EPHB2
Gene Ontology Biological Process
- angiogenesis [ISS]
- axon guidance [ISS, TAS]
- axonal fasciculation [ISS]
- commissural neuron axon guidance [ISS]
- corpus callosum development [ISS]
- dendritic spine development [ISS]
- dendritic spine morphogenesis [ISS]
- ephrin receptor signaling pathway [ISS]
- inner ear morphogenesis [ISS]
- nervous system development [TAS]
- palate development [ISS]
- peptidyl-tyrosine phosphorylation [ISS]
- phosphorylation [ISS]
- positive regulation of synapse assembly [ISS]
- regulation of body fluid levels [ISS]
- urogenital system development [ISS]
Gene Ontology Molecular Function
YES1
Gene Ontology Biological Process
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- T cell costimulation [TAS]
- blood coagulation [TAS]
- cell differentiation [IBA]
- cellular protein modification process [TAS]
- cellular response to peptide hormone stimulus [IBA]
- innate immune response [IBA, TAS]
- leukocyte migration [TAS]
- peptidyl-tyrosine autophosphorylation [IBA]
- regulation of cell proliferation [IBA]
- regulation of vascular permeability [TAS]
- transmembrane receptor protein tyrosine kinase signaling pathway [IBA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region.
The cellular components of the neuronal signaling pathways of Eph receptor tyrosine kinases are only beginning to be elucidated. Here we show that in vivo tyrosine phosphorylation sites of the Eph receptors EphA3, EphA4, and EphB2 in embryonic retina serve as binding sites for the Src-homology 2 (SH2) domain of Src kinase. Furthermore, tyrosine-phosphorylated EphB2 was detected in Src immunoprecipitates ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID