| + |
DMD | form complex 
binding
|
DGC |
0.682 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255998 |
|
|
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: |
1 |
Organism: |
Homo Sapiens |
| + |
ANK2 | up-regulates quantity 
relocalization
|
DMD |
0.546 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266712 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 19109891 |
We present evidence for an ankyrin-based mechanism for sarcolemmal localization of dystrophin and beta-DG. Ankyrin-B thus is an adaptor required for sarcolemmal localization of dystrophin, as well as dynactin-4. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Skeletal Muscle |
| + |
ANK3 | up-regulates quantity
relocalization
|
DMD |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266715 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 19109891 |
We present evidence for an ankyrin-based mechanism for sarcolemmal localization of dystrophin and beta-DG. Ankyrin-B thus is an adaptor required for sarcolemmal localization of dystrophin, as well as dynactin-4. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Skeletal Muscle |
3.0
DMD
- 
- 