+ |
TRIM62 | up-regulates activity
polyubiquitination
|
CARD9 |
0.525 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272420 |
Lys125 |
LLMTEVMkLQKKVQD |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
26488816 |
We identified TRIM62 as a CARD9 binding partner and showed that TRIM62 facilitated K27-linked poly-ubiquitination of CARD9. We identified K125 as the ubiquitinated residue on CARD9 and demonstrated that this ubiquitination was essential for CARD9 activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
TRIM62 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270964 |
|
|
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 |
+ |
TRIM62 | down-regulates quantity by destabilization
polyubiquitination
|
TRIM62 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272102 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23402750 |
A ubiquitination assay performed in HEK293T cells further confirmed the E3 ubiquitin ligase activity and self-ubiquitination activity of TRIM62 and the requirement of the RING finger domain. Importantly, the treatment of HEK293T cells with a proteasome inhibitor stabilized poly-ubiquitinated TRIM62, indicating that self-ubiquitination promoted the proteasomal degradation of TRIM62. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |