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
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
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.
Publication
Oligomeric structure of the human EphB2 receptor SAM domain.
The sterile alpha motif (SAM) domain is a protein interaction module that is present in diverse signal-transducing proteins. SAM domains are known to form homo- and hetero-oligomers. The crystal structure of the SAM domain from an Eph receptor tyrosine kinase, EphB2, reveals two large interfaces. In one interface, adjacent monomers exchange amino-terminal peptides that insert into a hydrophobic groove on ... [more]
Throughput
- Low Throughput
Additional Notes
- Crystallized fragment
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| EPHB2 EPHB2 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 677324 |
Curated By
- BioGRID