RAPSN
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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]
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
Interactions of the rapsyn RING-H2 domain with dystroglycan.
Rapsyn, a peripheral membrane protein of skeletal muscle, is necessary for the formation of the highly organized structure of the vertebrate neuromuscular junction. For mice lacking rapsyn, there is a failure of postsynaptic specialization characterized by an absence of nicotinic acetylcholine receptors (nAChRs) and other integral and peripheral membrane proteins such as beta-dystroglycan and utrophin. Dystroglycan is necessary for the ... [more]
Throughput
- Low Throughput
Additional Notes
- assayed using a modified yeast two-hybrid assay examining interaction at the cell membrane
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RAPSN DAG1 | Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments. | Low | - | BioGRID | - |
Curated By
- BioGRID