RAB3A

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This article is about the human gene. For the hand gesture, see Rabia sign.
RAB3A, member RAS oncogene family
Protein RAB3A PDB 1zbd.png
PDB rendering based on 1zbd.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbol RAB3A
External IDs OMIM179490 MGI97843 HomoloGene20629 GeneCards: RAB3A Gene
RNA expression pattern
PBB GE RAB3A 204974 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5864 19339
Ensembl ENSG00000105649 ENSMUSG00000031840
UniProt P20336 P63011
RefSeq (mRNA) NM_002866 NM_001166399
RefSeq (protein) NP_002857 NP_001159871
Location (UCSC) Chr 19:
18.31 – 18.31 Mb
Chr 8:
70.75 – 70.76 Mb
PubMed search [1] [2]

Ras-related protein Rab-3A is a protein that in humans is encoded by the RAB3A gene.[1][2][3] It is involved in calcium exocytosis in neurons.


Interactions[edit]

RAB3A has been shown to interact with CHM,[4][5] RPH3A[6][7][8] and RIMS1.[6][9]

References[edit]

  1. ^ Rousseau-Merck MF, Zahraoui A, Bernheim A, Touchot N, Miglierina R, Tavitian A, Berger R (January 1990). "Chromosome mapping of the human ras-related rab3A gene to 19p13.2". Genomics 5 (4): 694–8. doi:10.1016/0888-7543(89)90110-9. PMID 2687157. 
  2. ^ Brondyk WH, McKiernan CJ, Fortner KA, Stabila P, Holz RW, Macara IG (March 1995). "Interaction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3A". Mol Cell Biol 15 (3): 1137–43. PMC 230335. PMID 7532276. 
  3. ^ "Entrez Gene: RAB3A RAB3A, member RAS oncogene family". 
  4. ^ Cremers, F P; Armstrong S A, Seabra M C, Brown M S, Goldstein J L (January 1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". J. Biol. Chem. (UNITED STATES) 269 (3): 2111–7. ISSN 0021-9258. PMID 8294464. 
  5. ^ Pereira-Leal, José B; Strom Molly, Godfrey Richard F, Seabra Miguel C (January 2003). "Structural determinants of Rab and Rab Escort Protein interaction: Rab family motifs define a conserved binding surface". Biochem. Biophys. Res. Commun. (United States) 301 (1): 92–7. doi:10.1016/S0006-291X(02)02963-7. ISSN 0006-291X. PMID 12535645. 
  6. ^ a b Fukuda, Mitsunori (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J. Biol. Chem. (United States) 278 (17): 15373–80. doi:10.1074/jbc.M212341200. ISSN 0021-9258. PMID 12578829. 
  7. ^ Ostermeier, C; Brunger A T (February 1999). "Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A". Cell (UNITED STATES) 96 (3): 363–74. doi:10.1016/S0092-8674(00)80549-8. ISSN 0092-8674. PMID 10025402. 
  8. ^ Weber, E; Jilling T, Kirk K L (March 1996). "Distinct functional properties of Rab3A and Rab3B in PC12 neuroendocrine cells". J. Biol. Chem. (UNITED STATES) 271 (12): 6963–71. doi:10.1074/jbc.271.12.6963. ISSN 0021-9258. PMID 8636125. 
  9. ^ Betz, A; Thakur P, Junge H J, Ashery U, Rhee J S, Scheuss V, Rosenmund C, Rettig J, Brose N (April 2001). "Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming". Neuron (United States) 30 (1): 183–96. doi:10.1016/S0896-6273(01)00272-0. ISSN 0896-6273. PMID 11343654. 

Further reading[edit]

  • Khosravi-Far R, Lutz RJ, Cox AD, et al. (1991). "Isoprenoid modification of rab proteins terminating in CC or CXC motifs.". Proc. Natl. Acad. Sci. U.S.A. 88 (14): 6264–8. doi:10.1073/pnas.88.14.6264. PMC 52063. PMID 1648736. 
  • Zahraoui A, Touchot N, Chardin P, Tavitian A (1989). "The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion.". J. Biol. Chem. 264 (21): 12394–401. PMID 2501306. 
  • Farnsworth CC, Seabra MC, Ericsson LH, et al. (1995). "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A.". Proc. Natl. Acad. Sci. U.S.A. 91 (25): 11963–7. doi:10.1073/pnas.91.25.11963. PMC 45356. PMID 7991565. 
  • McKiernan CJ, Brondyk WH, Macara IG (1993). "The Rab3A GTPase interacts with multiple factors through the same effector domain. Mutational analysis of cross-linking of Rab3A to a putative target protein.". J. Biol. Chem. 268 (32): 24449–52. PMID 8226995. 
  • Trask B, Fertitta A, Christensen M, et al. (1993). "Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers.". Genomics 15 (1): 133–45. doi:10.1006/geno.1993.1021. PMID 8432525. 
  • Johannes L, Perez F, Laran-Chich MP, et al. (1996). "Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II.". Eur. J. Biochem. 239 (2): 362–8. doi:10.1111/j.1432-1033.1996.0362u.x. PMID 8706741. 
  • Burton JL, Slepnev V, De Camilli PV (1997). "An evolutionarily conserved domain in a subfamily of Rabs is crucial for the interaction with the guanyl nucleotide exchange factor Mss4.". J. Biol. Chem. 272 (6): 3663–8. doi:10.1074/jbc.272.6.3663. PMID 9013620. 
  • Geppert M, Goda Y, Stevens CF, Südhof TC (1997). "The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion.". Nature 387 (6635): 810–4. doi:10.1038/42954. PMID 9194562. 
  • Martincic I, Peralta ME, Ngsee JK (1997). "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor.". J. Biol. Chem. 272 (43): 26991–8. doi:10.1074/jbc.272.43.26991. PMID 9341137. 
  • Ostermeier C, Brunger AT (1999). "Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A.". Cell 96 (3): 363–74. doi:10.1016/S0092-8674(00)80549-8. PMID 10025402. 
  • Jung YJ, Lee TH, Lee JY, et al. (1999). "Phosphatidic acid is important to the translocation of Rab3A from the cytosol to phospholipid membranes.". Neuroreport 10 (13): 2859–63. doi:10.1097/00001756-199909090-00029. PMID 10511453. 
  • Sullivan M, Olsen AS, Houslay MD (2000). "Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND.". Cell. Signal. 11 (10): 735–42. doi:10.1016/S0898-6568(99)00037-6. PMID 10574328. 
  • Clabecq A, Henry JP, Darchen F (2000). "Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP.". J. Biol. Chem. 275 (41): 31786–91. doi:10.1074/jbc.M003705200. PMID 10859313. 
  • Haynes LP, Evans GJ, Morgan A, Burgoyne RD (2001). "A direct inhibitory role for the Rab3-specific effector, Noc2, in Ca2+-regulated exocytosis in neuroendocrine cells.". J. Biol. Chem. 276 (13): 9726–32. doi:10.1074/jbc.M006959200. PMID 11134008. 
  • Zhang Y, Luan Z, Liu A, Hu G (2001). "The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins.". FEBS Lett. 497 (2-3): 99–102. doi:10.1016/S0014-5793(01)02450-4. PMID 11377421. 
  • Luo HR, Saiardi A, Nagata E, et al. (2001). "GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase.". Neuron 31 (3): 439–51. doi:10.1016/S0896-6273(01)00384-1. PMID 11516400. 
  • Piiper A, Leser J, Lutz MP, et al. (2001). "Subcellular distribution and function of Rab3A-D in pancreatic acinar AR42J cells.". Biochem. Biophys. Res. Commun. 287 (3): 746–51. doi:10.1006/bbrc.2001.5651. PMID 11563859. 
  • Kuroda TS, Fukuda M, Ariga H, Mikoshiba K (2002). "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain.". J. Biol. Chem. 277 (11): 9212–8. doi:10.1074/jbc.M112414200. PMID 11773082.