EC Number   |
Natural Substrates |
|---|
   5.6.1.3 | ATP + H2O + a kinesin associated with a microtubule at position n |
kinesin-2 is required for the normal steady-state localization of late endosomes/lysosomes but not early ensosomes or recycling endosomes. Kinesin-2 contributes significantly to the plus-end-directed movement of late endosomes and lysosomes |
| 5.6.1.3 | ATP + H2O + a kinesin associated with a microtubule at position n |
kinesin-5 Eg5 drives the sliding of microtubules depending on their relative orientation. Eg5 has the capability of simultaneously moving at about 20 nm/s towards the plus-ends of each of the two microtubules it crosslinks. For anti-parallel microtubules, this results in relative sliding at about 40 nm/s, comparable to spindle pole separation rates in vivo. Eg5 can tether microtubule plus-ends, suggesting an additional microtubule-binding mode for Eg5 |
| 5.6.1.3 | ATP + H2O + a kinesin associated with a microtubule at position n |
Kip3p destabilizes microtubules by depolymerizing them. Kip3p disassembles microtubules exclusively at the plus end and depolymerizes longer microtubules faster than shorter ones |
| 5.6.1.3 | ATP + H2O + a kinesin associated with a microtubule at position n |
Kip3P is both a plus-end-specific depolymerase and a plus end-directed motor |
| 5.6.1.3 | ATP + H2O + a kinesin associated with a microtubule at position n |
monomeric kinesin Eg5 has a motor tightly bound to the microtubule during a majority of its ATPase cycle to generate and sustain force in the mitotic spindle |
| 5.6.1.3 | ATP + H2O + a kinesin associated with a microtubule at position n |
plus-end-enriched motor that targets regions of podosome turnover. Kinesin KIF1C is a central player in the microtubule-dependent regulation of podosomes. The KIF1C-myosin IIA interface may play a role in facilitating podosomes dynamics in a subcellular fine-tuned manner |
| 5.6.1.3 | ATP + H2O + a kinesin associated with a microtubule at position n |
the enzyme KIF3 promotes microtubule gliding |
| 5.6.1.3 | ATP + H2O + a kinesin associated with a microtubule at position n |
the majority of moving phagosomes are minus-end directed, the remainder moves towards microtubule plus-ends and a small subset moves bi-directionally. Minus-end movement showes pharmacological characteristics expected for dyneins, plus-end movement displayed pharmacological properties of kinesin |
| 5.6.1.3 | ATP + H2O + a kinesin associated with a microtubule at position n |
the rate of ER tubule extensions toward microtubule plus ends is lower than minus end-directed motility. Initiation of plus end-directed ER motility in somatic cytosol is likely to occur via activation of membrane-associated kinesin |
| 5.6.1.3 | ATP + H2O + a kinesin associated with a microtubule at position n |
the enzyme has a critical role during the metaphase-anaphase transition and cytokinesis. While the MKLP2 neck-linker is directed towards the microtubule plus-end in an ATP-like state, it does not fully dock along the motor domain. The footprint of the MKLP2 motor domain on the microtubule surface is altered compared to motile kinesins, and enhanced by kinesin-6-specific sequences |
