+ |
RNF5 | down-regulates quantity by destabilization
ubiquitination
|
STING1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271484 |
Lys150 |
EISAVCEkGNFNVAH |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19285439 |
The ubiquitin ligase RNF5 regulates antiviral responses by mediating degradation of the adaptor protein MITA. RNF5 targeted MITA at Lys150 for ubiquitination and degradation after viral infection. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF5 | down-regulates quantity by destabilization
ubiquitination
|
MAVS |
0.468 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271488 |
Lys362 |
RAGMVPSkVPTSMVL |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
20483786 |
In this study, we showed that the E3 ubiquitin ligase RING-finger protein 5 (RNF5) interacted with VISA at mitochondria in a viral infection-dependent manner. Domain mapping experiments indicated that the C-terminal transmembrane domain of VISA was required for its interaction with RNF5. RNF5 targeted VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection, whereas knockdown of RNF5 reversed virus-induced downregulation of VISA at the early phase. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271489 |
Lys461 |
GPEENEYkSEGTFGI |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
20483786 |
In this study, we showed that the E3 ubiquitin ligase RING-finger protein 5 (RNF5) interacted with VISA at mitochondria in a viral infection-dependent manner. Domain mapping experiments indicated that the C-terminal transmembrane domain of VISA was required for its interaction with RNF5. RNF5 targeted VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection, whereas knockdown of RNF5 reversed virus-induced downregulation of VISA at the early phase. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
RNF5 | down-regulates quantity by destabilization
ubiquitination
|
SLC26A4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271497 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
22750442 |
E3 ubiquitin ligase Rma1 is involved in Pendrin degradation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF5 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270998 |
|
|
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 |
+ |
RNF5 | down-regulates activity
ubiquitination
|
JKAMP |
0.525 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271483 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19269966 |
RNF5 is a ubiquitin ligase anchored to the ER membrane implicated in ERAD via ubiquitination of misfolded proteins. This association results in Ubc13-dependent RNF5-mediated noncanonical ubiquitination of JAMP. This ubiquitination does not alter JAMP stability but rather inhibits its association with Rpt5 and p97. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF5 | down-regulates quantity by destabilization
ubiquitination
|
CFTR |
0.651 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271494 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21148293 |
JB12 cooperates with cytosolic Hsc70 and the ubiquitin ligase RMA1 to target CFTR and CFTRΔF508 for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HSPA8 | up-regulates activity
binding
|
RNF5 |
0.397 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271493 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21148293 |
JB12 cooperates with cytosolic Hsc70 and the ubiquitin ligase RMA1 to target CFTR and CFTRΔF508 for degradation. JB12 drives Hsc70 to associate with CFTR and the RMA1 E3 complex |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF5 | down-regulates quantity
ubiquitination
|
PXN |
0.416 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271479 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
12861019 |
Here we demonstrate that the human homologue of RNF5 associates with the amino-terminal domain of paxillin, resulting in its ubiquitination. RNF5 requires intact RING and C-terminal domains to mediate paxillin ubiquitination. Concomitantly, RNF5 expression results in inhibition of cell motility. Via targeting of paxillin ubiquitination, which alters its localization, RNF5 emerges as a novel regulator of cell motility. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |