| + |
CAMK1 | up-regulates activity 
phosphorylation
|
GCM1 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262680 |
Ser47 |
YAKHIYSsEDKNAQR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21791615 |
We show that Epac1 and Rap1, in response to cAMP, activate CaMKI to phosphorylate Ser47 in GCM1. This phosphorylation facilitates the interaction between GCM1 and the desumoylating enzyme SENP1 and thereby leads to GCM1 desumoylation and activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW2 | down-regulates quantity 
binding
|
GCM1 |
0.559 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271524 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15640526 |
FBW2 targets GCMa to the ubiquitin-proteasome degradation system. Here, we report the identification of an SCF complex as the GCM ubiquitin-protein isopeptide ligase (E3) that regulates human GCMa (hGCMa) degradation. We found that SKP1 and CUL1, two key components of the SCF complex, associate with hGCMa in vivo. We further identify the human F-box protein FBW2 (hFBW2) as the substrate recognition subunit in the SCF E3 complex for hGCMa. We show that hFBW2 interacts with hGCMa in a phosphorylation-dependent manner and promotes hGCMa ubiquitination. Supporting a critical role for hFBW2 in hGCMa degradation, knockdown of hFBW2 expression by RNA interference leads to a reduction in hGCMa ubiquitination and a concomitant increase in hGCMa protein stability. Our study identifies the SCF(hFBW2) E3 complex as the key machinery that targets hGCMa to the ubiquitin-proteasome degradation system |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW2 | down-regulates quantity by destabilization
polyubiquitination
|
GCM1 |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271528 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15640526 |
FBW2 targets GCMa to the ubiquitin-proteasome degradation system. Here, we report the identification of an SCF complex as the GCM ubiquitin-protein isopeptide ligase (E3) that regulates human GCMa (hGCMa) degradation. We found that SKP1 and CUL1, two key components of the SCF complex, associate with hGCMa in vivo. We further identify the human F-box protein FBW2 (hFBW2) as the substrate recognition subunit in the SCF E3 complex for hGCMa. We show that hFBW2 interacts with hGCMa in a phosphorylation-dependent manner and promotes hGCMa ubiquitination. Supporting a critical role for hFBW2 in hGCMa degradation, knockdown of hFBW2 expression by RNA interference leads to a reduction in hGCMa ubiquitination and a concomitant increase in hGCMa protein stability. Our study identifies the SCF(hFBW2) E3 complex as the key machinery that targets hGCMa to the ubiquitin-proteasome degradation system |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SENP1 | up-regulates activity
desumoylation
|
GCM1 |
0.485 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262681 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21791615 |
We show that Epac1 and Rap1, in response to cAMP, activate CaMKI to phosphorylate Ser47 in GCM1. This phosphorylation facilitates the interaction between GCM1 and the desumoylating enzyme SENP1 and thereby leads to GCM1 desumoylation and activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
GCM1
- 
- 