Disease relevance of EPHB3

• OBJECTIVE: The RYK, EPHB2, and EPHB3 genes are attractive candidates for cleft lip and/or palate and cleft palate only pathogenesis [1].
• In a protein kinase assay with HEK 2-specific immunoprecipitates from the human epidermoid carcinoma cell line A431, a protein of 130 kDa was found phosphorylated [2].

High impact information on EPHB3

• This interaction could be inhibited by preincubation of HEK2 expressing cells with soluble LERK-2 [3].
• Membrane-bound and soluble forms of LERK-2 were demonstrated to signal through HEK2 as judged by receptor phosphorylation [3].
• In order to analyze functional effects between the LERKs and the HEK2 receptor, we expressed HEK2 cDNA in an interleukin-3-dependent progenitor cell line 32D that grows as single cells in culture [3].
• Human embryonal kinase 2 (HEK2) is a protein-tyrosine kinase that is a member of the EPH family of receptors [3].
• Transcripts for HEK2 have a wide tissue distribution [3].

Biological context of EPHB3

• Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions [4].
• Sequence analysis of 3.8 kb of overlapping PCR products allowed to identify a novel receptor-PTK, HEK 2 (human embryo kinase 2), as an additional member of this family, without the need to screen a cDNA library [2].

Anatomical context of EPHB3

• The ETK2/TYRO3 receptor is a tyrosine kinase expressed in embryonic stem cells, brain and testis that has recently been cloned by several groups [5].

Associations of EPHB3 with chemical compounds

• Furthermore, we demonstrated that a single amino acid substitution (Y614F) clearly reduces the phosphotyrosine content of HEK2 and abrogates its ability to bind rasGAP, Crk and Fyn indicating that this residue functions as major phosphorylation and multi-docking site [4].

Physical interactions of EPHB3

• Within the group of LERKs, LERK-2 and -5 were shown to bind to HEK2 [3].

Other interactions of EPHB3

• No mutations in EPHB2 and EPHB3 were found in any patients examined [1].

Analytical, diagnostic and therapeutic context of EPHB3

• PCR mediated detection of a new human receptor-tyrosine-kinase, HEK 2 [2].
• Sequence analysis demonstrated that this gene is the ortholog to the previously cloned human Hek2 gene [6].

References