| + |
CDK1 | up-regulates activity 
phosphorylation
|
TOB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273591 |
Ser254 |
PAPQSQLsPNAKEFV |
in vitro |
|
| pmid |
sentence |
| 32404348 |
Taken together, these observations strongly support the notion that several different CDK-cyclin complexes are involved in the phosphorylation of Tob2 at S254.A more detailed regulatory context of Tob2 phosphorylation at S254 is provided by our findings from mass-spec and in vitro kinase analyses that suggest connections to PP2B and PP2C phosphatases and CDK-cyclin complexes, particularly CDK1, CDK2, and CDK4 (Table 1; Supplemental Table S2).One possibility is that the phosphorylation of S254 helps stabilize the interaction of Tob2 with the Ccr4–Not complex, which could contribute to Tob2's ability to recruit the entire Ccr4–Not complex and thus further enhances deadenylation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CDK4 | up-regulates activity
phosphorylation
|
TOB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273602 |
Ser254 |
PAPQSQLsPNAKEFV |
in vitro |
|
| pmid |
sentence |
| 32404348 |
Taken together, these observations strongly support the notion that several different CDK-cyclin complexes are involved in the phosphorylation of Tob2 at S254.A more detailed regulatory context of Tob2 phosphorylation at S254 is provided by our findings from mass-spec and in vitro kinase analyses that suggest connections to PP2B and PP2C phosphatases and CDK-cyclin complexes, particularly CDK1, CDK2, and CDK4 (Table 1; Supplemental Table S2).One possibility is that the phosphorylation of S254 helps stabilize the interaction of Tob2 with the Ccr4–Not complex, which could contribute to Tob2's ability to recruit the entire Ccr4–Not complex and thus further enhances deadenylation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CDK2 | up-regulates activity
phosphorylation
|
TOB2 |
0.25 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273601 |
Ser254 |
PAPQSQLsPNAKEFV |
in vitro |
|
| pmid |
sentence |
| 32404348 |
Taken together, these observations strongly support the notion that several different CDK-cyclin complexes are involved in the phosphorylation of Tob2 at S254.A more detailed regulatory context of Tob2 phosphorylation at S254 is provided by our findings from mass-spec and in vitro kinase analyses that suggest connections to PP2B and PP2C phosphatases and CDK-cyclin complexes, particularly CDK1, CDK2, and CDK4 (Table 1; Supplemental Table S2).One possibility is that the phosphorylation of S254 helps stabilize the interaction of Tob2 with the Ccr4–Not complex, which could contribute to Tob2's ability to recruit the entire Ccr4–Not complex and thus further enhances deadenylation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
TOB2 | down-regulates activity 
binding
|
CCR4-NOT complex |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273615 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18377426 |
We found that Tob associates with the CCR4-NOT complex. The carboxyl-terminal half of Tob interacted with Cnot1, a core protein of the CCR4-NOT complex. We further showed that the deadenylase activity associated with the complex was suppressed in vitro by Tob. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
TOB2
- 
- 