Biology:KIF5B

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Kinesin family member 5B (KIF5B) is a protein that in humans is encoded by the KIF5B gene. It is part of the kinesin family of motor proteins.

Interactions

KIF5B has been shown to interact with:

• KLC1,
• KLC2,
• SNAP-25,
• SNAP23, and
• YWHAH.

Further reading

• "Cloning and localization of a conventional kinesin motor expressed exclusively in neurons". Neuron 12 (5): 1059–72. May 1994. doi:10.1016/0896-6273(94)90314-X. PMID 7514426. 
• "Crystal structure of the kinesin motor domain reveals a structural similarity to myosin". Nature 380 (6574): 550–5. Apr 1996. doi:10.1038/380550a0. PMID 8606779. Bibcode: 1996Natur.380..550J. 
• "Two kinesin light chain genes in mice. Identification and characterization of the encoded proteins". The Journal of Biological Chemistry 273 (25): 15395–403. Jun 1998. doi:10.1074/jbc.273.25.15395. PMID 9624122. 
• "Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria". Cell 93 (7): 1147–58. Jun 1998. doi:10.1016/S0092-8674(00)81459-2. PMID 9657148. 
• "Defective kinesin heavy chain behavior in mouse kinesin light chain mutants". The Journal of Cell Biology 146 (6): 1277–88. Sep 1999. doi:10.1083/jcb.146.6.1277. PMID 10491391. 
• "Kinectin-kinesin binding domains and their effects on organelle motility". The Journal of Biological Chemistry 275 (42): 32854–60. Oct 2000. doi:10.1074/jbc.M005650200. PMID 10913441. 
• "KIF5C, a novel neuronal kinesin enriched in motor neurons". The Journal of Neuroscience 20 (17): 6374–84. Sep 2000. doi:10.1523/JNEUROSCI.20-17-06374.2000. PMID 10964943. 
• "Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites". Nature 417 (6884): 83–7. May 2002. doi:10.1038/nature743. PMID 11986669. Bibcode: 2002Natur.417...83S. 
• "The motor protein kinesin-1 links neurofibromin and merlin in a common cellular pathway of neurofibromatosis". The Journal of Biological Chemistry 277 (40): 36909–12. Oct 2002. doi:10.1074/jbc.C200434200. PMID 12191989. 
• "The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23". Biochemistry 41 (50): 14906–15. Dec 2002. doi:10.1021/bi026417u. PMID 12475239. 
• "Beta-dystrobrevin interacts directly with kinesin heavy chain in brain". Journal of Cell Science 116 (Pt 23): 4847–56. Dec 2003. doi:10.1242/jcs.00805. PMID 14600269. 
• "The ribosome receptor, p180, interacts with kinesin heavy chain, KIF5B". Biochemical and Biophysical Research Communications 319 (3): 987–92. Jul 2004. doi:10.1016/j.bbrc.2004.05.069. PMID 15184079. 
• "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology 14 (16): 1436–50. Aug 2004. doi:10.1016/j.cub.2004.07.051. PMID 15324660. 
• "Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons". Nature Cell Biology 6 (10): 941–53. Oct 2004. doi:10.1038/ncb1169. PMID 15459722. 
• "GRIF-1 and OIP106, members of a novel gene family of coiled-coil domain proteins: association in vivo and in vitro with kinesin". The Journal of Biological Chemistry 280 (15): 14723–32. Apr 2005. doi:10.1074/jbc.M409095200. PMID 15644324. 
• "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Molecular & Cellular Proteomics 4 (6): 785–95. Jun 2005. doi:10.1074/mcp.M500021-MCP200. PMID 15778465. 

External links

• Overview of all the structural information available in the PDB for UniProt: P33176 (Kinesin-1 heavy chain) at the PDBe-KB.