| + |
Ub:E2 | up-regulates activity 
ubiquitination
|
VPS11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271125 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VPS11 | up-regulates activity
binding
|
RDX |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261312 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21148287 |
Vps11 was found to interact with radixin. ERM proteins and the HOPS complex are required for the transition from early to late endosomes. We report that an interaction between subunits of the HOPS complex and the ERM (ezrin, radixin, moesin) proteins is required for the delivery of EGF receptor (EGFR) to lysosomes. Inhibiting either ERM proteins or the HOPS complex leads to the accumulation of the EGFR into early endosomes, delaying its degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VPS11 | up-regulates activity
binding
|
EZR |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261311 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21148287 |
The interaction between the full-length Vps11 and ezrin was confirmed by immunoprecipitation and GST-pull down. ERM proteins and the HOPS complex are required for the transition from early to late endosomes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VPS11 | form complex 
binding
|
CORVET tethering complex |
0.839 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273694 |
|
|
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 |
| + |
VPS11 | form complex
binding
|
HOPS tethering complex |
0.902 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273686 |
|
|
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 |
3.0
VPS11
- 
- 