EFNA2
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ADAM10
Gene Ontology Biological Process
- Notch receptor processing [TAS]
- Notch signaling pathway [ISS, TAS]
- PMA-inducible membrane protein ectodomain proteolysis [IMP]
- cell-cell signaling [NAS]
- collagen catabolic process [TAS]
- constitutive protein ectodomain proteolysis [IDA]
- epidermal growth factor receptor signaling pathway [TAS]
- extracellular matrix disassembly [TAS]
- extracellular matrix organization [TAS]
- in utero embryonic development [ISS]
- integrin-mediated signaling pathway [NAS]
- membrane protein ectodomain proteolysis [IDA, IMP]
- monocyte activation [IMP]
- negative regulation of cell adhesion [IDA, NAS]
- positive regulation of T cell chemotaxis [IMP]
- positive regulation of cell growth [IMP]
- positive regulation of cell migration [IMP]
- positive regulation of cell proliferation [IMP]
- protein phosphorylation [ISS]
- response to tumor necrosis factor [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- Golgi apparatus [IDA]
- Golgi-associated vesicle [IDA]
- cell surface [IDA]
- cytoplasm [ISS]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- integral component of membrane [NAS]
- intracellular membrane-bounded organelle [IDA]
- membrane [IDA]
- nucleus [ISS]
- perinuclear endoplasmic reticulum [IDA]
- plasma membrane [TAS]
- tetraspanin-enriched microdomain [IDA]
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
Regulated cleavage of a contact-mediated axon repellent.
Contact-mediated axon repulsion by ephrins raises an unresolved question: these cell surface ligands form a high-affinity multivalent complex with their receptors present on axons, yet rather than being bound, axons can be rapidly repelled. We show here that ephrin-A2 forms a stable complex with the metalloprotease Kuzbanian, involving interactions outside the cleavage region and the protease domain. Eph receptor binding ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID