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Information on EC 5.6.1.3 - plus-end-directed kinesin ATPase

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EC Tree
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.
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UNIPROT: Q12756
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
kinesin, kinesin-1, kif3a, kinesin-5, kif1a, kif11, kif4a, kifc1, kinesin-2, kif5b, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
kinesin-1
-
kinesin-888
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kinesin
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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)
show the reaction diagram
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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)
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
additional information
residue 175 does not fall within the microtubule-binding domain or the ATP-binding domain of kinesin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
KIF1A_HUMAN
1690
0
191064
Swiss-Prot
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant heavy chain residues 1-432 from Escherichia coli strain BL21 by nickel affinity chormatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of C-terminally His-and biotin-tagged heavy chain residues 1-432 in Escherichia coli strain BL21
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
DeBerg, H.A.; Blehm, B.H.; Sheung, J.; Thompson, A.R.; Bookwalter, C.S.; Torabi, S.F.; Schroer, T.A.; Berger, C.L.; Lu, Y.; Trybus, K.M.; Selvin, P.R.
Motor domain phosphorylation modulates kinesin-1 transport
J. Biol. Chem.
288
32612-32621
2013
Homo sapiens (Q12756), Mus musculus (Q61768)
Manually annotated by BRENDA team