KIF5B

VALUE_ERROR (nil)
Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

Kinesin-1 heavy chain is a protein that in humans is encoded by the KIF5B gene.

Interactions

KIF5B has been shown to interact with:

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

Further reading

• Niclas J, Navone F, Hom-Booher N, Vale RD (May 1994). "Cloning and localization of a conventional kinesin motor expressed exclusively in neurons". Neuron. 12 (5): 1059–72. doi:10.1016/0896-6273(94)90314-X. PMID 7514426.
• Kull FJ, Sablin EP, Lau R, Fletterick RJ, Vale RD (Apr 1996). "Crystal structure of the kinesin motor domain reveals a structural similarity to myosin". Nature. 380 (6574): 550–5. doi:10.1038/380550a0. PMC 2851642. PMID 8606779.
• Rahman A, Friedman DS, Goldstein LS (Jun 1998). "Two kinesin light chain genes in mice. Identification and characterization of the encoded proteins". The Journal of Biological Chemistry. 273 (25): 15395–403. doi:10.1074/jbc.273.25.15395. PMID 9624122.
• Tanaka Y, Kanai Y, Okada Y, Nonaka S, Takeda S, Harada A, Hirokawa N (Jun 1998). "Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria". Cell. 93 (7): 1147–58. doi:10.1016/S0092-8674(00)81459-2. PMID 9657148.
• Rahman A, Kamal A, Roberts EA, Goldstein LS (Sep 1999). "Defective kinesin heavy chain behavior in mouse kinesin light chain mutants". The Journal of Cell Biology. 146 (6): 1277–88. doi:10.1083/jcb.146.6.1277. PMC 2156125. PMID 10491391.
• Ong LL, Lim AP, Er CP, Kuznetsov SA, Yu H (Oct 2000). "Kinectin-kinesin binding domains and their effects on organelle motility". The Journal of Biological Chemistry. 275 (42): 32854–60. doi:10.1074/jbc.M005650200. PMID 10913441.
• Kanai Y, Okada Y, Tanaka Y, Harada A, Terada S, Hirokawa N (Sep 2000). "KIF5C, a novel neuronal kinesin enriched in motor neurons". The Journal of Neuroscience. 20 (17): 6374–84. PMID 10964943.
• Setou M, Seog DH, Tanaka Y, Kanai Y, Takei Y, Kawagishi M, Hirokawa N (May 2002). "Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites". Nature. 417 (6884): 83–7. doi:10.1038/nature743. PMID 11986669.
• Hakimi MA, Speicher DW, Shiekhattar R (Oct 2002). "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. doi:10.1074/jbc.C200434200. PMID 12191989.
• Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL (Dec 2002). "The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23". Biochemistry. 41 (50): 14906–15. doi:10.1021/bi026417u. PMID 12475239.
• Macioce P, Gambara G, Bernassola M, Gaddini L, Torreri P, Macchia G, Ramoni C, Ceccarini M, Petrucci TC (Dec 2003). "Beta-dystrobrevin interacts directly with kinesin heavy chain in brain". Journal of Cell Science. 116 (Pt 23): 4847–56. doi:10.1242/jcs.00805. PMID 14600269.
• Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL (Jul 2004). "The ribosome receptor, p180, interacts with kinesin heavy chain, KIF5B". Biochemical and Biophysical Research Communications. 319 (3): 987–92. doi:10.1016/j.bbrc.2004.05.069. PMID 15184079.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (Aug 2004). "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. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
• Su Q, Cai Q, Gerwin C, Smith CL, Sheng ZH (Oct 2004). "Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons". Nature Cell Biology. 6 (10): 941–53. doi:10.1038/ncb1169. PMID 15459722.
• Brickley K, Smith MJ, Beck M, Stephenson FA (Apr 2005). "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. doi:10.1074/jbc.M409095200. PMID 15644324.
• Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (Jun 2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Molecular & Cellular Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.