KIF5B

Protein-coding gene in the species Homo sapiens
KIF5B
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1BG2, 1MKJ, 2P4N, 3J8X, 3J8Y, 4HNA, 4LNU

Identifiers
AliasesKIF5B, HEL-S-61, KINH, KNS, KNS1, UKHC, kinesin family member 5B
External IDsOMIM: 602809; MGI: 1098268; HomoloGene: 55829; GeneCards: KIF5B; OMA:KIF5B - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for KIF5B
Genomic location for KIF5B
Band10p11.22Start32,009,015 bp[1]
End32,056,425 bp[1]
Gene location (Mouse)
Chromosome 18 (mouse)
Chr.Chromosome 18 (mouse)[2]
Chromosome 18 (mouse)
Genomic location for KIF5B
Genomic location for KIF5B
Band18 A1|18 4.46 cMStart6,201,002 bp[2]
End6,242,174 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • caput epididymis

  • optic nerve

  • corpus epididymis

  • inferior ganglion of vagus nerve

  • visceral pleura

  • lower lobe of lung

  • internal globus pallidus

  • subthalamic nucleus

  • superficial temporal artery

  • medulla oblongata
Top expressed in
  • globus pallidus

  • lateral geniculate nucleus

  • atrioventricular valve

  • ventral tegmental area

  • pontine nuclei

  • lateral hypothalamus

  • seminal vesicula

  • epithelium of stomach

  • mammillary body

  • medial vestibular nucleus
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
SpeciesHumanMouse
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 MbChr 18: 6.2 – 6.24 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Kinesin family member 5B (KIF5B) is a protein that in humans is encoded by the KIF5B gene.[5][6] It is part of the kinesin family of motor proteins.

Interactions

KIF5B has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000170759 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b c 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. ^ a b 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. ^ a b 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.
  • v
  • t
  • e
  • 1bg2: HUMAN UBIQUITOUS KINESIN MOTOR DOMAIN
    1bg2: HUMAN UBIQUITOUS KINESIN MOTOR DOMAIN
  • 1mkj: Human Kinesin Motor Domain With Docked Neck Linker
    1mkj: Human Kinesin Motor Domain With Docked Neck Linker
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Human
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See also: cytoskeletal defects


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