| + |
AKT2 | down-regulates activity 
phosphorylation
|
RALGAPA2 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269797 |
Ser486 |
SSWGRTYsFTSAMSR |
Mus musculus |
|
| pmid |
sentence |
| 21148297 |
RGC2 is an endogenous substrate for Akt2 downstream of PI 3-kinase. kt2 directly phosphorylated all three sites on RGC2 (Figure 5A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269798 |
Ser696 |
TTVGRSFsLSWRSHP |
Mus musculus |
|
| pmid |
sentence |
| 21148297 |
RGC2 is an endogenous substrate for Akt2 downstream of PI 3-kinase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269799 |
Thr715 |
PMRFRSAtTSGAPGV |
Mus musculus |
|
| pmid |
sentence |
| 21148297 |
RGC2 is an endogenous substrate for Akt2 downstream of PI 3-kinase |
|
| Publications: |
3 |
Organism: |
Mus Musculus |
| + |
RALGAPA2 | form complex 
binding
|
RalGAP2 |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269793 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 21148297 |
Here we report the identification and characterization of a Ral GAP complex (RGC) that mediates the activation of RalA downstream of the PI 3-kinase/Akt pathway. The complex is composed of an RGC1 regulatory subunit and an RGC2 catalytic subunit (previously identified as AS250) that directly stimulates the guanosine triphosphate hydrolysis of RalA. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
RALGAPA2
- 
- 