+ |
TRIM13 | down-regulates quantity by destabilization
polyubiquitination
|
AKT1 |
0.359 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271852 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21333377 |
Here, we demonstrate that overexpression of RFP2 in cells induced apoptosis through proteasomal degradation of MDM2 and AKT. We observed that RFP2 formed a complex with MDM2, a negative regulator of the p53 tumor suppressor, and AKT, a regulator of apoptosis inhibition at the cellular level. Additionally, we found that the interaction of RFP2 with MDM2 and AKT resulted in ubiquitination and proteasomal degradation of MDM2 and AKT in vivo and in vitro. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM13 | down-regulates quantity by destabilization
polyubiquitination
|
MDM2 |
0.381 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271851 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21333377 |
Here, we demonstrate that overexpression of RFP2 in cells induced apoptosis through proteasomal degradation of MDM2 and AKT. We observed that RFP2 formed a complex with MDM2, a negative regulator of the p53 tumor suppressor, and AKT, a regulator of apoptosis inhibition at the cellular level. Additionally, we found that the interaction of RFP2 with MDM2 and AKT resulted in ubiquitination and proteasomal degradation of MDM2 and AKT in vivo and in vitro. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM13 | down-regulates quantity by destabilization
polyubiquitination
|
TRIM13 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272219 |
|
|
Homo sapiens |
|
pmid |
sentence |
31744379 |
In this study, we showed that the N-degron pathway mediates ubiquitin (Ub)-dependent reticulophagy. During this 2-step process, the ER transmembrane E3 ligase TRIM13 undergoes auto-ubiquitination via lysine 63 (K63) linkage chains and acts as a ligand for the autophagic receptor SQSTM1/p62 (sequestosome 1). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ionizing radiation | up-regulates
|
TRIM13 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271854 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21333377 |
These data suggest that irradiation causes RFP2 overexpression, which enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TRIM13 | down-regulates quantity by destabilization
polyubiquitination
|
AKT2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271853 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21333377 |
Here, we demonstrate that overexpression of RFP2 in cells induced apoptosis through proteasomal degradation of MDM2 and AKT. We observed that RFP2 formed a complex with MDM2, a negative regulator of the p53 tumor suppressor, and AKT, a regulator of apoptosis inhibition at the cellular level. Additionally, we found that the interaction of RFP2 with MDM2 and AKT resulted in ubiquitination and proteasomal degradation of MDM2 and AKT in vivo and in vitro. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
TRIM13 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271145 |
|
|
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 |
+ |
TRIM13 | down-regulates quantity by destabilization
polyubiquitination
|
CD3D |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271644 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17314412 |
RFP2, a gene frequently lost in various malignancies, encodes a protein with RING finger, B-box, and coiled-coil domains that belongs to the RBCC/TRIM family of proteins.Rfp2 Regulates the Stability of the ERAD Substrate CD3-δ. In summary, these experiments demonstrate that Rfp2 functions as a RING-dependent ERAD E3 ubiquitin ligase and regulates the degradation of the ER substrate, CD3-δ. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |