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ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
210546, 210548, 210557, 210558, 210559, 210560, 210561, 210562, 210563, 210567, 210571, 210572, 210574
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
kinetics, comparison of wild-type enzyme and enzyme with N-terminal glutathione S-transferase tag, mechanism
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
mechanism, model of movement
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
model for enzymic coupling of depolymerizing microtubule plus ends to the cell cortex
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
a molecular mechanical model for the Kar3/Vik1 heterodimer is described based on structural, kinetic and motility data revealing a long-range chemomechanical transmission mechanism that resembles a familiar fishing tactic. By this this molecular fishing, ATP-binding to Kar3 dissociates catalytically inactive Vik1 off microtubule to facilitate minus-end sliding of the dimer on the microtubule lattice. When the dimer binds the frayed ends of the microtubules, the fishing channels ATP hydrolysis energy into the microtubule depolymerization by a mechanochemical effect
-
ATP + H2O + a kinesin associated with a microtubule at position n = ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2',3'-dideoxy-ATP + H2O + a kinesin associated with a microtubule at position n
2',3'-dideoxy-ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
2'-dATP + H2O + a kinesin associated with a microtubule at position n
2'-dADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
3'-dATP + H2O + a kinesin associated with a microtubule at position n
3'-dADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
N6-methyl-ATP + H2O + a kinesin associated with a microtubule at position n
N6-methyl-ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
additional information
?
-
2',3'-dideoxy-ATP + H2O + a kinesin associated with a microtubule at position n
2',3'-dideoxy-ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
Drosophila sp. (in: flies)
-
-
-
-
?
2',3'-dideoxy-ATP + H2O + a kinesin associated with a microtubule at position n
2',3'-dideoxy-ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
2'-dATP + H2O + a kinesin associated with a microtubule at position n
2'-dADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
2'-dATP + H2O + a kinesin associated with a microtubule at position n
2'-dADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
2'-dATP + H2O + a kinesin associated with a microtubule at position n
2'-dADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
Drosophila sp. (in: flies)
-
-
-
-
?
3'-dATP + H2O + a kinesin associated with a microtubule at position n
3'-dADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
3'-dATP + H2O + a kinesin associated with a microtubule at position n
3'-dADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
3'-dATP + H2O + a kinesin associated with a microtubule at position n
3'-dADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
Drosophila sp. (in: flies)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
minus-end microtubule motor. The motor domain is present at the C terminus of the ncd protein, rather than the N-terminus as in kinesin heavy chain and the other plus-end kinesin motors (EC 3.6.5.5)
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
dimeric KLP-15 construct supports gliding and moves towards microtubule minus end
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
dimeric KLP-15 construct supports gliding at 0.0023 mm per min and moves towards microtubule minus end
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
minus-end microtubule motor. The motor domain is present at the C terminus of the ncd protein, rather than the N-terninus as in kinesin heavy chain and the other plus-end kinesin motors (EC 3.6.5.5)
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
210546, 210548, 210557, 210558, 210559, 210560, 210561, 210562, 210563, 210567, 210571, 210572, 210574, 210575, 669577, 719190, 719508 -
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
Ncd is primarily responsible for focusing kinetochore microtubule bundles (K fibers)
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
the heterodimer E585A/wild-type Ncd construct exhibits 16% of the wild-type activity
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
Drosophila sp. (in: flies)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
Drosophila sp. (in: flies)
-
ncd motor domain interacts with both alpha- and beta-tubulin
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
Drosophila sp. (in: flies)
-
minus-end microtubule motor. The motor domain is present at the C terminus of the ncd protein, rather than the N-terminus as in kinesin heavy chain and the other plus-end kinesin motors (EC 3.6.5.5)
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
Drosophila sp. (in: flies)
-
ncd switches from weak to strong binding via ADP release, and back again via ADP trapping
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
minus-end microtubule motor. The motor domain is present at the C terminus of the ncd protein, rather than the N-terminus as in kinesin heavy chain and the other plus-end kinesin motors (EC 3.6.5.5)
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
the Kif18A motor domain depolymerizes microtubule plus and minus ends
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
the C-terminal region in kinesin-14, namely the neck mimic plays a crucial role in coupling the chemical ATPase reaction with the mechanical cycle to produce the minus-end-directed motility of kinesin-14
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
minus-end kinesin depolymerase Kar3 forms a heterodimer with either Cik1 or Vik1, both of which are noncatalytic polypeptides. Cik1 targets Kar3 to the microtubule plus end. Kar3Cik1 then uses its minus-end-directed force to depolymerite microtubules from the plus end, with each tubulin-subunit release event tightly coupled to one ATP turnover
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
minus-end microtubule motor. The motor domain is present at the C terminus of the ncd protein, rather than the N-terminus as in kinesin heavy chain and the other plus-end kinesin motors (EC 3.6.5.5)
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
minus-end microtubule motor. The motor domain is present at the C terminus of the ncd protein, rather than the N-terminus as in kinesin heavy chain and the other plus-end kinesin motors (EC 3.6.5.5)
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
N6-methyl-ATP + H2O + a kinesin associated with a microtubule at position n
N6-methyl-ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
N6-methyl-ATP + H2O + a kinesin associated with a microtubule at position n
N6-methyl-ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
additional information
?
-
-
enzyme supports microtubule movement in an ATP-dependent manner and has a minus-end directed polarity, enzyme exhibits non-processive movement along the microtubule and requires four molecules bound to the microtubule to support movement
-
-
?
additional information
?
-
-
GTP is no substrate
-
-
?
additional information
?
-
-
GTP is no substrate
-
-
?
additional information
?
-
-
binding geometry between enzyme motor and microtubule which places the motor ahead of its cargo in the minus-end direction, after the uptake of ATP, the two heads rearrange their position relative to each other in a way that promotes a swing of the neck in the minus-end direction
-
-
?
additional information
?
-
-
measurement of Ncd affinity to microtubules, microtubule-stimulated ATPase, and motility of wild-type and mutant enzymes
-
-
?
additional information
?
-
involved in organizing the actin network in coordination with the cortical microtubule array
-
-
?
additional information
?
-
-
involved in organizing the actin network in coordination with the cortical microtubule array
-
-
?
additional information
?
-
interacts in vitro with actin filaments
-
-
?
additional information
?
-
-
interacts in vitro with actin filaments
-
-
?
additional information
?
-
-
GTP, 8-bromo ATP, 1,N6-etheno-adenosine 5'-triphosphate and 5'-O-(3-thiotriphosphate) are no substrates
-
-
?
additional information
?
-
-
kinesin-14 acts during mitosis to cross-link and slide between parallel microtubules to regulate spindle length
-
-
?
additional information
?
-
-
interaction of KifC3 and the AAA-protein PEX1, an ATPase associated with various cellular activities
-
-
?
additional information
?
-
-
required for protein transport in epithelial cells
-
-
?
additional information
?
-
-
required for coupling depolymerizing microtubule plus ends to the cell cortex, model of interactions
-
-
?
additional information
?
-
-
in microtubule gliding assays using microtubules assembled from pig brain tubulin, Klp2 drives minus-end-directed motility
-
-
?
additional information
?
-
-
Klp2 is required for the proper organization of interphase microtubules into bipolar arrays of parallel-overlapped microtubules
-
-
?
additional information
?
-
-
single molecules of Pkl1 are not highly processive but only exhibit biased one-dimensional diffusion along microtubules, whereas several molecules of Pkl1, probably fewer than 10 molecules, cooperatively move along microtubules and substantially reduce the diffusive component in the movement
-
-
?
additional information
?
-
-
kinesin-14 acts during mitosis to cross-link and slide between parallel microtubules to regulate spindle length
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
additional information
?
-
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
dimeric KLP-15 construct supports gliding and moves towards microtubule minus end
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
210546, 210548, 210557, 210558, 210559, 210560, 210561, 210562, 210563, 210567, 210571, 210572, 210574, 210575, 669577, 719508 -
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
Drosophila sp. (in: flies)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
Drosophila sp. (in: flies)
-
ncd motor domain interacts with both alpha- and beta-tubulin
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
the Kif18A motor domain depolymerizes microtubule plus and minus ends
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
ATP + H2O + a kinesin associated with a microtubule at position n
ADP + phosphate + a kinesin associated with a microtubule at position n-1 (toward the minus end)
-
-
-
-
?
additional information
?
-
involved in organizing the actin network in coordination with the cortical microtubule array
-
-
?
additional information
?
-
-
involved in organizing the actin network in coordination with the cortical microtubule array
-
-
?
additional information
?
-
-
kinesin-14 acts during mitosis to cross-link and slide between parallel microtubules to regulate spindle length
-
-
?
additional information
?
-
-
interaction of KifC3 and the AAA-protein PEX1, an ATPase associated with various cellular activities
-
-
?
additional information
?
-
-
required for protein transport in epithelial cells
-
-
?
additional information
?
-
-
required for coupling depolymerizing microtubule plus ends to the cell cortex, model of interactions
-
-
?
additional information
?
-
-
in microtubule gliding assays using microtubules assembled from pig brain tubulin, Klp2 drives minus-end-directed motility
-
-
?
additional information
?
-
-
Klp2 is required for the proper organization of interphase microtubules into bipolar arrays of parallel-overlapped microtubules
-
-
?
additional information
?
-
-
single molecules of Pkl1 are not highly processive but only exhibit biased one-dimensional diffusion along microtubules, whereas several molecules of Pkl1, probably fewer than 10 molecules, cooperatively move along microtubules and substantially reduce the diffusive component in the movement
-
-
?
additional information
?
-
-
kinesin-14 acts during mitosis to cross-link and slide between parallel microtubules to regulate spindle length
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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additional information
ATP
0.0008
ATP
-
-
0.1
ATP
-
mutant NcN-E585D, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
0.16
ATP
-
motor domain, 25 mM potassium acetate, Vmax/2 at 0.0007 mM microtubles, pH 6.9, 22°C
0.17
ATP
-
motor domain, 0 mM potassium acetate, Vmax/2 at 0.00008 mM microtubles, pH 6.9, 22°C
0.19
ATP
-
E585D/E585E, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
0.2
ATP
-
mutant E585A/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
0.6
ATP
-
mutant E552A plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
0.6
ATP
-
mutant E552A/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
0.6
ATP
-
mutant N600K plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
0.6
ATP
-
mutant NcN-E585D plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
0.62
ATP
-
Ncd700SG (residue 250-700, residue 671-679 replaced by sequence GGSGGSGGS), microtuble stimulated, Vmax/2 at 0.00014 mM microtubles, pH 7.2, 25°C
0.62
ATP
-
mutant Ncd700SG, pH 7.2, 25°C, microtubule-stimulated ATPase activity
0.7
ATP
-
mutant E585A plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
0.7
ATP
-
mutant E585D plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
0.83
ATP
-
Ncd670 (residue 250-670), microtuble stimulated, Vmax/2 at 0.00014 mM microtubles, pH 7.2, 25°C
0.83
ATP
-
mutant Ncd670, pH 7.2, 25°C, microtubule-stimulated ATPase activity
0.9
ATP
-
E585D/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
1.3
ATP
-
wild-type/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
1.4
ATP
-
mutant N600K/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
1.9
ATP
-
green fluorescent protein-tagged Pkl1H, in 12 mM PIPES-KOH, 2 mM MgCl2, 1 mM EGTA, pH 6.8, containing 1 mM dithiothreitol, 0.7 mg/ml casein, and 1% (v/v) Tween 20 at 25°C
1.9
ATP
-
mutant NcN, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C
2.49
ATP
-
NcdM672N (residue 250-679, M672N mutation), microtuble stimulated, Vmax/2 at 0.00061 mM microtubles, pH 7.2, 25°C
2.49
ATP
-
mutant NcdM672N, pH 7.2, 25°C, microtubule-stimulated ATPase activity
2.58
ATP
-
NcdWT (residue 250-700), microtuble stimulated, Vmax/2 at 0.00022 mM microtubles, pH 7.2, 25°C
2.58
ATP
-
wild-type Ncd, pH 7.2, 25°C, microtubule-stimulated ATPase activity
3.58
ATP
-
Ncd679 (residue 250-679), microtuble stimulated, Vmax/2 at 0.00026 mM microtubles, pH 7.2, 25°C
3.58
ATP
-
mutant Ncd679, pH 7.2, 25°C, microtubule-stimulated ATPase activity
5
ATP
in presence of microtubles, pH 7.2, 25°C
70
ATP
-
both wild-type and GST-fusion protein, pH 7.2, 25°C
additional information
ATP
-
addition of the ATP analog adenylyl-imidodiphosphate (AMPPNP, 1 mM) dramatically increases the microtuble affinity
additional information
additional information
-
turnover-numbers of KLP-15 constructs with different length extensions preceding the motor domain in presence or absence of 300 mM NaCl and microtubules
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Q1LZ38_DROME
390
0
46156
TrEMBL
other Location (Reliability: 2)
A0A2P6RL70_ROSCH
1269
0
143395
TrEMBL
Chloroplast (Reliability: 5)
Q0KI05_DROME
4842
0
553527
TrEMBL
other Location (Reliability: 1)
Q5LJP0_DROME
4459
1
516851
TrEMBL
other Location (Reliability: 1)
A0A396HQZ4_MEDTR
895
0
100647
TrEMBL
other Location (Reliability: 2)
A0A7C8YRB0_OPUST
250
0
28909
TrEMBL
other Location (Reliability: 3)
A0A2P6P6W5_ROSCH
635
0
71259
TrEMBL
other Location (Reliability: 3)
M9PHG8_DROME
4660
0
532322
TrEMBL
other Location (Reliability: 1)
A0A0B4LH20_DROME
4724
0
541540
TrEMBL
other Location (Reliability: 2)
A0A2G9G775_9LAMI
310
0
34798
TrEMBL
other Location (Reliability: 1)
A0A396GT55_MEDTR
686
0
77698
TrEMBL
other Location (Reliability: 2)
M9PE73_DROME
4647
0
530849
TrEMBL
other Location (Reliability: 1)
A0A0B4K614_DROME
4716
0
540662
TrEMBL
other Location (Reliability: 1)
M9PBQ0_DROME
4651
0
531378
TrEMBL
other Location (Reliability: 1)
A0A396H6W4_MEDTR
562
0
63374
TrEMBL
other Location (Reliability: 5)
A0A7C9CGW4_OPUST
319
0
35889
TrEMBL
other Location (Reliability: 4)
A0A396JHT7_MEDTR
1036
0
117011
TrEMBL
other Location (Reliability: 2)
A0A396HUV2_MEDTR
969
0
109604
TrEMBL
other Location (Reliability: 2)
A0A072VN40_MEDTR
631
0
71009
TrEMBL
other Location (Reliability: 1)
A0A6H2EJG3_DROME
4065
0
466027
TrEMBL
other Location (Reliability: 5)
E1JJ04_DROME
5073
0
580457
TrEMBL
other Location (Reliability: 1)
M9PBQ3_DROME
4661
0
532601
TrEMBL
other Location (Reliability: 1)
A0A2G9HTI0_9LAMI
1071
0
121322
TrEMBL
other Location (Reliability: 2)
A0A7C8YI23_OPUST
194
0
21649
TrEMBL
other Location (Reliability: 3)
G7KGK0_MEDTR
1054
0
118912
TrEMBL
other Location (Reliability: 2)
A0A2P6RPX6_ROSCH
1293
0
142489
TrEMBL
Chloroplast (Reliability: 4)
A0A2P6P3N9_ROSCH
365
0
39310
TrEMBL
other Location (Reliability: 5)
A0A3R7JWR0_9TRYP
668
0
74731
TrEMBL
Mitochondrion (Reliability: 3)
A0A396JYA0_MEDTR
1011
0
112028
TrEMBL
other Location (Reliability: 4)
A8Y5B7_DROME
4593
0
532023
TrEMBL
Mitochondrion (Reliability: 4)
A0A396JVK4_MEDTR
579
0
64569
TrEMBL
other Location (Reliability: 2)
A0A2P6R7C9_ROSCH
430
0
47090
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6PGN3_ROSCH
1048
0
118782
TrEMBL
Chloroplast (Reliability: 2)
A0A3R7RD86_TRYRA
802
0
89153
TrEMBL
Mitochondrion (Reliability: 3)
A0A0B4KI48_DROME
4445
0
510158
TrEMBL
other Location (Reliability: 5)
A0A0B4KI68_DROME
376
0
42353
TrEMBL
other Location (Reliability: 3)
A0A2G9H5I6_9LAMI
1125
0
126242
TrEMBL
other Location (Reliability: 2)
A0A396H6V5_MEDTR
481
0
52652
TrEMBL
Chloroplast (Reliability: 5)
A0A396HHS6_MEDTR
240
0
26458
TrEMBL
other Location (Reliability: 5)
A0A396GW54_MEDTR
566
0
62622
TrEMBL
Chloroplast (Reliability: 5)
A0A7C8ZDX2_OPUST
158
0
17477
TrEMBL
other Location (Reliability: 3)
A0A7C9EFQ4_OPUST
109
0
12591
TrEMBL
other Location (Reliability: 4)
A0A2G9GCF8_9LAMI
1125
0
126315
TrEMBL
other Location (Reliability: 2)
A0A2G9H8Y5_9LAMI
224
0
24590
TrEMBL
other Location (Reliability: 4)
G7KWI8_MEDTR
999
0
110402
TrEMBL
other Location (Reliability: 4)
A0A2P6QNR3_ROSCH
967
0
108788
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6RPW4_ROSCH
1072
0
121798
TrEMBL
other Location (Reliability: 2)
A0A2P6RMK3_ROSCH
144
1
16666
TrEMBL
other Location (Reliability: 3)
M9PEC8_DROME
4648
0
531128
TrEMBL
other Location (Reliability: 1)
A0A0B4KHJ4_DROME
4496
0
515012
TrEMBL
other Location (Reliability: 3)
A0A2G9HCB7_9LAMI
929
0
103409
TrEMBL
other Location (Reliability: 2)
A0A072TRU7_MEDTR
1297
0
143338
TrEMBL
Chloroplast (Reliability: 4)
M9PEN4_DROME
4652
0
531657
TrEMBL
other Location (Reliability: 1)
Q9VDG0_DROME
4486
0
514002
TrEMBL
other Location (Reliability: 3)
Q9VZ77_DROME
4385
0
504629
TrEMBL
other Location (Reliability: 2)
A0A7C8YI75_OPUST
107
0
11563
TrEMBL
other Location (Reliability: 3)
Q9VJC6_DROME
4024
0
461158
TrEMBL
other Location (Reliability: 5)
A0A2G9I332_9LAMI
983
0
108484
TrEMBL
other Location (Reliability: 4)
A0A2P6R6A8_ROSCH
650
0
72727
TrEMBL
other Location (Reliability: 4)
A0A2P6Q930_ROSCH
1038
0
116213
TrEMBL
other Location (Reliability: 2)
A0A2P6QJE1_ROSCH
351
0
38906
TrEMBL
other Location (Reliability: 2)
Q9VWZ3_DROME
4081
0
469076
TrEMBL
other Location (Reliability: 2)
A0A396HPL2_MEDTR
496
0
58011
TrEMBL
other Location (Reliability: 2)
A0A396HXM5_MEDTR
1168
0
131290
TrEMBL
Chloroplast (Reliability: 3)
A0A396GX16_MEDTR
662
0
75550
TrEMBL
other Location (Reliability: 3)
A0A396JTG5_MEDTR
285
0
31310
TrEMBL
other Location (Reliability: 3)
A0A2P6QLF9_ROSCH
499
0
55847
TrEMBL
other Location (Reliability: 3)
A0A2P6PX18_ROSCH
431
0
46915
TrEMBL
Mitochondrion (Reliability: 3)
A0A0B4K648_DROME
4700
0
538744
TrEMBL
other Location (Reliability: 2)
A0A2G9H4X1_9LAMI
1265
0
143839
TrEMBL
Chloroplast (Reliability: 4)
A0A2G9H6G9_9LAMI
400
0
44858
TrEMBL
other Location (Reliability: 3)
G7K2P2_MEDTR
1265
0
143535
TrEMBL
other Location (Reliability: 4)
A0A2P6PWX3_ROSCH
556
0
62054
TrEMBL
other Location (Reliability: 3)
A0A2P6P3Q1_ROSCH
749
0
85436
TrEMBL
other Location (Reliability: 3)
Q9VAV5_DROME
5080
0
581089
TrEMBL
other Location (Reliability: 1)
A0A2G9H404_9LAMI
242
0
26672
TrEMBL
other Location (Reliability: 5)
A0A2P6R7D5_ROSCH
395
0
43519
TrEMBL
other Location (Reliability: 5)
A0A2P6QBQ2_ROSCH
758
0
86356
TrEMBL
Mitochondrion (Reliability: 4)
A0A2P6REF2_ROSCH
1130
0
125640
TrEMBL
other Location (Reliability: 4)
A0A2P6QLF5_ROSCH
509
0
56244
TrEMBL
Mitochondrion (Reliability: 3)
A0A7C9AG21_OPUST
118
0
13369
TrEMBL
other Location (Reliability: 2)
A0A7C9DXJ0_OPUST
122
0
14551
TrEMBL
other Location (Reliability: 5)
Q9VH97_DROME
4692
0
537866
TrEMBL
other Location (Reliability: 1)
A0A2G9HEY6_9LAMI
1034
0
115065
TrEMBL
Mitochondrion (Reliability: 5)
A0A396GV39_MEDTR
417
0
45863
TrEMBL
Chloroplast (Reliability: 2)
A0A396IP02_MEDTR
1124
0
125431
TrEMBL
other Location (Reliability: 5)
A0A7C9EDA8_OPUST
1034
0
117630
TrEMBL
other Location (Reliability: 4)
A0A7C9AH38_OPUST
107
0
12629
TrEMBL
other Location (Reliability: 2)
G7L7W2_MEDTR
1254
0
142235
TrEMBL
Chloroplast (Reliability: 4)
Q7KVA7_DROME
3964
0
455353
TrEMBL
other Location (Reliability: 2)
A0A2G9FZW6_9LAMI
1010
0
111549
TrEMBL
other Location (Reliability: 4)
A0A2G9HHJ9_9LAMI
1294
0
143373
TrEMBL
other Location (Reliability: 3)
A0A396H3D8_MEDTR
1059
0
118438
TrEMBL
other Location (Reliability: 2)
G3V6L4_RAT
955
0
109182
TrEMBL
-
KAR3_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
729
0
84004
Swiss-Prot
-
CTK2_XENLA
643
0
71949
Swiss-Prot
-
Q5MNW6_GOSHI
1018
0
112114
TrEMBL
-
KI18A_HUMAN
898
0
102281
Swiss-Prot
other Location (Reliability: 2)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Endow, S.A.
Determinants of motor polarity in the kinesin proteins
Biophys. J.
68
271S-274S
1995
Aspergillus sp., Cricetulus griseus, Drosophila sp. (in: flies), Homo sapiens, Saccharomyces sp., Schizosaccharomyces pombe
brenda
Kuriyama, R.; Kofron, M.; Essner, R.; Kato, T.; Dragas-Granoic, S.; Omoto, C.K.; Khodjakov, A.
Characterization of a minus end-directed kinesin-like motor protein from cultured mammalian cells
J. Cell Biol.
129
1049-1059
1995
Arabidopsis sp., Aspergillus sp., Saccharomyces cerevisiae, Cricetulus griseus, Drosophila melanogaster, Homo sapiens
brenda
Song, H.; Endow, S.A.
Binding sites on microtubules of kinesin motors of the same or opposite polarity
Biochemistry
35
11203-11209
1996
Saccharomyces cerevisiae, Drosophila melanogaster, Drosophila sp. (in: flies), Xenopus laevis
brenda
Lane, J.D.; Allan, V.J.
Microtubule-based endoplasmic reticulum motility in Xenopus laevis: activation of membrane-associated kinesin during development
Mol. Biol.
10
1909-1922
1999
Xenopus laevis
brenda
Walker, R.A.; Salmon, E.D.; Endow, S.A.
The Drosophila claret segregation protein is a minus-end directed motor molecule
Nature
347
780-782
1990
Drosophila melanogaster
brenda
McDonald, H.B.; Stewart, R.J.; Goldstein, L.S.
The kinesin-like ncd protein of Drosophila is a minus end-directed microtubule motor
Cell
63
1159-1165
1990
Drosophila melanogaster
brenda
Endow, S.A.; Kang, S.J.; Satterwhite, L.L.; Rose, M.D.; Skeen, V.P.; Salmon, E.D.
Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus ends
EMBO J.
13
2708-2713
1994
Arabidopsis sp., Saccharomyces cerevisiae, Drosophila melanogaster
brenda
Middleton, K.; Carbon, J.
KAR3-encoded kinesin is a minus-end-directed motor that functions with centromere binding proteins (CBF3) on an in vitro yeast kinetochore
Proc. Natl. Acad. Sci. USA
91
7212-7216
1994
Saccharomyces cerevisiae, Drosophila melanogaster
brenda
Lombillo, V.A.; Stewart, R.J.; McIntosh, J.R.
Minus-end-directed motion of kinesin-coated microspheres driven by microtubule depolymerization
Nature
373
161-164
1995
Dictyostelium sp., Drosophila melanogaster, Homo sapiens, Tetrahymena sp.
brenda
Walker, R.A.
Ncd and kinesin motor domains interact with both alpha- and beta-tubulin
Proc. Natl. Acad. Sci. USA
92
5960-5964
1995
Drosophila melanogaster, Drosophila sp. (in: flies)
brenda
Shimizu, T.; Toyoshima, Y.Y.; Edamatsu, M.; Vale, R.D.
Comparison of the motile and enzymatic properties of two microtubule minus-end-directed motors, ncd and cytoplasmic dynein
Biochemistry
34
1575-1582
1995
Bos taurus, Doryteuthis pealeii, Drosophila melanogaster, Drosophila sp. (in: flies), Tetrahymena sp.
brenda
Thrower, D.A.; Jordan, M.A.; Schaar, B.T.; Yen, T.J.; Wilson, L.
Mitotic HeLa cells contain a CENP-E-associated minus end-directed microtubule motor
EMBO J.
14
918-926
1995
Dictyostelium sp., Homo sapiens, Xenopus laevis
brenda
Crevel, I.M.; Lockhart, A.; Cross, R.A.
Weak and strong states of kinesin and ncd
J. Mol. Biol.
257
66-76
1996
Saccharomyces cerevisiae, Drosophila melanogaster, Drosophila sp. (in: flies)
brenda
Blocker, A.; Severin, F.F.; Burkhardt, J.K.; Bingham, J.B.; Yu, H.; Olivo, J.C.; Schroer, T.A.; Hyman, A.A.; Griffiths, G.
Molecular requirements for bi-directional movement of phagosomes along microtubules
J. Cell Biol.
137
113-129
1997
Bos taurus, Gallus gallus, Mus musculus, Rattus norvegicus
brenda
Sharp, D.J.; Kuriyama, R.; Essner, R.; Baas, P.W.
Expression of a minus-end-directed motor protein induces Sf9 cells to form axon-like processes with uniform microtubule polarity orientation
J. Cell Sci.
110
2373-2380
1997
Cricetulus griseus
brenda
Henningsen, U.; Schliwa, M.
Reversal in the direction of movement of a molecular motor
Nature
389
93-96
1997
Neurospora crassa
brenda
Sablin, E.P.; Case, R.B.; Dai, S.C.; Hart, C.L.; Ruby, A.; Vale, R.D.; Fletterick, R.J.
Direction determination in the minus-end-directed kinesin motor ncd
Nature
395
813-816
1998
Drosophila melanogaster, Rattus norvegicus
brenda
Matuliene, J.; Essner, R.; Ryu, J.; Hamaguchi, Y.; Baas, P.W.; Haraguchi, T.; Hiraoka, Y.; Kuriyama, R.
Function of a minus-end-directed kinesin-like motor protein in mammalian cells
J. Cell Sci.
112
4041-4050
1999
Saccharomyces cerevisiae, Cricetulus griseus, Drosophila melanogaster, Homo sapiens, Mus musculus
brenda
Kozielski,F.; De Bonis, S.; Burmeister, W.P.; Cohen-Addad, C.; Wade, R.H.
The crystal structure of the minis-end-directed microtubule motor protein ncd reveals variable dimer conformations
Structure Fold. Des.
7
1407-1416
1999
Drosophila melanogaster
brenda
Mackey, A.T.; Gilbert, S.P.
Moving a microtubule may require two heads: a kinetic investigation of monomeric Ncd
Biochemistry
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Drosophila melanogaster
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Drosophila melanogaster
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Structural basis of human kinesin-8 function and inhibition
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Homo sapiens (Q8NI77)
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Structure
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2016
Rattus norvegicus (G3V6L4)
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