@article{oai:sapmed.repo.nii.ac.jp:00014234,
 author = {Sasaki, Hiroko and Nagura, Kazuko and Ishino, Masaho and Ohba, Takeaki and Matsuya, Manabu and Sasaki, Terukatsu},
 journal = {Tumor Research, Tumor Research},
 month = {},
 note = {Cell adhesion kinase beta (CAKbeta) is the second protein-tyrosine kinase (PTK) of the focal adhesion kinase (FAK) subfamily with large N- and C-domains in addition to the central kinase domain but without Src homology 2 and 3 (SH-2 and SH-3) domains. In this paper, cloning and sequencing of a cDNA encoding human CAKβ are described. A full-length clone (clone B) contained 4,157- base pairs of human CAKβ cDNA including 243-base pairs of the 5'-untranslated sequence and 881-base pairs of the 3'-untranslated sequence with a polyadenyla-tion signal (ATTAAA). The clone B of human CAKβ cDNA has an open read-ing frame encoding 1009 amino acid residues ; the human CAKβ has the same number of amino acid residues in the N-, C-, and kinase-domains as rat CAKβ . The amino acid sequence of human CAKβ is 95.4% identical with that of rat CAKβ . The species difference is most prominent in the C-domain. All three previously-recognized, subfamily-specific residues in the kinase domains of FAK and the rat CAKβ are also found in the human CAKβ . The residues V??? and A???, which have been considered to be characteristic to CAKβ , are found to be conserved also in the human CAK? . It has been postulated that CAKβ is important as a docking protein. The autophosphorylation site and also the ligand site to the SH-2 domains of the Src-family PTKs, Y???AEI, are found to be conserved in the human CAKβ . The ligand sequence for the Grb2 SH-2 domain, Y???HNV of the rat CAKβ , is found functionally conserved in the human CAKβ , Y???LNV. The third ligand sequence, E???PPPKPSR, participating in the binding to the SH-3 domains of pp130cas and Efs, is also found conserved in the human CAKβ . The extreme N- terminal 88 amino acid residues of the rat CAKβ were previously found entirely different from FAK and found unique to CAK? . Ninety four percent of those 88 residues in the human CAKβ are found identical with the rat CAKβ . This high sequence homology strongly suggeststhat this region is involved in the specific function of CAKβ different from FAK.},
 pages = {37--46},
 title = {Cloning of a cDNA for the Human Cell Adhesion Kinase  β},
 volume = {30},
 year = {1995}
}