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Using the CHO1 monoclonal antibody, Sellitto and Kuriyama (1988) identified a spindle antigen that was shown by Nislow et al. (1990) to be required for mitotic progression. By using the CHO1 antibody to screen a HeLa cell cDNA library, Nislow et al. (1992) isolated a KNSL5 cDNA, which they called MKLP1 (mitotic kinesin-like protein-1), that encodes this antigen. The N-terminal region of the deduced 961-amino acid protein contains a 350-residue domain that shares 30 to 45% identity with the motor domains of other members of the kinesin superfamily. The C-terminal region shows little identity with other kinesins. A central region contains heptad repeats of hydrophobic residues that may assemble into a coiled-coil structure similar to kinesin and myosin heavy chain proteins. The protein also contains a putative nuclear localization signal and 2 consensus phosphorylation sites characteristic of nuclear proteins.
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