Open Access Articles- Top Results for EPHB3


SymbolsEPHB3 ; ETK2; HEK2; TYRO6
External IDsOMIM601839 MGI104770 HomoloGene20938 IUPHAR: 1832 ChEMBL: 4901 GeneCards: EPHB3 Gene
EC number2.7.10.1
RNA expression pattern
File:PBB GE EPHB3 1438 at tn.png
File:PBB GE EPHB3 204600 at tn.png
More reference expression data
RefSeq (mRNA)NM_004443NM_010143
RefSeq (protein)NP_004434NP_034273
Location (UCSC)Chr 3:
184.28 – 184.3 Mb
Chr 16:
21.2 – 21.22 Mb
PubMed search[1][2]

Ephrin type-B receptor 3 is a protein that in humans is encoded by the EPHB3 gene.[1][2]


Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of 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. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members.[2]


EPHB3 has been shown to interact with MLLT4[3] and RAS p21 protein activator 1.[4]


  1. ^ Böhme B, Holtrich U, Wolf G, Luzius H, Grzeschik KH, Strebhardt K et al. (Oct 1993). "PCR mediated detection of a new human receptor-tyrosine-kinase, HEK 2". Oncogene 8 (10): 2857–62. PMID 8397371. 
  2. ^ a b "Entrez Gene: EPHB3 EPH receptor B3". 
  3. ^ Hock B, Böhme B, Karn T, Yamamoto T, Kaibuchi K, Holtrich U et al. (Aug 1998). "PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor". Proc. Natl. Acad. Sci. U.S.A. 95 (17): 9779–84. PMC 21413. PMID 9707552. doi:10.1073/pnas.95.17.9779. 
  4. ^ Hock B, Böhme B, Karn T, Feller S, Rübsamen-Waigmann H, Strebhardt K (Jul 1998). "Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions". Oncogene 17 (2): 255–60. PMID 9674711. doi:10.1038/sj.onc.1201907. 

Further reading


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