| + |
GSK3B |
phosphorylation
|
CTNND1 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251234 |
Ser252 |
MEGYRAPsRQDVYGP |
in vitro |
|
| pmid |
sentence |
| 12885254 |
GSK3beta selectively phosphorylates p120 on S252 and T310 in Vitro |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251235 |
Thr310 |
GTARRTGtPSDPRRR |
in vitro |
|
| pmid |
sentence |
| 12885254 |
GSK3beta selectively phosphorylates p120 on S252 and T310 in Vitro |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCE | down-regulates 
phosphorylation
|
CTNND1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201600 |
Ser268 |
PQVRVGGsSVDLHRF |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Lung Cancer Cell |
| pmid |
sentence |
| 23542175 |
We find that ctnnd1/p120ctn phosphorylation at serine 268 (p-s268) occurs in a strictly pkc_-dependent manner,serine/threonine phosphorylation of p120-ctn has been reported to affect the integrity of ajs [12], [24] and [25]. Xia et al. (2003) reported that several residues (ser122, ser252, ser268, ser288, thr310, ser312, ser873, and thr910) in p120ctn can be either phosphorylated or dephosphorylated upon pkc activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171712 |
Ser268 |
PQVRVGGsSVDLHRF |
Homo sapiens |
|
| pmid |
sentence |
| 21251911 |
We find that ctnnd1/p120ctn phosphorylation at serine 268 (p-s268) occurs in a strictly pkc_-dependent manner,serine/threonine phosphorylation of p120-ctn has been reported to affect the integrity of ajs [12], [24] and [25]. Xia et al. (2003) reported that several residues (ser122, ser252, ser268, ser288, thr310, ser312, ser873, and thr910) in p120ctn can be either phosphorylated or dephosphorylated upon pkc activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK1E | down-regulates
phosphorylation
|
CTNND1 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-24443 |
Ser268 |
PQVRVGGsSVDLHRF |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 3133391 |
Moreover, in response to wnt3a, p120-catenin is phosphorylated at ser268, a modification dependent on ck1epsilon activity, which disrupts its interaction with e-cadherin and, subsequently, with lrp5/6, promoting the release of ck1epsilon/p120-catenin from the wnt receptor complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates
phosphorylation
|
CTNND1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198288 |
Ser879 |
LIDRNQKsDKKPDRE |
Homo sapiens |
|
| pmid |
sentence |
| 22798526 |
We showed that pkc_ phosphorylation of p120 at serine (s)879 in response to thrombin or lipopolysaccharide challenge reduced p120 binding affinity for ve-cadherin and mediated aj disassembly secondary to ve-cadherin internalization |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Lung |
| + |
MAPK3 | down-regulates activity
phosphorylation
|
CTNND1 |
0.299 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277506 |
Thr906 |
SLDNNYStPNERGDH |
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 32010791 |
Upon TGFβ treatment, activated extracellular signal-regulated kinase 1/2 (ERK1/2) phosphorylates T900 of p120-catenin to promote its interaction with Smurf1 and subsequent monoubiquitination. TGFβ promotes monoubiquitination of p120-catenin through Smurf1 to induce junction dissociation. |
|
| Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
| + |
MAPK1 | down-regulates activity
phosphorylation
|
CTNND1 |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277505 |
Thr906 |
SLDNNYStPNERGDH |
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 32010791 |
Upon TGFβ treatment, activated extracellular signal-regulated kinase 1/2 (ERK1/2) phosphorylates T900 of p120-catenin to promote its interaction with Smurf1 and subsequent monoubiquitination. TGFβ promotes monoubiquitination of p120-catenin through Smurf1 to induce junction dissociation. |
|
| Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
| + |
SRC | up-regulates activity 
phosphorylation
|
CTNND1 |
0.92 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246480 |
Tyr112 |
PGQIVETyTEEDPEG |
in vitro |
|
| pmid |
sentence |
| 11382764 |
Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246484 |
Tyr228 |
YPGGSDNyGSLSRVT |
in vitro |
|
| pmid |
sentence |
| 11382764 |
Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246488 |
Tyr257 |
APSRQDVyGPQPQVR |
in vitro |
|
| pmid |
sentence |
| 11382764 |
Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246492 |
Tyr280 |
HRFHPEPyGLEDDQR |
in vitro |
|
| pmid |
sentence |
| 11382764 |
Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246496 |
Tyr291 |
DDQRSMGyDDLDYGM |
in vitro |
|
| pmid |
sentence |
| 11382764 |
Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246500 |
Tyr296 |
MGYDDLDyGMMSDYG |
in vitro |
|
| pmid |
sentence |
| 11382764 |
Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246504 |
Tyr302 |
DYGMMSDyGTARRTG |
in vitro |
|
| pmid |
sentence |
| 11382764 |
Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246508 |
Tyr96 |
QDHSHLLySTIPRMQ |
in vitro |
|
| pmid |
sentence |
| 11382764 |
Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302 |
|
| Publications: |
8 |
Organism: |
In Vitro |
| + |
EGFR |
phosphorylation
|
CTNND1 |
0.625 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251092 |
Tyr228 |
YPGGSDNyGSLSRVT |
Homo sapiens |
A-431 Cell |
| pmid |
sentence |
| 14996911 |
In A431 cells, epidermal growth factor induced striking p120 phosphorylation at Y228. Y228-phosphorylated p120 localized to adherens junctions and lamellipodia, and was significantly enhanced in cells around the colony periphery. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTNND1 | up-regulates quantity by stabilization
binding
|
CDH3 |
0.742 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252124 |
|
|
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 |
| + |
CTNND1 | up-regulates
binding
|
RAC1 |
0.568 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198938 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22946057 |
We demonstrate that p120-catenin participates in the stimulation of rac1 activity, binding directly to this protein. In addition we show that vav2 also binds to p120-catenin and is required for rac1 activation and for beta-catenin translocation to the nucleus.Vav2 And rac1 association with p120-catenin was modulated by phosphorylation of this protein, which was stimulated upon serine/threonine phosphorylation by ck1 and inhibited by tyrosine phosphorylation by src or fyn |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTNND1 | up-regulates quantity by stabilization
binding
|
CDH2 |
0.726 |
| 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 |
| + |
CTNND1 | up-regulates quantity by stabilization
binding
|
CDH1 |
0.945 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252123 |
|
|
Homo sapiens |
Epithelial Cell |
| pmid |
sentence |
| 14610055 |
P120 regulates E-cadherin turnover at the cell membrane. Because direct binding of p120 to E-cadherin is required, it is possible that p120 binding blocks the interaction of an unknown binding partner (or event) that targets E-cadherin for degradation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SMURF1 | down-regulates activity
monoubiquitination
|
CTNND1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277507 |
|
|
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 32010791 |
Upon TGFβ treatment, activated extracellular signal-regulated kinase 1/2 (ERK1/2) phosphorylates T900 of p120-catenin to promote its interaction with Smurf1 and subsequent monoubiquitination. TGFβ promotes monoubiquitination of p120-catenin through Smurf1 to induce junction dissociation. |
|
| Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
| + |
CTNND1 | down-regulates 
|
ZBTB33 |
0.818 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192369 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23481205 |
Nuclear signaling is affected by the interaction ofp120with kaiso, a transcription factor regulatingwnt-responsive genes. in addition, p120 cytoplasmic localization results in sequestration of kaiso in the cytoplasm and its inactivation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTNND1 | up-regulates quantity by stabilization
binding
|
CDH5 |
0.768 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252126 |
|
|
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 |
| + |
CTNND1 | up-regulates
binding
|
VAV2 |
0.595 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198941 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22946057 |
We demonstrate that p120-catenin participates in the stimulation of rac1 activity, binding directly to this protein. In addition we show that vav2 also binds to p120-catenin and is required for rac1 activation and for beta-catenin translocation to the nucleus.Vav2 And rac1 association with p120-catenin was modulated by phosphorylation of this protein, which was stimulated upon serine/threonine phosphorylation by ck1 and inhibited by tyrosine phosphorylation by src or fyn |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRM | down-regulates quantity
dephosphorylation
|
CTNND1 |
0.524 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277042 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21998202 |
Specifically, RPTP\u03bc dephosphorylated p120 catenin, subsequently leading to a lower level of cytoplasmic protein compared with that observed with the vector control and RPTP\u03bc-CS. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CTNND1
- 
- 