| + |
FES | up-regulates activity 
phosphorylation
|
FES |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277898 |
Tyr139 |
Y-->K |
in vitro |
|
| pmid |
sentence |
| 18775312 |
In addition, we analyzed Fes SH2-kinase that had been autophosphorylated on the kinase activation segment (Y713) in complex with a substrate peptide. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
FES | down-regulates activity 
phosphorylation
|
BCR |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251136 |
Tyr177 |
ADAEKPFyVNVEFHH |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 8955135 |
Mutagenesis of BCR Tyr-177 to Phe completely abolished FES-induced BCR binding to the GRB2 SH2 domain, identifying Tyr-177 as an additional phosphorylation site for FES. Co-expression of BCR and FES in human 293T cells stimulated the tyrosine autophosphorylation of FES. By contrast, tyrosine phosphorylation of BCR by FES suppressed BCR serine/threonine kinase activity toward the 14-3-3 protein and BCR substrate, BAP-1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251137 |
Tyr246 |
SCGVDGDyEDAELNP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 8955135 |
In the present study, we demonstrate that BCR Tyr-246 and at least one of the closely spaced tyrosine residues, Tyr-279, Tyr-283, and Tyr-289 (3Y cluster), are phosphorylated by FES both in vitro and in 32Pi-labeled cells. Co-expression of BCR and FES in human 293T cells stimulated the tyrosine autophosphorylation of FES. By contrast, tyrosine phosphorylation of BCR by FES suppressed BCR serine/threonine kinase activity toward the 14-3-3 protein and BCR substrate, BAP-1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FES | down-regulates
phosphorylation
|
BCR |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-45330 |
Tyr246 |
SCGVDGDyEDAELNP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 8955135 |
In the present study, we demonstrate that bcr tyr-246 and at least one of the closely spaced tyrosine residues, tyr-279, tyr-283, and tyr- 289 (3y cluster), are phosphorylated by fes both in vitro and in 32p(i)- labeled cells. tyrosine phosphorylation of bcr by fes suppressed bcr serine/threonine kinase activity toward the 14-3-3 protein and bcr substrate, bap-1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-45334 |
Tyr279 |
PPLEYQPyQSIYVGG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 8955135 |
In the present study, we demonstrate that bcr tyr-246 and at least one of the closely spaced tyrosine residues, tyr-279, tyr-283, and tyr- 289 (3y cluster), are phosphorylated by fes both in vitro and in 32p(i)- labeled cells. tyrosine phosphorylation of bcr by fes suppressed bcr serine/threonine kinase activity toward the 14-3-3 protein and bcr substrate, bap-1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-45343 |
Tyr283 |
YQPYQSIyVGGMMEG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 8955135 |
In the present study, we demonstrate that bcr tyr-246 and at least one of the closely spaced tyrosine residues, tyr-279, tyr-283, and tyr- 289 (3y cluster), are phosphorylated by fes both in vitro and in 32p(i)- labeled cells. tyrosine phosphorylation of bcr by fes suppressed bcr serine/threonine kinase activity toward the 14-3-3 protein and bcr substrate, bap-1. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
FES | up-regulates activity
phosphorylation
|
PECAM1 |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262867 |
Tyr690 |
PLNSDVQyTEVQVSS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12972546 |
PECAM-1 Is Phosphorylated by Fer and, To a Lesser Extent, by Fes. These results suggest that Fer not only functions as a tyrosine kinase for PECAM-1 but also that Fer modulates the downstream signaling of PECAM-1 by inducing phosphorylation of SHP-2 and Gab1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262868 |
Tyr713 |
KKDTETVySEVRKAV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12972546 |
PECAM-1 Is Phosphorylated by Fer and, To a Lesser Extent, by Fes. These results suggest that Fer not only functions as a tyrosine kinase for PECAM-1 but also that Fer modulates the downstream signaling of PECAM-1 by inducing phosphorylation of SHP-2 and Gab1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FES | up-regulates activity
phosphorylation
|
STAT3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278937 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
|
| pmid |
sentence |
| 15003822 |
Fes also induced Tyr 705 phosphorylation and DNA binding activity of STAT3, in agreement with the idea that Fes can regulate transcriptional activation through Fes dependent phosphorylation of transcription factors.On the basis of these findings, we propose that Fes activation of critical transcriptional regulators such as PU.1 is part of the mechanism by which this kinase induces macrophage differentiation of myeloid progenitors.|We conclude that Fes may regulate granulocytic differentiation at least in part through activation of C/EBP-alpha and STAT3.In 32D cells, Fes activated STAT3 and C/EBP-alpha, two important regulators of granulocytic differentiation [14,15]. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FES | up-regulates
phosphorylation
|
FES |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42655 |
Tyr713 |
REEADGVyAASGGLR |
Homo sapiens |
|
| pmid |
sentence |
| 8663427 |
Substitution of kinase domain tyrosine residues 713 or 811 with phenylalanine resulted in a loss of the 10- and 4-kda phosphopeptides, respectively, identifying these tyrosines as in vitro autophosphorylation sites. Cnbr cleavage analysis of fes isolated from 32po4-labeled 293t cells showed that tyr-713 and tyr-811 are also autophosphorylated in vivo. . Mutagenesis of tyr-713 reduced both autophosphorylation of tyr-811 and transphosphorylation of bcr, a recently identified fes substrate, supporting a major regulatory role for tyr-713. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-42659 |
Tyr811 |
RPSFSTIyQELQSIR |
Homo sapiens |
|
| pmid |
sentence |
| 8663427 |
Substitution of kinase domain tyrosine residues 713 or 811 with phenylalanine resulted in a loss of the 10- and 4-kda phosphopeptides, respectively, identifying these tyrosines as in vitro autophosphorylation sites. Cnbr cleavage analysis of fes isolated from 32po4-labeled 293t cells showed that tyr-713 and tyr-811 are also autophosphorylated in vivo. . Mutagenesis of tyr-713 reduced both autophosphorylation of tyr-811 and transphosphorylation of bcr, a recently identified fes substrate, supporting a major regulatory role for tyr-713. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
EZR | up-regulates
relocalization
|
FES |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159496 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18046454 |
The recruitment and the activation of fes to the cell-cell contacts in confluent cells depend on its interaction with ezrin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
FES
- 
- 