EOG88971H	GO:0005524	2/21	ATP binding	molecular_function	"Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator." [ISBN:0198506732]
EOG88971H	GO:0005874	2/21	microtubule	cellular_component	"Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle." [ISBN:0879693568]
EOG88971H	GO:0003777	2/21	microtubule motor activity	molecular_function	"Catalysis of movement along a microtubule, coupled to the hydrolysis of a nucleoside triphosphate (usually ATP)." [GOC:mah, ISBN:0815316194]
EOG88971H	GO:0007018	2/21	microtubule-based movement	biological_process	"A microtubule-based process that is mediated by motor proteins and results in the movement of organelles, other microtubules, or other particles along microtubules." [GOC:cjm, ISBN:0815316194]
EOG88971H	GO:0005871	2/21	kinesin complex	cellular_component	"Any complex that includes a dimer of molecules from the kinesin superfamily, a group of related proteins that contain an extended region of predicted alpha-helical coiled coil in the main chain that likely produces dimerization. The native complexes of several kinesin family members have also been shown to contain additional peptides, often designated light chains as all of the noncatalytic subunits that are currently known are smaller than the chain that contains the motor unit. Kinesin complexes generally possess a force-generating enzymatic activity, or motor, which converts the free energy of the gamma phosphate bond of ATP into mechanical work." [GOC:mah, http://www.proweb.org/kinesin//KinesinMotility.html, http://www.proweb.org/kinesin//KinesinStructure.html]