| + |
HCK | up-regulates activity 
phosphorylation
|
CSF3R |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251263 |
Tyr752 |
GTSDQVLyGQLLGSP |
in vitro |
|
| pmid |
sentence |
| 9790917 |
Hck becomes activated upon G-CSF treatment and is, in turn, able to phosphorylate the G-CSF-R, indicating a clear functional and physical involvement in G-CSF signaling. the ability of Hck to phosphorylate the G-CSF-R in vitro, both Y728 and Y763 fit the Src consensus phosphorylation site |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251264 |
Tyr787 |
LTPSPKSyENLWFQA |
in vitro |
|
| pmid |
sentence |
| 9790917 |
Hck becomes activated upon G-CSF treatment and is, in turn, able to phosphorylate the G-CSF-R, indicating a clear functional and physical involvement in G-CSF signaling. the ability of Hck to phosphorylate the G-CSF-R in vitro, both Y728 and Y763 fit the Src consensus phosphorylation site. we investigated the activation of Hck by the G-CSF-R in intact cells as well as in vitro. These studies revealed recruitment of Hck to activated G-CSF-R, mediated by direct binding via its SH2 domain to multiple phosphotyrosines of the receptor. In addition, we show that Hck becomes activated upon G-CSF treatment and is, in turn, able to phosphorylate the G-CSF-R, indicating a clear functional and physical involvement in G-CSF signaling. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CSF1 | up-regulates
binding
|
CSF3R |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144737 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16492764 |
A crystal structure of the signaling complex between human granulocyte colony-stimulating factor (gcsf) and a ligand binding region of gcsf receptor (gcsf-r), has been determined to 2.8 a resolution |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSF3 | up-regulates
binding
|
CSF3R |
0.779 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144743 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16492764 |
The gcsf:gcsf-r complex formed a 2:2 stoichiometry by means of a cross-over interaction between the ig-like domains of gcsf-r and gcsf. the ig-like domain cross-over structure necessary for gcsf-r activation is consistent with previously reported thermodynamic and mutational analyses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSF2 | up-regulates
binding
|
CSF3R |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144740 |
|
|
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 16492764 |
A g-csfr expression plasmid was introduced into interleukin-3 (il-3)-dependent mouse myeloid precursor fdc-p1 cells that normally do not respond to g-csf. G-csf stimulated proliferation of the transformants. These results suggested that the g-csfr, but not the il-3/gm-csf receptors, transduced the neutrophilic differentiation signal into cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-31963 |
|
|
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 7691413 |
A g-csfr expression plasmid was introduced into interleukin-3 (il-3)-dependent mouse myeloid precursor fdc-p1 cells that normally do not respond to g-csf. G-csf stimulated proliferation of the transformants these results suggested that the g-csfr, but not the il-3/gm-csf receptors, transduced the neutrophilic differentiation signal into cells. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
4.0
CSF3R
- 
- 