3.6.4.B1: kinesin K16
This is an abbreviated version!
For detailed information about kinesin K16, go to the full flat file.
Word Map on EC 3.6.4.B1
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3.6.4.B1
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microtubule
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cargo
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testis-specific
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crem
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microtubule-dependent
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plant-specific
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kinesin-related
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phragmoplast
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phosphorylation-independent
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male-specific
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analysis
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medicine
- 3.6.4.B1
- microtubule
-
cargo
-
testis-specific
- crem
-
microtubule-dependent
-
plant-specific
-
kinesin-related
- phragmoplast
-
phosphorylation-independent
-
male-specific
- analysis
- medicine
Reaction
Synonyms
AtPAKRP1, AtPAKRP1L, GhKCH1, K16MD, KCBP, KIF 14, KIF18A, KIF4, KIF5, KIF5B, KIF5C, KIFC5A, kinesin K-16, kinesin K16, kinesin K16MD, kinesin KIF17b, kinesin kif5c, kinesin superfamily protein 5B, kinesin-1 motor protein, kinesin-like calmodulin-binding protein, KLP-6 kinesin, MS-KIF18A
ECTree
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Subunits
Subunits on EC 3.6.4.B1 - kinesin K16
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x * 60000, calculated for full-length protein, x * 38000, SDS-PAGE and calculated for motor domain
additional information
additional information
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interaction of kinesin heavy chain KIF5C with gamma-aminobutyric acid type A receptor interacting factor-1 GRIF-1. Direct association between the two proteins at the KIF5C C-terminal and GRIF-1 N-terminal regions. GRIF-1 can bind to the tetrameric kinesin light chain/kinesin heavy-chain complex
additional information
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isoform KIF14 interacts with microtubule-bundling protein PRC1 and targets to the central spindle via this interaction
additional information
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Ran-binding protein 2 associates selectively with kinesins KIF5B and KIF5C, but not KIF5A. A single residue conserved in KIF5B and KIF5C, but not KIF5A, confers KIF5-isotype-specific association with RanBP2. Interaction is also mediated by a conserved leucine-like heptad motif present in KIF5s and KBD of RanBP2. Selective inhibition of the interaction between kinesin-bindiing domain of RanBP2 and KIF5B/KIF5C in cell lines causes perinuclear clustering of mitochondria, but not of lysosomes, deficits inmitochondrialmembrane potential and cell shrinkage
additional information
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contrary to Oryza sativa, modification of brain or skeletal muscle K16 with photoreactive ATP derivative, 2'(3')-O-(4-benzoylbenzoyl)-1,N6-etheno-ATP and UV-irradiation does not result in intermolecular cross-linking
additional information
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KIFC5A interacts with nucleotide-binding proteins 1 and 2. Knockdown of nucleotide-binding protein 1 or double knockdown of nucleotide-binding proteins 1 and 2 both phenocopy the KIFC5A silencing effect
additional information
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modification of K16 with photoreactive ATP derivative, 2'(3')-O-(4-benzoylbenzoyl)-1,N6-etheno-ATP and UV-irradiation results in intermolecular cross-linking in presence of ADP or ATP. No cross-linking is observed in absence of nucleotide
additional information
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in kinesin-like calmodulin binding protein, calmodulin binds to helix alpha4 and inserts itself between the motor and the microtubule. Positioning of the calmodulin binding helix is not decided by crystal packing forces but is determined by the conformational state of the motor