| + |
HSPA1B | up-regulates quantity by stabilization 
binding
|
PACRG |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272891 |
|
|
in vitro |
|
| pmid |
sentence |
| 12150907 |
Our in vitro data suggest that CHIP competes with Hsp70 in binding to Parkin, probably via suppression of the ATPase activity of Hsc/Hsp70 (Figure 4E).In fact, it acts as an inhibitory factor that suppresses the ubiquitination of Pael-R mediated by Parkin in vitro, and Hsp70 enhances the efficiency of folding of overexpressed Pael-R in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKN | down-regulates quantity by destabilization 
polyubiquitination
|
PACRG |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272889 |
|
|
in vitro |
|
| pmid |
sentence |
| 12150907 |
In this study, we found that CHIP promotes Parkin-mediated Pael-R ubiquitination and subsequent degradation. In vitro ubiquitination assays suggested that only a combination of both Parkin and its cofactor CHIP function as a ubiquitin ligase, which is able to sufficiently ubiquitinate Pael-R in vivo (Figure 6). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HSPA1A | up-regulates quantity by stabilization
binding
|
PACRG |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272890 |
|
|
in vitro |
|
| pmid |
sentence |
| 12150907 |
Our in vitro data suggest that CHIP competes with Hsp70 in binding to Parkin, probably via suppression of the ATPase activity of Hsc/Hsp70 (Figure 4E).In fact, it acts as an inhibitory factor that suppresses the ubiquitination of Pael-R mediated by Parkin in vitro, and Hsp70 enhances the efficiency of folding of overexpressed Pael-R in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
PACRG
- 
- 