background:
The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date (1–3). While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development (1–3). The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8 (Hek3), EphB1 (Hek6), EphB2 (Hek5), EphB3 (Cek10, Hek2), EphB4 (Htk), EphB5 (Hek9) and EphB6 (Mep). Ligands for Eph receptors include ephrin-A4 (LERK-4) which binds EphA3 and EphB1. In addition, ephrin-A2 (ELF-1) has been described as the ligand for EphA4, ephrin-A3 (Ehk1-L) as the ligand for EphA5 and ephrin-B2 (Htk-L) as the ligand for EphB4 (Htk) (4–7).
Function:
Receptor for members of the ephrin-B family. Binds to ephrin-B1 and -B2.
Subunit:
Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses (By similarity).
Subcellular Location:
Cell membrane; Single-pass type I membrane protein. Cell projection, dendrite (By similarity).
Tissue Specificity:
Ubiquitous.
Post-translational modifications:
Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-614 is required for interaction with SH2 domain-containing proteins.
Similarity:
Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.
Contains 2 fibronectin type-III domains.
Contains 1 protein kinase domain.
Contains 1 SAM (sterile alpha motif) domain.
Database links:
UniProtKB/Swiss-Prot: P54753.2
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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