| + |
FES | down-regulates activity 
phosphorylation
|
BCR |
0.376 |
| 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 |
0.376 |
| 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 |
0.281 |
| 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
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 |
0.405 |
| 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
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- 