+ |
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 |
+ |
FYN | down-regulates activity
phosphorylation
|
JUP |
0.541 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251177 |
Tyr550 |
AAGTQQPyTDGVRME |
Rattus norvegicus |
|
pmid |
sentence |
14517306 |
Phosphorylation of plakoglobin by Fer and Fyn kinases decreases plakoglobin-desmoplakin interaction and increases plakoglobin-α-catenin association. Fyn mainly phosphorylated Tyr549 |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
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 |
+ |
FYN | up-regulates activity
phosphorylation
|
JUP |
0.541 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251176 |
Tyr550 |
AAGTQQPyTDGVRME |
Rattus norvegicus |
|
pmid |
sentence |
14517306 |
Phosphorylation of plakoglobin by Fer and Fyn kinases decreases plakoglobin-desmoplakin interaction and increases plakoglobin-α-catenin association. Fyn mainly phosphorylated Tyr549 and that it phosphorylated Tyr133 with a much lower activity |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
SRC | up-regulates activity
phosphorylation
|
JUP |
0.655 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-247310 |
Tyr644 |
RNEGTATyAAAVLFR |
Homo sapiens |
|
pmid |
sentence |
14517306 |
Tyrosine phosphorylation of plakoglobin causes contrary effects on its association with desmosomes and adherens junction components and modulates beta-catenin-mediated transcriptionFor instance, Src, which mainly phosphorylates Tyr86 in beta-catenin, modifies Tyr643 in plakoglobin, decreasing the interaction with E-cadherin and alpha-catenin and increasing the interaction with the alpha-catenin-equivalent protein in desmosomes, desmoplakin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
α-Catenin | up-regulates quantity
relocalization
|
JUP |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265819 |
|
|
Homo sapiens |
Colonic Cancer Cell |
pmid |
sentence |
21598020 |
Overexpression of CTNNA3 in a CTNNA1 negative colon carcinoma cell line resulted in the reassembly of the adherens and tight junctions through the recruitment of CTNNA3 interacting partners such as E-cadherin, β-catenin, plakoglobin, and ZO-14 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CTNNA3 | up-regulates quantity
relocalization
|
JUP |
0.497 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265494 |
|
|
Homo sapiens |
Colonic Cancer Cell |
pmid |
sentence |
21598020 |
Overexpression of CTNNA3 in a CTNNA1 negative colon carcinoma cell line resulted in the reassembly of the adherens and tight junctions through the recruitment of CTNNA3 interacting partners such as E-cadherin, β-catenin, plakoglobin, and ZO-14 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |