Ephb6
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).
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).
Post-translational modifications
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.
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.
Cellular localization
- Isoform 1
- Cell membrane
- Single-pass type I membrane protein
- Isoform 2
- Secreted
- Isoform 3
- Secreted
Alternative names
Cekl, Ephrin type-B receptor 6, MEP, Tyrosine-protein kinase-defective receptor EPH-6