DMD
Gene Ontology Biological Process
- cardiac muscle cell action potential [ISS]
- cardiac muscle contraction [IMP]
- cellular protein complex assembly [ISS]
- cellular protein localization [IMP]
- extracellular matrix organization [TAS]
- motile cilium assembly [TAS]
- muscle filament sliding [TAS]
- muscle organ development [NAS]
- negative regulation of peptidyl-cysteine S-nitrosylation [ISS]
- negative regulation of peptidyl-serine phosphorylation [ISS]
- peptide biosynthetic process [IDA]
- positive regulation of neuron differentiation [IMP]
- positive regulation of neuron projection development [IMP]
- positive regulation of sodium ion transmembrane transporter activity [ISS]
- regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [ISS]
- regulation of cellular response to growth factor stimulus [IMP]
- regulation of heart rate [IMP]
- regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [ISS]
- regulation of ryanodine-sensitive calcium-release channel activity [ISS]
- regulation of skeletal muscle contraction [ISS]
- regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion [ISS]
- regulation of voltage-gated calcium channel activity [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- actin cytoskeleton [TAS]
- cell surface [IDA]
- costamere [IDA]
- cytosol [TAS]
- dystrophin-associated glycoprotein complex [IDA, NAS, TAS]
- filopodium [IDA]
- filopodium membrane [IDA]
- lateral plasma membrane [TAS]
- membrane raft [TAS]
- nucleus [IDA, TAS]
- plasma membrane [TAS]
- protein complex [IDA]
- sarcolemma [IDA]
- syntrophin complex [TAS]
DAG1
Gene Ontology Biological Process
- NLS-bearing protein import into nucleus [IDA]
- cytoskeletal anchoring at plasma membrane [IMP]
- extracellular matrix organization [TAS]
- membrane protein ectodomain proteolysis [IDA]
- microtubule anchoring [IMP]
- modulation by virus of host morphology or physiology [IDA]
- negative regulation of MAPK cascade [IMP]
- negative regulation of cell migration [IMP]
- negative regulation of protein kinase B signaling [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- basement membrane [IDA]
- contractile ring [IDA]
- cytoplasm [IDA]
- dystrophin-associated glycoprotein complex [IDA]
- extracellular region [TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- filopodium [IDA]
- focal adhesion [IDA]
- integral component of membrane [IDA]
- lamellipodium [IDA]
- nucleoplasm [IDA]
- plasma membrane [IDA, TAS]
Affinity Capture-Western
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
Identification and characterization of the dystrophin anchoring site on beta-dystroglycan.
Dystrophin, the product of the Duchenne muscular dystrophy gene, is tightly associated with the sarcolemmal membrane to a large glycoprotein complex. One function of the dystrophin-glycoprotein complex is to link the cytoskeleton to the extracellular matrix in skeletal muscle. However, the molecular interactions of dystrophin with the membrane components of the dystrophin-glycoprotein complex are still elusive. Here, we demonstrate and ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| DMD DAG1 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - |
Curated By
- BioGRID