| + |
ACVR1 | up-regulates activity 
binding
|
VPS39 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261376 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12941698 |
TLP interacts with TGF-β and activin receptors in vivo. Endogenous TLP associates with both active and kinase-deficient TGF-beta and activin type II receptors, but interacts with the common-mediator Smad4 only in the presence of TGF-beta/activin signaling. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
TGFBR2 | up-regulates activity
binding
|
VPS39 |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261374 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12941698 |
TLP interacts with TGF-β and activin receptors in vivo. Endogenous TLP associates with both active and kinase-deficient TGF-beta and activin type II receptors, but interacts with the common-mediator Smad4 only in the presence of TGF-beta/activin signaling. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
VPS39 | down-regulates quantity 
binding
|
SMAD3/SMAD4 |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261378 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12941698 |
Overexpression of TLP blocks TGF-β-induced formation of Smad3/4 complexes while it does not alter Smad2/4 complex levels. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
VPS39 | down-regulates activity
relocalization
|
SMAD4 |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261377 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12941698 |
The data demonstrating binding of TLP to TGF-β and activin type II receptors and selective inhibition of Smad3/Smad4 complex formation by deregulated TLP suggest that TLP is involved in localizing these receptors and Smad4 to specific intracellular compartments, where it regulates formation of Smad3/Smad4 but not Smad2/Smad4 complexes. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
VPS39 | form complex 
binding
|
HOPS tethering complex |
0.88 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273690 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23351085 |
The two Vps-C complexes CORVET (class C core vacuole/endosome tethering) and HOPS (homotypic fusion and vacuole protein sorting) perform diverse biochemical functions in endocytosis: they tether membranes, interact with Rab GTPases, activate and proof-read SNARE assembly to drive membrane fusion, and possibly attach endosomes to the cytoskeleton. The core subunits Vps11, Vps16 and Vps18 present the SNARE-interacting Vps33 subunit on one side and bind the Rab GTPase interaction module through Vps3/Vps8 (in CORVET) or Vps39/Vps41 (in HOPS) on the other side (Fig. 3A) The core subunits Vps11, Vps16 and Vps18 present the SNARE-interacting Vps33 subunit on one side and bind the Rab GTPase interaction module through Vps3/Vps8 (in CORVET) or Vps39/Vps41 (in HOPS) on the other side (Fig. 3A) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TGFBR1 | up-regulates activity
binding
|
VPS39 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261375 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12941698 |
TLP interacts with TGF-β and activin receptors in vivo. Endogenous TLP associates with both active and kinase-deficient TGF-beta and activin type II receptors, but interacts with the common-mediator Smad4 only in the presence of TGF-beta/activin signaling. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
3.0
VPS39
- 
- 