| + |
PLK1 | down-regulates quantity by destabilization 
phosphorylation
|
CDH1 |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274054 |
Ser146 |
LLTFPNSsPGLRRQK |
|
|
| pmid |
sentence |
| 23972993 |
Priming phosphorylation of Cdh1 by the Cdk2/cyclin A kinase complex allows Plk1 to bind to Cdh1 and phosphorylate Cdh1 at Ser138 and Ser146. Phosphorylation of Cdh1 at Ser138 and Ser146 then triggers its interaction with, and subsequent ubiquitination by, SCFbeta-TRCP |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274053 |
|
|
|
|
| pmid |
sentence |
| 23972993 |
Priming phosphorylation of Cdh1 by the Cdk2/cyclin A kinase complex allows Plk1 to bind to Cdh1 and phosphorylate Cdh1 at Ser138 and Ser146. Phosphorylation of Cdh1 at Ser138 and Ser146 then triggers its interaction with, and subsequent ubiquitination by, SCFbeta-TRCP |
|
| Publications: |
2 |
| + |
CyclinA2/CDK2 | down-regulates quantity by destabilization
phosphorylation
|
CDH1 |
0.419 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274051 |
Ser36 |
HPGFDAEsYTFTVPR |
|
|
| pmid |
sentence |
| 23972993 |
Priming phosphorylation of Cdh1 by the Cdk2/cyclin A kinase complex allows Plk1 to bind to Cdh1 and phosphorylate Cdh1 at Ser138 and Ser146. Phosphorylation of Cdh1 at Ser138 and Ser146 then triggers its interaction with, and subsequent ubiquitination by, SCFbeta-TRCP |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274052 |
Thr40 |
DAESYTFtVPRRHLE |
|
|
| pmid |
sentence |
| 23972993 |
Priming phosphorylation of Cdh1 by the Cdk2/cyclin A kinase complex allows Plk1 to bind to Cdh1 and phosphorylate Cdh1 at Ser138 and Ser146. Phosphorylation of Cdh1 at Ser138 and Ser146 then triggers its interaction with, and subsequent ubiquitination by, SCFbeta-TRCP |
|
| Publications: |
2 |
| + |
CDK2 | down-regulates quantity by destabilization
phosphorylation
|
CDH1 |
0.441 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274049 |
Ser36 |
HPGFDAEsYTFTVPR |
|
|
| pmid |
sentence |
| 23972993 |
Priming phosphorylation of Cdh1 by the Cdk2/cyclin A kinase complex allows Plk1 to bind to Cdh1 and phosphorylate Cdh1 at Ser138 and Ser146. Phosphorylation of Cdh1 at Ser138 and Ser146 then triggers its interaction with, and subsequent ubiquitination by, SCFbeta-TRCP |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274050 |
Thr40 |
DAESYTFtVPRRHLE |
|
|
| pmid |
sentence |
| 23972993 |
Priming phosphorylation of Cdh1 by the Cdk2/cyclin A kinase complex allows Plk1 to bind to Cdh1 and phosphorylate Cdh1 at Ser138 and Ser146. Phosphorylation of Cdh1 at Ser138 and Ser146 then triggers its interaction with, and subsequent ubiquitination by, SCFbeta-TRCP |
|
| Publications: |
2 |
| + |
CSNK2A1 | up-regulates activity 
phosphorylation
|
CDH1 |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250839 |
Ser838 |
LVFDYEGsGSEAASL |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 10671552 |
Casein kinase II phosphorylation of E-cadherin increases E-cadherin/beta-catenin interaction and strengthens cell-cell adhesion. | All mutants showed a clear reduction in phosphorylation. Phosphorylation was completely abolished in the single mutant S855A and the double mutant S853/855A, and phosphorylation in S840A and S853A mutants was reduced to 43 and 28% that of wt GST-ECT. | Expression of the E-cadherin double mutant S853A/S855A in NIH3T3 cells expressing Wnt-1 reduces cell-cell adhesion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250840 |
Ser851 |
SLSSLNSsESDKDQD |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 10671552 |
Casein kinase II phosphorylation of E-cadherin increases E-cadherin/beta-catenin interaction and strengthens cell-cell adhesion. | Under these conditions, phosphorylation of the E-cadherin double mutant S853A/S855A was reduced by 25% as compared with wt E-cadherin. | Expression of the E-cadherin double mutant S853A/S855A in NIH3T3 cells expressing Wnt-1 reduces cell-cell adhesion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250841 |
Ser853 |
SSLNSSEsDKDQDYD |
Mus musculus |
|
| pmid |
sentence |
| 10671552 |
Casein kinase II phosphorylation of E-cadherin increases E-cadherin/beta-catenin interaction and strengthens cell-cell adhesion. | Under these conditions, phosphorylation of the E-cadherin double mutant S853A/S855A was reduced by 25% as compared with wt E-cadherin. | Expression of the E-cadherin double mutant S853A/S855A in NIH3T3 cells expressing Wnt-1 reduces cell-cell adhesion. |
|
| Publications: |
3 |
Organism: |
Mus Musculus |
| + |
CSNK1A1 | down-regulates activity
phosphorylation
|
CDH1 |
0.317 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274045 |
Ser844 |
GSGSEAAsLSSLNSS |
|
|
| pmid |
sentence |
| 17353278 |
Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts|CK1 colocalizes with E-cadherin and phosphorylates the cytoplasmic domain of E-cadherin in vitro and in a cell culture system. We show that the major CK1 phosphorylation site of E-cadherin is serine 846 |
|
| Publications: |
1 |
| + |
CSNK1E | down-regulates activity
phosphorylation
|
CDH1 |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274047 |
Ser844 |
GSGSEAAsLSSLNSS |
|
|
| pmid |
sentence |
| 17353278 |
Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts|CK1 colocalizes with E-cadherin and phosphorylates the cytoplasmic domain of E-cadherin in vitro and in a cell culture system. We show that the major CK1 phosphorylation site of E-cadherin is serine 846 |
|
| Publications: |
1 |
| Pathways: | Hippo Signaling |
| + |
CSNK1D | down-regulates activity
phosphorylation
|
CDH1 |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274046 |
Ser844 |
GSGSEAAsLSSLNSS |
|
|
| pmid |
sentence |
| 17353278 |
Casein kinase 1 is a novel negative regulator of E-cadherin-based cell-cell contacts|CK1 colocalizes with E-cadherin and phosphorylates the cytoplasmic domain of E-cadherin in vitro and in a cell culture system. We show that the major CK1 phosphorylation site of E-cadherin is serine 846 |
|
| Publications: |
1 |
| Pathways: | Hippo Signaling |
| + |
GSK3B | up-regulates activity
phosphorylation
|
CDH1 |
0.575 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251225 |
Ser847 |
SEAASLSsLNSSESD |
in vitro |
|
| pmid |
sentence |
| 10671552 |
Phosphorylation of the E-cadherin Cytoplasmic Domain by CKII and GSK-3β Increases the Binding to β-catenin. pre-phosphorylation by CKII at Ser-855 and/or Ser-853 of E-cadherin is required before GSK-3β can phosphorylate at Ser-849. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCD | down-regulates activity
phosphorylation
|
CDH1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260893 |
Thr790 |
TRNDVAPtLMSVPRY |
Cricetulus griseus |
|
| pmid |
sentence |
| 27203386 |
Phosphorylation of E-cadherin at threonine 790 by protein kinase Cδ reduces β-catenin binding and suppresses the function of E-cadherin. |
|
| Publications: |
1 |
Organism: |
Cricetulus Griseus |
| + |
SRC | down-regulates quantity by destabilization
phosphorylation
|
CDH1 |
0.747 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274048 |
Tyr797 |
TLMSVPRyLPRPANP |
|
|
| pmid |
sentence |
| 31286874 |
Activated c-Src phosphorylated E-cadherin at the tyrosine 797 site to initiate RNF43-mediated E-cadherin ubiquitination at lysine 816 and subsequent degradation |
|
| Publications: |
1 |
| + |
CTBP2 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.391 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261578 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21315774 |
Overexpression of the CtBP2 protein enhanced the repression activity of the E-cadherin promoter in a dose-dependent manner, whereas overexpression of ataxin-1 increased the activity of the E-cadherin promoter in a dose-dependent manner |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-betaTRCP | down-regulates quantity by destabilization
ubiquitination
|
CDH1 |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274055 |
|
|
|
|
| pmid |
sentence |
| 23972993 |
Priming phosphorylation of Cdh1 by the Cdk2/cyclin A kinase complex allows Plk1 to bind to Cdh1 and phosphorylate Cdh1 at Ser138 and Ser146. Phosphorylation of Cdh1 at Ser138 and Ser146 then triggers its interaction with, and subsequent ubiquitination by, SCFbeta-TRCP |
|
| Publications: |
1 |
| Pathways: | Hippo Signaling |
| + |
SNAI1 | down-regulates quantity by repression 
transcriptional regulation
|
CDH1 |
0.75 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255156 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15311212 |
known E-cadherin transcriptional repressors, such as SLUG (SNAI2), SIP1 (ZEB2), TWIST1, SNAIL (SNAI1) and ZEB1 (TCF8), but not E12/E47 (TCF3), had a lack of upregulation in cells expressing mutated E-cadherin compared to WT. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MEIS2 | up-regulates quantity by expression
transcriptional regulation
|
CDH1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267242 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 21746878 |
We show that the Pbx1 and Meis2 homeodomain proteins interact with Klf4 and can be recruited to DNA elements comprising a Klf4 site or G C box, with adjacent Meis and Pbx sites. Meis2d and Pbx1a activate expression of p15(Ink4a) and E-cadherin, dependent on the Meis2d transcriptional activation domain. We suggest a model in which genes with Klf4 sites can be cooperatively activated by Meis2/Pbx1 and Klf4, dependent primarily on recruitment by Klf4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKD1 | up-regulates
phosphorylation
|
CDH1 |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133856 |
|
|
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 15695390 |
Our study has identified e-cadherin as a novel substrate of pkd1, and phosphorylation of e-cadherin by pkd1 is associated with increased cellular aggregation and decreased cellular motility in prostate cancer. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HDAC3 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275662 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 25726523 |
GATA1 is a new substrate of p21-activated kinase 5 (PAK5), which is phosphorylated on serine 161 and 187 (S161 and S187). GATA1 recruits HDAC3/4 to E-cadherin promoter, which is reduced by GATA1 S161A S187A mutant. These data indicate that phosphorylated GATA1 recruits more HDAC3/4 to promote transcriptional repression of E-cadherin, leading to the EMT of breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ARVCF | up-regulates quantity by stabilization
binding
|
CDH1 |
0.432 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252133 |
|
|
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 |
| + |
CDH1 | up-regulates
binding
|
LRP6 |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168464 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20940130 |
P12Beta-catenin_ also associates to the_ wnt_ co-receptor lrp5/6, an interaction mediated by e-cadherin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SALL4 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255124 |
|
|
Homo sapiens |
Breast Cancer Cell Line |
| pmid |
sentence |
| 23954296 |
Our shRNA-mediated SALL4 knockdown system and SALL4 overexpression system revealed that SALL4 suppresses the expression of adhesion gene CDH1, and positively regulates the CDH1 suppressor ZEB1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TCF3 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275654 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 26212009 |
The p21-activated kinase 5 (PAK5) is overexpressed in advanced cancer and the transcription factor E47 is a direct repressor of E-cadherin and inducer of epithelial-mesenchymal transition (EMT). |In this study, we found that PAK5-mediated E47 phosphorylation promoted EMT in advanced colon cancer. PAK5 interacted with E47 and phosphorylated E47 on Ser39 under hepatocyte growth factor (HGF) stimulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ZEB2 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255159 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15311212 |
known E-cadherin transcriptional repressors, such as SLUG (SNAI2), SIP1 (ZEB2), TWIST1, SNAIL (SNAI1) and ZEB1 (TCF8), but not E12/E47 (TCF3), had a lack of upregulation in cells expressing mutated E-cadherin compared to WT. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ANK3 | up-regulates activity
binding
|
CDH1 |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266710 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17620337 |
Ankyrin-G is a molecular partner of E-cadherin in epithelial cells and early embryos. Ankyrin-G also recruits beta-2-spectrin to E-cadherin-beta-catenin complexes, thus providing a direct connection between E-cadherin and the spectrin/actin skeleton. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDH1 | up-regulates
binding
|
AE/b7 integrin |
0.638 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-35210 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 7969453 |
Here we show that heterotypic adhesive interactions between epithelial cells and intraepithelial lymphocytes in vitro are mediated by e-cadherin and the alpha e beta 7 integrin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTBP1 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259197 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21681822 |
Carboxyl-terminal binding protein 1 (CtBP1) is a transcriptional co-repressor with oncogenic potential. We found CtBP1 was recruited to the promoter regions of Brca1 and E-cadherin genes in breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTNNA3 | up-regulates quantity
relocalization
|
CDH1 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265492 |
|
|
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 |
| + |
TWIST1 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.498 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255157 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15311212 |
known E-cadherin transcriptional repressors, such as SLUG (SNAI2), SIP1 (ZEB2), TWIST1, SNAIL (SNAI1) and ZEB1 (TCF8), but not E12/E47 (TCF3), had a lack of upregulation in cells expressing mutated E-cadherin compared to WT. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATXN1 | up-regulates quantity by expression
transcriptional regulation
|
CDH1 |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261577 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21315774 |
Overexpression of the CtBP2 protein enhanced the repression activity of the E-cadherin promoter in a dose-dependent manner, whereas overexpression of ataxin-1 increased the activity of the E-cadherin promoter in a dose-dependent manner |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ZEB2 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268950 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11430829 |
SIP 1 downregulates mammalian E-cadherin transcription via binding to both conserved E2 boxes of the minimal E-cadh promoter.SIP1 induction resulted in the loss of cell-cell adhesion, in activation of invasion and in at random, multidirectional migration instead of unidirectional coherent migration (required in neurulation). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDH1 | up-regulates activity
binding
|
APC-c |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274058 |
|
|
|
|
| pmid |
sentence |
| 18662541 |
In early mitosis, APC/C is activated through binding to Cdc20, and in late M, Cdc20 is replaced by Cdh1, the second activator of APC/C. |
|
| Publications: |
1 |
| + |
CDC14B | up-regulates activity
dephosphorylation
|
CDH1 |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277017 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18662541 |
Cdc14B activates APC/C Cdh1 after DNA damage in G2.|Importantly, after DNA damage, thein vivo phosphorylation of wild type Cdh1 - but not that of Cdh1 (4xA) - increased after Cdc14B silencing (XREF_FIG), indicating that in response to genotoxic stress, Cdc14B dephosphorylates Cdh1 on the four sites phosphorylated by Cdk2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Cell-Cell_contact | up-regulates 
|
CDH1 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-230707 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24532814 |
Adherens junctions and the cadheriBeta-catenin complex have been found to activate the Hippo signaling pathway and inhibit cell growth. Cadherin-mediated stimulation of the Hippo signaling pathway requires cadherin ligation and the formation of a homophilic bond consistent with a role in cell-cell contact and works owing to phosphorylation of YAP by Lats and nuclear exclusion of YAP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Hippo Signaling |
| + |
calcium(2+) | up-regulates activity
chemical activation
|
CDH1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265841 |
|
|
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 |
| + |
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 |
| + |
CBX7 | up-regulates quantity by expression
transcriptional regulation
|
CDH1 |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253767 |
|
|
Homo sapiens |
Thyroid Cancer Cell |
| pmid |
sentence |
| 19706751 |
We confirmed by coimmunoprecipitation that CBX7 physically interacts with the HDAC2 protein and is able to inhibit its activity. Then, we showed that both these proteins bind the E-cadherin promoter and that CBX7 up-regulates E-cadherin expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TBX3 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.421 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-223537 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25595898 |
AKT phosphorylation potentiates the ability of TBX3 to repress the transcription of the E-cadherin gene |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDH1 | up-regulates
binding
|
CTNNA1 |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203468 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24336504 |
Additionally, the E-cadherin associated protein _-catenin regulates YAP directly by sequestering YAP/14-3-3 complexes in the cytoplasm. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Hippo Signaling |
| + |
PBX1 | up-regulates quantity by expression
transcriptional regulation
|
CDH1 |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267241 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 21746878 |
We show that the Pbx1 and Meis2 homeodomain proteins interact with Klf4 and can be recruited to DNA elements comprising a Klf4 site or G C box, with adjacent Meis and Pbx sites. Meis2d and Pbx1a activate expression of p15(Ink4a) and E-cadherin, dependent on the Meis2d transcriptional activation domain. We suggest a model in which genes with Klf4 sites can be cooperatively activated by Meis2/Pbx1 and Klf4, dependent primarily on recruitment by Klf4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDH1 | up-regulates activity
binding
|
α-Catenin |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265821 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24336504 |
Additionally, the E-cadherin associated protein _-catenin regulates YAP directly by sequestering YAP/14-3-3 complexes in the cytoplasm. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ADAM10 | up-regulates activity
cleavage
|
CDH1 |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259846 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26284334 |
The ADAM proteases are best known for their role in shedding the extracellular domain of transmembrane proteins. Among the transmembrane proteins shed by ADAM10 are notch, HER2, E-cadherin, CD44, L1 and the EGFR ligands, EGF and betacellulin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
USP28 | up-regulates quantity by stabilization
deubiquitination
|
CDH1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274057 |
|
|
|
|
| pmid |
sentence |
| 18662541 |
Usp28 deubiquitylates and consequently stabilizes Claspin in response to DNA damage |
|
| Publications: |
1 |
| + |
MTA1 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254594 |
|
|
Homo sapiens |
OVCAR-3 Cell |
| pmid |
sentence |
| 18719363 |
MTA1 overexpression resulted in downregulation of E-cadherin and MTA3 expression and enhanced expression of the transcriptional repressors SNAIL and SLUG. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TWIST2 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.454 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255536 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 19581928 |
we showed aberrant IL-6 production and STAT3 activation in MCF-7 cells that constitutively express Twist, a metastatic regulator and direct transcriptional repressor of E-cadherin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDH1 | down-regulates
|
Epithelial-mesenchymal_transition |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252261 |
|
|
|
|
| pmid |
sentence |
| 15601859 |
A hallmark characteristic of epithelial tumor progression as well as some processes of normal development is the loss of the epithelial phenotype and acquisition of a motile or mesenchymal phenotype. Such epithelial to mesenchymal transitions are accompanied by the loss of E-cadherin function by either transcriptional or posttranscriptional mechanisms. |
|
| Publications: |
1 |
| + |
α-Catenin | up-regulates quantity
relocalization
|
CDH1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265817 |
|
|
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 |
| + |
ZEB1 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.674 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255158 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15311212 |
known E-cadherin transcriptional repressors, such as SLUG (SNAI2), SIP1 (ZEB2), TWIST1, SNAIL (SNAI1) and ZEB1 (TCF8), but not E12/E47 (TCF3), had a lack of upregulation in cells expressing mutated E-cadherin compared to WT. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ZNF503 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261190 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25538248 |
We asked whether higher pFAK staining in cells expressing Zpo2 correlates with reduced E-cadherin levels. Immunostaining for E-cadherin in the EpH4.9 and PyMT stable cell lines indicated a decrease in overall E-cadherin staining in Zpo2-overexpressing cells compared with the control (Fig. 6C). Similarly, Western blot analysis indicated a reduction in E-cadherin expression in Zpo2-expressing cells compared with the control (Fig. 6D). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CDH1 | down-regulates quantity by destabilization
binding
|
FBXO31 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277377 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 29343641 |
Here we show that the low levels of FBXO31 are maintained through proteasomal degradation by anaphase-promoting complex/cyclosome (APC/C). We find that the APC/C coactivators CDH1 and CDC20 bind to a destruction-box (D-box) motif present in FBXO31 to promote its polyubiquitination and degradation in a cell-cycle-regulated manner, which requires phosphorylation of FBXO31 on serine-33 by the prosurvival kinase AKT. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HDAC4 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275663 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 25726523 |
GATA1 is a new substrate of p21-activated kinase 5 (PAK5), which is phosphorylated on serine 161 and 187 (S161 and S187). GATA1 recruits HDAC3/4 to E-cadherin promoter, which is reduced by GATA1 S161A S187A mutant. These data indicate that phosphorylated GATA1 recruits more HDAC3/4 to promote transcriptional repression of E-cadherin, leading to the EMT of breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YBX1 | up-regulates quantity by expression
transcriptional regulation
|
CDH1 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255610 |
|
|
Homo sapiens |
Ovary Cancer Cell |
| pmid |
sentence |
| 17072343 |
YB-1 knockdown by siRNA upregulated 344 genes, including MDR1, thymidylate synthetase, S100 calcium binding protein and cyclin B, and downregulated 534 genes, including CXCR4, N-myc downstream regulated gene 1, E-cadherin and phospholipase C. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDH1 | up-regulates activity
binding
|
CTNNB1 |
0.959 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265863 |
|
|
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 |
| + |
SNAI2 | down-regulates quantity by repression
transcriptional regulation
|
CDH1 |
0.669 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255155 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15311212 |
known E-cadherin transcriptional repressors, such as SLUG (SNAI2), SIP1 (ZEB2), TWIST1, SNAIL (SNAI1) and ZEB1 (TCF8), but not E12/E47 (TCF3), had a lack of upregulation in cells expressing mutated E-cadherin compared to WT. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNAI1 | down-regulates quantity
transcriptional regulation
|
CDH1 |
0.75 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252260 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19055748 |
Taken together these results suggest that SNAI1 functional blockade is leading to partial re-expression of E-cadherin (i.e. at the level of transcription), to a decrease in PAI-1 and to a more collective migration, while the parental cells expressing SNAI1 have less E-cadherin, more PAI 1, and migrate individually. We suggest that the present study establishes a relation between SNAI1 function, PAI-1 distribution and EMT status. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTNND2 | up-regulates quantity by stabilization
binding
|
CDH1 |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252134 |
|
|
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 |
3.0
CDH1
- 
- 