| + |
PPM1G | up-regulates quantity by stabilization 
dephosphorylation
|
SNRPN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277021 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17984321 |
Dephosphorylation of survival motor neurons (SMN) by PPM1G and PP2Cgamma governs Cajal body localization and stability of the SMN complex.|This indicates that the catalytic activity of PPM1G promotes accumulation of the SMN complex in CBs and suggests that PPM1G is a major determinant of the SMN-complex localization in the nucleus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TDRD3 |
binding
|
SNRPN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253518 |
|
|
in vitro |
|
| pmid |
sentence |
| 15955813 |
the TDRD3 GST-Tudor protein interacted strongly with methylated SmB/B′ and SmD but not with SmE. These results suggest that the Tudor domains of SMN and SPF30 likely interact with assembled snRNPs, whereas the Tudor domain of TDRD3 might bind unassembled methylated Sm proteins. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MIB1 | down-regulates quantity by destabilization 
ubiquitination
|
SNRPN |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278632 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23615451 |
These data indicate that Mib1 reduces SMN protein stability by targeting it for degradation by the proteasome and represents a new modifier of the SMA phenotype.|Through this study, we provide evidence that the E3 ligase Mib1 ubiquitinates and catalyzes SMN protein degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SNRPN
- 
- 