| + |
FER | down-regulates activity 
phosphorylation
|
CTNNB1 |
0.721 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251131 |
Tyr142 |
AVVNLINyQDDAELA |
in vitro |
|
| pmid |
sentence |
| 12640114 |
Interaction of beta-catenin with alpha-catenin is regulated by the phosphorylation of beta-catenin Tyr-142. This residue can be phosphorylated in vitro by Fer or Fyn tyrosine kinases. Transfection of these kinases to epithelial cells disrupted the association between both catenins. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
FER | up-regulates 
phosphorylation
|
AR |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194749 |
Tyr225 |
PTSSKDNyLGGTSTI |
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 23906537 |
Fer is required for il-6 mediated ar activation by phosphorylating ar tyrosine 223 and binding via its sh2 domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FER | up-regulates activity
phosphorylation
|
PRKCD |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277546 |
Tyr374 |
ELKGRGEyFAIKALK |
Homo sapiens |
BT-549 Cell |
| pmid |
sentence |
| 33411917 |
We show that the tyrosine kinase FER alters PKCδ function by phosphorylating it on Y374, and that phospho-Y374-PKCδ prevents RAB5 release from nascent late endosomes, thereby inhibiting EGFR degradation and promoting the recycling of endosomal EGFR to the cell surface. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FER | up-regulates activity
phosphorylation
|
JUP |
0.525 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251134 |
Tyr550 |
AAGTQQPyTDGVRME |
Rattus norvegicus |
IEC-18 Cell |
| pmid |
sentence |
| 14517306 |
The tyrosine kinase Fer, which modifies beta-catenin Tyr142, lessening its association with alpha-catenin, phosphorylates plakoglobin Tyr549 and exerts the contrary effect: it raises the binding of plakoglobin to alpha-catenin. Fer stimulation, through modification of Tyr549, causes diminished binding of plakoglobin to components of desmosomes (desmoplakin) and increased interaction with adherens junction proteins (α-catenin) |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
FER | down-regulates activity
phosphorylation
|
JUP |
0.525 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251135 |
Tyr550 |
AAGTQQPyTDGVRME |
Rattus norvegicus |
IEC-18 Cell |
| pmid |
sentence |
| 14517306 |
The tyrosine kinase Fer, which modifies beta-catenin Tyr142, lessening its association with alpha-catenin, phosphorylates plakoglobin Tyr549 and exerts the contrary effect: it raises the binding of plakoglobin to alpha-catenin. Fer stimulation, through modification of Tyr549, causes diminished binding of plakoglobin to components of desmosomes (desmoplakin) and increased interaction with adherens junction proteins (α-catenin) |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
FER | up-regulates activity
phosphorylation
|
PTK2 |
0.251 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279409 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 19339212 |
The Fer mediated phosphorylation of specific tyrosine residues of FAK was abolished by cotransfection of shRNA against Fer (i.e., shFer), but not by control shRNA, indicating that the phosphorylation of Tyr577, 861, or 925 of FAK in suspended cells was indeed caused by Fer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FER | up-regulates activity
phosphorylation
|
PECAM1 |
0.322 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262865 |
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-262866 |
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 |
| + |
FER | up-regulates activity
phosphorylation
|
FER |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251133 |
Tyr714 |
RQEDGGVySSSGLKQ |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 10998246 |
P94fer undergoes autophosphorylation in-trans in vivo and that oligomerization mediates this process. the N-terminal sequences of the FER tyrosine kinases direct their different cellular autophosphorylation states, thereby dictating their different cellular functions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276236 |
Tyr714 |
RQEDGGVySSSGLKQ |
in vitro |
|
| pmid |
sentence |
| 19159681 |
Mutation analysis unveiled a tyrosine (Tyr(616)) embedded in the Hsp90 recognition loop, which is required for the kinase activity of Fer. Replacement of this tyrosine by phenylalanine (Y616F) disabled the auto-phosphorylation activity of Fer and abolished its ability to phosphorylate Stat3. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops, In Vitro |
| + |
HSP90AA1 | down-regulates activity
phosphorylation
|
FER |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277818 |
Tyr714 |
RQEDGGVySSSGLKQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 19159681 |
Hsp90 and tyrosine616 are required for Fer tyrosine kinase activity.Taken together, our findings underscore the importance of Hsp90 and the residue, tyrosine616, which resides in the Hsp90 recognition loop, in maintaining Fer tyrosine kinase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FER | down-regulates activity
phosphorylation
|
ARHGDIA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279042 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21122136 |
Fer interferes with binding of RhoGDI\u03b1 and Rac. (A) GST-RhoGDI\u03b1 was pre-incubated with Rac, after which GST-Fer (G-Fer) or GST (G) was added and GST fusion proteins were pulled down with glutathione agarose, followed by kinase reactions. (B) GST-RhoGDI\u03b1 was pre-incubated with GST-Fer or GST in kinase buffer, after which Rac was added and RhoGDI\u03b1 was immunoprecipitated. 50 pmol of RhoGDI\u03b1 and Rac1, with 25 pmol of GST and GST-Fer were used.|These results identify tyrosine phosphorylation of RhoGDIalpha by Fer as a mechanism to regulate binding of RhoGDIalpha to Rac. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FER | up-regulates activity
phosphorylation
|
STAT3 |
0.403 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279713 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10878010 |
Replacing the unique 43-amino acid-long N-terminal tail of p51 (ferT) with a parallel segment from the N-terminal tail of p94 (fer) did not change the subcellular localization of p51 (ferT) but enabled it to activate Stat3.|When combined with immunoprecipitation analysis, this assay showed that p94 (fer) can lead to the tyrosine phosphorylation and activation of Stat3 but not of Stat1 or Stat2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
FER
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