This gene encodes a member of the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. The protein encoded by this gene functions as a receptor for ephrin A2, A3 and A5 and plays a role in short-range contact-mediated axonal guidance during development of the mammalian nervous system.[6]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Chan J, Watt VM (Aug 1991). "eek and erk, new members of the eph subclass of receptor protein-tyrosine kinases". Oncogene. 6 (6): 1057–61. PMID1648701.
^Choi S, Park S (Sep 1999). "Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn binding to the Tyr-615 site by enhancing tyrosine kinase activity". Oncogene. 18 (39): 5413–22. doi:10.1038/sj.onc.1202917. PMID10498895. S2CID11001580.
Holder N, Klein R (1999). "Eph receptors and ephrins: effectors of morphogenesis". Development. 126 (10): 2033–44. doi:10.1242/dev.126.10.2033. PMID10207129.
Wilkinson DG (2000). Eph receptors and ephrins: regulators of guidance and assembly. International Review of Cytology. Vol. 196. pp. 177–244. doi:10.1016/S0074-7696(00)96005-4. ISBN 978-0-12-364600-2. PMID10730216. {{cite book}}: |journal= ignored (help)
Park S, Sánchez MP (1997). "The Eek receptor, a member of the Eph family of tyrosine protein kinases, can be activated by three different Eph family ligands". Oncogene. 14 (5): 533–42. doi:10.1038/sj.onc.1200857. PMID9053851. S2CID21779523.
Choi S, Park S (1999). "Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn binding to the Tyr-615 site by enhancing tyrosine kinase activity". Oncogene. 18 (39): 5413–22. doi:10.1038/sj.onc.1202917. PMID10498895. S2CID11001580.