Function: Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2
By similarity.
Subunit structure: Interacts with CBL and EPHB1. Interacts with FYN; this interaction takes place in a ligand-independent manner
By similarity.
Subcellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted. Isoform 3: Secreted.
Tissue specificity: High level in thymus, and brain. Very low levels of expression in kidney, lung, liver, bone marrow, skeletal muscle, spleen from 2 week old and adult mice, heart, testes and embryonic stem cells. Ref.1
Domain: The protein kinase domain is predicted to be catalytically inactive. Its extracellular domain is capable of promoting cell adhesion and migration in response to low concentrations of ephrin-B2, but its cytoplasmic domain is essential for cell repulsion and inhibition of migration induced by high concentrations of ephrin-B2
By similarity.
Post-translational modification: Ligand-binding increases phosphorylation on tyrosine residues. Phosphorylation on tyrosine residues is mediated by transphosphorylation by the catalytically active EPHB1 in a ligand-independent manner. Tyrosine phosphorylation of the receptor may act as a switch on the functional transition from cell adhesion/attraction to de-adhesion/repulsion
By similarity.
Sequence similarities: Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.Contains 1 Eph LBD (Eph ligand-binding) domain.Contains 2 fibronectin type-III domains.Contains 1 protein kinase domain.Contains 1 SAM (sterile alpha motif) domain.
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