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- W995556031 abstract "The tyrosine kinase activity of Hek has been formally demonstrated in vitro. Although the in vivo function(s) of Hek has yet to be confirmed, the expression pattern of Hek in both B and T lymphoid cell lines, and in a subset of poorly differentiated acute leukemias, suggests that the molecule may act as a growth factor receptor in normal lymphoid precursor cells, and in some hematopoietic malignancies. The isolation of the murine and avian homologues of Hek (Mek4 and Cek4, respectively) from embryonic tissues may also suggest a role for Hek in development. The predicted protein product of HEK cDNA has the features of a type lA integral membrane protein. Amino acid sequence of peptides derived from purified Hek confirmed E21 as the N-terminal residue of the mature protein. The extracellular domain of 521 residues contains five possible sites for N-linked glycosylation and comprises a Cys-rich region and two regions with homology to fibronectin type III repeats. The cytoplasmic domain contains a characteristic PTK domain. Other features include a putative autophosphorylation site and three possible PI-3-kinase binding sites." @default.
- W995556031 created "2016-06-24" @default.
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- W995556031 date "1995-01-01" @default.
- W995556031 modified "2023-09-25" @default.
- W995556031 title "Hek" @default.
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- W995556031 doi "https://doi.org/10.1016/b978-012324719-3/50172-2" @default.
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