+ |
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 |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF167 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271224 |
|
|
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 |
+ |
UBE2E1 | up-regulates activity
binding
|
RNF167 |
0.554 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271552 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16314844 |
Here, we present evidences indicating that RING105, a novel conserved RING-finger protein with a PA (protease-associated) domain and a PEST sequence, is a ubiquitin ligase for TSSC5 that can function in concert with the ubiquitin-conjugating enzyme UbcH6. The polyubiquitin target site on TSSC5 was mapped to a region in the 6th hydrophilic loop. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF167 | down-regulates quantity by destabilization
polyubiquitination
|
SLC22A18 |
0.541 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271551 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16314844 |
Here, we present evidences indicating that RING105, a novel conserved RING-finger protein with a PA (protease-associated) domain and a PEST sequence, is a ubiquitin ligase for TSSC5 that can function in concert with the ubiquitin-conjugating enzyme UbcH6. The polyubiquitin target site on TSSC5 was mapped to a region in the 6th hydrophilic loop. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |