Information on EC 3.6.4.5 - minus-end-directed kinesin ATPase:
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The expected taxonomic range for this enzyme is: Eukaryota

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EC NUMBERCOMMENTARY
3.6.4.5-

RECOMMENDED NAMEGeneOntology No.
minus-end-directed kinesin ATPaseGO:0008569

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + H2O = ADP + phosphate
show the reaction diagram		----
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesArabidopsis sp. AtkdsA2, Arabidopsis sp. ixr1-1 ixr1-2, Aspergillus sp., Aspergillus sp. AF, Aspergillus sp. Cafe-I, Aspergillus sp. MT-0204, Aspergillus sp. N12, Aspergillus sp. No.319, Aspergillus sp. PCS6, Aspergillus sp. Rs-1a, Aspergillus sp. S1-13, Aspergillus sp. SHL 6-210546
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesArabidopsis sp.-210546, 210559
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesDoryteuthis pealeii-210563
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesTetrahymena sp., Tetrahymena sp. GCN5-210561, 210563
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesDictyostelium sp.-210561, 210565
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesXenopus laevis-210548, 210551, 210565
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesBos taurus-210563, 210568
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesGallus gallus-210568
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesNeurospora crassa-210570
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesRattus norvegicus-210568, 210571
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesCricetulus griseus-210546, 210569, 210572
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesHomo sapiens-210546, 210561, 210565, 210572
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesMus musculus-210568, 210572
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesSaccharomyces cerevisiae-210546, 210548, 210559, 210560, 210567, 210572
ATP + H2O = ADP + phosphate
show the reaction diagram		structurally almost identical to EC3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubulesDrosophila melanogaster-210546, 210548, 210557, 210558, 210559, 210560, 210561, 210562, 210563, 210567, 210571, 210572, 210574
ATP + H2O = ADP + phosphate
show the reaction diagram		model for enzymic coupling of depolymerizing microtubule plus ends to the cell cortexSchizosaccharomyces pombe-655282
ATP + H2O = ADP + phosphate
show the reaction diagram		mechanism, model of movementDrosophila melanogaster-655330
ATP + H2O = ADP + phosphate
show the reaction diagram		kinetics, comparison of wild-type enzyme and enzyme with N-terminal glutathione S-transferase tag, mechanismSaccharomyces cerevisiae-656259
ATP + H2O = ADP + phosphate
show the reaction diagram		a molecular mechanical model for the Kar3/Vik1 heterodimer is described based on structural, kinetic and motility data revealing a long-range chemomechanical transmission mechanism that resembles a familiar fishing tactic. By this this molecular fishing, ATP-binding to Kar3 dissociates catalytically inactive Vik1 off microtubule to facilitate minus-end sliding of the dimer on the microtubule lattice. When the dimer binds the frayed ends of the microtubules, the fishing channels ATP hydrolysis energy into the microtubule depolymerization by a mechanochemical effectSaccharomyces cerevisiae-713213

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
hydrolysis of phosphoric ester----

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
kinesin ATP phosphohydrolase (minus-end-directed)Structurally almost identical to EC 3.6.4.3 (microtubule-severing ATPase) but the movement it catalyses is towards the minus end of microtubules.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
AgKar3Eremothecium gossypii, Eremothecium gossypii AG33--721005
ATK1Arabidopsis thaliana--655191
C-terminal motor kinesinAspergillus sp., Cricetulus griseus, Drosophila sp., Homo sapiens, Saccharomyces sp., Schizosaccharomyces pombe--210545
CHO1/MKLP1Cricetulus griseus--210569
CHO2Cricetulus griseus--210569, 210572
claret motor proteinDrosophila melanogaster--210557
GhKCH1Gossypium hirsutumQ5MNW6-657073
HSETHomo sapiens-minus-end-directed microtubule motor700097
Kar3Saccharomyces sp.--210545
Kar3Saccharomyces cerevisiae--210546, 210548, 210559, 210560, 210572, 656259, 668405, 713213
KAR3-encoded kinesinSaccharomyces cerevisiae--210560
Kar3-like kinesinEremothecium gossypii, Eremothecium gossypii AG33--721005
KIFC3Mus musculus--656339
KIFC5ARattus norvegicus-a C-terminal motor, which belongs to a family of kinesins that move toward the minus end of the microtubules698412
kinesinRattus norvegicus--698412
kinesin Kar3Cik1 ATPaseSaccharomyces cerevisiaeP17119a kinesin-14719954
kinesin-14Homo sapiens--700097
kinesin-14Schizosaccharomyces pombe--698861, 700350
kinesin-14Xenopus laevis--700097, 720088
kinesin-14 NcdDrosophila melanogaster-Ncd, non-claret disjunctional is an often studied minus-end-directed motor in Drosophila melanogaster712404
kinesin-14 NcdDrosophila melanogaster--719190, 719508
KLP-15Caenorhabditis elegans--667670
Klp2Schizosaccharomyces pombe--700350
klpAAspergillus sp.--210546
MC1Drosophila melanogaster-dimeric ncd210575
MC6Drosophila melanogaster-monomeric ncd210575
minnus-end nonclaret disjunctional kinesinDrosophila sp.--210548
minus end-directed kinesin-like motor proteinCricetulus griseus--210546
minus end-directed kinesin-like motor proteinNeurospora crassa--210570
minus-end kinesin depolymerase Kar3Saccharomyces cerevisiae--668333
minus-end nonclaret disjunctional kinesinDrosophila sp.--210548
MT minus-end-directed non claret disjunctionalDrosophila sp.--210567
ncdDoryteuthis pealeii--210563
ncdDrosophila sp.--210545, 210548, 210562, 210563, 210567
ncdNeurospora crassa--210570
ncdDrosophila melanogaster--210546, 210548, 210558, 210559, 210561, 210562, 210563, 210567, 210571, 210572, 210575, 655338, 669577
Pkl1Schizosaccharomyces pombe-Pkl1 is a slow, minus end-directed microtubule motor698861
XCTK2Xenopus laevis-minus-end-directed microtubule motor700097
XCTK2Xenopus laevisP79955-720088

CAS REGISTRY NUMBERCOMMENTARY
9000-83-3-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Arabidopsis sp.-210546, 210559--Manually annotated by BRENDA team
Arabidopsis thaliana-655191--Manually annotated by BRENDA team
Aspergillus sp.-210545, 210546--Manually annotated by BRENDA team
Bos taurus-210568--Manually annotated by BRENDA team
Bos taurusbovine210563--Manually annotated by BRENDA team
Caenorhabditis elegans-667670--Manually annotated by BRENDA team
Chlorocebus aethiops-656342--Manually annotated by BRENDA team
Cricetulus griseus-210545--Manually annotated by BRENDA team
Cricetulus griseuschinese hamster210546, 210569, 210572--Manually annotated by BRENDA team
Dictyostelium sp.-210561, 210565--Manually annotated by BRENDA team
Doryteuthis pealeiisquid210563--Manually annotated by BRENDA team
Drosophila melanogaster-210546, 210548, 210557, 210558, 210559, 210560, 210561, 210562, 210563, 210567, 210571, 210572, 210574, 210575, 655330, 655338, 669577, 712404, 719190, 719508--Manually annotated by BRENDA team
Drosophila melanogasterisoform Ncd685072, 689146--Manually annotated by BRENDA team
Drosophila sp.-210545, 210548, 210562, 210567--Manually annotated by BRENDA team
Drosophila sp.recombinantly expressed in Escherichia coli210563--Manually annotated by BRENDA team
Eremothecium gossypiiATCC 10895721005--Manually annotated by BRENDA team
Gallus galluschicken, cell line HD-11210568--Manually annotated by BRENDA team
Gossypium hirsutum-657073Q5MNW6SwissProtManually annotated by BRENDA team
Homo sapiens-210545, 210546, 210572, 700097--Manually annotated by BRENDA team
Homo sapienshuman, HeLa cells210561, 210565--Manually annotated by BRENDA team
Mus musculus-210572, 656339--Manually annotated by BRENDA team
Mus musculusmouse, strain J774210568--Manually annotated by BRENDA team
Neurospora crassa-210570--Manually annotated by BRENDA team
Potorous tridactylus-656342--Manually annotated by BRENDA team
Rattus norvegicus-210568, 210571, 698412--Manually annotated by BRENDA team
Saccharomyces cerevisiae-210546, 210548, 210559, 210560, 210567, 210572, 668333, 668405, 713213--Manually annotated by BRENDA team
Saccharomyces cerevisiae-719954P17119UniProtManually annotated by BRENDA team
Saccharomyces cerevisiaecomparison of wild-type enzyme and enzyme fused with N-terminal glutathione S-transferase656259--Manually annotated by BRENDA team
Saccharomyces cerevisiaeisoform Kar3688934--Manually annotated by BRENDA team
Saccharomyces sp.-210545--Manually annotated by BRENDA team
Schizosaccharomyces pombe-210545, 655282, 698861, 700350--Manually annotated by BRENDA team
Tetrahymena sp.-210561, 210563--Manually annotated by BRENDA team
Xenopus laevis-210548, 210551, 210565, 700097--Manually annotated by BRENDA team
Xenopus laevis-720088P79955UniProtManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionDrosophila melanogaster-the non-processive minus-end-directed kinesin-14 Ncd is involved in the organization of the microtubule network during mitosis. Only one of the two domains is involved in the interaction with the microtubules712404
physiological functionSaccharomyces cerevisiae-Kar3 is a kinesin motor that facilitates chromosome segregation during cell division713213
physiological functionXenopus laevisP79955can form microtubule asters without additional factors720088

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
2'-dATP + H2O2'-dADP + phosphate
show the reaction diagram		Drosophila sp.--210563--?
2'-deoxy-ATP + H2O2'-dADP + phosphate
show the reaction diagram		Drosophila melanogaster, Doryteuthis pealeii--210563--?
3'-dATP + H2O3'-dADP + phosphate
show the reaction diagram		Drosophila sp.--210563--?
3'-deoxy-ATP + H2O3'-dADP + phosphate
show the reaction diagram		Drosophila melanogaster, Doryteuthis pealeii--210563--?
ATP + H2O?
show the reaction diagram		Arabidopsis thaliana--655191--?
ATP + H2OADP + phosphate
show the reaction diagram		Gallus gallus--210568--?
ATP + H2OADP + phosphate
show the reaction diagram		Cricetulus griseus--210546, 210569, 210572--?
ATP + H2OADP + phosphate
show the reaction diagram		Drosophila melanogaster--210546, 210548, 210557, 210558, 210559, 210560, 210561, 210562, 210563, 210567, 210571, 210572, 210574, 210575, 669577, 719190, 719508--?
ATP + H2OADP + phosphate
show the reaction diagram		Drosophila sp.--210548, 210562, 210563, 210567--?
ATP + H2OADP + phosphate
show the reaction diagram		Mus musculus--210568, 210572--?
ATP + H2OADP + phosphate
show the reaction diagram		Homo sapiens--210546, 210561, 210565, 210572, 700097--?
ATP + H2OADP + phosphate
show the reaction diagram		Rattus norvegicus--210568, 210571, 698412--?
ATP + H2OADP + phosphate
show the reaction diagram		Saccharomyces cerevisiae--210546, 210548, 210559, 210560, 210567, 210572, 656259, 668405--?
ATP + H2OADP + phosphate
show the reaction diagram		Bos taurus--210563, 210568--?
ATP + H2OADP + phosphate
show the reaction diagram		Neurospora crassa--210570--?
ATP + H2OADP + phosphate
show the reaction diagram		Xenopus laevis--210548, 210551, 210565, 700097--?
ATP + H2OADP + phosphate
show the reaction diagram		Schizosaccharomyces pombe--698861, 700350--?
ATP + H2OADP + phosphate
show the reaction diagram		Arabidopsis sp.--210546, 210559--?
ATP + H2OADP + phosphate
show the reaction diagram		Aspergillus sp.--210546--?
ATP + H2OADP + phosphate
show the reaction diagram		Doryteuthis pealeii--210563--?
ATP + H2OADP + phosphate
show the reaction diagram		Tetrahymena sp.--210561, 210563--?
ATP + H2OADP + phosphate
show the reaction diagram		Dictyostelium sp.--210561, 210565--?
ATP + H2OADP + phosphate
show the reaction diagram		Eremothecium gossypii--721005--?
ATP + H2OADP + phosphate
show the reaction diagram		Saccharomyces cerevisiaeP17119-719954--?
ATP + H2OADP + phosphate
show the reaction diagram		Caenorhabditis elegans-dimeric KLP-15 construct supports gliding and moves towards microtubule minus end667670--?
ATP + H2OADP + phosphate
show the reaction diagram		Drosophila sp.-ncd motor domain interacts with both alpha- and beta-tubulin210562--?
ATP + H2OADP + phosphate
show the reaction diagram		Caenorhabditis elegans-dimeric KLP-15 construct supports gliding at 0.0023 mm per min and moves towards microtubule minus end667670--?
ATP + H2OADP + phosphate
show the reaction diagram		Saccharomyces cerevisiae-minus-end kinesin depolymerase Kar3 forms a heterodimer with either Cik1 or Vik1, both of which are noncatalytic polypeptides. Cik1 targets Kar3 to the microtubule plus end. Kar3Cik1 then uses its minus-end-directed force to depolymerite microtubules from the plus end, with each tubulin-subunit release event tightly coupled to one ATP turnover668333--?
ATP + H2OADP + phosphate
show the reaction diagram		Drosophila sp., Homo sapiens, Schizosaccharomyces pombe, Saccharomyces sp., Aspergillus sp.-minus-end microtubule motor. The motor domain is present at the C terminus of the ncd protein, rather than the N-terminus as in kinesin heavy chain and the other plus-end kinesin motors (EC 3.6.5.5)210545--?
ATP + H2OADP + phosphate
show the reaction diagram		Cricetulus griseus-minus-end microtubule motor. The motor domain is present at the C terminus of the ncd protein, rather than the N-terninus as in kinesin heavy chain and the other plus-end kinesin motors (EC 3.6.5.5)210545--?
ATP + H2OADP + phosphate
show the reaction diagram		Drosophila melanogaster-Ncd is primarily responsible for focusing kinetochore microtubule bundles (K fibers)669577--?
ATP + H2OADP + phosphate
show the reaction diagram		Drosophila sp.-ncd switches from weak to strong binding via ADP release, and back again via ADP trapping210567--?
ATP + H2OADP + phosphate
show the reaction diagram		Drosophila melanogaster-the heterodimer E585A/wild-type Ncd construct exhibits 16% of the wild-type activity712404--?
ATP + H2OADP + phosphate
show the reaction diagram		Eremothecium gossypii AG33--721005--?
ddATP + H2O2',3'-dideoxyADP + phosphate
show the reaction diagram		Homo sapiens--210565--?
dideoxy-ATP + H2Omonomethyl-ADP + phosphate
show the reaction diagram		Drosophila sp.--210563--?
monomethyl-ATP + H2O?
show the reaction diagram		Drosophila melanogaster, Doryteuthis pealeii--210563--?
additional information?-Homo sapiens-GTP, 8-bromo ATP, 1,N6-etheno-adenosine 5'-triphosphate and 5'-O-(3-thiotriphosphate) are no substrates210565---
additional information?-Drosophila melanogaster, Doryteuthis pealeii-GTP is no substrate210563---
additional information?-Gossypium hirsutumQ5MNW6involved in organizing the actin network in coordination with the cortical microtubule array657073---
additional information?-Schizosaccharomyces pombe-required for coupling depolymerizing microtubule plus ends to the cell cortex, model of interactions655282---
additional information?-Mus musculus-required for protein transport in epithelial cells656339---
additional information?-Drosophila melanogaster-binding geometry between enzyme motor and microtubule which places the motor ahead of its cargo in the minus-end direction, after the uptake of ATP, the two heads rearrange their position relative to each other in a way that promotes a swing of the neck in the minus-end direction655330---
additional information?-Arabidopsis thaliana-enzyme supports microtubule movement in an ATP-dependent manner and has a minus-end directed polarity, enzyme exhibits non-processive movement along the microtubule and requires four molecules bound to the microtubule to support movement655191---
additional information?-Gossypium hirsutumQ5MNW6interacts in vitro with actin filaments657073---
additional information?-Schizosaccharomyces pombe-in microtubule gliding assays using microtubules assembled from pig brain tubulin, Klp2 drives minus-end-directed motility700350---
additional information?-Homo sapiens, Xenopus laevis-kinesin-14 acts during mitosis to cross-link and slide between parallel microtubules to regulate spindle length700097---
additional information?-Schizosaccharomyces pombe-Klp2 is required for the proper organization of interphase microtubules into bipolar arrays of parallel-overlapped microtubules700350---
additional information?-Schizosaccharomyces pombe-single molecules of Pkl1 are not highly processive but only exhibit biased one-dimensional diffusion along microtubules, whereas several molecules of Pkl1, probably fewer than 10 molecules, cooperatively move along microtubules and substantially reduce the diffusive component in the movement698861---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + H2OADP + phosphate
show the reaction diagram		Gallus gallus--210568--
ATP + H2OADP + phosphate
show the reaction diagram		Cricetulus griseus--210546, 210569, 210572--
ATP + H2OADP + phosphate
show the reaction diagram		Drosophila melanogaster--210546, 210548, 210557, 210558, 210559, 210560, 210561, 210562, 210563, 210567, 210571, 210572, 210574, 210575, 669577--
ATP + H2OADP + phosphate
show the reaction diagram		Drosophila sp.--210548, 210567--
ATP + H2OADP + phosphate
show the reaction diagram		Mus musculus--210568, 210572--
ATP + H2OADP + phosphate
show the reaction diagram		Homo sapiens--210546, 210561, 210565, 210572--
ATP + H2OADP + phosphate
show the reaction diagram		Rattus norvegicus--210568, 210571--
ATP + H2OADP + phosphate
show the reaction diagram		Saccharomyces cerevisiae--210546, 210548, 210559, 210560, 210567, 210572, 668405--
ATP + H2OADP + phosphate
show the reaction diagram		Bos taurus--210563, 210568--
ATP + H2OADP + phosphate
show the reaction diagram		Neurospora crassa--210570--
ATP + H2OADP + phosphate
show the reaction diagram		Xenopus laevis--210548, 210551, 210565--
ATP + H2OADP + phosphate
show the reaction diagram		Arabidopsis sp.--210546, 210559--
ATP + H2OADP + phosphate
show the reaction diagram		Aspergillus sp.--210546--
ATP + H2OADP + phosphate
show the reaction diagram		Doryteuthis pealeii--210563--
ATP + H2OADP + phosphate
show the reaction diagram		Tetrahymena sp.--210561, 210563--
ATP + H2OADP + phosphate
show the reaction diagram		Dictyostelium sp.--210561, 210565--
ATP + H2OADP + phosphate
show the reaction diagram		Caenorhabditis elegans-dimeric KLP-15 construct supports gliding and moves towards microtubule minus end667670--
ATP + H2OADP + phosphate
show the reaction diagram		Drosophila sp.-ncd motor domain interacts with both alpha- and beta-tubulin210562--
additional information?-Gossypium hirsutumQ5MNW6involved in organizing the actin network in coordination with the cortical microtubule array657073--
additional information?-Schizosaccharomyces pombe-required for coupling depolymerizing microtubule plus ends to the cell cortex, model of interactions655282--
additional information?-Mus musculus-required for protein transport in epithelial cells656339--
additional information?-Schizosaccharomyces pombe-in microtubule gliding assays using microtubules assembled from pig brain tubulin, Klp2 drives minus-end-directed motility700350--
additional information?-Homo sapiens, Xenopus laevis-kinesin-14 acts during mitosis to cross-link and slide between parallel microtubules to regulate spindle length700097--
additional information?-Schizosaccharomyces pombe-Klp2 is required for the proper organization of interphase microtubules into bipolar arrays of parallel-overlapped microtubules700350--
additional information?-Schizosaccharomyces pombe-single molecules of Pkl1 are not highly processive but only exhibit biased one-dimensional diffusion along microtubules, whereas several molecules of Pkl1, probably fewer than 10 molecules, cooperatively move along microtubules and substantially reduce the diffusive component in the movement698861--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
NaClDrosophila sp.-maximal stimulation at 0.15-0.2 M210563
NaClCaenorhabditis elegans-300 mM, stimulates by a factor of up to 2667670

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
5'-adenylylimidodiphosphateDrosophila melanogaster-AMP-PNP above 2.5 mM210557 2D-image
5'-adenylylimidodiphosphateHomo sapiens--210565 2D-image
AcrylamideRattus norvegicus-kinesin inhibition is observed at acrylamide concentrations as low as 0.1 mM698412 2D-image
glycidamideRattus norvegicus-kinesin inhibition is observed at glycidamide concentrations as low as 0.1 mM698412 2D-image
importin alpha/betaXenopus laevis-binding of importin alpha/beta to XCTK2 inhibits its association with microtubules and blocks its ability to cross-link microtubules700097-
Kar3Drosophila sp.-Ncd and Kar3, both minus-end motors, severely inhibit the binding of one another to microtubules210548-
N-ethylmaleimideDrosophila melanogaster-claret210557 2D-image
N-ethylmaleimideHomo sapiens--210565 2D-image
PropionamideRattus norvegicus-weak inhibition698412 2D-image
V5+Drosophila melanogaster-claret210557 2D-image
V5+Drosophila melanogaster-dynein210563 2D-image
VO43-Homo sapiens--210565 2D-image
monastrolChlorocebus aethiops, Potorous tridactylus-application results in kinetochore fibers oriented away fom, and not directly connected to, centrosomes and incorporated into the spindle by the sliding of their distal ends toward centrosomes656342 2D-image
additional informationDrosophila sp.-in contrast to cytoplasmic dynein, ncd polypeptide is not cleaved by UV-vanadate treatment, and its ATPase and motility are unaffected by vanadate (up to 0.1 mM)210563-
additional informationHomo sapiens-Ran regulates the association of kinesin-14 with importin alpha/beta to prevent aberrant cross-linking and bundling of microtubules by sequestering kinesin-14 in the nucleus during interphase700097-
additional informationXenopus laevis-XCTK2 is regulated by Ran via the association of a bipartite nuclear localization signal in the tail of XCTK2 with importin alpha/beta, which regulates its ability to cross-link microtubules during spindle formation700097-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
Cik1Saccharomyces cerevisiae-Cik1 and Kar3 stalk regions preferentially associate with one another rather than forming homodimers. Kar3/Cik1 moves on microtubules at 0.002-0.0024 mm/min, 2-5fold faster than Kar3, and destabilizes microtubules at the lagging ends. Structural changes in Kar3 upon dimerization with Cik1 alter the motor velocity and likely regulate Kar3 activity in vivo668405-
microtubuleDrosophila sp., Drosophila sp. Kc-in presence of microtubule, ncd ATPase activity is stimulated by ca. 30fold210563-
microtubuleCaenorhabditis elegans-ATP hydrolysis is stimulated 100-150fold in the presence of microtubules667670-
microtubuleSchizosaccharomyces pombe--698861-
microtubuleSchizosaccharomyces pombe-the solution Klp2 ATPase is activated 15fold more effectively by Schizosaccharomyces pombe microtubules than by pig brain microtubules700350-
microtubulesDrosophila melanogaster-stimulates ncd ATPase activity by ca. 30fold210563-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0016-ATPEremothecium gossypii, Eremothecium gossypii AG33-motor domain, 0 mM potassium acetate, pH 6.9, 22°C721005 2D-image
0.012-ATPSaccharomyces cerevisiae-both wild-type and GST-fusion protein, pH 7.2, 25°C656259 2D-image
0.0271-ATPSaccharomyces cerevisiaeP17119in presence of microtubles, Vmax/2 at 0.0004 mM microtubles, pH 7.2, 25°C719954 2D-image
0.0278-ATPDrosophila melanogaster--210575 2D-image
0.059-ATPSchizosaccharomyces pombe-green fluorescent protein-tagged Pkl1H, in 12 mM PIPES-KOH, 2 mM MgCl2, 1 mM EGTA, pH 6.8, containing 1 mM dithiothreitol, 0.7 mg/ml casein, and 1% (v/v) Tween 20 at 25°C698861 2D-image
additional information-additional informationSaccharomyces cerevisiae-ATP-binding is significantly faster for enzyme-GST fusion protein than for wild-type enzyme656259-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0008-ATPSaccharomyces cerevisiae--210559 2D-image
0.1-ATPDrosophila melanogaster-mutant NcN-E585D, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C712404 2D-image
0.16-ATPEremothecium gossypii, Eremothecium gossypii AG33-motor domain, 25 mM potassium acetate, Vmax/2 at 0.0007 mM microtubles, pH 6.9, 22°C721005 2D-image
0.17-ATPEremothecium gossypii, Eremothecium gossypii AG33-motor domain, 0 mM potassium acetate, Vmax/2 at 0.00008 mM microtubles, pH 6.9, 22°C721005 2D-image
0.19-ATPDrosophila melanogaster-E585D/E585E, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C712404 2D-image
0.2-ATPDrosophila melanogaster-mutant E585A/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C712404 2D-image
0.6-ATPDrosophila melanogaster-mutant E552A plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C; mutant E552A/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C; mutant N600K plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C; mutant NcN-E585D plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C712404 2D-image
0.62-ATPDrosophila melanogaster-Ncd700SG (residue 250-700, residue 671-679 replaced by sequence GGSGGSGGS), microtuble stimulated, Vmax/2 at 0.00014 mM microtubles, pH 7.2, 25°C719508 2D-image
0.7-ATPDrosophila melanogaster-mutant E585A plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C; mutant E585D plus wild-type mix, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C712404 2D-image
0.83-ATPDrosophila melanogaster-Ncd670 (residue 250-670), microtuble stimulated, Vmax/2 at 0.00014 mM microtubles, pH 7.2, 25°C719508 2D-image
0.9-ATPDrosophila melanogaster-E585D/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C712404 2D-image
1.3-ATPDrosophila melanogaster-wild-type/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C712404 2D-image
1.4-ATPDrosophila melanogaster-mutant N600K/wild-type, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C712404 2D-image
1.9-ATPSchizosaccharomyces pombe-green fluorescent protein-tagged Pkl1H, in 12 mM PIPES-KOH, 2 mM MgCl2, 1 mM EGTA, pH 6.8, containing 1 mM dithiothreitol, 0.7 mg/ml casein, and 1% (v/v) Tween 20 at 25°C698861 2D-image
1.9-ATPDrosophila melanogaster-mutant NcN, Ncd construct, ATPase activity of Ncd heterodimers and equimolar mixtures of homodimers at 5 microM microtubules, pH 7.2, 25°C712404 2D-image
2.49-ATPDrosophila melanogaster-NcdM672N (residue 250-679, M672N mutation), microtuble stimulated, Vmax/2 at 0.00061 mM microtubles, pH 7.2, 25°C719508 2D-image
2.58-ATPDrosophila melanogaster-NcdWT (residue 250-700), microtuble stimulated, Vmax/2 at 0.00022 mM microtubles, pH 7.2, 25°C719508 2D-image
3.58-ATPDrosophila melanogaster-Ncd679 (residue 250-679), microtuble stimulated, Vmax/2 at 0.00026 mM microtubles, pH 7.2, 25°C719508 2D-image
5-ATPSaccharomyces cerevisiaeP17119in presence of microtubles, pH 7.2, 25°C719954 2D-image
additional information-ATPEremothecium gossypii, Eremothecium gossypii AG33-addition of the ATP analog adenylyl-imidodiphosphate (AMPPNP, 1 mM) dramatically increases the microtuble affinity721005 2D-image
70-ATPSaccharomyces cerevisiae-both wild-type and GST-fusion protein, pH 7.2, 25°C656259 2D-image
additional information-additional informationCaenorhabditis elegans-turnover-numbers of KLP-15 constructs with different length extensions preceding the motor domain in presence or absence of 300 mM NaCl and microtubules667670-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7-Drosophila melanogaster-ncd and cytoplasmic dynein210563
7-Drosophila sp.--210563
7.2-Drosophila melanogaster-assay at712404

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
25-Drosophila melanogaster-assay at712404

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
7.1-Gossypium hirsutumQ5MNW6calculated from amino acid sequence657073
10-Schizosaccharomyces pombe-theoretical pI-value700350

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
brainBos taurus--210563, 210568Manually annotated by BRENDA team
brainRattus norvegicus--210568, 210571Manually annotated by BRENDA team
brainMus musculus--656339Manually annotated by BRENDA team
CV-1 cellChlorocebus aethiops--656342Manually annotated by BRENDA team
eggXenopus laevis--210551, 210565, 700097Manually annotated by BRENDA team
embryoXenopus laevis--210551Manually annotated by BRENDA team
embryoDrosophila melanogaster--210575Manually annotated by BRENDA team
kidneyRattus norvegicus--210568Manually annotated by BRENDA team
kidneyMus musculus-predominantly, tubular epithelial and MDCK II cells656339Manually annotated by BRENDA team
macrophageGallus gallus, Mus musculus--210568Manually annotated by BRENDA team
ovaryMus musculus--656339Manually annotated by BRENDA team
Pt-K2 cellPotorous tridactylus--656342Manually annotated by BRENDA team
SCHNEIDER-2 cellDrosophila melanogaster--669577Manually annotated by BRENDA team
testisMus musculus--656339Manually annotated by BRENDA team
testisRattus norvegicus--698412Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
centrosomeCricetulus griseus--5813210572Manually annotated by BRENDA team
cytoplasmDictyostelium sp., Homo sapiens--5737210561, 210565Manually annotated by BRENDA team
cytoplasmBos taurus--5737210563, 210568Manually annotated by BRENDA team
cytoplasmMus musculus, Rattus norvegicus--5737210568Manually annotated by BRENDA team
cytosolXenopus laevis--5829210551Manually annotated by BRENDA team
membraneMus musculus-associated with Triton X-100 insoluble membrane organelles16020656339Manually annotated by BRENDA team
microtubuleDrosophila sp.-binding-site of Ncd on microtubule5874210548Manually annotated by BRENDA team
microtubuleDrosophila sp.-ncd motor domain interacts with both alpha- and beta-tubulin5874210562Manually annotated by BRENDA team
microtubuleDrosophila sp.--5874210563Manually annotated by BRENDA team
microtubuleGossypium hirsutumQ5MNW6cortical microtubule5874657073Manually annotated by BRENDA team
microtubuleDrosophila melanogaster-growing tip of centrosomal microtubule5874669577Manually annotated by BRENDA team
nucleusCricetulus griseus--5634210572Manually annotated by BRENDA team
nucleusRattus norvegicus--5634698412Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
No entries in this field

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
15000-Saccharomyces cerevisiae-His6Kar3/Cik1-S tag protein, gel filtration668405
31200-Homo sapiens-calculated from predicted amino acid sequence210565
38910-Saccharomyces cerevisiae-Kar3, molecular mass calculated from the amino acid sequence predicted from the nucleic acid sequence210548
41600-Drosophila melanogaster-ncd, molecular mass calculated from the amino acid sequence predicted from the nucleic acid sequence210548
73000-Drosophila melanogaster-ncd polypeptide, SDS-PAGE210563
74000-Mus musculus, Rattus norvegicus-gel filtration210568
80000-Drosophila melanogaster--210560
80000-Saccharomyces cerevisiae-Kar3p, SDS-PAGE210560
80000-Drosophila melanogaster-ncd210563
8500090000Xenopus laevis-dynein, SDS-PAGE210551
87400-Homo sapiens-gel filtration210565
94000-Caenorhabditis elegans-gel filtration667670
105000-Neurospora crassa-ncd-Nkin chimaera, gel filtration210570
182000-Schizosaccharomyces pombe-theoretical molecular weight700350

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Gossypium hirsutumQ5MNW6x * 112000, deduced from gene sequence, x * 120000, SDS-PAGE657073
dimerDrosophila melanogaster-ncd polypeptide expressed in Escherichia coli210563, 210571
dimerDrosophila melanogaster-crystallization data655338
dimerCaenorhabditis elegans-2 * 50839, MALDI-TOF MS, the monomer is immobile whereas the fully dimeric KLP-15 construct supports gliding at 0.0023 mm per min and moves towards microtubule minus end667670
dimerSchizosaccharomyces pombe-Pkl1 has a predicted coiled-coil region at amino acid residues 196-481, suggesting that the native form of Pkl1 is at least dimeric698861
dimerSchizosaccharomyces pombe--700350
dimerDrosophila melanogaster--210575, 719508
dimerXenopus laevisP79955-720088
heterodimerDrosophila melanogaster-although the heterodimers have one fully active and one inactive head, the ATPase and motility of Ncd heterodimers vary dramatically, clearly demonstrating that interactions between motor domains exist in Ncd712404
heterodimerSaccharomyces cerevisiae-unlike many members of the kinesin superfamily, Kar3 forms a hetereodimer with non-motor protein Vik1 or Cik1 in vivo. The heterodimers show ATP-driven minus-end directed motility along a microtubule lattice, and also serve a depolymerase at the microtubule ends713213
heterodimerSaccharomyces cerevisiaeP17119truncated subunits, predicted 95892 Da (52833 Da + 43059 Da)719954
homodimerDrosophila melanogaster-mutated homodimers have no microtubule-activated ATPase and no motility, whereas NcN have motility comparable with that of the wild-type Ncd712404
monomerSaccharomyces cerevisiae--210548
monomerDrosophila melanogaster--210548, 210575
additional informationSaccharomyces cerevisiae-minus-end kinesin depolymerase Kar3 forms a heterodimer with either Cik1 or Vik1, both of which are noncatalytic polypeptides668333
additional informationSaccharomyces cerevisiae-Cik1 and Kar3 stalk regions preferentially associate with one another rather than forming homodimers. Kar3/Cik1 moves on microtubules at 0.002-0.0024 mm/min, 2-5fold faster than Kar3, and destabilizes microtubules at the lagging ends. Structural changes in Kar3 upon dimerization with Cik1 alter the motor velocity and likely regulate Kar3 activity in vivo668405
additional informationDrosophila melanogaster-domains 252-272, 276-330, and 336-346 on the C-terminal side of the stalk region have a relatively high potential to form coiled coils, although they are not self-sustaining individually. Residues S331 and R335 may act as a breaking point for alpha-helix continuity685072

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Drosophila melanogaster-210571, 210575
dimeric ncd, crystals with the C222(1) space groupDrosophila melanogaster-210574
hanging drops,room temperature, PEG 8000Drosophila melanogaster-719190
mutant N600KDrosophila melanogaster-655338
upon ATP binding, a coiled-coil mechanical element of microtubule-bound Ncd rotates about 79° towards the minus endDrosophila melanogaster-689146
motor domain MgADP complex, hanging drop vapor diffusion method, room temperature, 14% PEG 3350, pH 8.5Eremothecium gossypii, Eremothecium gossypii AG33-721005
-Rattus norvegicus-210571
structure of microtubules decorated with Kar3 in the nucleotide-free state, as well as with ADP and 5'-adenylyl-beta,gamma-imidotriphosphate. The empty motor shows large structural changes, including melting of the switch II helix alpha4, closure of nucleotide-binding pocket, and changes in the central beta sheet. Structural changes in switch II control interactions of the Kar3 head with its neck and are transmitted via changes in the central beta sheet of the motorSaccharomyces cerevisiae-688934

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-80°C, 0.3 M NaCl, stored in liquid nitrogenDrosophila melanogaster-210563

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Drosophila melanogaster-210562
immobilized metal ion affinity chromatography (Ni2+)Drosophila melanogaster-719508
ion exchange chromatography (SP Sepharose) and ion exchange chromatography (MonoQ) or gel filtrationDrosophila melanogaster-719190
MC1 and MC6Drosophila melanogaster-210575
mutated protein molecules carrying point mutations in one of the heads, thus producing heterodimeric motorsDrosophila melanogaster-712404
partial, recombinant protein, expressed in Escherichia coliDrosophila melanogaster-210558, 210563
-Eremothecium gossypii, Eremothecium gossypii AG33-721005
glutathione Sepharose column chromatographyHomo sapiens-700097
partiallyHomo sapiens-210565
ncd-Nkin chimaeraNeurospora crassa-210570
-Saccharomyces cerevisiae-210560, 719954
fusion protein GST-Kar3Saccharomyces cerevisiae-210559
His6Kar3/Cik1-S tag proteinSaccharomyces cerevisiae-668405
6His-tagged full-length Klp2. a Klp2 protein lacking the motor domain (Klp2-tail) and a Klp2 protein containing only the motor domain and a short coiled coil to mediate dimerization (Klp2-motor) are purified by ammonium sulfate precipitation and HisTrapHP column chromatographySchizosaccharomyces pombe-700350
GST-bind resin chromatography and NAP-5 gel filtrationSchizosaccharomyces pombe-698861
-Xenopus laevis-700097
immobilized metal ion affinity chromatography (Ni2+), gel filtrationXenopus laevisP79955720088

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Arabidopsis thaliana-655191
KLP-15 constructs with different length extensions preceding the motor domain are expressed in Escherichia coliCaenorhabditis elegans-667670
baculovirus constructs encoding the entire CHO2 molecule expressed in Sf9 cellsCricetulus griseus-210569
-Drosophila melanogaster-210571
claret segregation protein cloned and expressed in bacteriaDrosophila melanogaster-210557
expressed in Escherichia coli BL21(DE3) pLys strainDrosophila melanogaster-712404
His tagged truncated proteins (e.g. wild type, residue 250-700) expressed in Escherichia coliDrosophila melanogaster-719508
PCR from a ncd cDNA, ncd cloned, polypeptide expressed in Escherichia coliDrosophila melanogaster-210563
pET-ncd, ncd cloned and expressed in Escherichia coliDrosophila melanogaster-210558
pET/MC1 and pET/MC6 encoding dimeric and monomeric ncd expressed in Escherichia coli Bl21(DE3)Drosophila melanogaster-210575
residues H293-K700 for crystallization, GST fusion protein (residues K210-K700) for biochemical and motility assays expressed in Escherichia coli BL21(DE3)pLysS or Rosetta2(DE3)pLysSDrosophila melanogaster-719190
motor domain construct MC6 is expressed in Escherichia coliDrosophila sp.-210548
motor domain (Leu363-Arg709) expressed in Escherichia coli BL21(DE3)-RIL CodonPlusEremothecium gossypii, Eremothecium gossypii AG33-721005
-Gossypium hirsutumQ5MNW6657073
expressed in HeLa cellsHomo sapiens-700097
pt7-7, PCR amplification, chimaera of ncd and Neurospora kinesin, cloned and expressed in Escherichia coli Bl21Neurospora crassa-210570
DNA sequence analysis of KAR3, Kar3 cloned and expressed in Escherichia coli BL21(DE3)pLysS as fusion protein with glutathione S-transferase, GST-Kar3Saccharomyces cerevisiae-210559
expression in Escherichia coliSaccharomyces cerevisiae-688934
His6Kar3/Cik1-S tag proteinSaccharomyces cerevisiae-668405
KAR3 gene cloned, Kar3p overexpressed in Escherichia coliSaccharomyces cerevisiae-210560
truncated KAR3 (Lys268-Lys729) and truncated CIK1 (Lys252-Asp594) coexpressed in Escherichia coli BL21-CodonPlus(DE3)-RIL yielding a heterodimerSaccharomyces cerevisiaeP17119719954
expressed in Escherichia coli BL21 cellsSchizosaccharomyces pombe-700350
expressed in Escherichia coli BL21 Star (DE3) or BL21-CodonPlus (DE3) RIL cellsSchizosaccharomyces pombe-698861
expressed in Sf9 insect cellsXenopus laevis-700097
truncated proteins and GFP fusion proteins expressed in Sf9 cells and in Escherichia coli BL21-RILXenopus laevisP79955720088

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
E585ADrosophila melanogaster-the mutated amino acids are key residues that are involved in the mediation of structural changes in the head that follow the hydrolysis of the nucelotide. The mutant retains the basal, very low ATPase activity but shows negligible microtubule-stimulated ATPase712404
E585DDrosophila melanogaster-the mutated amino acids are key residues that are involved in the mediation of structural changes in the head that follow the hydrolysis of the nucelotide. The mutant retains the basal, very low ATPase activity but shows negligible microtubule-stimulated ATPase712404
G347ADrosophila melanogaster-binds poorly to microtubules in gliding assays, reduced microtubule gliding velocity655338
N600KDrosophila melanogaster-may bind ADP less stably than wild-type, crystallization data655338
N600KDrosophila melanogaster-mutant lacks directional preference. Mutant shows unstable nucleotide-dependent conformations of its coiled coil689146
N600KDrosophila melanogaster-a decoupling mutant, Asn600 is essential for integrity of the Ncd dimeric structure and transmission of conformational changes from the switch region to the microtubule-binding site. The mutant retains the basal, very low ATPase activity but shows negligible microtubule-stimulated ATPase712404
R552ADrosophila melanogaster-the mutated amino acids are key residues that are involved in the mediation of structural changes in the head that follow the hydrolysis of the nucelotide. The mutant retains the basal, very low ATPase activity but shows negligible microtubule-stimulated ATPase712404
T436SDrosophila melanogaster-the mutant enzyme permits more rapid nucleotide exchange and moves more slowly along microtubles in gliding assays719190
G347TDrosophila melanogaster-binds poorly to microtubules in gliding assays, reduced microtubule gliding velocity655338
additional informationDrosophila melanogaster-construction of a single-headed Ncd heterodimer in which one polypeptide consists of an intact Ncd catalytic core and neck (residues 280–700) and the second polypeptide consists of the neck region alone (residues 281–347). This motor elicits microtubule gliding at a velocity comparable to that of the normal twoheaded Ncd homodimer with a similar ATPase kcat-value689146
additional informationDrosophila melanogaster-a deletion in the motor domain in one of the subunits resulting in a single-headed molecule, NcN, resulting in a low affinity for microtubules. Mutated homodimers have no microtubule-activated ATPase and no motility, whereas NcN have motility comparable with that of the wild-type Ncd712404
additional informationDrosophila melanogaster-truncated versions: residue 250-700 (wild type), residue 346-700 (motor domain 700), residue 250-670 (Ncd670), residue 346-700 (motor domain 670), residue 250-679 (Ncd679), residue 250-670 + GGSGGSGGS + 680-700 (Ncd700SG, residue 671-679 replaced by sequence GGSGGSGGS), residue 250-670 with M672N exchange (NcdM672N)719508
N593KHomo sapiens-inactive700097
additional informationMus musculus-overexpression of full-length enzyme, accumulation in the apical sub-plasma membrane region. COOH-terminal deletion mutant lacking amino acids 1-515, distribution of enzyme homogenously throughout the cytoplasm656339

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
analysis of thermal and urea-induced unfolding of dimeric peptide fragments for identification of coiled coilsDrosophila melanogaster, Drosophila melanogaster AANAT2, Drosophila melanogaster Canton S, Drosophila melanogaster CuZn-SOD, Drosophila melanogaster MH19, Drosophila melanogaster Oregon K, Drosophila melanogaster Oregon R, Drosophila melanogaster Oregon-R, Drosophila melanogaster OregonR, Drosophila melanogaster S-2, Drosophila melanogaster Samarkand-685072

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
Bardet-Biedl Syndrome- PubMed
Breast Neoplasms- PubMed
Influenza, Human- PubMed
Retinal Degeneration- PubMed
Stroke- PubMed,  PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
210545Endow, S.A.Determinants of motor polarity in the kinesin proteinsBiophys. J.68271S-274S1995Aspergillus sp., Cricetulus griseus, Drosophila sp., Homo sapiens, Saccharomyces sp., Schizosaccharomyces pombe PubMed
210546Kuriyama, R.; Kofron, M.; Essner, R.; Kato, T.; Dragas-Granoic, S.; Omoto, C.K.; Khodjakov, A.Characterization of a minus end-directed kinesin-like motor protein from cultured mammalian cellsJ. Cell Biol.1291049-10591995Arabidopsis sp., Aspergillus sp., Cricetulus griseus, Drosophila melanogaster, Homo sapiens, Saccharomyces cerevisiae PubMed
210548Song, H.; Endow, S.A.Binding sites on microtubules of kinesin motors of the same or opposite polarityBiochemistry3511203-112091996Drosophila melanogaster, Drosophila sp., Saccharomyces cerevisiae, Xenopus laevis PubMed
210551Lane, J.D.; Allan, V.J.Microtubule-based endoplasmic reticulum motility in Xenopus laevis: activation of membrane-associated kinesin during developmentMol. Biol.101909-19221999Xenopus laevis PubMed
210557Walker, R.A.; Salmon, E.D.; Endow, S.A.The Drosophila claret segregation protein is a minus-end directed motor moleculeNature347780-7821990Drosophila melanogaster PubMed
210558McDonald, H.B.; Stewart, R.J.; Goldstein, L.S.The kinesin-like ncd protein of Drosophila is a minus end-directed microtubule motorCell631159-11651990Drosophila melanogaster PubMed
210559Endow, S.A.; Kang, S.J.; Satterwhite, L.L.; Rose, M.D.; Skeen, V.P.; Salmon, E.D.Yeast Kar3 is a minus-end microtubule motor protein that destabilizes microtubules preferentially at the minus endsEMBO J.132708-27131994Arabidopsis sp., Drosophila melanogaster, Saccharomyces cerevisiae PubMed
210560Middleton, K.; Carbon, J.KAR3-encoded kinesin is a minus-end-directed motor that functions with centromere binding proteins (CBF3) on an in vitro yeast kinetochoreProc. Natl. Acad. Sci. USA917212-72161994Drosophila melanogaster, Saccharomyces cerevisiae PubMed
210561Lombillo, V.A.; Stewart, R.J.; McIntosh, J.R.Minus-end-directed motion of kinesin-coated microspheres driven by microtubule depolymerizationNature373161-1641995Dictyostelium sp., Drosophila melanogaster, Homo sapiens, Tetrahymena sp. PubMed
210562Walker, R.A.Ncd and kinesin motor domains interact with both alpha- and beta-tubulinProc. Natl. Acad. Sci. USA925960-59641995Drosophila melanogaster, Drosophila sp. PubMed
210563Shimizu, T.; Toyoshima, Y.Y.; Edamatsu, M.; Vale, R.D.Comparison of the motile and enzymatic properties of two microtubule minus-end-directed motors, ncd and cytoplasmic dyneinBiochemistry341575-15821995Bos taurus, Doryteuthis pealeii, Drosophila melanogaster, Drosophila sp., Tetrahymena sp. PubMed
210565Thrower, D.A.; Jordan, M.A.; Schaar, B.T.; Yen, T.J.; Wilson, L.Mitotic HeLa cells contain a CENP-E-associated minus end-directed microtubule motorEMBO J.14918-9261995Dictyostelium sp., Homo sapiens, Xenopus laevis PubMed
210567Crevel, I.M.; Lockhart, A.; Cross, R.A.Weak and strong states of kinesin and ncdJ. Mol. Biol.25766-761996Drosophila melanogaster, Drosophila sp., Saccharomyces cerevisiae PubMed
210568Blocker, A.; Severin, F.F.; Burkhardt, J.K.; Bingham, J.B.; Yu, H.; Olivo, J.C.; Schroer, T.A.; Hyman, A.A.; Griffiths, G.Molecular requirements for bi-directional movement of phagosomes along microtubulesJ. Cell Biol.137113-1291997Bos taurus, Gallus gallus, Mus musculus, Rattus norvegicus PubMed
210569Sharp, D.J.; Kuriyama, R.; Essner, R.; Baas, P.W.Expression of a minus-end-directed motor protein induces Sf9 cells to form axon-like processes with uniform microtubule polarity orientationJ. Cell Sci.1102373-23801997Cricetulus griseus PubMed
210570Henningsen, U.; Schliwa, M.Reversal in the direction of movement of a molecular motorNature38993-961997Neurospora crassa PubMed
210571Sablin, E.P.; Case, R.B.; Dai, S.C.; Hart, C.L.; Ruby, A.; Vale, R.D.; Fletterick, R.J.Direction determination in the minus-end-directed kinesin motor ncdNature395813-8161998Drosophila melanogaster, Rattus norvegicus PubMed
210572Matuliene, J.; Essner, R.; Ryu, J.; Hamaguchi, Y.; Baas, P.W.; Haraguchi, T.; Hiraoka, Y.; Kuriyama, R.Function of a minus-end-directed kinesin-like motor protein in mammalian cellsJ. Cell Sci.1124041-40501999Cricetulus griseus, Drosophila melanogaster, Homo sapiens, Mus musculus, Saccharomyces cerevisiae PubMed
210574Kozielski,F.; De Bonis, S.; Burmeister, W.P.; Cohen-Addad, C.; Wade, R.H.The crystal structure of the minis-end-directed microtubule motor protein ncd reveals variable dimer conformationsStructure Fold. Des.71407-14161999Drosophila melanogaster PubMed
210575Mackey, A.T.; Gilbert, S.P.Moving a microtubule may require two heads: a kinetic investigation of monomeric NcdBiochemistry391346-13552000Drosophila melanogaster PubMed
655191Marcus, A.I.; Ambrose, J.C.; Blickley, L.; Hancock, W.O.; Cyr, R.J.Arabidopsis thaliana protein, ATK1, is a minus-end directed kinesin that exhibits non-processive movementCell Motil. Cytoskeleton52144-1502002Arabidopsis thaliana PubMed
655282Maddox, P.S.; Stemple, J.K.; Satterwhite, L.; Salmon, E.D.; Bloom, K.The minus end-directed motor Kar3 is required for coupling dynamic microtubule plus ends to the cortical shmoo tip in budding yeastCurr. Biol.131423-14282003Schizosaccharomyces pombe PubMed
655330Wendt, T.G.; Volkmann, N.; Skiniotis, G.; Goldie, K.N.; Muller, J.; Mandelkow, E.; Hoenger, A.Microscopic evidence for a minus-end-directed power stroke in the kinesin motor ncdEMBO J.215969-59782002Drosophila melanogaster PubMed
655338Yun, M.; Bronner, C.E.; Park, C.G.; Cha, S.S.; Park, H.W.; Endow, S.A.Rotation of the stalk/neck and one head in a new crystal structure of the kinesin motor protein, NcdEMBO J.225382-53892003Drosophila melanogaster PubMed
656259Mackey, A.T.; Sproul, L.R.; Sontag, C.A.; Satterwhite, L.L.; Correia, J.J.; Gilbert, S.P.Mechanistic analysis of the Saccharomyces cerevisiae kinesin Kar3J. Biol. Chem.27951354-513612004Saccharomyces cerevisiae PubMed
656339Noda, Y.; Okada, Y.; Saito, N.; Setou, M.; Xu, Y.; Zhang, Z.; Hirokawa, N.KIFC3, a microtubule minus end-directed motor for the apical transport of annexin XIIIb-associated Triton-insoluble membranesJ. Cell Biol.15577-882001Mus musculus PubMed
656342Khodjakov, A.; Copenagle, L.; Gordon, M.B.; Compton, D.A.; Kapoor, T.M.Minus-end capture of preformed kinetochore fibers contributes to spindle morphogenesisJ. Cell Biol.160671-6832003Chlorocebus aethiops, Potorous tridactylus PubMed
657073Preuss, M.L.; Kovar, D.R.; Lee, Y.R.; Staiger, C.J.; Delmer, D.P.; Liu, B.A plant-specific kinesin binds to actin microfilaments and interacts with cortical microtubules in cotton fibersPlant Physiol.1363945-39552004Gossypium hirsutum, Gossypium hirsutum (Q5MNW6) PubMed
667670Robin, G.; DeBonis, S.; Dornier, A.; Cappello, G.; Ebel, C.; Wade, R.H.; Thierry-Mieg, D.; Kozielski, F.Essential kinesins: characterization of Caenorhabditis elegans KLP-15Biochemistry446526-65362005Caenorhabditis elegans PubMed
668333Sproul, L.R.; Anderson, D.J.; Mackey, A.T.; Saunders, W.S.; Gilbert, S.P.Cik1 targets the minus-end kinesin depolymerase Kar3 to microtubule plus endsCurr. Biol.151420-14272005Saccharomyces cerevisiae PubMed
668405Chu, H.M.; Yun, M.; Anderson, D.E.; Sage, H.; Park, H.W.; Endow, S.A.Kar3 interaction with Cik1 alters motor structure and functionEMBO J.243214-32232005Saccharomyces cerevisiae PubMed
669577Goshima, G.; Nedelec, F.; Vale, R.D.Mechanisms for focusing mitotic spindle poles by minus end-directed motor proteinsJ. Cell Biol.171229-2402005Drosophila melanogaster PubMed
685072Ito, M.; Morii, H.; Shimizu, T.; Tanokura, M.Coiled coil in the stalk region of ncd motor protein is nonlocally sustainedBiochemistry453315-33242006Drosophila melanogaster PubMed
688934Hirose, K.; Akimaru, E.; Akiba, T.; Endow, S.A.; Amos, L.A.Large conformational changes in a kinesin motor catalyzed by interaction with microtubulesMol. Cell23913-9232006Saccharomyces cerevisiae PubMed
689146Endres, N.F.; Yoshioka, C.; Milligan, R.A.; Vale, R.D.A lever-arm rotation drives motility of the minus-end-directed kinesin NcdNature439875-8782006Drosophila melanogaster PubMed
698412Friedman, M.A.; Zeiger, E.; Marroni, D.E.; Sickles, D.W.Inhibition of rat testicular nuclear kinesins (krp2; KIFC5A) by acrylamide as a basis for establishing a genotoxicity thresholdJ. Agric. Food Chem.566024-60302008Rattus norvegicus PubMed
698861Furuta, K.; Edamatsu, M.; Maeda, Y.; Toyoshima, Y.Y.Diffusion and directed movement: in vitro motile properties of fission yeast kinesin-14 Pkl1J. Biol. Chem.28336465-364732008Schizosaccharomyces pombe PubMed
700097Cai, S.; Weaver, L.N.; Ems-McClung, S.C.; Walczak, C.E.Kinesin-14 family proteins HSET/XCTK2 control spindle length by cross-linking and sliding microtubulesMol. Biol. Cell201348-13592009Homo sapiens, Xenopus laevis PubMed
700350Braun, M.; Drummond, D.R.; Cross, R.A.; McAinsh, A.D.The kinesin-14 Klp2 organizes microtubules into parallel bundles by an ATP-dependent sorting mechanismNat. Cell Biol.11724-7302009Schizosaccharomyces pombe PubMed
712404Kocik, E.; Skowronek, K.J.; Kasprzak, A.A.Interactions between subunits in heterodimeric Ncd moleculesJ. Biol. Chem.28435735-357452009Drosophila melanogaster PubMed
713213Hou, R.; Wang, Z.A coordinated molecular fishing mechanism in heterodimeric kinesinPhys. Biol.70360032010Saccharomyces cerevisiae PubMed
719190Heuston, E.; Bronner, C.E.; Kull, F.J.; Endow, S.A.A kinesin motor in a force-producing conformationBMC Struct. Biol.10192010Drosophila melanogaster PubMed
719508Szczesna, E.; Kasprzak, A.A.The C-terminus of kinesin-14 Ncd is a crucial component of the force generating mechanismFEBS Lett.586854-8582012Drosophila melanogaster PubMed
719954Chen, C.J.; Rayment, I.; Gilbert, S.P.Kinesin Kar3Cik1 ATPase pathway for microtubule cross-linkingJ. Biol. Chem.28629261-292722011Saccharomyces cerevisiae, Saccharomyces cerevisiae (P17119) PubMed
720088Hentrich, C.; Surrey, T.Microtubule organization by the antagonistic mitotic motors kinesin-5 and kinesin-14J. Cell Biol.189465-4802010Xenopus laevis, Xenopus laevis (P79955) PubMed
721005Duan, D.; Hnatchuk, D.; Brenner, J.; Davis, D.; Allingham, J.Crystal structure of the Kar3-like kinesin motor domain from the filamentous fungus Ashbya gossypiiProteins Struct. Funct. Bioinform.801016-10272012Eremothecium gossypii PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 3.6.4.5)
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NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
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Protein Mutant Database
InterPro (database of protein families, domains and functional sites)