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KIF5B
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1BG2, 1MKJ, 2P4N, 3J8X, 3J8Y, 4HNA, 4LNU
Identifiers
Aliases	KIF5B, HEL-S-61, KINH, KNS, KNS1, UKHC, kinesin family member 5B
External IDs	OMIM: 602809; MGI: 1098268; HomoloGene: 55829; GeneCards: KIF5B; OMA:KIF5B - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10p11.22 Start 32,009,015 bp End 32,056,425 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18 A1|18 4.46 cM Start 6,201,002 bp End 6,242,174 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tail of epididymis caput epididymis optic nerve corpus epididymis mucosa of paranasal sinus inferior ganglion of vagus nerve visceral pleura lower lobe of lung internal globus pallidus Skeletal muscle tissue of biceps brachii Top expressed in globus pallidus lateral geniculate nucleus atrioventricular valve ventral tegmental area pontine nuclei epithelium of lens lateral hypothalamus deep cerebellar nuclei seminal vesicula epithelium of stomach More reference expression data BioGPS More reference expression data
Gene ontology Molecular function microtubule motor activity nucleotide binding microtubule binding protein binding plus-end-directed microtubule motor activity ATP binding JUN kinase binding cadherin binding microtubule lateral binding identical protein binding ATPase activity Cellular component vesicle membrane kinesin complex endocytic vesicle microtubule organizing center membrane-bounded organelle ciliary rootlet perinuclear region of cytoplasm neuron projection microtubule cytoskeleton axonal growth cone cytoplasm cytosol microtubule cytoskeleton phagocytic vesicle axon cytoplasm Biological process cytoskeleton-dependent intracellular transport plus-end-directed vesicle transport along microtubule cytoplasm organization vesicle transport along microtubule positive regulation of potassium ion transport regulation of membrane potential positive regulation of synaptic transmission, GABAergic axon guidance microtubule-based movement stress granule disassembly positive regulation of insulin secretion involved in cellular response to glucose stimulus positive regulation of intracellular protein transport positive regulation of voltage-gated sodium channel activity positive regulation of vesicle fusion centrosome localization brain development hippocampus development positive regulation of protein localization to plasma membrane cellular response to interferon-gamma anterograde axonal protein transport anterograde neuronal dense core vesicle transport retrograde neuronal dense core vesicle transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3799 16573 Ensembl ENSG00000170759 ENSMUSG00000006740 UniProt P33176 Q61768 RefSeq (mRNA) NM_004521 NM_008448 RefSeq (protein) NP_004512 NP_032474 Location (UCSC) Chr 10: 32.01 – 32.06 Mb Chr 18: 6.2 – 6.24 Mb PubMed search
Wikidata
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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.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000170759 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000006740 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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 2289507. PMID 1607388.
6. "Entrez Gene: KIF5B kinesin family member 5B".
7. ^ 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.
8. ^ 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.
9. ^ 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.
10. 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. S2CID 32927183.
• 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. Bibcode:1996Natur.380..550J. 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. S2CID 17524297.
• 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. doi:10.1523/JNEUROSCI.20-17-06374.2000. PMC 6772948. 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. Bibcode:2002Natur.417...83S. doi:10.1038/nature743. PMID 11986669. S2CID 4400494.
• 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. Bibcode:2004CBio...14.1436J. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
• 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. S2CID 6875457.
• 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.

External links

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

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