| + |
Ub:E2 | up-regulates activity 
ubiquitination
|
PDZRN3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271069 |
|
|
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 |
| + |
PDZRN3 | down-regulates quantity 
ubiquitination
|
MUSK |
0.565 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271664 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 17576800 |
We have identified a PDZ domain containing RING finger 3 (PDZRN3) as a synapse-associated E3 ubiquitin ligase and have demonstrated that it regulates the surface expression of muscle-specific receptor tyrosine kinase (MuSK), the key organizer of postsynaptic development at the mammalian neuromuscular junction. PDZRN3 binds to MuSK and promotes its ubiquitination. Together, these data demonstrate that PDZRN3 is a catalytically active RING-type E3 ubiquitin ligase |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
UBE2D2 | up-regulates activity
binding
|
PDZRN3 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271663 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 17576800 |
Our initial tests of various E2s showed that the RING domain of PDZRN3 exhibits ubiquitin ligase activity in the presence of E1 and the UbcH5 family of E2 enzymes (Fig. 3 A). Consistent with this finding, GST pull-down assays showed that PDZRN3 directly interacts with the UbcH5B ubiquitin conjugating enzyme (Fig. 3 B). |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
3.0
PDZRN3
- 
- 