| + |
SRC | down-regulates 
phosphorylation
|
CDH2 |
0.413 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143234 |
Tyr852 |
NDPTAPPyDSLLVFD |
Homo sapiens |
|
| pmid |
sentence |
| 16371504 |
Src-mediated phosphorylation of the n-cadherin cytoplasmic domain results in a significant reduction in beta-catenin bindingbeta-catenin dissociates from n-cadherin and redistributes to the nucleus of transmigrating melanoma cells to activate gene transcription.Because there were only four tyrosine residues (y852, y860, y884, and y886) in this peptide, all of them were phosphorylated. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143238 |
Tyr860 |
DSLLVFDyEGSGSTA |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 16371504 |
Src-mediated phosphorylation of the n-cadherin cytoplasmic domain results in a significant reduction in beta-catenin bindingbeta-catenin dissociates from n-cadherin and redistributes to the nucleus of transmigrating melanoma cells to activate gene transcription.Because there were only four tyrosine residues (y852, y860, y884, and y886) in this peptide, all of them were phosphorylated. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143242 |
Tyr884 |
SSGGEQDyDYLNDWG |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 16371504 |
Src-mediated phosphorylation of the n-cadherin cytoplasmic domain results in a significant reduction in beta-catenin bindingbeta-catenin dissociates from n-cadherin and redistributes to the nucleus of transmigrating melanoma cells to activate gene transcription.Because there were only four tyrosine residues (y852, y860, y884, and y886) in this peptide, all of them were phosphorylated. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143246 |
Tyr886 |
GGEQDYDyLNDWGPR |
Homo sapiens |
Melanoma Cell |
| pmid |
sentence |
| 16371504 |
Src-mediated phosphorylation of the n-cadherin cytoplasmic domain results in a significant reduction in beta-catenin bindingbeta-catenin dissociates from n-cadherin and redistributes to the nucleus of transmigrating melanoma cells to activate gene transcription.Because there were only four tyrosine residues (y852, y860, y884, and y886) in this peptide, all of them were phosphorylated. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
ARVCF | up-regulates quantity by stabilization 
binding
|
CDH2 |
0.481 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252128 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 14610055 |
To clarify the role of p120 in mammalian cells, we have knocked down p120 with siRNA in cells expressing epithelial (E-), placental (P-), neuronal (N-), and vascular endothelial (VE-) cadherins. We report that each of these cadherins, as well as α- and β-catenins, were rapidly degraded in the absence of p120, resulting in loss of cell–cell adhesion. The effect was clearly dose dependent, indicating that p120 expression levels may directly determine cadherin levels. Degradation of p120-uncoupled cadherin occurred after its arrival at the surface, indicating that p120 regulates cadherin turnover at the level of internalization or recycling. p120 homologues ARVCF and δ-catenin could substitute for p120, so at least one family member is likely required to maintain adhesion. Thus, cadherin complexes are rapidly turned over and degraded in mammalian cells in the absence of direct interaction with p120 or a p120 family member. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTNND2 | up-regulates quantity by stabilization
binding
|
CDH2 |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252131 |
|
|
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 14610055 |
To clarify the role of p120 in mammalian cells, we have knocked down p120 with siRNA in cells expressing epithelial (E-), placental (P-), neuronal (N-), and vascular endothelial (VE-) cadherins. We report that each of these cadherins, as well as α- and β-catenins, were rapidly degraded in the absence of p120, resulting in loss of cell–cell adhesion. The effect was clearly dose dependent, indicating that p120 expression levels may directly determine cadherin levels. Degradation of p120-uncoupled cadherin occurred after its arrival at the surface, indicating that p120 regulates cadherin turnover at the level of internalization or recycling. p120 homologues ARVCF and δ-catenin could substitute for p120, so at least one family member is likely required to maintain adhesion. Thus, cadherin complexes are rapidly turned over and degraded in mammalian cells in the absence of direct interaction with p120 or a p120 family member. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
calcium(2+) | up-regulates activity
chemical activation
|
CDH2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265842 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22535893 |
Cadherins are Ca(2+)-dependent cell-cell adhesion molecules that play critical roles in animal morphogenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDH4 | down-regulates quantity by repression 
|
CDH2 |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253107 |
|
|
Mus musculus |
C2C12 Cell |
| pmid |
sentence |
| 18701479 |
Taken together, these data show that (a) R-cadherin decreases the expression of M-cadherin and (b) N-cadherin and M-cadherin only slightly accumulate at the cell contacts in R-cadherin–expressing myoblasts. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
NEXMIF | up-regulates quantity by expression 
transcriptional regulation
|
CDH2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269660 |
|
|
Rattus norvegicus |
Neuron |
| pmid |
sentence |
| 27822498 |
Xpn regulates N-cadherin and β1-integrin expression at the transcriptional level in PC12 cells |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CTNND1 | up-regulates quantity by stabilization
binding
|
CDH2 |
0.725 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252125 |
|
|
Homo sapiens |
HUAEC Cell |
| pmid |
sentence |
| 14610055 |
To clarify the role of p120 in mammalian cells, we have knocked down p120 with siRNA in cells expressing epithelial (E-), placental (P-), neuronal (N-), and vascular endothelial (VE-) cadherins. We report that each of these cadherins, as well as α- and β-catenins, were rapidly degraded in the absence of p120, resulting in loss of cell–cell adhesion. The effect was clearly dose dependent, indicating that p120 expression levels may directly determine cadherin levels. Degradation of p120-uncoupled cadherin occurred after its arrival at the surface, indicating that p120 regulates cadherin turnover at the level of internalization or recycling. p120 homologues ARVCF and δ-catenin could substitute for p120, so at least one family member is likely required to maintain adhesion. Thus, cadherin complexes are rapidly turned over and degraded in mammalian cells in the absence of direct interaction with p120 or a p120 family member. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDH2 | up-regulates activity
binding
|
CTNNB1 |
0.812 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265864 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21255999 |
At its C-terminus, cadherin interacts with β-catenin, which dynamically associates with α-catenin, a direct binding partner of filamentous actin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDH2 | up-regulates
binding
|
CDON |
0.63 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163844 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20160094 |
We report here that n-cadherin ligation activates p38alpha/beta in myoblasts in a cdo-, bnip-2-, and jlp-dependent manner |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDH2 | up-regulates
binding
|
CDON/SPAG9 |
0.525 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217517 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20160094 |
We report here that n-cadherin ligation activates p38alpha/beta in myoblasts in a cdo-, bnip-2-, and jlp-dependent manner |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDH2
- 
- 