| + |
EGFR |
phosphorylation
|
RASA1 |
0.637 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21875 |
Tyr460 |
TVDGKEIyNTIRRKT |
Homo sapiens |
|
| pmid |
sentence |
| 1850098 |
We conclude that tyr-460 is a site of gap tyrosine phosphorylation by the egf receptor in vitro and likely in vivo. Gap tyr-460 is located immediately c terminal to the second gap sh2 domain, suggesting that its phosphorylation might have a role in regulating protein-protein interactions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glioblastoma Multiforme |
| + |
RASA1 | down-regulates 
binding
|
HRAS |
0.84 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-68990 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10394594 |
The Ras protein sits at the center of a many-tiered cascade of molecular interactions. Most of the proteins along this cascade are activated by phosphorylation, but Ras uses a bound guanine nucleotide to toggle between its on and off states. Ras hydrolyzes GTP to GDP fairly quickly, turning itself off, and a collection of GTPase-activating proteins (GAPs) speed up the processthe complex between human h-ras bound to guanosine diphosphate and the guanosine triphosphatase (gtpase)-activating domain of the human gtpase-activating protein p120gap (gap-334) in the presence of aluminum fluoride was solved. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-49477 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9219684 |
The three-dimensional structure of the complex between human h-ras bound to guanosine diphosphate and the guanosine triphosphatase (gtpase)-activating domain of the human gtpase-activating protein p120gap (gap-334) in the presence of aluminum fluoride was solved at a resolution of 2.5 angstroms. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glioblastoma Multiforme |
| + |
PDGFRB | up-regulates 
binding
|
RASA1 |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-115843 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11896619 |
The gtpase activating protein (gap) of ras binds only to beta-receptors / we have previously shown that the binding site for gtpase activating protein of ras (rasgap) in the pdgf beta-receptor, tyr771, is phosphorylated to a much lower extent in the heterodimeric configuration of pdgf alpha- and beta-receptors, compared to the pdgf beta-receptor homodimer. / the decreased recruitment of the rasgap to the receptor leads to prolonged activation of the ras/map kinase pathway |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EPHB2 | up-regulates
binding
|
RASA1 |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-50100 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9233798 |
We have localized an in vitro rasgap-binding site to conserved tyrosine residues y604 and y610 in the juxtamembrane region of ephb2, and demonstrated that substitution of these amino acids abolishes ephrin-b1-induced signalling events in ephb2-expressing ng108-15 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | down-regulates
phosphorylation
|
RASA1 |
0.595 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-86008 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11389730 |
The phosphorylation of p120-gap by p60c-src inhibited its ability to stimulate the ha-ras-gtpase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
RASA1
- 
- 