cdk2 activity and upregulating p21, is prevented by Akt phosphorylation and 14-3-3 binding. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
14-3-3 | down-regulates activity
binding
|
CABLES1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276758 |
|
|
in vitro |
|
| pmid |
sentence |
| 25361894 |
Here, we report that Cables1 levels are controlled by a phosphorylation and 14-3-3-dependent mechanism. Mutagenic analyses identified two residues, T44 and T150, that are specifically critical for 14-3-3 binding and that serve as substrates for phosphorylation by the cell survival kinase Akt, which by binding directly to Cables1 recruits 14-3-3 to the complex.Ectopic expression of activated Akt (AKT1) prevented Cables1-induced apoptosis. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
CABLES1
- 
- 