+ |
CyclinA2/CDK2 |
phosphorylation
|
CABLES1 |
0.477 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250756 |
Ser273 |
PGQGGSTsAFEQLQR |
in vitro |
|
pmid |
sentence |
11733001 |
Here, we report that Ser274 of p70ik3-1 is phosphorylated by cdk2 or cdk3 bound to cyclin A and to cyclin E in vitro. We also found that in COS7 cells in which cyclin E and cdk3 were ectopically overexpressed, the phosphorylation level of Ser274 in coexpressed p70ik3-1 is upregulated. We therefore conclude that p70ik3-1 is a substrate for cdk3-mediated phosphorylation. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CyclinE1/CDK3 |
phosphorylation
|
CABLES1 |
0.488 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273183 |
Ser273 |
PGQGGSTsAFEQLQR |
in vitro |
|
pmid |
sentence |
11733001 |
Here, we report that Ser274 of p70ik3-1 is phosphorylated by cdk2 or cdk3 bound to cyclin A and to cyclin E in vitro. We also found that in COS7 cells in which cyclin E and cdk3 were ectopically overexpressed, the phosphorylation level of Ser274 in coexpressed p70ik3-1 is upregulated. We therefore conclude that p70ik3-1 is a substrate for cdk3-mediated phosphorylation. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CDK3 |
phosphorylation
|
CABLES1 |
0.499 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250679 |
Ser273 |
PGQGGSTsAFEQLQR |
in vitro |
|
pmid |
sentence |
11733001 |
Here, we report that Ser274 of p70ik3-1 is phosphorylated by cdk2 or cdk3 bound to cyclin A and to cyclin E in vitro. We also found that in COS7 cells in which cyclin E and cdk3 were ectopically overexpressed, the phosphorylation level of Ser274 in coexpressed p70ik3-1 is upregulated. We therefore conclude that p70ik3-1 is a substrate for cdk3-mediated phosphorylation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-112418 |
Ser313 |
RCRTLSGsPRPKNFK |
Homo sapiens |
|
pmid |
sentence |
11733001 |
Here, we report that ser274 of p70ik3-1 is phosphorylated by cdk2 or cdk3 bound to cyclin a and to cyclin e in vitro. Currently, however, the question of how ik3-1 function is modified by its cdk3-mediated phosphorylation of ser274 remains to be adressed. |
|
Publications: |
2 |
Organism: |
In Vitro, Homo Sapiens |