KIF5B

KIF5B
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases KIF5B, HEL-S-61, KINH, KNS, KNS1, UKHC, kinesin family member 5B
External IDs MGI: 1098268 HomoloGene: 55829 GeneCards: KIF5B
Genetically Related Diseases
bipolar disorder[1]
RNA expression pattern


More reference expression data
Orthologs
Species Human Mouse
Entrez

3799

16573

Ensembl

ENSG00000170759

ENSMUSG00000006740

UniProt

P33176

Q61768

RefSeq (mRNA)

NM_004521

NM_008448

RefSeq (protein)

NP_004512.1

NP_032474.2

Location (UCSC) Chr 10: 32.01 – 32.06 Mb Chr 18: 6.2 – 6.24 Mb
PubMed search [2] [3]
Wikidata
View/Edit HumanView/Edit Mouse

Kinesin-1 heavy chain is a protein that in humans is encoded by the KIF5B gene.[4][5]

Interactions

KIF5B has been shown to interact with:

References

  1. ↑ "Diseases that are genetically associated with KIF5B view/edit references on wikidata".
  2. ↑ "Human PubMed Reference:".
  3. ↑ "Mouse PubMed Reference:".
  4. ↑ Navone F, Niclas J, Hom-Booher N, Sparks L, Bernstein HD, McCaffrey G, Vale RD (Jun 1992). "Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells". The Journal of Cell Biology. 117 (6): 1263–75. doi:10.1083/jcb.117.6.1263. PMC 2289507Freely accessible. PMID 1607388.
  5. ↑ "Entrez Gene: KIF5B kinesin family member 5B".
  6. 1 2 3 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.
  7. 1 2 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.
  8. 1 2 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 2156125Freely accessible. PMID 10491391.
  9. ↑ Ichimura T, Wakamiya-Tsuruta A, Itagaki C, Taoka M, Hayano T, Natsume T, Isobe T (Apr 2002). "Phosphorylation-dependent interaction of kinesin light chain 2 and the 14-3-3 protein". Biochemistry. 41 (17): 5566–72. doi:10.1021/bi015946f. PMID 11969417.

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 2851642Freely accessible. 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 2156125Freely accessible. 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. 


This article is issued from Wikipedia - version of the 5/20/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.