+ |
PPP2CB | down-regulates
dephosphorylation
|
RALA |
0.293 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155349 |
Ser183 |
RARKMEDsKEKNGKK |
Homo sapiens |
|
pmid |
sentence |
17540176 |
Pp2a abeta-containing complexes dephosphorylate rala at ser183 and ser194, inactivating rala and abolishing its transforming function |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155353 |
Ser194 |
NGKKKRKsLAKRIRE |
Homo sapiens |
|
pmid |
sentence |
17540176 |
Pp2a abeta-containing complexes dephosphorylate rala at ser183 and ser194, inactivating rala and abolishing its transforming function |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
RALA | up-regulates activity
phosphorylation
|
FOXO4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248003 |
Thr451 |
PIPKALGtPVLTPPT |
Mus musculus |
|
pmid |
sentence |
11689711 |
We conclude that Ral-mediated phosphorylation of threonines 447 and 451 is required for proper activity of AFX-WT. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249665 |
Thr455 |
ALGTPVLtPPTEAAS |
Mus musculus |
|
pmid |
sentence |
11689711 |
We conclude that Ral-mediated phosphorylation of threonines 447 and 451 is required for proper activity of AFX-WT. |
|
Publications: |
2 |
Organism: |
Mus Musculus |
+ |
RALA | up-regulates activity
phosphorylation
|
FOXO |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252984 |
Thr451 |
PIPKALGtPVLTPPT |
Mus musculus |
|
pmid |
sentence |
11689711 |
We conclude that Ral-mediated phosphorylation of threonines 447 and 451 is required for proper activity of AFX-WT. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252985 |
Thr455 |
ALGTPVLtPPTEAAS |
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
11689711 |
We conclude that Ral-mediated phosphorylation of threonines 447 and 451 is required for proper activity of AFX-WT. |
|
Publications: |
2 |
Organism: |
Mus Musculus |
+ |
RalGAP2 | down-regulates activity
guanine nucleotide exchange factor
|
RALA |
0.497 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269796 |
|
|
Mus musculus |
3T3-L1 Cell |
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. RGC2 negatively regulates RalA activity in adipocytes. When immunoprecipitated from cell lysates of 3T3-L1 adipocytes by an anti-RGC2 antibody, RGC proteins efficiently enhanced GTP hydrolysis of recombinant RalA in vitro, compared with RalA alone or RalA incubated with various control immunoprecipitates (Figure 2C). |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
RalGAP1 | down-regulates activity
guanine nucleotide exchange factor
|
RALA |
0.43 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269795 |
|
|
Mus musculus |
3T3-L1 Cell |
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 |