EPHA8

EPHA8
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesEPHA8, EEK, EK3, HEK3, EPH receptor A8
External IDsOMIM: 176945; MGI: 109378; HomoloGene: 22436; GeneCards: EPHA8; OMA:EPHA8 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001006943
NM_020526

NM_007939

RefSeq (protein)

NP_001006944
NP_065387

NP_031965

Location (UCSC)Chr 1: 22.56 – 22.6 MbChr 4: 136.93 – 136.96 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ephrin type-A receptor 8 is a protein that in humans is encoded by the EPHA8 gene.[5][6]

Function

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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]

Interactions

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EPHA8 has been shown to interact with FYN.[7]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000070886Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028661Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. PMID 1648701.
  6. ^ a b "Entrez Gene: EPHA8 EPH receptor A8".
  7. ^ 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. PMID 10498895. S2CID 11001580.

Further reading

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