Kinesins are a superfamily of related motor proteins that use a microtubule track in anterograde movement. They are vital to spindle formation in mitotic and meiotic  chromosome separation during cell division and are also responsible for shuttling mitochondria, Golgi bodies, and vesicles within eukaryotic cells. Kinesins have two heavy chains and two light chains per active motor. The two globular head motor domains in heavy chains can convert the chemical energy of ATP hydrolysis into mechanical work to move along microtubules. The direction in which cargo is transported can be towards the plus-end or the minus-end, depending on the type of kinesin. In general, kinesins with N-terminal motor domains move their cargo towards the plus ends of microtubules located at the cell periphery, while kinesins with C-terminal motor domains move cargo towards the minus ends of microtubules located at the nucleus. Fourteen distinct kinesin families are known, with some additional kinesin-like proteins that cannot be classified into these families.
Genomic representation of kinesin motors:
* Fungi (yeast): 6
* Plants (Arabidopsis thaliana): 61
* Insects (Drosophila melanogaster): 25
* Mammals (human): 45