| + |
SNTB1 | down-regulates 
binding,
|
MAPK12 |
0.376 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255901 |
|
|
Mus musculus |
Satellite Cell |
| pmid |
sentence |
| 29681515 |
Basal localization of the p38g/p-Carm1 complex in muscle stem cells occurs via binding to the dystrophin-glycoprotein complex (DGC) through b1-syntrophin. In dystrophin-deficient muscle stem cells undergoing asymmetric division, p38g/b1-syntrophin interactions are abrogated, resulting in enhanced Carm1 phosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255903 |
|
|
Mus musculus |
Satellite Cell |
| pmid |
sentence |
| 29681515 |
[...] suggesting that, during an asymmetric cell division, p38gamma localization would be basally restricted by the DGC complex via its interaction with beta-1-syntrophin. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| Tissue: |
Skeletal Muscle |
| + |
MAPK12/CARM1 | up-regulates activity 
binding
|
SNTB1 |
0.376 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255978 |
|
|
|
|
| pmid |
sentence |
| 29681515 |
Basal localization of the p38γ/p-Carm1 complex in muscle stem cells occurs via binding to the dystrophin-glycoprotein complex (DGC) through β1-syntrophin. In dystrophin-deficient muscle stem cells undergoing asymmetric division, p38γ/β1-syntrophin interactions are abrogated |
|
| Publications: |
1 |
| + |
SNTB1 | form complex 
binding
|
DGC |
0.497 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255979 |
|
|
|
|
| pmid |
sentence |
| 29681515 |
Basal localization of the p38γ/p-Carm1 complex in muscle stem cells occurs via binding to the dystrophin-glycoprotein complex (DGC) through β1-syntrophin. In dystrophin-deficient muscle stem cells undergoing asymmetric division, p38γ/β1-syntrophin interactions are abrogated |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255992 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15117830 |
The DGC is composed of dystrophin (blue), an elongated cytoskeletal protein that links to cytoplasmic γ-actin and the transmembrane components of the DGC. Dystrophin binds to the tail of β-dystroglycan (orange). Dystroglycan is composed of 2 subunits, α and β, each produced from the same gene. Dystroglycan binds to the extracellular matrix protein laminin-α2. The sarcoglycan complex (blue-green) is composed of multiple subunits. Mutations in the genes encoding α-, β-, γ-, and δ-sarcoglycan lead to a similar phenotype as dystrophin mutations and include cardiomyopathy and muscular dystrophy in humans and mice. Additional subcomplexes in the DGC in skeletal muscle include α and β dystrobrevin, the syntrophins, nNOS, and caveolin 3 (pink). |
|
| Publications: |
2 |
Organism: |
, Homo Sapiens |
| Tissue: |
Skeletal Muscle |
3.0
SNTB1
- 
- 