| + |
RNF167 | down-regulates quantity by destabilization 
ubiquitination
|
VAMP3 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272093 |
Lys66 |
QFETSAAkLKRKYWW |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23353890 |
Here, we show that Godzilla/RNF167 regulates endosome recycling by the ubiquitylation of VAMP3 on Lys66, Lys68 and Lys77; namely, two adjacent Lys residues on the both sides of the critical interface of SNARE complex are ubiquitylated. In agreement with VAMP3 being a target for Goliath family ubiquitin ligases, we show that recycling endosome trafficking is abrogated in response to their activity. While we observed ubiquitylation of VAMP3 by Godzilla, we are unable to describe the nature of this ubiquitination, be it mono-ubiquitin or extended ubiquitin chains. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272094 |
Lys68 |
ETSAAKLkRKYWWKN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23353890 |
Here, we show that Godzilla/RNF167 regulates endosome recycling by the ubiquitylation of VAMP3 on Lys66, Lys68 and Lys77; namely, two adjacent Lys residues on the both sides of the critical interface of SNARE complex are ubiquitylated. In agreement with VAMP3 being a target for Goliath family ubiquitin ligases, we show that recycling endosome trafficking is abrogated in response to their activity. While we observed ubiquitylation of VAMP3 by Godzilla, we are unable to describe the nature of this ubiquitination, be it mono-ubiquitin or extended ubiquitin chains. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272095 |
Lys77 |
KYWWKNCkMWAIGIT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23353890 |
Here, we show that Godzilla/RNF167 regulates endosome recycling by the ubiquitylation of VAMP3 on Lys66, Lys68 and Lys77; namely, two adjacent Lys residues on the both sides of the critical interface of SNARE complex are ubiquitylated. In agreement with VAMP3 being a target for Goliath family ubiquitin ligases, we show that recycling endosome trafficking is abrogated in response to their activity. While we observed ubiquitylation of VAMP3 by Godzilla, we are unable to describe the nature of this ubiquitination, be it mono-ubiquitin or extended ubiquitin chains. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
VAMP3 | form complex 
binding
|
LE-TGN SNARE |
0.716 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253082 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18195106 |
We show in human cells that a soluble NSF attachment protein receptor (SNARE) complex comprised of syntaxin 10 (STX10), STX16, Vti1a, and VAMP3 is required for this MPR transport |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BVES | up-regulates activity 
binding
|
VAMP3 |
0.432 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-237771 |
|
|
in vitro |
|
| pmid |
sentence |
| 20057356 |
Taken together, these data demonstrate that Bves interacts with VAMP3 and facilitates receptor recycling both in vitro and during early development. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
VAMP3
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