| + |
TNIK | up-regulates 
phosphorylation
|
TCF7L2 |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165946 |
Ser177 |
QALKDARsPSPAHIV |
Homo sapiens |
Colonic Cancer Cell |
| pmid |
sentence |
| 20530691 |
Here, we report that tnik is an activating kinase for tcf4 and essential for colorectal cancer growth. Tnik, but not its catalytically inactive mutant, phosphorylated the conserved serine 154 residue of tcf4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | up-regulates activity
phosphorylation
|
TCF7L2 |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250962 |
Ser58 |
ESETNQNsSSDSEAE |
in vitro |
|
| pmid |
sentence |
| 11711551 |
We show here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58-Ser-59-Ser-60. Phosphorylation of these residues does not modify the interaction of Tcf-4 with beta-catenin but reduces its association to plakoglobin. | Experiments performed using a Tcf-4 mutant with decreased interaction to plakoglobin demonstrated that binding to this protein negatively affected the transcriptional activity of Tcf-4. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250963 |
Ser59 |
SETNQNSsSDSEAER |
in vitro |
|
| pmid |
sentence |
| 11711551 |
We show here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58-Ser-59-Ser-60. Phosphorylation of these residues does not modify the interaction of Tcf-4 with beta-catenin but reduces its association to plakoglobin. | Experiments performed using a Tcf-4 mutant with decreased interaction to plakoglobin demonstrated that binding to this protein negatively affected the transcriptional activity of Tcf-4. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250964 |
Ser60 |
ETNQNSSsDSEAERR |
in vitro |
|
| pmid |
sentence |
| 11711551 |
We show here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58-Ser-59-Ser-60. Phosphorylation of these residues does not modify the interaction of Tcf-4 with beta-catenin but reduces its association to plakoglobin. | Experiments performed using a Tcf-4 mutant with decreased interaction to plakoglobin demonstrated that binding to this protein negatively affected the transcriptional activity of Tcf-4. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CSNK2A2 | up-regulates activity
phosphorylation
|
TCF7L2 |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251044 |
Ser58 |
ESETNQNsSSDSEAE |
in vitro |
|
| pmid |
sentence |
| 11711551 |
We show here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58-Ser-59-Ser-60. Phosphorylation of these residues does not modify the interaction of Tcf-4 with beta-catenin but reduces its association to plakoglobin. | Experiments performed using a Tcf-4 mutant with decreased interaction to plakoglobin demonstrated that binding to this protein negatively affected the transcriptional activity of Tcf-4. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251045 |
Ser59 |
SETNQNSsSDSEAER |
in vitro |
|
| pmid |
sentence |
| 11711551 |
We show here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58-Ser-59-Ser-60. Phosphorylation of these residues does not modify the interaction of Tcf-4 with beta-catenin but reduces its association to plakoglobin. | Experiments performed using a Tcf-4 mutant with decreased interaction to plakoglobin demonstrated that binding to this protein negatively affected the transcriptional activity of Tcf-4. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251046 |
Ser60 |
ETNQNSSsDSEAERR |
in vitro |
|
| pmid |
sentence |
| 11711551 |
We show here that Tcf-4 can be phosphorylated in vitro by protein kinase CK2 stoichiometrically in amino acids Ser-58-Ser-59-Ser-60. Phosphorylation of these residues does not modify the interaction of Tcf-4 with beta-catenin but reduces its association to plakoglobin. | Experiments performed using a Tcf-4 mutant with decreased interaction to plakoglobin demonstrated that binding to this protein negatively affected the transcriptional activity of Tcf-4. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
NLK | down-regulates 
phosphorylation
|
TCF7L2 |
0.763 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97819 |
Thr201 |
PHHVHPLtPLITYSN |
Homo sapiens |
|
| pmid |
sentence |
| 12556497 |
Nlk phosphorylates lef-1/tcf on two serine/threonine residues located in its central region. Mutation of both residues to alanine enhanced lef-1 transcriptional activity and rendered it resistant to inhibition by nlk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97873 |
Thr212 |
TYSNEHFtPGNPPPH |
Homo sapiens |
|
| pmid |
sentence |
| 12556497 |
Nlk phosphorylates lef-1/tcf on two serine/threonine residues located in its central region. Mutation of both residues to alanine enhanced lef-1 transcriptional activity and rendered it resistant to inhibition by nlk. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
NLK | down-regulates quantity
phosphorylation
|
TCF7L2 |
0.763 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271597 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16714285 |
NLK Augments the Ubiquitylation Activity of NARF against TCF/LEF. ctivation of NLK induced by unknown ligands leads to the phosphorylation of TCF/LEF. NARF then acts on TCF/LEF as an E3 ubiquitin-ligase and, together with E1 and E2 ubiquitylation enzymes, catalyze the ubiquitylation of TCF/LEF. Finally, ubiquitylated TCF/LEF is degraded by the 26 S proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TCF7L2 | down-regulates activity 
transcriptional regulation
|
Adipogenesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253519 |
|
|
|
|
| pmid |
sentence |
| 20492721 |
These findings suggested that miR-210 could promote adipogenesis by repressing WNT signaling through targeting Tcf7l2. |
|
| Publications: |
1 |
| + |
RNF138 | down-regulates quantity by destabilization
polyubiquitination
|
TCF7L2 |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271593 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16714285 |
Here, we show that NARF induces the ubiquitylation of TCF/LEF in vitro and in vivo, and functions as an E3 ubiquitin-ligase that specifically cooperates with the E2 conjugating enzyme E2-25K. We found that NLK augmented NARF binding and ubiquitylation of TCF/LEF, and this required NLK kinase activity. The ubiquitylated TCF/LEF was subsequently degraded by the proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTNNB1 | up-regulates activity
binding
|
TCF7L2 |
0.897 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85757 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20492721 |
Hypophosphorylation of β-catenin and translocation into the nucleus leads to binding with members of the lymphoid-enhancer-binding factor/T-cell-specific transcription factor (LEF/TCF) family and activation of WNT target genesAs a member of LEF/TCF family, transcription factor 7 like 2 (Tcf7l2, formerly called Tcf4) is an important transcription factor triggering the downstream responsive genes of WNT signaling |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
TCF7L2
- 
- 