EC Number   |
Subunits |
Reference |
|---|
   3.6.4.B1 | ? |
x * 60000, calculated for full-length protein, x * 38000, SDS-PAGE and calculated for motor domain |
669159 |
| 3.6.4.B1 | More |
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 |
687437 |
| 3.6.4.B1 | More |
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 |
688699 |
| 3.6.4.B1 | More |
interaction of KIF18A with estrogen receptor ERalpha |
669593 |
| 3.6.4.B1 | More |
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 |
687519 |
| 3.6.4.B1 | More |
isoform KIF14 interacts with microtubule-bundling protein PRC1 and targets to the central spindle via this interaction |
687900 |
| 3.6.4.B1 | More |
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 |
687910 |
| 3.6.4.B1 | More |
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 |
687437 |
| 3.6.4.B1 | More |
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 |
690151 |
