RAB3B

Protein-coding gene in the species Homo sapiens
RAB3B
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3DZ8

Identifiers
AliasesRAB3B, member RAS oncogene family
External IDsOMIM: 179510; MGI: 1917158; HomoloGene: 2149; GeneCards: RAB3B; OMA:RAB3B - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for RAB3B
Genomic location for RAB3B
Band1p32.3Start51,907,956 bp[1]
End51,990,700 bp[1]
Gene location (Mouse)
Chromosome 4 (mouse)
Chr.Chromosome 4 (mouse)[2]
Chromosome 4 (mouse)
Genomic location for RAB3B
Genomic location for RAB3B
Band4|4 C7Start108,736,260 bp[2]
End108,800,521 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • islet of Langerhans

  • stromal cell of endometrium

  • beta cell

  • gonad

  • entorhinal cortex

  • anterior pituitary

  • hypothalamus

  • superior vestibular nucleus

  • placenta

  • testicle
Top expressed in
  • facial motor nucleus

  • superior frontal gyrus

  • zygote

  • arcuate nucleus

  • paraventricular nucleus of hypothalamus

  • subiculum

  • primary visual cortex

  • supraoptic nucleus

  • dorsomedial hypothalamic nucleus

  • primary oocyte
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • GDP binding
  • GTP binding
  • myosin V binding
  • protein binding
  • GTP-dependent protein binding
  • GTPase activity
Cellular component
  • cytoplasm
  • vesicle
  • cytosol
  • membrane
  • synaptic vesicle
  • plasma membrane
  • secretory granule
  • perinuclear region of cytoplasm
  • extracellular exosome
  • anchored component of synaptic vesicle membrane
  • endosome
  • Golgi apparatus
  • dopaminergic synapse
Biological process
  • antigen processing and presentation
  • positive regulation of dopamine uptake involved in synaptic transmission
  • peptidyl-cysteine methylation
  • regulation of exocytosis
  • regulation of vesicle size
  • protein transport
  • transport
  • intracellular protein transport
  • vesicle docking involved in exocytosis
  • protein secretion
  • Rab protein signal transduction
  • protein localization to plasma membrane
  • regulation of synaptic vesicle cycle
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5865

69908

Ensembl

ENSG00000169213

ENSMUSG00000003411

UniProt

P20337

Q9CZT8

RefSeq (mRNA)

NM_002867

NM_023537

RefSeq (protein)

NP_002858

NP_076026

Location (UCSC)Chr 1: 51.91 – 51.99 MbChr 4: 108.74 – 108.8 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ras-related protein Rab-3B is a protein that in humans is encoded by the RAB3B gene.[5]

Interactions

RAB3B has been shown to interact with RPH3A.[6][7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000169213 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003411 – 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. ^ "Entrez Gene: RAB3B RAB3B, member RAS oncogene family".
  6. ^ Fukuda M (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". The Journal of Biological Chemistry. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
  7. ^ Weber E, Jilling T, Kirk KL (March 1996). "Distinct functional properties of Rab3A and Rab3B in PC12 neuroendocrine cells". The Journal of Biological Chemistry. 271 (12): 6963–71. doi:10.1074/jbc.271.12.6963. PMID 8636125.

Further reading

  • Rousseau-Merck MF, Zahraoui A, Touchot N, Tavitian A, Berger R (February 1991). "Chromosome assignment of four RAS-related RAB genes". Human Genetics. 86 (4): 350–4. doi:10.1007/BF00201831. PMID 1999336. S2CID 30730416.
  • Zahraoui A, Touchot N, Chardin P, Tavitian A (July 1989). "The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion". The Journal of Biological Chemistry. 264 (21): 12394–401. doi:10.1016/S0021-9258(18)63872-4. PMID 2501306.
  • Weber E, Berta G, Tousson A, St John P, Green MW, Gopalokrishnan U, Jilling T, Sorscher EJ, Elton TS, Abrahamson DR (May 1994). "Expression and polarized targeting of a rab3 isoform in epithelial cells". The Journal of Cell Biology. 125 (3): 583–94. doi:10.1083/jcb.125.3.583. PMC 2119989. PMID 8175882.
  • Weber E, Jilling T, Kirk KL (March 1996). "Distinct functional properties of Rab3A and Rab3B in PC12 neuroendocrine cells". The Journal of Biological Chemistry. 271 (12): 6963–71. doi:10.1074/jbc.271.12.6963. PMID 8636125.
  • Regazzi R, Ravazzola M, Iezzi M, Lang J, Zahraoui A, Andereggen E, Morel P, Takai Y, Wollheim CB (September 1996). "Expression, localization and functional role of small GTPases of the Rab3 family in insulin-secreting cells". Journal of Cell Science. 109 ( Pt 9) (9): 2265–73. doi:10.1242/jcs.109.9.2265. PMID 8886977.
  • Sidhu RS, Bhullar RP (December 2001). "Rab3B in human platelet is membrane bound and interacts with Ca(2+)/calmodulin". Biochemical and Biophysical Research Communications. 289 (5): 1039–43. doi:10.1006/bbrc.2001.6113. PMID 11741295.
  • van IJzendoorn SC, Tuvim MJ, Weimbs T, Dickey BF, Mostov KE (February 2002). "Direct interaction between Rab3b and the polymeric immunoglobulin receptor controls ligand-stimulated transcytosis in epithelial cells". Developmental Cell. 2 (2): 219–28. doi:10.1016/S1534-5807(02)00115-6. PMID 11832247.
  • Fukuda M (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". The Journal of Biological Chemistry. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
  • Yamamoto Y, Nishimura N, Morimoto S, Kitamura H, Manabe S, Kanayama HO, Kagawa S, Sasaki T (August 2003). "Distinct roles of Rab3B and Rab13 in the polarized transport of apical, basolateral, and tight junctional membrane proteins to the plasma membrane". Biochemical and Biophysical Research Communications. 308 (2): 270–5. doi:10.1016/S0006-291X(03)01358-5. PMID 12901864.
  • Matsumoto M, Miki T, Shibasaki T, Kawaguchi M, Shinozaki H, Nio J, Saraya A, Koseki H, Miyazaki M, Iwanaga T, Seino S (June 2004). "Noc2 is essential in normal regulation of exocytosis in endocrine and exocrine cells". Proceedings of the National Academy of Sciences of the United States of America. 101 (22): 8313–8. Bibcode:2004PNAS..101.8313M. doi:10.1073/pnas.0306709101. PMC 420391. PMID 15159548.
  • Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (March 2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.


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