| + |
TGFBI | up-regulates activity 
|
A4/b1 integrin |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253283 |
|
|
Mus musculus |
Endothelial Progenitor Cell |
| pmid |
sentence |
| 25786978 |
First, EPCs incorporated into the neovascular region recognize the TGFBIp secreted by cells in the environment via binding to integrins a4 and a5. Second, binding of TGFBIp to integrins in EPCs induces phosphorylation of intracellular signaling molecules in a pathway necessary for TGFBIp-mediated angiogenic activity of EPCs. In addition, binding of TGFBIp to integrins activates the NF-kappaB signaling pathway that induces expression of DLL1 and JAG1 in EPCs. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
TGFBI | up-regulates activity
binding
|
A3/b1 integrin |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253267 |
|
|
|
|
| pmid |
sentence |
| 26387839 |
BIGH3 binds molecules of the ECM, including fibronectin, laminin and different collagens ( Hashimoto et al., 1997 ; Hanssen et al., 2003) and serves as a ligand for several integrins|BIGH3 has been shown to interact with α3β1, αvβ3, αvβ5, α1β1, α6β4 and α7β1 integrin heterodimers |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253211 |
|
|
Mus musculus |
Retina |
| pmid |
sentence |
| 10906123 |
In addition, we demonstrated the functional receptor for betaig-h3 is alpha(3)beta(1) integrin. These results, therefore, establish the essential motifs within the 2nd and the 4th domains of betaig-h3, which interact with alpha(3)beta(1) integrin to mediate HCE cell adhesion to betaig-h3 and suggest that other proteins containing Asp-Ile in their fas-1 domains could possibly function as cell adhesion molecules. |
|
| Publications: |
2 |
Organism: |
, Mus Musculus |
| + |
TGFBI | up-regulates activity
binding
|
a7/b1 integrin |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253266 |
|
|
|
|
| pmid |
sentence |
| 26387839 |
BIGH3 binds molecules of the ECM, including fibronectin, laminin and different collagens ( Hashimoto et al., 1997 ; Hanssen et al., 2003) and serves as a ligand for several integrins|BIGH3 has been shown to interact with α3β1, αvβ3, αvβ5, α1β1, α6β4 and α7β1 integrin heterodimers |
|
| Publications: |
1 |
| + |
KLF10 | up-regulates quantity by expression
transcriptional regulation
|
TGFBI |
0.244 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253212 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18359287 |
Analyzing the mechanism of TGFBI up-regulation in clear cell carcinoma, we identified a novel VHL target, a Kruppel-like transcriptional factor 10 (KLF10). The TGFBI promoter, which we isolated and studied in Luc-reporter assay, was induced by KLF10 but not hypoxia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TGFBI | up-regulates activity
binding
|
A1/b1 integrin |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253269 |
|
|
|
|
| pmid |
sentence |
| 26387839 |
BIGH3 binds molecules of the ECM, including fibronectin, laminin and different collagens ( Hashimoto et al., 1997 ; Hanssen et al., 2003) and serves as a ligand for several integrins|BIGH3 has been shown to interact with α3β1, αvβ3, αvβ5, α1β1, α6β4 and α7β1 integrin heterodimers |
|
| Publications: |
1 |
| + |
TGFBI | up-regulates activity
binding
|
A6/b4 integrin |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253268 |
|
|
|
|
| pmid |
sentence |
| 26387839 |
BIGH3 binds molecules of the ECM, including fibronectin, laminin and different collagens ( Hashimoto et al., 1997 ; Hanssen et al., 2003) and serves as a ligand for several integrins|BIGH3 has been shown to interact with α3β1, αvβ3, αvβ5, α1β1, α6β4 and α7β1 integrin heterodimers |
|
| Publications: |
1 |
| + |
TGFBI | up-regulates activity
binding
|
Av/b3 integrin |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253270 |
|
|
|
|
| pmid |
sentence |
| 26387839 |
BIGH3 binds molecules of the ECM, including fibronectin, laminin and different collagens ( Hashimoto et al., 1997 ; Hanssen et al., 2003) and serves as a ligand for several integrins|BIGH3 has been shown to interact with α3β1, αvβ3, αvβ5, α1β1, α6β4 and α7β1 integrin heterodimers |
|
| Publications: |
1 |
| + |
TGFBI | up-regulates activity
binding
|
Av/b5 integrin |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253271 |
|
|
|
|
| pmid |
sentence |
| 26387839 |
BIGH3 binds molecules of the ECM, including fibronectin, laminin and different collagens ( Hashimoto et al., 1997 ; Hanssen et al., 2003) and serves as a ligand for several integrins|BIGH3 has been shown to interact with α3β1, αvβ3, αvβ5, α1β1, α6β4 and α7β1 integrin heterodimers |
|
| Publications: |
1 |
| + |
TGFBI | up-regulates activity
|
A5/b1 integrin |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253284 |
|
|
Mus musculus |
Endothelial Progenitor Cell |
| pmid |
sentence |
| 25786978 |
First, EPCs incorporated into the neovascular region recognize the TGFBIp secreted by cells in the environment via binding to integrins a4 and a5. Second, binding of TGFBIp to integrins in EPCs induces phosphorylation of intracellular signaling molecules in a pathway necessary for TGFBIp-mediated angiogenic activity of EPCs. In addition, binding of TGFBIp to integrins activates the NF-kappaB signaling pathway that induces expression of DLL1 and JAG1 in EPCs. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
TGFBI
- 
- 