RAB3A

From Wikipedia, the free encyclopedia

RAB3A, member RAS oncogene family

PDB rendering based on 1zbd.

Available structures: 1zbd, 3rab

Identifiers

Symbol(s)

RAB3A;

External IDs

OMIM: 179490 MGI: 97843 HomoloGene: 20629

Gene ontology
Molecular Function:	• nucleotide binding • GTPase activity • protein binding • GTP binding
Cellular Component:	• synaptic vesicle • membrane
Biological Process:	• small GTPase mediated signal transduction • neurotransmitter secretion • protein transport • regulation of exocytosis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002866 (mRNA)
NP_002857 (protein)

NM_009001 (mRNA)
NP_033027 (protein)

Location

Chr 19: 18.17 - 18.18 Mb

Chr 8: 73.68 - 73.69 Mb

Pubmed search

[1]

[2]

RAB3A, member RAS oncogene family, also known as RAB3A, is a human gene.^[1]

[edit] References

^ Entrez Gene: RAB3A RAB3A, member RAS oncogene family.

[edit] Further reading

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. 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.
Rousseau-Merck MF, Zahraoui A, Bernheim A, et al. (1990). "Chromosome mapping of the human ras-related rab3A gene to 19p13.2.". Genomics 5 (4): 694–8. PMID 2687157.
Brondyk WH, McKiernan CJ, Fortner KA, et al. (1995). "Interaction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3A.". Mol. Cell. Biol. 15 (3): 1137–43. PMID 7532276.
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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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.