+ |
MAPK12 | up-regulates
phosphorylation
|
SNTA1 |
0.655 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-67061 |
Ser193 |
GWDSPPAsPLQRQPS |
Homo sapiens |
|
pmid |
sentence |
10212242 |
Sapk3 phosphorylates alpha1-syntrophin at serine residues 193 and 201 in vitro and phosphorylation is dependent on binding to the pdz domain of alpha1-syntrophin. The finding that sapk3 co-localizes with _1-syntrophin in skeletal muscle, that it binds to the pdz domain of _1-syntrophin, and that phosphorylation of _1-syntrophin depends on this interaction identifies a novel mechanism for targeting a protein kinase to its substrates. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-67065 |
Ser201 |
PLQRQPSsPGPTPRN |
Homo sapiens |
|
pmid |
sentence |
10212242 |
Sapk3 phosphorylates alpha1-syntrophin at serine residues 193 and 201 in vitro and phosphorylation is dependent on binding to the pdz domain of alpha1-syntrophin. The finding that sapk3 co-localizes with _1-syntrophin in skeletal muscle, that it binds to the pdz domain of _1-syntrophin, and that phosphorylation of _1-syntrophin depends on this interaction identifies a novel mechanism for targeting a protein kinase to its substrates. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Tissue: |
Skeletal Muscle |
+ |
SNTA1 | up-regulates
relocalization
|
NOS1 |
0.574 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236916 |
|
|
Homo sapiens |
|
pmid |
sentence |
12456711 |
biochemical studies showed that the N-terminal PDZ domain of nNOS binds to a similar PDZ domain of syntrophin (Fig. 1), a dystrophin-associated protein |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Skeletal Muscle |
+ |
SNTA1 | form complex
binding
|
DGC |
0.521 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255991 |
|
|
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 |