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Information on EC 5.6.1.3 - plus-end-directed kinesin ATPase
for references in articles please use BRENDA:EC5.6.1.3
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EC Tree 5 Isomerases
5.6 Isomerases altering macromolecular conformation
5.6.1 Enzymes altering polypeptide conformation or assembly
5.6.1.3 plus-end-directed kinesin ATPase
IUBMB Comments
Kinesins are a family of motor proteins that move unidirectionally along microtubules as they hydrolyse ATP. The enzymes described here move towards the plus end of the microtubule, in contrast to EC 5.6.1.2, dynein ATPase and EC 5.6.1.4, minus-end-directed kinesin ATPase. They are involved in organelle movement in mitosis and meiosis, and also power vesicular trafficking toward the synapse in neurons. The motor domain, which contains the ATP- and microtubule-binding activities, is located at the N-terminus while the C-terminus links to the cargo being transported.
The enzyme appears in viruses and cellular organisms
- 5.6.1.3
- microtubule
- spindle
-
cargo
- dynein
- axon
-
mitosis
- drosophila
- tubulin
- myosin
-
microtubule-based
-
anterograde
-
cytokinesis
- cytoskeleton
- actin
-
bipolar
- cilia
-
single-molecule
-
glide
-
depolymerization
- centrosome
-
microtubule-associated
-
retrograde
-
coiled-coil
-
metaphase
-
anaphase
-
interphase
-
gliding
-
mechanochemical
- kinetochore
-
microtubule-dependent
-
intraflagellar
- plus-ends
-
microtubule-binding
-
protofilaments
- medicine
-
microtubule-organizing
- pharmacology
-
dynactin
-
astral
-
mtocs
-
midzone
- axoneme
-
ciliogenesis
-
monopolar
- cdc20
-
aurora
-
prometaphase
-
depolymerase
-
actin-based
-
force-generating
- midbody
- ciliopathies
Reaction Schemes
show+
+
=
+
+
+
a kinesin associated with a microtubule at position n
=
+
phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
Synonyms
kinesin, kinesin-1, kif3a, kinesin-5, kif1a, kif11, kif4a, kifc1, kinesin-2, kif5b, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BC12
Brittle Culm12
conventional kinesin
EC 3.6.4.4
-
-
formerly
-
Eg5
KHC
KIF11
KIF13A
KIF13B
KIF16B
KIF1A
KIF3
KIF3A
KIF3B
KIF3C
KIF4
KIF5A
KIF5B
KIF5C
kinesin
kinesin Eg5
kinesin I
kinesin motor-protein
kinesin spindle protein
kinesin-1
kinesin-1 heavy chain
kinesin-13 MCAK
-
kinesin-13 subfamily members do not move directionally along microtubules but, instead, depolymerize them
kinesin-2
kinesin-3
kinesin-5
kinesin-6
kinesin-8
kinesin-8B
kinesin-like protein
kinetoplastid specific kinesin
Kip3
Klp6p
-
the motor-plus-neck domain of Klp6p forms soluble dimers that cross-link microtubules and show both microtubule-activated ATPase and plus-end-directed motor activities
mitotic kinesin
MKLP2
NcKin3
TbKIN-C
kinesin
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 plus 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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (a) chains (110kDa) and two more light (b) chains (65-75 kDa). Also hydrolyzes GTP.
-
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 plus end)
light
-
-
-
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 plus end)
the microtubule-Eg5 complex binds MgATP tightly, followed by rapid ATP hydrolysis with a subsequent slow step that limits steady-state turnover. Presence of microtubules accelerates the kinetics of each step in the ATPase pathway and amplifies the nucleotide-dependent structural transitions required for force generation. Phosphate product release and Eg5 detachment from the microtubule are coupled with a step occuring at the slow rate after ATP hydrolysis followed by the second step occuring more rapidly
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
kinesin ATP phosphohydrolase (plus-end-directed)
Kinesins are a family of motor proteins that move unidirectionally along microtubules as they hydrolyse ATP. The enzymes described here move towards the plus end of the microtubule, in contrast to EC 5.6.1.2, dynein ATPase and EC 5.6.1.4, minus-end-directed kinesin ATPase. They are involved in organelle movement in mitosis and meiosis, and also power vesicular trafficking toward the synapse in neurons. The motor domain, which contains the ATP- and microtubule-binding activities, is located at the N-terminus while the C-terminus links to the cargo being transported.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-chloro-2-(6-chloro-4-oxo-3,4-dihydroquinazolin-2-yl)phenyl trifluoromethanesulfonate + H2O + a kinesin associated with a microtubule at position n
6-chloro-2-(5-chloro-2-hydroxyphenyl)quinazolin-4(3H)-one + trifluoromethanesulfonate + a kinesin associated with a microtubule at position n+1 (toward the plus end)
Substrates: the compound yields a precipitating dye along its walking path on microtubules
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ADP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
ATP + H2O + a kinesin associated with a microtubule at position n =
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Substrates: -
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r
Alexa Fluor 647 ATP + H2O + a kinesin associated with a microtubule at position n
Alexa Fluor 647 ADP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: Alexa Fluor 647 ATP, a fluorescent ATP analog, activity determined by FRET-based assays, Förster resonance energy transfer assays. The fluorescent ATP analog can fuel kinesin-1'S processsive motion and is a suitable substrate analog, but it alters the motor's kinetic parameters
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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 plus 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 plus end)
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Substrates: -
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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 plus end)
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
methylanthraniloyl-ATP + H2O + a kinesin associated with a microtubule at position n
methylanthraniloyl-ADP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: unconventional ATPase cycle, adapted for microtubule depolymerization, low basal activity is accelerated by tubulin and microtubles
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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 plus end)
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Substrates: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
-
Substrates: conventional kinesin is required for the microtubule plus-end accumulation of cytoplasmic dynein and dynactin but not for NUDF
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
?
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 plus end)
Substrates: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: the movement of newly assembled african swine fever virus particles from the factory to the cell surface is dependent on conventional kinesin
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: kinesin-13 neck sequence makes a significant contribution to depolymerization afficiency, and is essential to enable these motors to control cellular microtubule dynamics
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: -
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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 plus end)
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Substrates: microtubules and kinesin I are required for the selective accumulation of oskar mRNA at the posterior cortex of the Drosophila melanogaster oocyte
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: centralspindlin is a plus-end-directed motor. Centralspindlin cannot utilize MgGTP to generate force for microtubule movement
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: kinesin motor domain interacts with both alpha- and beta-tubulin
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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 plus end)
-
Substrates: kinesin switches from weak to strong binding via ADP release, and back again via ADP trapping
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
-
Substrates: Eh Klp5 is a divergent member of the kinesin 5 family that regulates genome content and microtubular assembly
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: the enzyme KIF3 promotes microtubule gliding
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: 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
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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 plus end)
Substrates: in regulating plus end motility, KIF16B governs the spatial distribution of early endosomes in vivo and the balance between receptor recycling and degradation
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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 plus end)
-
Substrates: 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
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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 plus end)
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Substrates: 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
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: Eg5 is a homotetrameric kinesin-5 involved in centrosome separation and assembly of the bipolar mitotic spindle. The stable dimer Eg5-513 promotes robust plus-end-directed microtubule gliding at a rate similar to that of homotetrameric Eg5 in vitro. Eg5-513 exhibits slow ATP turnover, high affinity for ATP, and a weakened affinity for microtubules when compared to monomeric Eg5
Products: -
Products: -
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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 plus end)
-
Substrates: individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro
Products: -
Products: -
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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 plus end)
Substrates: KIF16B is a plus end-directed motor
Products: -
Products: -
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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 plus end)
-
Substrates: plus-end-enriched motor that targets regions of podosome turnover
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: MCAK moves along the microtubule lattice in one-dimensional random walk
Products: -
Products: -
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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 plus end)
-
Substrates: the microtubule-Eg5 complex binds MgATP tightly, followed by rapid ATP hydrolysis with a subsequent slow step that limits steady-state turnover. Presence of microtubules accelerates the kinetics of each step in the ATPase pathway and amplifies the nucleotide-dependent structural transitions required for force generation. Phosphate product release and Eg5 detachment from the microtubule are coupled with a step occuring at the slow rate after ATP hydrolysis followed by the second step occuring more rapidly
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: unconventional ATPase cycle, adapted for microtubule depolymerization, low basal activity is accelerated by tubulin and microtubles
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: analysis of structures of ADP-bound kinesin
Products: analysis of structures of ADP-bound kinesin
?
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 plus end)
Substrates: modeling reveals key nucleotide-dependent changes in the structure and flexibility of the nucleotide-binding pocket and the tubulin-binding site, and allosterically coupled motions driving the APO to ATP transition of ATPase states, extension and shortening of alpha4 helix during the ATPase cycle
Products: structural mechanism of ADP release
Products: structural mechanism of ADP release
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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 plus end)
Substrates: the Kif18A motor domain depolymerizes microtubule plus and minus ends
Products: -
Products: -
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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 plus end)
Substrates: 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
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: a single ATP hydrolysis triggers a single stepping movement of a single KIF1A monomer
Products: -
Products: -
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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 plus end)
-
Substrates: kinesin I and cytoplasmic dynein orchestrate glucose-stimulated insulin-containing vesicle movements in clonal MIN6 beta-cells. The majority of transport of large dense-core vesicles in beta-cells is mediated by kinesin I, whilst dynein probably contributes to the recovery of vesicles after rapid kiss-and-run exocytosis
Products: -
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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 plus end)
-
Substrates: 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
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: nucleotide-induced conformational change catalytic method
Products: -
Products: -
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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 plus end)
Substrates: 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
Products: -
Products: -
?
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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
?
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 plus end)
Substrates: -
Products: -
Products: -
?
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 plus end)
-
Substrates: -
Products: -
Products: -
?
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 plus end)
-
Substrates: kinesin-1 supports long-range hyphal growth. Kinesin-1, kinesin-3 and myosin-V cooperate in polarized growth. Kinesin-3 participates in acid phosphatase secretion in hyphae
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
?
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 plus end)
-
Substrates: kinesin-1 motor is required for efficient microtubule bundling and participates in microtubule bending in vivo
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
?
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 plus end)
-
Substrates: plus-end directed kinesin motor moves in a non-processive fashion to its destination
Products: -
Products: -
?
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 plus end)
-
Substrates: -
Products: existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head
Products: existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head
?
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 plus end)
-
Substrates: -
Products: -
Products: -
?
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 plus end)
AK065586
Substrates: -
Products: -
Products: -
?
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 plus end)
Substrates: -
Products: -
Products: -
?
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 plus end)
-
Substrates: -
Products: -
Products: -
?
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 plus end)
-
Substrates: -
Products: -
Products: -
?
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 plus end)
-
Substrates: -
Products: -
Products: -
?
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 plus end)
-
Substrates: alternating site ATPase pathway, including a captive head state as an intermediate in the kinesin ATPase cycle
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
?
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 plus end)
-
Substrates: -
Products: existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head
Products: existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head
?
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 plus end)
-
Substrates: KIF4 moves along microtubules toward the plus-end
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: Kip3P is both a plus-end-specific depolymerase and a plus end-directed motor
Products: -
Products: -
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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 plus end)
-
Substrates: Kip3p destabilizes microtubules by depolymerizing them. Kip3p disassembles microtubules exclusively at the plus end and depolymerizes longer microtubules faster than shorter ones
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
?
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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: kinesin-8/Kip3 uses ATP hydrolysis for stepping on the microtubule lattice, but at the plus-end, Kip3 undergoes a switch. Its ATPase activity is suppressed when it binds tightly to the curved conformation of tubulin. This prolongs plus-end binding, stabilizes protofilament curvature, and ultimately promotes microtubule disassembly
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: the DASH complex and Klp5/Klp6 kinesin coordinate bipolar chromosome attachment in fission yeast
Products: -
Products: -
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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 plus end)
-
Substrates: kinesin-8 expressed in insect cells forms a heterodimer that hydrolyzes ATP in a microtubule-dependent manner and moves on microtubules toward their plus ends
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: Kin5 is an intraciliary transport motor
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: in vitro ATPase activity of the purified motor domain of TbKIN-D
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: 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
Products: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
Products: -
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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 plus end)
-
Substrates: 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
Products: -
Products: -
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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 plus end)
-
Substrates: kinesin MCAK/XKCM1destabilizes microtubules. Kinesin MCAK/XKCM1 is essential for controlling the distribution of microtubules by inducing their depolymerization
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Q07866; P33176
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
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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 plus end)
Substrates: -
Products: -
Products: -
?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: -
Products: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: -
Products: -
Products: -
?
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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?
additional information
?
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Substrates: the enzyme gains processive motility with enhanced central stalk flexibility. Enhanced central stalk flexibility weakens microtubule crosslinking by the enzyme
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additional information
?
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Substrates: a unique loop of the FHA domain traps ADP-Mg2+ in the nucleotide-binding pocket, formation of the CFCMM supramodule, overview. Microtubule-stimulated ATPase assay
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additional information
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Substrates: the binding of tail peptides to head dimers is fast and readily reversible, the second tail peptide in a folded kinesin-1 may be available to bind other molecules while kinesin-1 remains folded
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additional information
?
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Substrates: NOD binds tightly to microtubules in the nucleotide-free state, yet other nucleotide states, including adenosine-5'-(beta,gamma-imido)triphosphate, are weakened, NOD interaction with microtubules occurs slowly with weak activation of ADP product release. Upon rapid substrate binding, NOD detaches from the microtubule prior to the rate-limiting step of ATP hydrolysis.
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?
additional information
?
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Substrates: KLP61F displays a 3fold higher preference for crosslinking microtubules in the antiparallel orientation, this polarity preference is observed in the presence of ADP or ATP plus AMPPNP, but not AMPPNP alone
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additional information
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Substrates: during morphogenesis of the Drosophila embryo mitotic spindle, KLP61F's crosslinking and sliding activities can facilitate the gradual accumulation of KLP61F within antiparallel interpolar microtubules at the equator, where the motor can generate force to drive poleward flux and pole-pole separation
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additional information
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Substrates: at low loads, kinesin-1 almost always steps forward, toward microtubule plus ends, but at higher loads, it can also step/slip backward. In each cycle of ATP turnover, forward kinesin steps can only occur before phosphate release, whereas backslips and detachments can only occur after phosphate release. Dwell times for forward steps are shorter than dwell times for backsteps. Added ADP inhibits forward steps and promotes backsteps and detachments
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additional information
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Substrates: during the ATP-waiting state, the mobile tethered head of kinesin1 containing ADP can transiently interact with the microtubule
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additional information
?
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Substrates: KIF4 regulates Gag stability and trafficking
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additional information
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Substrates: kinesin spindle protein is essential for mitotic spindle assembly in dividing human cells and is required for cell cycle progression through mitosis
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additional information
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Substrates: the KVD motif of kinesin Kif2C interacts directly with tubulin. ATP hydrolysis in Kif2C is not required for tubulin release
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additional information
?
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Substrates: key residues involved in kinesin-tubulin binding
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additional information
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Substrates: key residues involved in kinesin-tubulin binding
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additional information
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Substrates: animals survive lowered amounts of KIF3A and KIF3B through heterozygosity. Only in complete absence of KI3A do photoreceptor cells die, and homozygous null mutants of Kif3a are embryonic lethal in mice
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additional information
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Substrates: kinesin-2 binds the full-length variant of Hippel-Lindau tumour suppressor protein (pVHL30) in primary kidney cells, and mediate its association to microtubules
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additional information
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Substrates: KIF4 specifically binds to the microtubule, enzyme interaction with tubulin, the KIF4-specific Q248 and K249 form possible hydrogen bonds with Y108 of helix H3' of alpha-tubulin. Microtubule filament binding by enzyme KIF4, around the center line of the microtubule protofilament, the helix-alpha4-mediated microtubule-binding site is located and fitted into the intra-tubulin dimer groove
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additional information
?
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Substrates: kinesin-3 motors influence microtubule bending in vivo
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additional information
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Substrates: kinesin-3 motors influence microtubule bending in vivo
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additional information
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Substrates: kinesin-3 motors influence microtubule bending in vivo
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additional information
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Substrates: kinesin-3 motors influence microtubule bending in vivo
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additional information
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Substrates: the enzyme drives ATP-dependent microtubule gliding, but also catalyzes ATP-dependent microtubule depolymerisation
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additional information
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Substrates: the enzyme drives ATP-dependent microtubule gliding, but also catalyzes ATP-dependent microtubule depolymerisation
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additional information
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Substrates: individual motors sidestep with a bias to the left, the probability of which is increased with the time taken per forward step. Effective sidestepping probability increases at limiting ATP concentrations. Kinesin Kip3 switches protofilaments to avoid obstacles along the microtubule lattice and potentially also to navigate traffic jams at microtubule ends. Directed sidestepping incorporated within the motor step cycle enables the motor to reach the end of crowded microtubules in a single processive run, i.e., without obstacle-forced detachment
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additional information
?
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Substrates: kinesin-1 can only make unidirectional movement toward the plus end and kinesin-5 can make bidirectional movements on microtubules
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additional information
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Substrates: kinesin-8 contributes both to chromosome congression to the metaphase plate and to the coupling of spindle microtubules to kinetochores during anaphase A
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additional information
?
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Substrates: enzyme TbKIN-D associates with cytoskeletal microtubules in vivo, and TbKIN-D interacts with TbKIN-C, a kinetoplastid-specific kinesin
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additional information
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Substrates: enzyme TbKIN-D associates with cytoskeletal microtubules in vivo, and TbKIN-D interacts with TbKIN-C, a kinetoplastid-specific kinesin
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additional information
?
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Substrates: full-length Eg5's motility comprises an unbiased, diffusive mode independent of ATP hydrolysis and a plus end-directed processive mode that requires ATP hydrolysis, Eg5 can switch from diffusive motility to directional motility upon binding to a second microtubule
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 plus 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 plus end)
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Substrates: -
Products: -
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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 plus end)
GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus 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 plus end)
-
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
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Substrates: conventional kinesin is required for the microtubule plus-end accumulation of cytoplasmic dynein and dynactin but not for NUDF
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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 plus end)
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Substrates: -
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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 plus end)
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Substrates: -
Products: -
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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 plus end)
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Substrates: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
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Substrates: -
Products: -
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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 plus end)
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Substrates: -
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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 plus end)
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Substrates: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
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Substrates: -
Products: -
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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 plus end)
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Substrates: -
Products: -
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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 plus end)
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Substrates: kinesin motor domain interacts with both alpha- and beta-tubulin
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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 plus end)
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Substrates: Eh Klp5 is a divergent member of the kinesin 5 family that regulates genome content and microtubular assembly
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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 plus end)
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Substrates: -
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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 plus end)
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Substrates: the enzyme KIF3 promotes microtubule gliding
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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 plus end)
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Substrates: -
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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 plus end)
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Substrates: 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
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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 plus end)
Substrates: in regulating plus end motility, KIF16B governs the spatial distribution of early endosomes in vivo and the balance between receptor recycling and degradation
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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 plus end)
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Substrates: 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
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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 plus end)
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Substrates: 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
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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 plus end)
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Substrates: -
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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 plus end)
Substrates: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
Substrates: -
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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 plus end)
Substrates: the Kif18A motor domain depolymerizes microtubule plus and minus ends
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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 plus end)
Substrates: 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
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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 plus end)
Substrates: -
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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 plus end)
Substrates: -
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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 plus end)
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Substrates: -
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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 plus end)
Substrates: -
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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 plus end)
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Substrates: -
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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 plus end)
Substrates: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
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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 plus end)
-
Substrates: kinesin I and cytoplasmic dynein orchestrate glucose-stimulated insulin-containing vesicle movements in clonal MIN6 beta-cells. The majority of transport of large dense-core vesicles in beta-cells is mediated by kinesin I, whilst dynein probably contributes to the recovery of vesicles after rapid kiss-and-run exocytosis
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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 plus end)
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Substrates: 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
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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 plus end)
Substrates: -
Products: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
Substrates: 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
Products: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
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Substrates: kinesin-1 supports long-range hyphal growth. Kinesin-1, kinesin-3 and myosin-V cooperate in polarized growth. Kinesin-3 participates in acid phosphatase secretion in hyphae
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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 plus end)
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Substrates: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
-
Substrates: -
Products: -
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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 plus end)
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Substrates: alternating site ATPase pathway, including a captive head state as an intermediate in the kinesin ATPase cycle
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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 plus end)
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Substrates: -
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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 plus end)
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Substrates: Kip3P is both a plus-end-specific depolymerase and a plus end-directed motor
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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 plus end)
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Substrates: Kip3p destabilizes microtubules by depolymerizing them. Kip3p disassembles microtubules exclusively at the plus end and depolymerizes longer microtubules faster than shorter ones
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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 plus end)
Substrates: -
Products: -
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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 plus end)
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Substrates: -
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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 plus end)
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Substrates: -
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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 plus end)
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Substrates: -
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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 plus end)
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Substrates: -
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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 plus end)
Substrates: Kin5 is an intraciliary transport motor
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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 plus end)
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Substrates: -
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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 plus end)
Substrates: -
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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 plus end)
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Substrates: -
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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 plus end)
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Substrates: -
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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 plus end)
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Substrates: 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
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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 plus end)
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Substrates: 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
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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 plus end)
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Substrates: kinesin MCAK/XKCM1destabilizes microtubules. Kinesin MCAK/XKCM1 is essential for controlling the distribution of microtubules by inducing their depolymerization
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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 plus end)
Substrates: -
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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 plus end)
Q07866; P33176
Substrates: -
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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 plus end)
Substrates: -
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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 plus end)
Substrates: -
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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 plus end)
Substrates: -
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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 plus end)
Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
-
Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
Products: -
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GTP + H2O + a kinesin associated with a microtubule at position n
GDP + phosphate a kinesin associated with a microtubule at position n+1 (toward the plus end)
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Substrates: -
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additional information
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Substrates: the binding of tail peptides to head dimers is fast and readily reversible, the second tail peptide in a folded kinesin-1 may be available to bind other molecules while kinesin-1 remains folded
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additional information
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Substrates: NOD binds tightly to microtubules in the nucleotide-free state, yet other nucleotide states, including adenosine-5'-(beta,gamma-imido)triphosphate, are weakened, NOD interaction with microtubules occurs slowly with weak activation of ADP product release. Upon rapid substrate binding, NOD detaches from the microtubule prior to the rate-limiting step of ATP hydrolysis.
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additional information
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Substrates: KLP61F displays a 3fold higher preference for crosslinking microtubules in the antiparallel orientation, this polarity preference is observed in the presence of ADP or ATP plus AMPPNP, but not AMPPNP alone
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additional information
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Substrates: during morphogenesis of the Drosophila embryo mitotic spindle, KLP61F's crosslinking and sliding activities can facilitate the gradual accumulation of KLP61F within antiparallel interpolar microtubules at the equator, where the motor can generate force to drive poleward flux and pole-pole separation
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additional information
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Substrates: during the ATP-waiting state, the mobile tethered head of kinesin1 containing ADP can transiently interact with the microtubule
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additional information
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Substrates: KIF4 regulates Gag stability and trafficking
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additional information
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Substrates: kinesin spindle protein is essential for mitotic spindle assembly in dividing human cells and is required for cell cycle progression through mitosis
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additional information
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Substrates: the KVD motif of kinesin Kif2C interacts directly with tubulin. ATP hydrolysis in Kif2C is not required for tubulin release
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additional information
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Substrates: animals survive lowered amounts of KIF3A and KIF3B through heterozygosity. Only in complete absence of KI3A do photoreceptor cells die, and homozygous null mutants of Kif3a are embryonic lethal in mice
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additional information
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Substrates: kinesin-2 binds the full-length variant of Hippel-Lindau tumour suppressor protein (pVHL30) in primary kidney cells, and mediate its association to microtubules
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additional information
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Substrates: KIF4 specifically binds to the microtubule, enzyme interaction with tubulin, the KIF4-specific Q248 and K249 form possible hydrogen bonds with Y108 of helix H3' of alpha-tubulin. Microtubule filament binding by enzyme KIF4, around the center line of the microtubule protofilament, the helix-alpha4-mediated microtubule-binding site is located and fitted into the intra-tubulin dimer groove
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additional information
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Substrates: kinesin-8 contributes both to chromosome congression to the metaphase plate and to the coupling of spindle microtubules to kinetochores during anaphase A
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additional information
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Substrates: enzyme TbKIN-D associates with cytoskeletal microtubules in vivo, and TbKIN-D interacts with TbKIN-C, a kinetoplastid-specific kinesin
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additional information
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Substrates: enzyme TbKIN-D associates with cytoskeletal microtubules in vivo, and TbKIN-D interacts with TbKIN-C, a kinetoplastid-specific kinesin
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additional information
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Substrates: full-length Eg5's motility comprises an unbiased, diffusive mode independent of ATP hydrolysis and a plus end-directed processive mode that requires ATP hydrolysis, Eg5 can switch from diffusive motility to directional motility upon binding to a second microtubule
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methanamine
-
(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)(1-methylpiperidin-3-yl)methanone
-
(2R)-2-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-methylbutan-1-one
-
(2R)-2-amino-3-((1,1-bis(4-chlorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1,1-bis(4-fluorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1,1-bis(4-methylphenyl)-2-phenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(2-fluorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(3,4-dichlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(3-chlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(3-chlorophenyl)-1-(4-chlorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(3-hydroxyphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(4-chlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(4-fluorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(4-hydroxyphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((1-(4-methylphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((2-(3,4-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((2-(3-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R)-2-amino-3-((2-(4-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
-
-
(2R,4aS,5R,10bS)-2-((1H-1,2,4-triazol-1-yl)methyl)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(2S)-2-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-methylbutan-1-one
-
(4aS,10bS)-9-(tert-butyl)-5-(3-chlorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,10bS)-9-(tert-butyl)-5-(3-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline-9-carbonitrile
-
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline-9-carboxylic acid
-
(4aS,5R,10bS)-5-phenyl-9-(trifluoromethoxy)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-5-phenyl-9-propyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-7,9-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-7-fluoro-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-8,10-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-8,9-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-8-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-8-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(pentafluoro-lambda6-sulfanyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(1H-imidazol-2-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(2-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-chlorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-fluoro-4-methoxyphenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(4-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(pyridin-3-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-(thiazol-2-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-chloro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-ethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-isopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-9-methyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(4aS,5R,10bS)-N,N-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-amine
-
(4aS,5S,10bS)-9-(tert-butyl)-5-cyclohexyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
-
(5E)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(2Z)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-1,3-thiazol-4(5H)-one
-
(5E)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(2Z)-3-phenylprop-2-en-1-ylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-benzylidene-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(2,3-dimethoxyphenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(2-chlorophenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(2-fluorophenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(2-nitrophenyl)methylidene]-1,3-thiazol-4(5H)-one
partial inhibition
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(3,4-dimethoxyphenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(3-chlorophenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(3-methoxyphenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(3-nitrophenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(3Z)-4-[4-(dimethylamino)cyclohexa-2,4-dien-1-yl]but-3-en-1-ylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(4-bromophenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(4-chlorophenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(4-methoxyphenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(4-methylphenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(4-nitrophenyl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(benzyloxy)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(furan-2-yl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(pyridin-2-yl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(thiophen-2-yl)methylidene]-1,3-thiazol-4(5H)-one
-
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[[4-(dimethylamino)phenyl]methylidene]-1,3-thiazol-4(5H)-one
-
(Z)-2-(4-((5-(4-chlorophenyl)-6-(isopropoxycarbonyl)-7-methyl-3-oxo-3,5-dihydro-2H-thiazolo[3,2-a]pyrimidin-2-ylidene)methyl)phenoxy)acetic acid
i.e. DHTP
1-((2R,4aS,5R,10bS)-5-(4-fluorophenyl)-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
-
1-((2R,4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
-
1-((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
-
1-((2R,4aS,5R,10bS)-9-cyclopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
-
1-(1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
i.e. tetrahydro-beta-carboline
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-(piperidin-1-yl)propan-1-one
-
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
-
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
1-(2-(dimethylamino)ethyl)-3-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)urea
-
1-(3,6-dichloro-9H-carbazol-9-yl)-3-phenethylamino-2-propanol
-
induces cell death
1-(3-hydroxypropyl)-3-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)urea
-
1-(4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenyl)ethanone
-
1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-2-(piperidin-4-yl)ethanone
-
1-(benzenesulfonyl)-4-chloro-2-nitrobenzene
i.e. BTB-1, reversibly inhibits the microtubule-stimulated ATPase activity of Kif18A
1-phenethylamino-3-phenothiazin-10-yl-propan-2-ol
-
induces strong mitotic arrest followed by cell death. More than 90% of cells exhibit the monoastral spindle instead of the normal mitotic spindle. Inhibitor selectively kills transformed culture cells; the inhibitor selectively kills transformed cell cultures
2-((((2R,4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)(ethyl)amino)ethanol
-
2-((((2R,4aS,5R,10bS)-9-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)amino)ethanol
-
2-((1-(3-chlorophenyl)-1,2-diphenylethyl)sulfanyl)ethanaminium tetrafluoroborate
-
-
2-((2R,4aS,5R,10bS)-9-(tert-butyl)-2-((methylamino)methyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
-
2-((4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-yl)acetonitrile
-
2-((4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-yl)ethanol
-
2-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)-4-chlorobenzenethiol
-
2-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
-
2-(2,4-difluorophenyl)-9-(3,4-dimethylphenyl)-8-oxo-8,9-dihydro-7H-purine-6-carboxamide
-
-
2-(2-sulfanylethoxy)ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
-
2-(dimethylamino)ethyl (((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)carbamate
-
2-(methylamino)-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)ethanesulfonothioamide
-
2-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
-
2-[1-(4-methoxyphenyl)-5-oxo-3-[2-(thiophen-2-yl)ethyl]-2-thioxoimidazolidin-4-yl]-N-phenylacetamide
-
-
2-[2-(acetylsulfanyl)ethoxy]ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
-
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)aniline
-
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
-
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
-
3-(2-((2-aminoethyl)sulfonyl)-6-chloro-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)phenol
-
3-(dimethylamino)-N-(((2R,4aS,5R,10bS)-9-isopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)propane-1-sulfonamide
-
3-amino-1-(1-(2-aminopyridin-4-yl)-6-chloro-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-fluorophenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-hydroxyphenyl)-6-(trifluoromethoxy)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-hydroxyphenyl)-6-isopropyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-hydroxyphenyl)-6-phenyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(1-(3-methoxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-bromo-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-chloro-1-cyclohexyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-ethyl-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-fluoro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-hydroxy-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-1-(6-methyl-1-phenyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
-
3-amino-N-methyl-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)propane-1-sulfonothioamide
-
4-((((2R)-2-ammonio-2-carboxyethyl)sulfanyl)(diphenyl)-methyl)pyridinium tetrafluoroborate
-
-
4-((2R,4aS,5R,10bS)-2-((methylamino)methyl)-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
-
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)-2-fluorophenol
-
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzene-1,2-diol
-
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
-
4-((4aS,5S,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)butan-1-ol
-
4-(2-[1-(4-fluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
treatmebnt of cells results in inhibition of proliferation and induction of caspase 3 activity with EC50 values of 0.0017 and 0.0011 mM, respectively. Compound induces monoastral spindles in A2780 cells when incubated at concentrations above that required to induce a full mitotic arrest
4-(N-(2-(N-acetylcysteine-S-yl)acetyl) amino)-4'-(N-(2-(N-(triphenylmethyl)amino)acetyl)amino)azobenzene
-
4-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)butan-1-one
-
4-[[3-(methoxycarbonyl)-2-methyl-5a,9a-dihydronaphtho[1,2-b]furan-5-yl]sulfamoyl]benzoic acid
-
-
5-(2-(3-aminopropanoyl)-6-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)benzo[d]oxazol-2(3H)-one
-
adenosine 5'-[beta,gamma-imido]triphosphate
-
nonhydrolyzable analogue of ATP, blocks enzyme by rapid replacement of ATP
BTB-1
BTB-1 inhibits both of the microtubule-based Kif18A activities. Allosteric BTB-1-binding site near loop5, where it blocks the ATP-dependent conformational changes
Calmodulin
-
activated calmodulin inhibits KCBP interaction with microtubules thereby abolishing its motor- and microtubules-dependent ATPase activity
cis-2,3-bis[(2,5-dioxo-1-[4-[(E)-2-phenyldiazen-1-yl]phenyl]pyrrolidin-3-yl)sulfanyl]butanedioic acid
weak effects on the microtubule-dependent ATPase activity of kinesin Eg5
curcumin
disturbs the dynamic interactions of kinesin Eg5 and microtubules and inhibits the basal and microtubule-stimulated ATPase activity of the enzyme. Curcumin (0.04 mM) reduces the rate of ATP hydrolysis of the enzyme by 22%. Further, the extent of ATP hydrolysis is inhibited by 6.25, 12.5 and 19.5% in the presence of 0.005, 0.01, and 0.02 mM curcumin, respectively
ethyl 3-acetyl-4-[3-(acetyloxy)phenyl]-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
no inhibition in vitro, inhibitory in cell-based assay
ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
i.e. monastrol
ethyl 4-[3-(acetyloxy)phenyl]-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
no inhibition in vitro, inhibitory in cell-based assay
furan-2-yl[4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl]methanone
-
-
kinesin spindle protein activator-1
-
inhibits kinesin spindle protein ATP turnover in the presence of microtubules
-
N,N-diethyl-5,5-dimethyl-2-(2-thienylcarboxamido)-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide
-
N-(((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)-4-(dimethylamino)butanamide
-
N-(((2R,4aS,5R,10bS)-9-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)-2-(dimethylamino)ethanesulfonamide
-
N-(2-((((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)amino)ethyl)acetamide
-
N-(2-aminoethyl)-4-methyl-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)benzamide
-
N-(3-(2-(3-aminopropanoyl)-6-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)phenyl)methanesulfonamide
-
N-(3-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-oxopropyl)methanesulfonamide
-
N-(3-aminopropyl)-N-[(1R)-1-(3-benzyl-7-chloro-4-oxo-3,4-dihydroquinazolin-2-yl)-2-methylpropyl]-3-fluoro-4-methylbenzamide
-
-
N-(4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenyl)acetamide
-
N-(4-fluorophenyl)-2-[1-(4-fluorophenyl)-3-[2-(3-methylthiophen-2-yl)ethyl]-5-oxo-2-thioxoimidazolidin-4-yl]acetamide
-
-
N-(4-methoxyphenyl)-2-[3-[2-(3-methylthiophen-2-yl)ethyl]-5-oxo-1-phenyl-2-thioxoimidazolidin-4-yl]acetamide
-
-
N1-phenyl-N1-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)ethane-1,2-diamine
-
PVZB1194
allosteric inhibitor, biphenyl-type inhibitor, binding structure of the inhibitor in complex with the Eg5 motor domain: inhibitor PVZB1194 binds to the alpha4/alpha6 allosteric pocket 15 A from the ATP-binding pocket, which differs from conventional allosteric inhibitors that bind to the allosteric L5/alpha2/alpha 3 pocket of Eg5. Binding of the inhibitor is involved in the neck-linker conformation and also causes conformational changes around the ATP-binding pocket through Tyr104 to affect the interaction of ATP with the pocket. Folding rearrangement of enzyme Eg5 induced by PVZB1194 in the absence of nucleotides and microtubules. Residue Tyr104 is involved in ATP-competitive inhibition by PVZB1194
trans-2,3-bis[(2,5-dioxo-1-[4-[(E)-2-phenyldiazen-1-yl]phenyl]pyrrolidin-3-yl)sulfanyl]butanedioic acid
significantly inhibits microtubule-dependent ATPase activity of kinesin Eg5
ispinesib
-
SB-715992, a potent and selective inhibitor of kinesin spindle protein
monastrol
-
0.2 mM, 25% inhibition. Compared to vertebrate Eg5, Eh Klp5 is less sensitive to monastrol
monastrol
-
model for dimeric Eg5 in which monastrol stabilizes a conformation with the neck linker of each motor domain locked onto its catalytic core, resulting in dissociation of the MT. Eg5 complex or an inhibition of MT binding
monastrol
monastrol (0.08 mM) inhibits the basal ATPase activity of the enzyme by 25%
monastrol
-
suppresses the directional processive motility of microtubule-bound Eg5
S-trityl-L-cysteine
-
tight binding inhibitor, specific for kinesin Eg5. Inhibits Eg5-driven microtubule sliding velocity in a reversible fashion with a IC50 of 500 nM. The S and D-enantiomers of tritylcysteine are nearly equally potent. No inhibition of KIF2A/Kif2 (kinesin-13 family), KIF2C/MCAK (kinesin-13 family), KIF5B/HsuKHC (kinsin-1 family), KIF19/HsCENP-E (kinesin-7 family), KIF20A/HsRabK6 (kinsin-6 family), KIF22A/HsKid (kinesin-10 family), KIF23/HsMKLP1 (kinesin-6 family), KIFC1/HsKIFC1 (kinesin-14 family)
additional information
the architecture of kinesin-3 KLP-6 reveals a cooperative multilevel-lockdown mechanism for autoinhibition. Autoinhibition of kinesin-3 ensures the proper spatiotemporal control of the motor activity for intracellular transport. All the internal coiled-coil segments and domains in KLP-6 cooperate to successively lock down the neck and motor domains. The first coiled-coil segment is melted into several short helices that work with the motor domain to restrain the entire neck domain. The second coiled-coil segment associates with its neighboring FHA and MBS domains and integrates with the tail MATH domain to form a supramodule that synergistically wraps around the motor domain to trap the nucleotide and hinder the microtubule binding. This multilevel-lockdown mechanism for autoinhibition could be applicable to other kinesin-3 motors
-
additional information
-
synthetic peptides derived from the tail of kinesin inhibit the protein's ATPase and motor activities. A peptide that spans residues 904-933 exhibits the strongest inhibitory effect on steady-state motility and ATPase activity, reflecting diminished binding of the ADP-bound kinesin head to the microtubule. Tail-mediated inhibition of kinesin activity is mainly the product of allosteric inhibition induced by the intramolecular binding of kinesin tail domain to the motor domain
-
additional information
study of the discovery and optimization of hexahydro-2H-pyranol[3,2-c]quinolines, HHPQs, as inhibitors. Crystallographic data demonstrate that these potent and selectve inhibitors bind in an allosteric pocket of kinesin-5 distant from the nucleotide and microtubule binding sites; the activity assay for inhibition analysis are performed with a coupled ATP regeneration system with a total concentration of the kinesin-5 protein of approximately 50 nM in the reaction
-
additional information
-
study of the discovery and optimization of hexahydro-2H-pyranol[3,2-c]quinolines, HHPQs, as inhibitors. Crystallographic data demonstrate that these potent and selectve inhibitors bind in an allosteric pocket of kinesin-5 distant from the nucleotide and microtubule binding sites; the activity assay for inhibition analysis are performed with a coupled ATP regeneration system with a total concentration of the kinesin-5 protein of approximately 50 nM in the reaction
-
additional information
development of small molecule inhibitors of the enzyme Kif11 ATPase activity
-
additional information
identification of optimized small molecule inhibitors of the mitotic kinesin Kif18A, usage of BTB-1 as a lead compound, structure-activity relationship studies and inhibition mechanism of BTB-1 and its analogues, overview
-
additional information
-
identification of optimized small molecule inhibitors of the mitotic kinesin Kif18A, usage of BTB-1 as a lead compound, structure-activity relationship studies and inhibition mechanism of BTB-1 and its analogues, overview
-
additional information
kinesin performs autoinhibition, addition of a negative charge at Ser175 favors the autoinhibited conformation of kinesin
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kinesin spindle protein activator-1
-
accelerates the basal ATP turnover rate circa 10fold in the absence of microtubules
-
microtubules
-
strong increase in ATPase activity in the presence of microtubules
-
microtubuli
-
ATPase activity of Kip3p is activated by both microtubules and unpolymerized tubulin
-
potassium acetate
-
full-length protein and truncated protein Kif3-592, optimum concentration 200 mM leading to maximum speed of 2 micrometer per s
tubulin-vinblastine assemblies
stimulation of the ATPase activity of the enzyme
-
unpolymerized tubulin
-
ATPase activity of Kip3p is activated by both microtubules and unpolymerized tubulin
-
microtubule
the ATPase activity of KLP-12 is stimulated about 33times by microtubules
-
microtubule
-
half-maximal activation for full-length protein 0.00029 mM, for truncated form Kif3-592 0.000304 mM, for truncated form Kif3-342 0.002146 mM
-
microtubule
-
concentration for half-maximal stimulation of wild-type 0.0009 mM. Analysis of stimulation for mutants G272C, S275C, A247C, L249C, A252C in native form and modified with 4-phenylazophenyl maleimid
-
tubulin heterodimer
-
half-maximal activation at 0.00129 mM for Schizosaccharamyces pombe tubulin, at 0.00062 mM for rat brain tubulin
-
tubulin heterodimer
-
half-maximal activation at 0.00203 mM for Schizosaccharamyces pombe tubulin, at 0.00086 mM for brain tubulin
-
additional information
-
Switch I is a common regulatory target for kinesin-1, a conserved essential regulatory element in the kinesin-1 tail interacts directly and specifically with the enzymatically critical Switch I region of the head. This interaction suggests a mechanism for tail-mediated regulation of the ATPase activity of kinesin-1
-
additional information
microtubule-stimulated ATPase activity of wild-type monomeric KIF4
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.032
Alexa Fluor 647 ATP
-
+/-0.022 mM, Vmax: 247 nmol/s, pH and temperature not specified in the publication. The fluorescent ATP analog can fuel kinesin-1'S processsive motion and is a suitable substrate analog, but it alters the motor's kinetic parameters
0.000047
ATP
pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DSK
0.000058
ATP
pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DVK
0.00008
ATP
pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain wild-type
0.00018
ATP
pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain mutant L2
0.0006
ATP
pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant DSK
0.00062
ATP
pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain mutant L2
0.00105
ATP
pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant DVK
0.0013
ATP
pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant L2
0.00243
ATP
KIF16B, at 25°C, pH not specified in the publication
0.00388
ATP
pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain wild-type
0.004
ATP
-
in 12.5 mM ACES-KOH, 25 mM potassium acetate, 5 mM MgCl2, 0.5 M EGTA, pH 6.8, at 22°C
0.00423
ATP
KIF13B, at 25°C, pH not specified in the publication
0.00516
ATP
KIF13A, at 25°C, pH not specified in the publication
0.00634
ATP
wild-type KIF4 enzyme, pH and temperature not specified in the publication
0.00703
ATP
KIF1A, at 25°C, pH not specified in the publication
0.01023
ATP
KHC, at 25°C, pH not specified in the publication
0.0134
ATP
-
+/-0.0006 mM, Vmax: 575 nmol/s, pH and temperature not specified in the publication
0.035
ATP
recombinant wild-type K888, pH and temperature not specified in the publication
0.044
ATP
recombinant K888 mutants S175A and S175D, pH and temperature not specified in the publication
46
ATP
-
in the absence of microtubules with 0.05 mM kinesin spindle protein activator-1
103
ATP
-
in the presence of microtubules, with 0.03 mM kinesin spindle protein activator-1
additional information
additional information
-
the kinetic analysis suggests futile ATP hydrolysis cycles, because a representative monomer shows a faster ATP turnover than the dimer while supporting slower motility. The K0.5MT (microtubule) is 70fold lower, the microtubule-bound portion of the kinetic cycle 8fold longer and the microtubule detachment rate almost 15fold slower than the dimer
-
additional information
additional information
-
overview, comparison of the kinetic parameters of monomeric and dimeric NcKin3
-
additional information
additional information
-
steady state and transient kinetics studies of fluorescence-labeled W127C mutant
-
additional information
additional information
microtubule-activated ATPase kinetics of wild-type and mutant enzymes
-
additional information
additional information
Michaelis-Menten kinetics, and steady-state ATPase activities of three types of chimeric construct, overview
-
additional information
additional information
modeling reveals allosterically coupled motions driving the APO to ATP transition of ATPase states, binding free energy analysis
-
additional information
additional information
-
modeling reveals allosterically coupled motions driving the APO to ATP transition of ATPase states, binding free energy analysis
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
34
ADP
-
in presence of microtubule the ATP hydrolysis is activated 3fold to 4fold compared to kcat, 125 vs. 34 s-1, while phosphate release is approximately equally fast: 29 s-1, pH and temperature not specified in the publication
0.0009
methylanthraniloyl-ATP
-
basal activity, in absence of tubulin or microtubles, pH 6.9, 25°C
29
phosphate
-
in presence of microtubule the ATP hydrolysis is activated 3fold to 4fold compared to kcat, 125 vs. 34 s-1, while phosphate release is approximately equally fast: 29 s-1, pH and temperature not specified in the publication
0.00095
ATP
-
basal activity, in absence of tubulin or microtubles, pH 6.9, 25°C
0.069
ATP
pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain mutant L2
0.079
ATP
pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DSK
0.1
ATP
pH 6.8, 25°C, tubuline-stimulated recombinant Kif2C functional domain mutant DVK
0.117
ATP
pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain mutant L2
0.152
ATP
pH 6.8, 25°C, tubulin-stimulated recombinant Kif2C functional domain wild-type
0.18
ATP
pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant DSK
0.21
ATP
pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant L2
0.62
ATP
pH 6.8, 25°C, tubulin-vinblastine-stimulated recombinant Kif2C functional domain wild-type
0.97
ATP
pH 6.8, 25°C, microtubule-stimulated recombinant Kif2C functional domain mutant DVK
1.4
ATP
-
in the absence of microtubules with 0.05 mM kinesin spindle protein activator-1
4.4
ATP
-
in the presence of microtubules, with 0.03 mM kinesin spindle protein activator-1
23.2
ATP
-
in 12.5 mM ACES-KOH, 25 mM potassium acetate, 5 mM MgCl2, 0.5 M EGTA, pH 6.8, at 22°C
42.1
ATP
wild-type KIF4 enzyme, pH and temperature not specified in the publication
95.44
ATP
KHC, at 25°C, pH not specified in the publication
124.7
ATP
KIF16B, at 25°C, pH not specified in the publication
171.8
ATP
KIF13B, at 25°C, pH not specified in the publication
181.7
ATP
KIF13A, at 25°C, pH not specified in the publication
290.9
ATP
KIF1A, at 25°C, pH not specified in the publication
additional information
additional information
-
in presence of microtubule the ATP hydrolysis is activated 3fold to 4fold compared to kcat, 125 vs. 34 s-1, while phosphate release is approximately equally fast: 29 s-1
-
additional information
additional information
-
steady state ATPase parameters, kcat values and gliding velocities of truncated NcKin3 constructs
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000001 - 0.00035
N-(3-aminopropyl)-N-[(1R)-1-(3-benzyl-7-chloro-4-oxo-3,4-dihydroquinazolin-2-yl)-2-methylpropyl]-3-fluoro-4-methylbenzamide
0.0000017
6-[4-(trifluoromethyl)phenyl]-3,4-dihydroquinolin-2(1H)-one
-
wild-type, pH 6.8
0.000066
6-[4-(trifluoromethyl)phenyl]-3,4-dihydroquinolin-2(1H)-one
-
mutant I299F, pH 6.8
0.000109
6-[4-(trifluoromethyl)phenyl]-3,4-dihydroquinolin-2(1H)-one
-
mutant A356T, pH 6.8
0.00045
ADP
motor domain (amino acid residues 1-358), competitive inhibition of 2'-(3')-O-(N-methylanthraniloyl)ATP binding in the absence of microtubles, pH 7.2, temperature not specified in the publication
0.0033
ADP
motor domain (amino acid residues 1-368), competitive inhibition of 2'-(3')-O-(N-methylanthraniloyl)ATP binding in the absence of microtubles, pH 7.2, temperature not specified in the publication
0.048
ADP
motor domain (amino acid residues 1-368), competitive inhibition of 2'-(3')-O-(N-methylanthraniloyl)ATP binding in the presence of microtubles, pH 7.2, temperature not specified in the publication
0.054
ADP
motor domain (amino acid residues 1-358), competitive inhibition of 2'-(3')-O-(N-methylanthraniloyl)ATP binding in the presence of microtubles, pH 7.2, temperature not specified in the publication
0.000001
N-(3-aminopropyl)-N-[(1R)-1-(3-benzyl-7-chloro-4-oxo-3,4-dihydroquinazolin-2-yl)-2-methylpropyl]-3-fluoro-4-methylbenzamide
-
wild-type
0.00035
N-(3-aminopropyl)-N-[(1R)-1-(3-benzyl-7-chloro-4-oxo-3,4-dihydroquinazolin-2-yl)-2-methylpropyl]-3-fluoro-4-methylbenzamide
-
mutant D130V
0.0000035
N-[3-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
-
wild-type
0.000006
N-[3-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]sulfuric diamide
-
mutant D130V
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methanamine
Homo sapiens
pH and temperature not specified in the publication
0.0009
(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)(1-methylpiperidin-3-yl)methanone
Homo sapiens
pH and temperature not specified in the publication
0.0081
(2R)-2-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-methylbutan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000138
(2R)-2-amino-3-((1,1,2-triphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0002518
(2R)-2-amino-3-((1,1-bis(4-chlorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001782
(2R)-2-amino-3-((1,1-bis(4-fluorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001065
(2R)-2-amino-3-((1,1-bis(4-methylphenyl)-2-phenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0002168
(2R)-2-amino-3-((1-(2-fluorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001912
(2R)-2-amino-3-((1-(3,4-dichlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001289
(2R)-2-amino-3-((1-(3-chlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0005675
(2R)-2-amino-3-((1-(3-chlorophenyl)-1-(4-chlorophenyl)-2-phenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0000676
(2R)-2-amino-3-((1-(3-hydroxyphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0000586
(2R)-2-amino-3-((1-(4-chlorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001505
(2R)-2-amino-3-((1-(4-fluorophenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001594
(2R)-2-amino-3-((1-(4-hydroxyphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001676
(2R)-2-amino-3-((1-(4-methylphenyl)-1,2-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.005278
(2R)-2-amino-3-((2-(3,4-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0002375
(2R)-2-amino-3-((2-(3-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0004558
(2R)-2-amino-3-((2-(4-chlorophenyl)-1,1-diphenylethyl)sulfanyl)propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.01584
(2R)-2-amino-3-[(1,1,3-triphenylpropyl)sulfanyl]propanoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000006
(2R,4aS,5R,10bS)-2-((1H-1,2,4-triazol-1-yl)methyl)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00076
(2S)-2-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-methylbutan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.01
(4aS,10bS)-9-(tert-butyl)-5-(3-chlorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00087
(4aS,10bS)-9-(tert-butyl)-5-(3-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.0003
(4aS,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline-9-carbonitrile
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline-9-carboxylic acid
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.0037
(4aS,5R,10bS)-5-phenyl-9-(trifluoromethoxy)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00011
(4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00036
(4aS,5R,10bS)-5-phenyl-9-propyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-7,9-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00009
(4aS,5R,10bS)-7-fluoro-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-8,10-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00125
(4aS,5R,10bS)-8,9-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-8-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00054
(4aS,5R,10bS)-8-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00091
(4aS,5R,10bS)-9-(pentafluoro-lambda6-sulfanyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-9-(tert-butyl)-5-(1H-imidazol-2-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00017
(4aS,5R,10bS)-9-(tert-butyl)-5-(2-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.0068
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-chlorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-fluoro-4-methoxyphenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00035
(4aS,5R,10bS)-9-(tert-butyl)-5-(3-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00027
(4aS,5R,10bS)-9-(tert-butyl)-5-(4-fluorophenyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.0011
(4aS,5R,10bS)-9-(tert-butyl)-5-(pyridin-3-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00053
(4aS,5R,10bS)-9-(tert-butyl)-5-(thiazol-2-yl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00012
(4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00072
(4aS,5R,10bS)-9-chloro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00013
(4aS,5R,10bS)-9-ethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00013
(4aS,5R,10bS)-9-isopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.00042
(4aS,5R,10bS)-9-methyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
pH and temperature not specified in the publication
0.0053
(4aS,5R,10bS)-N,N-dimethyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-amine
Homo sapiens
pH and temperature not specified in the publication
0.01
(4aS,5S,10bS)-9-(tert-butyl)-5-cyclohexyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinoline
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.4145
(5E)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(2Z)-3-(4-methoxyphenyl)prop-2-en-1-ylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.2476
(5E)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(2Z)-3-phenylprop-2-en-1-ylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0621
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-benzylidene-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0719
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(2,3-dimethoxyphenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0132
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(2-chlorophenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.1329
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(2-fluorophenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.1119
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(3,4-dimethoxyphenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0478
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(3-chlorophenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.051
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(3-methoxyphenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0275
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(3-nitrophenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.1287
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(3Z)-4-[4-(dimethylamino)cyclohexa-2,4-dien-1-yl]but-3-en-1-ylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0392
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(4-bromophenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.1062
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(4-chlorophenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0427
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(4-methoxyphenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0633
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(4-methylphenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0202
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(4-nitrophenyl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.0172
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(benzyloxy)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.3306
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(furan-2-yl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.12
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(pyridin-2-yl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.1335
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[(thiophen-2-yl)methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.2522
(5Z)-2-[(4-acetyl-5-methyl-5-phenyl-4,5-dihydro-1,3,4-thiadiazol-2-yl)amino]-5-[[4-(dimethylamino)phenyl]methylidene]-1,3-thiazol-4(5H)-one
Homo sapiens
pH and temperature not specified in the publication
0.000058
1-((2R,4aS,5R,10bS)-5-(4-fluorophenyl)-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
Homo sapiens
pH and temperature not specified in the publication
0.000004
1-((2R,4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
Homo sapiens
pH and temperature not specified in the publication
0.000003
1-((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
Homo sapiens
pH and temperature not specified in the publication
0.000011
1-((2R,4aS,5R,10bS)-9-cyclopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)-N-methylmethanamine
Homo sapiens
pH and temperature not specified in the publication
0.0025
1-(1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
Homo sapiens
i.e. tetrahydro-beta-carboline, pH and temperature not specified in the publication
0.0001
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-(piperidin-1-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0002
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
Homo sapiens
pH and temperature not specified in the publication
0.00046
1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000008
1-(2-(dimethylamino)ethyl)-3-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)urea
Homo sapiens
i.e. EMD 534085, pH and temperature not specified in the publication
0.00001
1-(3-hydroxypropyl)-3-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)urea
Homo sapiens
pH and temperature not specified in the publication
0.01
1-(4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenyl)ethanone
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00086
1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-2-(piperidin-4-yl)ethanone
Homo sapiens
pH and temperature not specified in the publication
0.0102
1-(benzenesulfonyl)-2,4-dinitrobenzene
Homo sapiens
pH and temperature not specified in the publication
0.0103
1-(benzenesulfonyl)-2-nitro-4-(trifluoromethyl)benzene
Homo sapiens
pH and temperature not specified in the publication
0.003
1-(benzenesulfonyl)-2-nitrobenzene
Homo sapiens
pH and temperature not specified in the publication
0.0017
1-(benzenesulfonyl)-4-chloro-2-nitrobenzene
Homo sapiens
pH and temperature not specified in the publication
0.0048
1-(benzenesulfonyl)-4-fluoro-2-nitrobenzene
Homo sapiens
pH and temperature not specified in the publication
0.000067
1-[4-(2,2,3,3-tetrafluoro-2,3-dihydro-1,4-benzodioxin-6-yl)phenyl]urea
Homo sapiens
-
-
0.000019
2-((((2R,4aS,5R,10bS)-9-(tert-butyl)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)(ethyl)amino)ethanol
Homo sapiens
pH and temperature not specified in the publication
0.000007
2-((((2R,4aS,5R,10bS)-9-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)amino)ethanol
Homo sapiens
pH and temperature not specified in the publication
0.0006845
2-((1,1,2-triphenylethyl)sulfanyl)ethanaminium tetrafluoroborate
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0004037
2-((1,1-bis(4-chlororophenyl)-2-phenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0005878
2-((1,1-bis(4-fluorophenyl)-2-phenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000261
2-((1,1-bis(4-methylphenyl)-2-phenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0007895
2-((1-(2-fluorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0002293
2-((1-(3,4-dichlorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000519
2-((1-(3-chlorophenyl)-1,2-diphenylethyl)sulfanyl)ethanaminium tetrafluoroborate
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0004367
2-((1-(3-chlorophenyl)-1-(4-chlorophenyl)-2-phenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0002561
2-((1-(3-hydroxyphenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001409
2-((1-(4-chlorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0005779
2-((1-(4-fluorophenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0006656
2-((1-(4-hydroxylphenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0001719
2-((1-(4-methylphenyl)-1,2-diphenylethyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000005
2-((2R,4aS,5R,10bS)-9-(tert-butyl)-2-((methylamino)methyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
Homo sapiens
pH and temperature not specified in the publication
0.0005
2-((4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-yl)acetonitrile
Homo sapiens
pH and temperature not specified in the publication
0.01
2-((4aS,5R,10bS)-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-9-yl)ethanol
Homo sapiens
pH and temperature not specified in the publication
0.0003
2-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)-4-chlorobenzenethiol
Homo sapiens
pH and temperature not specified in the publication
0.000025
2-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
Homo sapiens
pH and temperature not specified in the publication
0.0009422
2-((diphenyl(pyridin-4-yl)methyl)sulfanyl)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0415
2-(2,4-difluorophenyl)-9-(3,4-dimethylphenyl)-8-oxo-8,9-dihydro-7H-purine-6-carboxamide
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.004 - 0.0055
2-(2-sulfanylethoxy)ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
0.0064
2-(4-chloro-2-nitrobenzene-1-sulfonyl)thiophene
Homo sapiens
pH and temperature not specified in the publication
0.000014
2-(dimethylamino)ethyl (((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)carbamate
Homo sapiens
pH and temperature not specified in the publication
0.000004
2-(methylamino)-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)ethanesulfonothioamide
Homo sapiens
pH and temperature not specified in the publication
0.0002412
2-(tritylthio)ethanamine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000049
2-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)ethanone
Homo sapiens
pH and temperature not specified in the publication
0.001
2-[1-(4-methoxyphenyl)-5-oxo-3-[2-(thiophen-2-yl)ethyl]-2-thioxoimidazolidin-4-yl]-N-phenylacetamide
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.0045 - 0.0115
2-[2-(acetylsulfanyl)ethoxy]ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
0.0023
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)aniline
Homo sapiens
pH and temperature not specified in the publication
0.00012
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzenethiol
Homo sapiens
pH and temperature not specified in the publication
0.00004
3-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
Homo sapiens
pH and temperature not specified in the publication
0.000186
3-(2-((2-aminoethyl)sulfonyl)-6-chloro-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)phenol
Homo sapiens
pH and temperature not specified in the publication
0.000002
3-(dimethylamino)-N-(((2R,4aS,5R,10bS)-9-isopropyl-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)propane-1-sulfonamide
Homo sapiens
pH and temperature not specified in the publication
0.0066
3-amino-1-(1-(2-aminopyridin-4-yl)-6-chloro-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0001
3-amino-1-(1-(3-fluorophenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00063
3-amino-1-(1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0002
3-amino-1-(1-(3-hydroxyphenyl)-6-(trifluoromethoxy)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.025
3-amino-1-(1-(3-hydroxyphenyl)-6-isopropyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
above 0.025 mM, pH and temperature not specified in the publication
0.00002 - 0.000058
3-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
0.0017
3-amino-1-(1-(3-hydroxyphenyl)-6-phenyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.011
3-amino-1-(1-(3-methoxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000027
3-amino-1-(6-bromo-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000039
3-amino-1-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00023
3-amino-1-(6-chloro-1-cyclohexyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000011
3-amino-1-(6-ethyl-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00076
3-amino-1-(6-fluoro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0045
3-amino-1-(6-hydroxy-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000175
3-amino-1-(6-methyl-1-phenyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000007
3-amino-N-methyl-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)propane-1-sulfonothioamide
Homo sapiens
pH and temperature not specified in the publication
0.0005142
4-((((2R)-2-ammonio-2-carboxyethyl)sulfanyl)(diphenyl)-methyl)pyridinium tetrafluoroborate
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.000004
4-((2R,4aS,5R,10bS)-2-((methylamino)methyl)-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
Homo sapiens
pH and temperature not specified in the publication
0.000017
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)-2-fluorophenol
Homo sapiens
pH and temperature not specified in the publication
0.000095
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)benzene-1,2-diol
Homo sapiens
pH and temperature not specified in the publication
0.000034
4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenol
Homo sapiens
pH and temperature not specified in the publication
0.01
4-((4aS,5S,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)butan-1-ol
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.00023
4-(2-[1-(2,4,6-trifluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
Homo sapiens
-
0.00033
4-(2-[1-(2,4-difluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
Homo sapiens
-
0.00028
4-(2-[1-(2,6-difluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
Homo sapiens
-
0.00054
4-(2-[1-(4-fluorophenyl)cyclopropyl]-1,3-thiazol-4-yl)pyridine
Homo sapiens
pH 6.8, 22°C
0.000086
4-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)butan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.0791
4-[[3-(methoxycarbonyl)-2-methyl-5a,9a-dihydronaphtho[1,2-b]furan-5-yl]sulfamoyl]benzoic acid
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.025
5-(2-(3-aminopropanoyl)-6-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)benzo[d]oxazol-2(3H)-one
Homo sapiens
above 0.025 mM, pH and temperature not specified in the publication
0.0063
5-(2-fluorophenyl)-2,9-dimethyl-5,6-dihydropyrazolo[1,5-c]quinazoline
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.000532
5-[2-(1-phenylcyclopropyl)-1,3-thiazol-4-yl]pyridine-2-carbonitrile
Homo sapiens
-
0.0625
ethyl 3-acetyl-4-[3-(acetyloxy)phenyl]-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
cell-based assay on monoastral spindles
0.0061 - 0.0513
ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
0.05
ethyl 4-[3-(acetyloxy)phenyl]-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
cell-based assay on monoastral spindles
0.0015 - 0.0092
furan-2-yl[4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl]methanone
0.0031
N,N-diethyl-5,5-dimethyl-2-(2-thienylcarboxamido)-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000005
N-(((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)-4-(dimethylamino)butanamide
Homo sapiens
pH and temperature not specified in the publication
0.000002
N-(((2R,4aS,5R,10bS)-9-chloro-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)-2-(dimethylamino)ethanesulfonamide
Homo sapiens
pH and temperature not specified in the publication
0.000006
N-(2-((((2R,4aS,5R,10bS)-9-bromo-7-fluoro-5-phenyl-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)amino)ethyl)acetamide
Homo sapiens
pH and temperature not specified in the publication
0.000065
N-(2-aminoethyl)-4-methyl-N-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.025
N-(3-(2-(3-aminopropanoyl)-6-methyl-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indol-1-yl)phenyl)methanesulfonamide
Homo sapiens
above 0.025 mM, pH and temperature not specified in the publication
0.000155
N-(3-(6-chloro-1-(3-hydroxyphenyl)-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)-3-oxopropyl)methanesulfonamide
Homo sapiens
pH and temperature not specified in the publication
0.01
N-(4-((4aS,5R,10bS)-9-(tert-butyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-5-yl)phenyl)acetamide
Homo sapiens
above 0.01 mM, pH and temperature not specified in the publication
0.0006
N-(4-fluorophenyl)-2-[1-(4-fluorophenyl)-3-[2-(3-methylthiophen-2-yl)ethyl]-5-oxo-2-thioxoimidazolidin-4-yl]acetamide
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.0024
N-(4-methoxyphenyl)-2-[3-[2-(3-methylthiophen-2-yl)ethyl]-5-oxo-1-phenyl-2-thioxoimidazolidin-4-yl]acetamide
Homo sapiens
-
inhibition of basal ATPase activity, pH 6.9, 25°C
0.000019
N1-phenyl-N1-(((2R,4aS,5R,10bS)-5-phenyl-9-(trifluoromethyl)-3,4,4a,5,6,10b-hexahydro-2H-pyrano[3,2-c]quinolin-2-yl)methyl)ethane-1,2-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0742
trans-2,3-bis[(2,5-dioxo-1-[4-[(E)-2-phenyldiazen-1-yl]phenyl]pyrrolidin-3-yl)sulfanyl]butanedioic acid
Mus musculus
kinesin Eg5, at pH 7.2 and 25°C
0.004
2-(2-sulfanylethoxy)ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of basal ATPase activity
0.0055
2-(2-sulfanylethoxy)ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of microtubule-stimulated ATPase activity
0.0045
2-[2-(acetylsulfanyl)ethoxy]ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of basal ATPase activity
0.0115
2-[2-(acetylsulfanyl)ethoxy]ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of microtubule-stimulated ATPase activity
0.00002
3-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000058
3-amino-1-(1-(3-hydroxyphenyl)-6-methyl-3,4-dihydro-1H-pyrido[3,4-b]indol-2(9H)-yl)propan-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00000045
6-[4-(trifluoromethyl)phenyl]-3,4-dihydroquinolin-2(1H)-one
Homo sapiens
-
mutant D130V, pH 6.8
0.000036
6-[4-(trifluoromethyl)phenyl]-3,4-dihydroquinolin-2(1H)-one
Homo sapiens
-
wild-type, pH 6.8
0.0061
ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of basal ATPase activity
0.0123
ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
22°C, inhibition of microtubule-stimulated ATPase activity
0.0513
ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carboxylate
Homo sapiens
-
cell-based assay on monoastral spindles
0.0015
furan-2-yl[4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl]methanone
Homo sapiens
-
22°C, inhibition of basal ATPase activity
0.003
furan-2-yl[4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl]methanone
Homo sapiens
-
22°C, inhibition of microtubule-stimulated ATPase activity
0.0092
furan-2-yl[4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidin-5-yl]methanone
Homo sapiens
-
cell-based assay on monoastral spindles
0.0001859
S-trityl-L-cysteine
Homo sapiens
-
inhibition of basal ATPase activity, pH not specified in the publication, 25°C
0.0005
S-trityl-L-cysteine
Homo sapiens
-
tight binding inhibitor, specific for kinesin Eg5. Inhibits Eg5-driven microtubule sliding velocity in a reversible fashion with a IC50 of 500 nM. The S and D-enantiomers of tritylcysteine are nearly equally potent. No inhibition of KIF2A/Kif2 (kinesin-13
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the enzyme activity is proportional to the amount of microtubules. The motor domain with the stalk region shows higher enzyme activity than the motor domain alone in the presence of 0.04 mg of microtubules, suggesting that BC12 has microtubule-dependent ATPase activity and that the neck linker is critial for this activity
additional information
AK065586
1.19 mol phosphate/kinesin mol/min in the absence of microtubles, 90.6 mol phosphate/kinesin mol/min in the presence of microtubles, Vmax/2 at 0.0037 mM microtubles, pH 7.5, 25°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
monomeric and dimeric activation energies (Arrhenius equation) 5.2 kJ/mol and 4.1 kJ/mol, respectively
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 35
15 - 35
the velocity of the enzyme increases non-linearly, by a factor of about 3, from 15 to 35°C. The average run length increases by a factor 2-3 from 15 to 25°C
15 - 35
-
the velocity of the enzyme increases non-linearly, by a factor of about 3, from 15 to 35°C. The average run length increases by a factor 2-3 from 15 to 25°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q07866; P33176
KIF5B to be expressed in triple negative (TN)-basal-like/claudin lowbreast cancer subtype. KLC1 is expressed in epithelial/luminal breast cancer subtypes
brenda
additional information
-
BC12 is mainly expressed in tissues undergoing cell division and secondary wall thickening
brenda
-
KIF4 colocalizes with the ribosomal protein P0 in dorsal root ganglia neurons
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
kinesin KIF16B transports early endosomes to the plus end of microtubules
brenda
-
the FLA3 KAP subunit is required for localization of kinesin-2 to the site of flagellar assembly and processive anterograde intraflagellar transport
-
brenda
specifically to the phragmoplast midzone during telophase and cytokinesis
brenda
-
KIF1C is enriched at a subset of microtubule plus ends, that contact podosomes
brenda
additional information
-
KINA is important for cytoplasmic dynein accumulation to the plus ends of microtubules
brenda
-
the majority of large dense-core vesicle transport to the plasma membrane in beta-cells is mediated by kinesin I
brenda
-
binding site of plus-end-directed kinesin heavy chain (KHC) on microtubule
brenda
-
kinesin motor domain interacts with both alpha- and beta-tubulin
brenda
paclitaxel-stabilized microtubules are used for activity assays
brenda
structure of the kinesin-microtubule complex, overview
brenda
-
kinesins bind mainly to beta tubulin with the switch-2 helix close to the intradimer interface between alpha and beta tubulin
brenda
orphan kinesin TbKIN-D associates with cytoskeletal microtubules and is distributed throughout the cytoskeleton at all cell cycle stages
brenda
-
the motor is adapted to special requirements of mitochondrial shaping. A high local motor accumulation may allow microtubule interaction and local expansion of the mitochondrium
brenda
-
kinesin light chain KLC3 can associate with mitochobdria
brenda
-
KIFC1 accumulates at the nucleus after treatment with brefeldin A and nocodazole
brenda
additional information
wild-type KLP-6 is largely localized in the cell body, while most of the mutants show significantly increased accumulations at the cell tips, except for the E564A and F698Q mutants
-
brenda
additional information
-
KIFC1 is associated with membranous organelles, not associated with the mitotic spindle
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the enzyme is a mmember of the kinesin superfamily of molecular motors
evolution
conventional kinesin is the founding member of a superfamily of molecular motors that use the energy of ATP hydrolysis to transport cargo along microtubules, serving essential roles in a wide variety of cellular processes, most notably mitosis and neuronal transport
evolution
Q07866; P33176
kinesins encompass a large family of proteins that are well-known to mediate intracellular movement and cytoplasmic transport of membranous organelles and macromolecules along the microtubules network
evolution
kinesin-3 is a unique subfamily of processive kinesin motors in terms of autoinhibition. Instead of forming a constitutive dimer,most of kinesin-3 motors primarily exist as a self-folded monomer for autoinhibition, although some kinesin-3 members can adopt an autoinhibited dimeric conformation
evolution
kinesin-3s KIF13A and KIF13B are members of the plus-end directed kinesin-1 family (KIF5A/B/C)
malfunction
disruptions in microtubule motor transport are associated with a variety of neurodegenerative diseases. Phosphorylation at serine 175/176 via c-Jun N-terminal kinase-3 is associated with Huntington disease and spinal and bulbar muscular atrophy
malfunction
disruptions in microtubule motor transport are associated with a variety of neurodegenerative diseases. Phosphorylation at serine 175/176 via c-Jun N-terminal kinase-3 is associated with Huntington disease and spinal and bulbar muscular atrophy. The ATPase, microtubule-binding affinity, and processivity are unchanged between a phosphomimetic S175D and a nonphosphorylatable S175A construct of kinesin. Placement of negative charge at Ser175, through phosphorylation or mutation, leads to a lower stall force and decreased velocity, addition of a negative charge at Ser175 favors the autoinhibited conformation of kinesin
malfunction
depletion of TbKIN-D disrupts cell morphology, resulting in elongation of the posterior of the cell, which is filled with newly assembled microtubules. RNAi of TbKIN-D impairs organelle segregation and leads to severe growth inhibition and cell death, TbKIN-D deficiency significantly interferes with cytoskeletal microtubules, phenotype
malfunction
inhibition of Eg5 causes cell cycle arrest in mitosis with the irregular formation of monopolar spindles and subsequent apoptotic cell death
malfunction
cell division rate is reduced, cell-cycle progression is delayed and multinucleate cells are observed in an enzyme mutant. Reduction of ATPase activity in the enzyme inhibits cell division and organ development
malfunction
-
kinesin KIF4 knockdown suppresses both hepatitis B virus and hepatitis delta virus infection
malfunction
mutations in the neuronal kinesin motor (KIF5A) are linked to a neurodegenerative disease, hereditary spastic paraplegia
malfunction
-
mutant of kinesin 5-c (KRP125c) shows severe phragmoplast defects with enlarged cells, multiple nuclei and incomplete cell plate deposition
malfunction
conditional knockout of Kif5b (KIF5BcKO) in CaMKIIa-Cre-expressing neurons shows heightened turnover and lower stability of dendritic spines in layer 2/3 pyramidal neurons with reduced spine postsynaptic density protein 95 acquisition in the mouse cortex. Spine preceding transport of FMRP is abolished in KIF5B cKO mice, and learning-dependent localization is disrupted in KIF5B cKO mice. cKO of kif5b impairs fear-learning-dependent spine plasticity and the associated FMRP localization. Phenotype, overview
malfunction
loss of function of two Kifs, KIF3A, a kinesin-2 family member, and KIF5C, a kinesin-1 family member, expressed in the same hippocampal (HP) neuron, diminishes excitatory synaptic transmission, dendritic arborization, synapse density, and morphology. Both KIF5C and KIF3A knockdown (KD) reduce synaptic strength across excitatory synapses, meaning expression of both KIF5C and KIF3A is critical for excitatory synaptic transmission contributed by both functional and morphological changes at synapse
malfunction
autoinhibition of kinesin-3 ensures the proper spatiotemporal control of the motor activity for intracellular transport. Disruptions of the interdomain interfaces restore the motor activity of KLP-6. Microtubule-stimulated ATPase activities of the wild-type and various mutants of full-length KLP-6, overview
malfunction
-
loss of function of two Kifs, KIF3A, a kinesin-2 family member, and KIF5C, a kinesin-1 family member, expressed in the same hippocampal (HP) neuron, diminishes excitatory synaptic transmission, dendritic arborization, synapse density, and morphology. Both KIF5C and KIF3A knockdown (KD) reduce synaptic strength across excitatory synapses, meaning expression of both KIF5C and KIF3A is critical for excitatory synaptic transmission contributed by both functional and morphological changes at synapse
-
metabolism
a bias that favors motion toward the minus-end of microtubules might be used to tune transport in healthy cells when properly regulated but contribute to a disease state when misregulated
metabolism
KIF5B is involved in the dendritic targeting of synaptic proteins that underlies dendritic spine plasticity
metabolism
expression of both KIF5C and KIF3A is critical for excitatory synaptic transmission contributed by both functional and morphological changes at synapse. Expression of both KIF3A and KIF5C is critical for excitatory synaptic transmission contributed by both functional and morphological changes at synapse
metabolism
Q07866; P33176
KIF5B/KLC1 function downstream of TGF-beta and PRL in TN-basal-like/claudin low cells, in which, a nuclear accumulation of KIF5B and its interaction with the EMT transcriptional regulator Snail1, independent of KLC1, is found. In addition, TGF-beta mediated pro-invasive activity is dependent on KIF5B expression. In contrast, the epithelial differentiation factor and EMT suppressor prolactin (PRL) represses KIF5B gene expression and KIF5BSnail1 nuclear accumulation, but enhances KLC1 gene expression and KIF5B-KLC1 interaction. KIF5B shows high nuclear accumulation and interaction with Snail1 in TN-basal-like/claudin low cells. Kinesin-1 function in breast tumorigenesis by regulating EMP programing and aggressiveness, overview
metabolism
transport toward microtubule plus ends depends on several kinesin families, whereas minus-end directed movement in animal cells is mostly driven by cytoplasmic dynein (EC 5.6.1.4). Kinesin-driven Rab6 vesicle transport spatially regulates secretion in mammalian cells. Kinesins control the spatial distribution but not the efficiency of exocytosis
metabolism
-
expression of both KIF5C and KIF3A is critical for excitatory synaptic transmission contributed by both functional and morphological changes at synapse. Expression of both KIF3A and KIF5C is critical for excitatory synaptic transmission contributed by both functional and morphological changes at synapse
-
physiological function
-
BC12 functions as a dual-targeting kinesin protein and is implicated in cell-cycle progression, cellulose microfibril deposition and wall composition in the monocot plant rice. Perturbation of BC12 produces defects in cell number/plant height and mechanical properties. BC12 has a conserved ATPase-driven motor domain that is required for bindung to and moving along the microtubules
physiological function
-
kinesin-1 motor proteins move along microtubules in reptitive steps of 8 nm at the expense of ATP
physiological function
kinesin Eg5 is a member of the kinesin family of proteins, which hydrolyze ATP as they migrate along microtubules
physiological function
does not localize to the kinetochore region in the absence of kinetochore microtubules, strongly accumulates at the plus-end of kinetochore spindle microtubules during metaphase
physiological function
-
interacts with the mitochondrial outer membrane protein VDAC3 (voltage-dependent anion channel 3), regulates respiration during seed germination at low temperature
physiological function
the motor domain of kinesin-1 play a role in impaired fast axonal transport. When cargo is transported by both dynein and phosphorylated kinesin, a common occurrence in the cell, there may be a bias that favors motion toward the minus-end of microtubules, cf. EC 3.6.4.5
physiological function
the motor domain of kinesin-1 play a role in impaired fast axonal transport. When cargo is transported by both dynein and phosphorylated kinesin, a common occurrence in the cell, there may be a bias that favors motion toward the minus-end of microtubules
physiological function
the interaction of the kinesin-13 Kif2C KVD motif with tubulin is essential. The interaction of the KVD motif quantitatively determines the activities of Kif2C
physiological function
microtubules are a vital part of the cytoskeleton of eukaryotic cells and are involved in various cellular processes. The cytoskeleton of Trypanosoma brucei is characterized by an array of subpellicular microtubules and is essential for maintenance of cell shape and polarity, the orphan kinesin TbKIN-D in trypanosomes cooperates with a kinetoplastid-specific kinesin to maintain cell morphology by regulating subpellicular microtubules. The orphan kinesin TbKIN-D regulates the organization of subpellicular microtubules and is required for maintaining cell morphology, and TbKIN-D possesses in vitro ATPase activity and associates with cytoskeletal microtubules. Enzyme TbKIN-D is essential for cell proliferation and viability
physiological function
kinesin superfamily proteins are microtubule-based molecular motors driven by the energy derived from the hydrolysis of ATP. The ATP binding step is crucial both for the power stroke to produce motility and for the inter-domain regulation of ATPase activity to guarantee the processive movement of dimeric kinesin superfamily proteins. The binding of KIF4 to the microtubule may affect the interaction within the tubulin dimer by increasing or decreasing the curvature of the intra-tubulin dimer interface with some twist, molecular mechanism by which KIF4 inhibits microtubule dynamics
physiological function
microtubule-based transport by the kinesin motors, powered by ATP hydrolysis, is essential for a wide range of vital processes in eukaryotes
physiological function
kinesin spindle protein, i.e. Eg5 or KIF11, is a mitotic spindle motor protein
physiological function
the enzyme has a critical role during the metaphase-anaphase transition and cytokinesis
physiological function
Kif18A regulates spindle microtubules through its dual functionality (plus-end-directed and minus-end-directed), with microtubule-based stepping and regulation of microtubule dynamics
physiological function
the enzyme has a critical role during the metaphase-anaphase transition and cytokinesis
physiological function
the enzyme is involved in intraflagellar transport in the distal part of the cilium
physiological function
kinesin Eg5 plays a pivotal role in the separation of centrosomes during cell division
physiological function
-
the enzyme is required for flagella formation in male gametes
physiological function
-
the enzyme is required for flagella formation in male gametes
physiological function
the microtubule-dependent ATPase activity of the enzyme is indispensable in regulating normal cell division and organ development
physiological function
-
kinesin KIF4 plays an important role in hepatitis B virus/hepatitis delta virus infection and is a critical regulator of sodium taurocholate cox1etransporting polypeptide surface transport and localization
physiological function
-
the enzyme PAKRP2 is necessary for transporting vesicles to the phragmoplast midzone
physiological function
the enzyme is essential for proper length control of Caenorhabditis elegans axons in neurons, and its motor domain represses microtubule polymerization in vitro
physiological function
kinesin 1 (KIF5) is one major type of motor protein in neurons. Kinesin-1 heavy chain, KIF5B, plays important roles in dendritic spine plasticity and dendritic localization of PSD95 and FMRP in the mouse cortex in vivo, it promotes PSD95 gain and maintenance in dendritic spines. Translocation of synaptic proteins (PSD95 and gephyrin) and FMRP in dendrites in the mouse frontal cortex involving the enzyme, overview. KIF5B regulates synaptic protein composition and turnover of dendritic spines
physiological function
expression of KIF3A is critical for excitatory synaptic transmission contributed by both functional and morphological changes at synapse
physiological function
Q07866; P33176
kinesin family member 5B (KIF5B) and its partner protein kinesin light chain 1 (KLC1), subunits of kinesin-1, play differential roles in regulating EMP and tumorigenesis. KIF5B/KLC1 complex regulates epithelial mesenchymal plasticity programing in breast cancer determining breast cancer phenotype, stemness and aggressiveness. KIF5B is expressed in triple negative (TN)-basal-like/claudin low breast cancer subtype and is an inducer of epithelial-mesenchymal transition (EMT), stemness, invasiveness, tumor formation and metastatic colonization. KLC1 is expressed in epithelial/luminal breast cancer subtypes and is a suppressor of EMT, invasion, metastasis and stem cell markers expression as well as an inducer of epithelial/luminal phenotype. Kinesin-driven transport along microtubules is mediated by the concerted function of two kinesin subunits, the kinesin heavy chain (KHC) and the kinesin light chain (KLC)
physiological function
kinesins are microtubule-based molecular motors that drive longrange intracellular transport or organize intricate microtubule networks. Autoinhibition of kinesin-3 ensures the proper spatiotemporal control of the motor activity for intracellular transport
physiological function
Rab6-positive secretory vesicles are transported from the Golgi apparatus to the cell periphery by kinesin-1 KIF5B and kinesin-3 KIF13B, which determine the location of secretion events. KIF5B plays a dominant role, whereas KIF13B helps Rab6 vesicles to reach freshly polymerized microtubule ends, to which KIF5B binds poorly, likely because its cofactors, MAP7-family proteins, are slow in populating these ends. Concerted action of kinesins KIF5B and KIF13B promotes efficient secretory vesicle transport to microtubule plus ends. KIF5B and KIF13B are the main drivers of Rab6 vesicle transport in HeLa cells. During microtubule plus-end directed transport, both kinesins localize to the vesicle front and can be engaged on the same vesicle. When vesicles reverse direction, KIF13B relocates to the middle of the vesicle, while KIF5B shifts to the back, suggesting that KIF5B but not KIF13B undergoes a tug-of-war with a minus-end directed motor
physiological function
Rab6-positive secretory vesicles are transported from the Golgi apparatus to the cell periphery by kinesin-1 KIF5B and kinesin-3 KIF13B, which determine the location of secretion events. KIF5B plays a dominant role, whereas KIF13B helps Rab6 vesicles to reach freshly polymerized microtubule ends, to which KIF5B binds poorly, likely because its cofactors, MAP7-family proteins, are slow in populating these ends. Concerted action of kinesins KIF5B and KIF13B promotes efficient secretory vesicle transport to microtubule plus ends. While kinesin-3 KIF13B associates with Rab6-positive secretory vesicles, its closest homologue KIF13A displays little binding to Rab6 vesicles. KIF5B and KIF13B are the main drivers of Rab6 vesicle transport in HeLa cells. During microtubule plus-end directed transport, both kinesins localize to the vesicle front and can be engaged on the same vesicle. When vesicles reverse direction, KIF13B relocates to the middle of the vesicle, while KIF5B shifts to the back, suggesting that KIF5B but not KIF13B undergoes a tug-of-war with a minus-end directed motor
physiological function
-
expression of KIF3A is critical for excitatory synaptic transmission contributed by both functional and morphological changes at synapse
-
additional information
-
loop L5, the longest in the mitotic kinesin Eg5, assumes three distinct orientations during the ATPase cycle of the mitotic kinesin Eg5, L5 is in a dynamic equilibrium of three conformations whose relative proportions shift during the ATPase cycle. Loop L5 shapes the enzymology of kinesin motors to meet specific physiologic roles
additional information
residue 175 does not fall within the microtubule-binding domain or the ATP-binding domain of kinesin
additional information
residue 175 does not fall within the microtubule-binding domain or the ATPbinding domain of kinesin
additional information
kinesin-13s have a clearly longer loop 2 that folds as a beta-hairpin with a conserved KVD motif at its tip. This KVD motif is necessary for microtubule depolymerization by kinesin-13s. Structural modeling of the Kif2C motor domain in its ATP state in complex with tubulin, overview. The beta-hairpin structure of loop 2 is conserved but shortened. In the mutant, as in the wild type protein, the hairpin that displays the KVD motif interacts similarly with the neck helix, but the KVD motif contacts neither the rest of the motor domain nor the neck helix
additional information
enzyme TbKIN-D possesses an N-terminal motor domain and three coiled-coil motifs in the C-terminus. Although the microtubule-binding motif in the motor domain of TbKIN-D is conserved, the putative nucleotide-binding motif lacks the well-conserved lysine residue in the P-loop and two additional conserved motifs, SSRSH (switch I) and DLAGSE (switch II)
additional information
-
enzyme TbKIN-D possesses an N-terminal motor domain and three coiled-coil motifs in the C-terminus. Although the microtubule-binding motif in the motor domain of TbKIN-D is conserved, the putative nucleotide-binding motif lacks the well-conserved lysine residue in the P-loop and two additional conserved motifs, SSRSH (switch I) and DLAGSE (switch II)
additional information
tubulin and ATP binding structure analysis, sequential docking of the neck linker induced by ATP binding (isomerization), modeling. Backdoor formation stabilizes the two switch regions and induces full docking of the neck linker through a conformational change to switch II, affecting the conformation of loops L11-alpha4-L12-alpha5-L13 in switch II. Overall architecture of the KIF4 motor domain and structure-function relationship, overview
additional information
atomic models for no-nucleotide and ATP states of the monomeric kinesin motor domain on microtubules from cryo-electronmicrosopy reconstructions at 5-6 A resolution, overview. Microtubule attachment, mediated by a universally conserved linchpin residue in kinesin (N255), triggers a clamshell opening of the nucleotide cleft and accompanying release of ADP, modeling of crystal structures of ADP-bound enzyme and mechanism. Binding of ATP re-closes the cleft in a manner that tightly couples to translocation of cargo, via kinesin's neck linker element. These structural transitions are reminiscent of the analogous nucleotide-exchange steps in the myosin and F1-ATPase motors and inform how the two heads of a kinesin dimer gate each other to promote coordinated stepping along microtubules. Kinesin-1 dimerizes via an extended stalk domain that forms a coiled coil, so that the two catalytic motor domains are situated at one end of the coiled-coil, while cargo-binding domains are found at the opposite end. During active motility, the dimerized motor domains take alternating, eight nanometer steps toward the microtubule plus end, tracking along single protofilaments
additional information
analysis of the molecular mechanism responsible for regulating the motor activity of kinesins, it plays an essential role in centrosome separation and bipolar mitotic spindle formation during the early stage of mitosis
additional information
molecular dynamics simulation and atomic details of the structural dynamics and energetics of three major ATPase states (ADP, APO, and ATP state) of a human kinesin-1 monomer in complex with a tubulin dimer
additional information
-
molecular dynamics simulation and atomic details of the structural dynamics and energetics of three major ATPase states (ADP, APO, and ATP state) of a human kinesin-1 monomer in complex with a tubulin dimer
additional information
full-length structure of kinesin-3 KLP-6 in a compact self-folded state, molecular dynamics simulations, overview. All the internal coiled-coil segments and domains in KLP-6 cooperate to successively lock down the neck and motor domains. The first coiled-coil segment is melted into several short helices that work with the motor domain to restrain the entire neck domain. The second coiled-coil segment associates with its neighboring FHA and MBS domains and integrates with the tail MATH domain to form a supramodule that synergistically wraps around the motor domain to trap the nucleotide and hinder the microtubule binding. This multilevel-lockdown mechanism for autoinhibition could be applicable to other kinesin-3 motors
additional information
KIF1B and KIF1C are not sufficient for Rab6 vesicle transport. KIF5B and KIF13B have different velocities and set the speed range of Rab6 vesicles
additional information
KIF1B and KIF1C are not sufficient for Rab6 vesicle transport. KIF5B and KIF13B have different velocities and set the speed range of Rab6 vesicles
Show AA Sequence and Transmembrane Helices (4534 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
124000
-
2 * 124000 + 2 * 64000, molecule comprises 2 heavy chains and a pair of light chains
131000
-
2 * 131000, calculated, full-length protein. 2 * 68000, calculated, truncated protein Kif3-592
37360
-
1 * 37360, KHC, molecular mass calculated from amino acid sequence predicted from nucleic acid sequence
42119
-
1 * 42119, deduced from nucleotide sequence, N-terminal truncated, His-tagged Eg5-367
44600
-
1 * 44600, sedimentation velocity, N-terminal truncated, His-tagged Eg5-437
64000
-
2 * 124000 + 2 * 64000, molecule comprises 2 heavy chains and a pair of light chains
66000
68000
-
2 * 131000, calculated, full-length protein. 2 * 68000, calculated, truncated protein Kif3-592
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
homodimer
homotetramer
monomer
tetramer
additional information
dimer
-
2 * 131000, calculated, full-length protein. 2 * 68000, calculated, truncated protein Kif3-592
dimer
Kinesin-1 dimerizes via an extended stalk domain that forms a coiled coil, so that the two catalytic motor domains are situated at one end of the coiled-coil, while cargo-binding domains are found at the opposite end. During active motility, the dimerized motor domains take alternating, eight nanometer steps toward the microtubule plus end, tracking along single protofilaments, structure overview
dimer
molecular dynamics simulation and atomic details of the structural dynamics and energetics of three major ATPase states (ADP, APO, and ATP state) of a human kinesin-1 monomer in complex with a tubulin dimer
dimer
-
NcKin3 is dimeric but inactivates one of its motor heads to generate nonprocessive motility. The heads of the wild-type Nckin3 motor are strictly coupled via the neck domain, and the dimeric structure is required for proper detachment after one ATPase cycle
monomer
KLP-6 adopts a stable monomeric state in solution, gel filtration and sequence calculation
monomer
-
1 * 37360, KHC, molecular mass calculated from amino acid sequence predicted from nucleic acid sequence
monomer
-
1 * 44600, sedimentation velocity, N-terminal truncated, His-tagged Eg5-437
monomer
-
1 * 42119, deduced from nucleotide sequence, N-terminal truncated, His-tagged Eg5-367
tetramer
-
2 * 124000 + 2 * 64000, molecule comprises 2 heavy chains and a pair of light chains
tetramer
-
a homotetramer-specific diffusive mode keeps full-length Eg5 attached to a microtubule for longer times at near physiological conditions
additional information
domain organization of kinesin-3 KLP-6: KLP-6 contains an N-terminal motor domain (MD), a neck domain (composed of the neck linker (NL) and neck coil (NC)), the coiled-coil 1/fork head-associated/ CC2 coiled-coil 2 (2CC1-FHA-CC2) tandem followed by a MBS (membrane-associated guanylate kinase homolog (MAGUK)-binding stalk) domain, and another identified MATH domain. Structure conformation changes for autoinhibition, mechanism, detailed overview
additional information
-
the FLA3 KAP subunit is required for localization of kinesin-2 to the site of flagellar assembly and processive anterograde intraflagellar transport
additional information
-
Eg5 is a homotetrameric kinesin-5 involved in centrosome separation and assembly of the bipolar mitotic spindle. The stable dimer Eg5-513 promotes robust plus-end-directed microtubule gliding at a rate similar to that of homotetrameric Eg5 in vitro. Eg5-513 exhibits slow ATP turnover, high affinity for ATP, and a weakened affinity for microtubules when compared to monomeric Eg5
additional information
-
inhibition of kinesin activity by its tail is mainly the product of allosteric inhibition induced by the intramolecular binding of kinesin tail domain to the motor domain
additional information
-
unpolymerized tubulin binds to kinesin-1, causing tubulin-activated release of adenosine diphosphate. With no added nucleotide, each kinesin-1 dimer binds one tubulin heterodimer. In presence of adenylyl-imidodiphosphate, each kinesin-1 dimer binds two tubulin heterodimers. Existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head
additional information
-
the NcKin3 motor decorates microtubules at a stoichiometry of one head per alphabeta-tubulin heterodimer, forming an axial periodicity of 8 nm
additional information
-
unpolymerized tubulin binds to kinesin-1, causing tubulin-activated release of adenosine diphosphate. With no added nucleotide, each kinesin-1 dimer binds one tubulin heterodimer. In presence of adenylyl-imidodiphosphate, each kinesin-1 dimer binds two tubulin heterodimers. Existence of an ATP gate that operates independently of the microtubule lattice, by ATP-dependent release of steric or allosteric block on the tubulin binding site of the tethered kinesin-ADP head
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
phosphorylation at serine 175/176 via c-Jun N-terminal kinase-3. Phosphorylation of kinesin-1 light chains affects the association of cargo with the motor
phosphoprotein
phosphorylation at serine 175/176 via c-Jun N-terminal kinase-3. Phosphorylation of kinesin-1 light chains affects the association of cargo with the motor
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme or bound to ADP or to AMPPNP, vapor diffusion method, usingn 0.2 M KNO3 and 20% (w/v) polyethylene glycol 3350
enzyme complexed with tubulin, vapor diffusion method, using 0.2 M ammonium acetate, 0.1 M HEPES pH 7.2-7.8, 22-26% (w/v) polyethylene glycol 3350
purified recombinant monomeric enzyme, sitting-drop vapor-diffusion method, about 12 mg/ml protein in 5 mM HEPES, pH 7.5, 150 mM NaCl, 1 mM MgCl2, 1 mM EGTA, and 1 mM DTT, are mixed with crystallization solution containing 0.2 M sodium malonate, pH 7.0, 22% w/v PEG 3350, at 16°C, X-ray diffraction structure determination and analysis at 3.2 A resolution, molecular replacement method and modelling using the structures of the motor domain (PDB ID 6A1Z), the MBS domain (PDB ID 5B64) and the FHA domain (PDB ID 3FM8) from KIF13B as searching models. The extreme N-terminus, a stretch of the C-terminal tail and several internal loops cannot be resolved due to their poor electron density maps, the structure comprises residues from 5 to 842 with themissing of several flexible loops
catalytic domain in the ADP- and adenosine-5'-(beta,gamma-imido)triphosphate-bound states, hanging drop vapour diffusion method, using 0.1 MES (pH 6.5), 15% polyethylene glycol 20000, at 4°C
-
crystal structure analysis of ubiquitous kinesin motor domain and kinesin motor domain with docked neck linker, PDB IDs 1BG2 and 1MKJ, respectively
crystal structure analysis, PDB IDs 4HNA, 1BG2, and 1II6, structure modeling
purified recombinant Eg5 motor domain, residues 1-369, in complex with inhibitor PVZB1194, sitting drop vapor diffusion method, at 4°C, mixing of 500 nl of 6 mg/ml protein in 50 mM PIPES-NaOH, pH 6.8, 250 mM NaCl, 2 mM MgCl2, 1 mM EGTA-NaOH, 1 mM TCEP-HCl, and 10% w/v sucrose, and inhibitor PVZB1194 (ratio 1:3 or 1:4 with enzyme) solution with 500 nl of the reservoir solution containing 19% w/v PEG 3350, 0.1 M MES-NaOH, pH 6.0, and 200 mM NaNO3, 1 week, followed by microseeding, X-ray diffraction structure determination and analysis at 2.8 A resolution
purified recombinant minimal functional domain Kif2C-(sN+M)-sL2 in complex with ADP, by vapor diffusion using a crystallization buffer consisting of 0.1 M Tris-HCl, pH 8.0, 1.5 M ammonium sulfate, and 10% ethylene glycol, at 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using HsKif2C motor domain-ADP, PDB ID 2HEH, as a starting model
study of the discovery and optimization of hexahydr-2H-pyranol[3,2-c]quinolines, HHPQs as inhibitors. Crystallographic data demonstrate that these potent and selectve inhibitors bind in an allosteric pocket of kinesin-5 distant from the nucleotide and microtubule binding sites
His7-tagged KIF4 motor domain construct KIF4-344 in complex with AMPPNP, sitting drop vapour diffusion method, mixing of 15 mg/ml protein in 10 mM TrisHCl, pH 8.0, 100 mM NaCl, and 1 mM DTT with a reservoir solution containing 28% w/v PEG 4000, 100 mM Tris-HCl, pH 8.5, and 200 mM sodium acetate, in the presence of 5 mM AMPPNP, X-ray diffraction strcuture determination and analysis at 1.71 A resolution, molecular replacement and modeling
KIF1A-ADP crystals are grown by vapour diffusion, 0.002 ml protein solution containing approx. 15 mg/ml protein are mixed with 0.002 ml reservoir buffer consisting of 30% polyethylene glycol 4000, 100 mM Tris-HCl, pH 8.5, 200 mM sodium acetate, 8% sucrose, 4 mM ADP and 10 mM MgCl2, crystals of KIF1A-beta,gamma-methyleneadenosine 5-triphosphate are obtained using 27% polyethylene glycol 4000, 100 mM MES-NaOH, pH 6.5 and 200 mM sodium acetate as reservoir buffer, crystals are soaked in buffer containing 20 mM beta,gamma-methyleneadenosine 5-triphosphate and 40 mM MgCl2 before data collection, crystals of KIF1A and KIF1A-beta,gamma-methyleneadenosine 5-triphosphate diffract to 2.2 and 2.0 A, respectively
-
truncated protein comprised of the conserved motor domain of NcKin3, the following 14 amino acids, and a Cys-tag, in complex with MgADP bound to the active site. The NcKin3 motor decorates microtubules at a stoichiometry of one head per alphabeta-tubulin heterodimer, forming an axial periodicity of 8 nm
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D458A
site-directed mutagenesis, the mutant has highly increased ATPase activity compared to the wild-type enzyme
E457R
site-directed mutagenesis, the mutant has highly increased ATPase activity compared to the wild-type enzyme
E564A
site-directed mutagenesis, the mutant has moderately increased ATPase activity compared to the wild-type enzyme
F698Q
site-directed mutagenesis, the mutant has moderately increased ATPase activity compared to the wild-type enzyme
I570Q
site-directed mutagenesis, the mutant has highly increased ATPase activity compared to the wild-type enzyme
N410A
site-directed mutagenesis, the mutant has highly increased ATPase activity compared to the wild-type enzyme
R606A
site-directed mutagenesis, the mutant has moderately increased ATPase activity compared to the wild-type enzyme
R662A
site-directed mutagenesis, the mutant has highly increased ATPase activity compared to the wild-type enzyme
W421A
site-directed mutagenesis, the mutant has highly increased ATPase activity compared to the wild-type enzyme
R210A
-
approx. 0.6% of wild-type kcat, ATP binding is comparable with wild-type
R210K
-
essentially inactive, the point mutation in kinesin heavy chain disrups the ability of the enzyme active site to catalyze ATP P-O bond cleavage, pairing the inactive R210K subunit with a wild type subunit produces a dimer with essentially the full mechanochemical function of homodimeric wild type kinesin-1
A133D
A356T
-
substantially reduced sensitivity to ispinesib and other quinazoline Eg5 inhibitors
D130V
I299F
-
substantially reduced sensitivity to ispinesib and other quinazoline Eg5 inhibitors
N255S
the mutation produces very sluggish kinesin by reducing the rate of hydrolysis of ATP. This mutation at distal location to the active site disrupts pre-organization environment required for efficient ATP hydrolysis reaction in kinesin through a second sphere effect
R234K
motor domain amino acid residues 1-368, overall similar ATP affinity
S233C/R234K
motor domain amino acid residues 1-368, no ATP hydrolyzing mutant
W127C
-
site-directed mutagenesis, cysteine-light Eg5 monomer, the cysteine is located in the center of L5 and replaces a tryptophan residue that makes a hydrophobic ring stacking interaction with Tyr211 in alpha3 in AMPPNP, the mutant shows slowlier product release compared to the wild-type
Y274A/R278A/K281A
-
the mutant severely reduces microtubule binding in all nucleotide conditions
L249C
-
mutation in loop L11. Vmax value is reduced by 20%. After modification by 4-phenylazophenyl maleimide, mutant exhibits reversible alterations in ATPase activity accompanied by cis-trans isomerization upon UV and VIS light irradiation. The APTase activity exhibited by the cis-isomer of the 4-phenylazophenyl maleimide bound to the mutant is half of that of the trans-isomer
S175A
site-directed mutagenesis, modifying residue 175 decreases the kinesin stall force and its velocity while working against a load
S175D
site-directed mutagenesis, modifying residue 175 decreases the kinesin stall force and its velocity while working against a load
V40E
the mutation in the motor domain of the enzyme significantly reduces its microtubule-dependent ATPase activity
E1023A
-
the mutant does not exhibit microtubule-stimulated ATPase activity
K196A
additional information
A133D
-
substantially reduced sensitivity to ispinesib and other quinazoline Eg5 inhibitors
D130V
-
substantially reduced sensitivity to ispinesib and other quinazoline Eg5 inhibitors
D130V
-
mutation in the loop 5 region of the motor domain, screen of inhibitors against this mutant
additional information
-
when a flexible polypeptide linker is inserted into the coiled-coil central stalk, the processive plus-end-directed enzyme KlpA switches to become a processive minus-end-directed motor
additional information
wild-type KLP-6 is largely localized in the cell body, while most of the mutants show significantly increased accumulations at the cell tips, except for the E564A and F698Q mutants
additional information
-
mutant KHC-L5, loop L5 replaced by that of kinesin heavy chain. Substantially reduced sensitivity to ispinesib and other quinazoline Eg5 inhibitors
additional information
-
disrupting the function of kinesin KIF4 slows temporal progression of Gag through its trafficking intermediates and inhibits virus-like particle production
additional information
construction of L2, DVK, and DSK loop2 mutants of the functional domain of Kif2C, the microtubule depolymerization activity of the DVK mutant is remarkably decreased compared to the wild-type, while the DSK mutant does not show microtubule depolymerization activity even at high concentrations
additional information
the mutation of a residue cysteine in the NL domain (K-CL and K-CL-6AA) has no effect on the ATPase activity of the leading head and the interaction of the leading head with microtubule
additional information
Q07866; P33176
construction of KIF5B and/or KLC1 knockdown lines, phenotypes, overview. No change in cell viability or morphology was observed following KIF5B knockdown. No effect of loss of KIF5B on the clonogenic capacity of the luminal A T47D cells. Suppression of KLC1 results in a pronounced increase in expression of the EMT markers (ZEB1, ZEB2, Snail1, Slug, Vimentin and FN1) in the two epithelial/luminal breast cancer subtypes. Loss of KLC1 results in a significant downregulation of mRNA levels of the epithelialmarkers E-cadherin and the PRLR. Quantitative invasion assays of MDA-MB-231-Scr and MDA-MB-231-Sh1-KIF5B following TGFbeta stimulation, overview
additional information
generation of gene knockout cell lines lacking KIF5B, KIF13B, KIF5B and KIF13B together (KIF5B/KIF13B-KO), or KIF5B, KIF13B, KIF1B and KIF1C (4X-KO). The silencing of these kinesin genes leads to the loss of the respective proteins. All obtained mutant cell lines are viable and show no proliferation defects. Rab6 vesicles in 4X-KO cells rescued by expressing KIF13B move significantly faster than those in cells rescued with KIF5B. In cells rescued by expressing either KIF5B or KIF13B, vesicle tracks are distributed throughout the whole cytoplasm
additional information
generation of gene knockout cell lines lacking KIF5B, KIF13B, KIF5B and KIF13B together (KIF5B/KIF13B-KO), or KIF5B, KIF13B, KIF1B and KIF1C (4X-KO). The silencing of these kinesin genes leads to the loss of the respective proteins. All obtained mutant cell lines are viable and show no proliferation defects. Rab6 vesicles in 4X-KO cells rescued by expressing KIF13B move significantly faster than those in cells rescued with KIF5B. In cells rescued by expressing either KIF5B or KIF13B, vesicle tracks are distributed throughout the whole cytoplasm
additional information
generation of gene knockout cell lines lacking KIF5B, KIF13B, KIF5B and KIF13B together (KIF5B/KIF13B-KO), or KIF5B, KIF13B, KIF1B and KIF1C (4X-KO). Generation of GFP-KIF13B deletion constructs. The silencing of these kinesin genes leads to the loss of the respective proteins. All obtained mutant cell lines are viable and show no proliferation defects. Rab6 vesicles in 4X-KO cells rescued by expressing KIF13B move significantly faster than those in cells rescued with KIF5B. In cells rescued by expressing either KIF5B or KIF13B, vesicle tracks are distributed throughout the whole cytoplasm
additional information
generation of gene knockout cell lines lacking KIF5B, KIF13B, KIF5B and KIF13B together (KIF5B/KIF13B-KO), or KIF5B, KIF13B, KIF1B and KIF1C (4X-KO). Generation of GFP-KIF13B deletion constructs. The silencing of these kinesin genes leads to the loss of the respective proteins. All obtained mutant cell lines are viable and show no proliferation defects. Rab6 vesicles in 4X-KO cells rescued by expressing KIF13B move significantly faster than those in cells rescued with KIF5B. In cells rescued by expressing either KIF5B or KIF13B, vesicle tracks are distributed throughout the whole cytoplasm
additional information
conditional knockout of Kif5b (KIF5BcKO) in CaMKIIa-Cre-expressing neurons shows heightened turnover and lower stability of dendritic spines in layer 2/3 pyramidal neurons with reduced spine postsynaptic density protein 95 acquisition in the mouse cortex. The RNA-binding protein fragile X mental retardation protein (FMRP) is translocated to the proximity of newly formed spines several hours before the spine formation events in vivo in control mice, but this preceding transport of FMRP is abolished in KIF5B cKO mice. FMRP is localized closer to newly formed spines after fear extinction, but this learning-dependent localization is disrupted in KIF5B cKO mice. Crucial in vivo evidence that KIF5B is involved in the dendritic targeting of synaptic proteins that underlies dendritic spine plasticity
additional information
knockdown of KIF3A expression in DIV 14 neurons. Gain of function of KIF5C but not KIF3A in hippocampal neurons enhances excitatory postsynaptic currents (mEPSCs), and enhances dendritic arborization and synapse density. both KIF5C and KIF3A knockdown (KD) reduce synaptic strength across excitatory synapses, meaning expression of both KIF5C and KIF3A is critical for excitatory synaptic transmission contributed by both functional and morphological changes at synapse. Overexpression of KIF5C but depletion of KIF3A suggests that enhancements in spine density, mushroom spines, and dendritic arborization in KIF5C overexpressing neurons are independent of KIF3A levels. Overexpression of KIF5C but depletion of KIF3A suggests that enhancements in spine density, mushroom spines, and dendritic arborization in KIF5C overexpressing neurons are independent of KIF3A levels. Phenotypes of knockdown neurons, overview
additional information
-
knockdown of KIF3A expression in DIV 14 neurons. Gain of function of KIF5C but not KIF3A in hippocampal neurons enhances excitatory postsynaptic currents (mEPSCs), and enhances dendritic arborization and synapse density. both KIF5C and KIF3A knockdown (KD) reduce synaptic strength across excitatory synapses, meaning expression of both KIF5C and KIF3A is critical for excitatory synaptic transmission contributed by both functional and morphological changes at synapse. Overexpression of KIF5C but depletion of KIF3A suggests that enhancements in spine density, mushroom spines, and dendritic arborization in KIF5C overexpressing neurons are independent of KIF3A levels. Overexpression of KIF5C but depletion of KIF3A suggests that enhancements in spine density, mushroom spines, and dendritic arborization in KIF5C overexpressing neurons are independent of KIF3A levels. Phenotypes of knockdown neurons, overview
-
additional information
-
bc12 mutants display dwarfism resulting from a significant cell number reduction and brittleness due to an alteration in cellulose microfibril orientation and wall composition
additional information
RNAi knockdown 15 orphan kinesins in procyclic trypanosomes, RNAi of orphan kinesin TbKIN-D results in severe growth inhibition and cell death after 4 days, TbKIN-D mRNA is significantly depleted after RNAi for 2 days, and TbKIN-D protein is gradually depleted from the cells after RNAi impairing organelle segregation, while synthesis of the flagellum or flagellum attachment zone are not affected
additional information
-
RNAi knockdown 15 orphan kinesins in procyclic trypanosomes, RNAi of orphan kinesin TbKIN-D results in severe growth inhibition and cell death after 4 days, TbKIN-D mRNA is significantly depleted after RNAi for 2 days, and TbKIN-D protein is gradually depleted from the cells after RNAi impairing organelle segregation, while synthesis of the flagellum or flagellum attachment zone are not affected
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of orphan kinesin TbKIN-D and kinetoplastid-specific kinesin TbKIN-C by tandem affinity purification in a two-step chromatography
glutathione Sepharose column chromatography and Superdex 200 gel filtration
HisTrap Ni-NTA column chromatography
ion exchange chromatography (SP Sepharose), gel filtration, ion exchange chromatography (SourceQ column)
-
Ni-NTA affinity column chromatography and Superose 6 gel filtration
-
Ni-NTA column chromatography
Ni-NTA column chromatography, HiTrap Q column chromatography, and Superdex 200 gel filtration
Ni-NTA column chromatography, Superdex 200 gel filtration, and SP Sepharose column chromatography
-
recombinant C-terminally FLAG-tagged K888 heavy chain wild-type and mutants from Sf9 cells by affinity chromatography
recombinant C-terminally GFP-His6-Strep-tagged wild-type and mutant KLP-6 full-length enzymes from Spodoptera frugiperda Sf9 cells by nickel affinity and TActin affinity chromatography, followed by gel filtration
recombinant C-terminally His6-tagged wild-type Eg51-369 and mutants from Escherichia coli BL21(DE3)pLysS by nickel affinity and cation exchange chromatography
recombinant heavy chain residues 1-432 from Escherichia coli strain BL21 by nickel affinity chormatography
recombinant His7-tagged KIF4 motor domain construct KIF4-344 from Escherichia coli strain BL21(DE3) by nickel affinity and cation exchange chromatography, followed gel filtration and dialysis
the C-terminal truncated fragments of human Eg5 (amino acids 1-439 of human Eg5) fused to GST (E439GST) and amino acids 1-430 of Drosophila conventional kinesin (kinesin heavy chain: KHC) fused to GST (K430GST) are expressed in Escherichia coli
-
the purified protein co-sediments with microtubules, but the majority of the protein remains in the supernatant in the absence of microtubules, indicating that the motor domain of BC12 binds microtubules
-
Ni-NTA column chromatography, HiTrap Q column chromatography, and Superdex 200 gel filtration
-
Ni-NTA column chromatography, HiTrap Q column chromatography, and Superdex 200 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C-terminal motor domain (amino acid residues 372-717) expressed in Escherichia coli BL21(DE3)
AK065586
cDNA expression library CHO2 antigen cloned, subcloned into pVL1392 and expressed in ovarian Sf9 cells
-
cloning of the DdUnc104 gene, also known as ksnA gene, by PCR amplified cDNA
-
different parts of the protein and fusion proteins expressed in Arabidopsis thaliana, His tagged KP1-tail expressed in Escherichia coli BL21 (DE3)
-
expressed in Escherichia coli BL21 Star (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21-CodonPlus (DE3)-RIL cells
expressed in Escherichia coli Rosetta (DE3)pLysS cells or Sf9 cells, overexpression of Klp5p or Klp6p in fission yeast is lethal
-
expression in Escherichia coli
expression in Escherichia coli of C-terminally truncated fragment comprised of amino acids 1-439 fused to glutathione S-transferase
-
expression in Escherichia coli of full-length and truncated Kif3. Kif3-592 consists of amino acids 1-592, comprising motor domain, neck and partial stalk, Kif3-342 consists of amino acids 1-342 and comprises motor domain and partial neck
-
expression in Escherichia coli of human conventional kinesin in which the C-terminus is truncated at residue 560 and 6-His is fused at the C-terminus
-
expression in Escherichia coli of truncated protein comprised of the conserved motor domain of NcKin3, the following 14 amino acids, and a Cys-tag. The polypeptide NcKin3-434 is 434 + 9 residues long
-
expression of N-terminal truncated, His-tagged Eg5-437 and Eg5-367 in Escherichia coli
-
gene KIF11, recombinant expression of C-terminally His6-tagged wild-type Eg51-369 and mutants in Escherichia coli BL21(DE3)pLysS
GST fusions of TbKIN-C and the motor domain of TbKIN-C expressed in Escherichia coli BL21
His tagged motor domains, amino acid residues 1-368 and 1-358, expressed in Escherichia coli B834(DE3)
overexpression of dominant negative forms of the KIF3A motor subunit and the KAp3 accessory subunit in HeLa cells
-
rat kinesin heavy chain (amino acid residues 1-430) is introduced to the BamHI site of the pET14b-catchin and expressed in Escherichia coli BL21-CodonPlus (DE3) RIL cells
-
recombinant expression of a KIF4 motor domain construct, KIF4-344 comprising residues 1-344 of KIF4 followed by a His7-tag in Escherichia coli strain BL21(DE3)
recombinant expression of C-terminally GFP-His6-Strep-tagged wild-type and mutant KLP-6 full-length enzymes in Spodoptera frugiperda Sf9 cells using the baculovirus expression system, subcloning in Escherichia coli strain DH10Bac
recombinant expression of C-terminally His-and biotin-tagged heavy chain residues 1-432 in Escherichia coli strain BL21
recombinant expression of mouse KIF5B kinesin heavy chain, truncated at alanine 888 with a C-terminal biotin tag and N-terminal His6-tagged enzyme KIF5B, expression of C-terminally FLAG-tagged K888 heavy chain wild-type and mutants in Spodoptera frugiperda Sf9 cells using a baculovirus expression system
recombinant expression of the wild-type and mutant minimal functional domain of Kif2C, a fragment comprising the proximal part of the neck region and the motor domain
the C-terminal truncated fragments of human Eg5 (amino acids 1-439 of human Eg5) fused to GST (E439GST) and amino acids 1-430 of Drosophila conventional kinesin (kinesin heavy chain: KHC) fused to GST (K430GST) are expressed in Escherichia coli
-
wild type and R210K mutant enzymes are expressed in Escherichia coli BL21(DE3) pLysS cells
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the epithelial differentiation factor and EMT suppressor prolactin (PRL) enhances KLC1 gene expression and KIF5B-KLC1 interaction
Q07866; P33176
the epithelial differentiation factor and EMT suppressor prolactin (PRL) represses KIF5B gene expression and KIF5BSnail1 nuclear accumulation
Q07866; P33176
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
Q07866; P33176
KIF5B is essential for metastatic colonization propensity and is a clinically relevant marker of high-grade invasive breast cancer
medicine
pharmacology
medicine
-
appears tempting to test whether blocking KIF2beta expression in host cells may inhibit parasite entry without affecting host cell viability, KIF2beta antisense oligonucleotides could act as preventive agents for parasite infection
medicine
inhibition of mitotic spindles is a pharmaceutically validated strategy for cancer therapeutics, human Eg5 in addition to microtubules represents an attractive target molecule for novel clinical therapies in the treatment of human malignancies, kinesin spindle protein Eg5 is a target for anticancer therapies
pharmacology
a bias that favors motion toward the minus-end of microtubules, cf. EC 3.6.4.5, might be used to tune transport in healthy cells when properly regulated but contribute to a disease state when misregulated
pharmacology
a bias that favors motion toward the minus-end of microtubules might be used to tune transport in healthy cells when properly regulated but contribute to a disease state when misregulated
EXTERNAL LINKS (specific for EC-Number 5.6.1.3)
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Release 2026.1 (March 2026)
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