| + |
UBE2E1 | up-regulates activity 
binding
|
RNF167 |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271552 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16314844 |
Here, we present evidences indicating that RING105, a novel conserved RING-finger protein with a PA (protease-associated) domain and a PEST sequence, is a ubiquitin ligase for TSSC5 that can function in concert with the ubiquitin-conjugating enzyme UbcH6. The polyubiquitin target site on TSSC5 was mapped to a region in the 6th hydrophilic loop. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ub:E1 (UBA6 substrate) | up-regulates activity
ubiquitination
|
UBE2E1 |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271359 |
|
|
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 |
| + |
Ub:E1 (UBA1 substrate) | up-regulates activity
ubiquitination
|
UBE2E1 |
0.709 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271325 |
|
|
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 |
| + |
UBE2E1 | up-regulates activity
binding
|
MPG |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271929 |
|
|
in vitro |
|
| pmid |
sentence |
| 25207814 |
Here we report that MID1 catalyzes the in vitro ubiquitination of the catalytic subunit of PP2A (PP2Ac) in the absence of alpha4. In the presence of alpha4, the level of PP2Ac ubiquitination is reduced.The high molecular weight smear pattern was not as obvious, suggesting that domains within the C-terminal half of MID1 may contribute to the polyubiquitination of PP2Ac. We observed that PP2Ac was ubiquitinated in the presence of UbcH5a-c and UbcH6, similar to results obtained with MID1-catalyzed ubiquitination of alpha4 (Figure 2E) |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
UBE2E1 | up-regulates activity
binding
|
ZSWIM2 |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271555 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16522193 |
MEX can act as an E3, Ub (ubiquitin) ligase, through the E2, Ub-conjugating enzymes UbcH5a, UbcH5c or UbcH6. A region of MEX that contains the RING fingers and the ZZ zinc finger was required for interaction with UbcH5a and MEX self-association, whereas the SWIM domain was critical for MEX ubiquitination. The expression of MEX promoted apoptosis that was induced through Fas, DR (death receptor) 3 and DR4 signalling, but not that mediated by the BH3 (Bcl-2 homology 3)-only protein BimEL or the chemotherapeutic drug adriamycin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
UBE2E1
- 
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