+ |
RNF126 | down-regulates quantity by destabilization
polyubiquitination
|
EGFR |
0.331 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272103 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
23418353 |
RNF126 and Rabring7 associate with the EGFR through a ubiquitin-binding zinc finger domain and both E3 ubiquitin ligases promote ubiquitylation of EGFR. In HeLa cells depleted of either RNF126 or Rabring7 the EGFR is retained in a late endocytic compartment and is inefficiently degraded. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF126 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270963 |
|
|
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 |
+ |
RNF126 | down-regulates quantity by destabilization
ubiquitination
|
FXN |
0.39 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278663 |
|
|
Homo sapiens |
|
pmid |
sentence |
28228265 |
Depletion of RNF126 by specific small interfering RNA delays the degradation of frataxin precursor and increases its stability.|Here we report on the identification of really interesting new gene finger protein 126 (RNF126) as the E3 ligase that ubiquitinates frataxin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF126 | down-regulates quantity by destabilization
polyubiquitination
|
CDKN1A |
0.334 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272033 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23026136 |
E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation.We showed that RNF126 interacts with p21 and RNF126 overexpression increased p21 protein ubiquitination in an E3 ligase activity-dependent manner. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |