+ |
Ub:E2 | up-regulates activity
ubiquitination
|
ARIH1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271012 |
|
|
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 |
+ |
CUL1 | up-regulates activity
binding
|
ARIH1 |
0.363 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268844 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24076655 |
Here, we provide evidence that Ariadne RBR E3 ubiquitin ligases such as TRIAD1 and HHARI can bind and be activated by CRL complexes. Whereas TRIAD1 specifically associates with CUL5–RBX2, HHARI is more promiscuous towards cullin types and associates with RBX1-associated cullins 1, 2, 3, and 4A. Interestingly, both TRIAD1 and HHARI show a strong preference for binding the neddylated form of the cullin. Our data suggest a novel function of NEDD8 in directing specific CRLs to Ariadne RBR ligases, which in turn exert influence on the levels of their cognate neddylated cullin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ARIH1 | down-regulates quantity by destabilization
ubiquitination
|
EIF4E2 |
0.665 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268848 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
14623119 |
Human homologue of Drosophila ariadne (HHARI) is a RING-IBR-RING domain protein identified through its ability to bind the human ubiquitin-conjugating enzyme, UbcH7. Thus, by promoting the ubiquitin-mediated degradation of 4EHP, HHARI may have a role in both protein degradation and protein translation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CUL4A | up-regulates activity
binding
|
ARIH1 |
0.284 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268847 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24076655 |
Here, we provide evidence that Ariadne RBR E3 ubiquitin ligases such as TRIAD1 and HHARI can bind and be activated by CRL complexes. Whereas TRIAD1 specifically associates with CUL5–RBX2, HHARI is more promiscuous towards cullin types and associates with RBX1-associated cullins 1, 2, 3, and 4A. Interestingly, both TRIAD1 and HHARI show a strong preference for binding the neddylated form of the cullin. Our data suggest a novel function of NEDD8 in directing specific CRLs to Ariadne RBR ligases, which in turn exert influence on the levels of their cognate neddylated cullin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CUL3 | up-regulates activity
binding
|
ARIH1 |
0.319 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268846 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24076655 |
Here, we provide evidence that Ariadne RBR E3 ubiquitin ligases such as TRIAD1 and HHARI can bind and be activated by CRL complexes. Whereas TRIAD1 specifically associates with CUL5–RBX2, HHARI is more promiscuous towards cullin types and associates with RBX1-associated cullins 1, 2, 3, and 4A. Interestingly, both TRIAD1 and HHARI show a strong preference for binding the neddylated form of the cullin. Our data suggest a novel function of NEDD8 in directing specific CRLs to Ariadne RBR ligases, which in turn exert influence on the levels of their cognate neddylated cullin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ARIH1 | down-regulates quantity by destabilization
polyubiquitination
|
CD274 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277553 |
|
|
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
33879767 |
We find EGFR inhibitors promote PD-L1 ubiquitination and proteasomal degradation following GSK3α-mediated phosphorylation of Ser279/Ser283. We identify ARIH1 as the E3 ubiquitin ligase responsible for targeting PD-L1 to degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CUL2 | up-regulates activity
binding
|
ARIH1 |
0.315 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268845 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24076655 |
Here, we provide evidence that Ariadne RBR E3 ubiquitin ligases such as TRIAD1 and HHARI can bind and be activated by CRL complexes. Whereas TRIAD1 specifically associates with CUL5–RBX2, HHARI is more promiscuous towards cullin types and associates with RBX1-associated cullins 1, 2, 3, and 4A. Interestingly, both TRIAD1 and HHARI show a strong preference for binding the neddylated form of the cullin. Our data suggest a novel function of NEDD8 in directing specific CRLs to Ariadne RBR ligases, which in turn exert influence on the levels of their cognate neddylated cullin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |