+ |
FER | down-regulates activity
phosphorylation
|
CTNNB1 |
0.706 |
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 |
0.262 |
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 | down-regulates activity
phosphorylation
|
JUP |
0.504 |
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
|
JUP |
0.504 |
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 | up-regulates activity
phosphorylation
|
PECAM1 |
0.329 |
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 |