+ |
VPS18 | down-regulates activity
monoubiquitination
|
GGA3 |
0.506 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271610 |
Lys258 |
LFDQCENkRRTLFKL |
in vitro |
|
pmid |
sentence |
16996030 |
Monoubiquitylation of GGA3 by hVPS18 regulates its ubiquitin-binding ability. By in vitro ubiquitylation assays, we have identified lysine 258 in the GAT domain as a major ubiquitylation site that resides adjacent to the ubiquitin-binding site. Furthermore, the GAT domain ubiquitylated by hVPS18 no longer binds to ubiquitin, indicating that ubiquitylation negatively regulates the ubiquitin-binding ability of the GAT domain. These results suggest that the ubiquitin binding and ubiquitylation of GGA3-GAT domain are mutually inseparable through a ubiquitin ligase activity of hVPS18. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
VPS18 | form complex
binding
|
HOPS tethering complex |
0.906 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273688 |
|
|
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 |
+ |
UBE2D2 | up-regulates activity
binding
|
VPS18 |
0.325 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271549 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16203730 |
VPS18 Ubiquitylates SNK in Vitro and in Vivo. The ubiquitylation of proteins by hVPS18 was selectively mediated by UbcH4. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VPS18 | form complex
binding
|
CORVET tethering complex |
0.865 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273698 |
|
|
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 |
+ |
VPS18 | down-regulates quantity by destabilization
ubiquitination
|
PLK2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271550 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16203730 |
VPS18 Ubiquitylates SNK in Vitro and in Vivo. The ubiquitylation of proteins by hVPS18 was selectively mediated by UbcH4. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
VPS18 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271231 |
|
|
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 |