RAB5A

RAB5A, member RAS oncogene family

PDB rendering based on 1huq.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsRAB5A ; RAB5
External IDsOMIM: 179512 MGI: 105926 HomoloGene: 68142 GeneCards: RAB5A Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez5868271457
EnsemblENSG00000144566ENSMUSG00000017831
UniProtP20339Q9CQD1
RefSeq (mRNA)NM_001292048NM_025887
RefSeq (protein)NP_001278977NP_080163
Location (UCSC)Chr 3:
19.99 – 20.03 Mb		Chr 17:
53.48 – 53.51 Mb
PubMed search

Ras-related protein Rab-5A is a protein that in humans is encoded by the RAB5A gene.[1][2]

Function

RAB5A localizes to early endosomes where it is involved in the recruitment of RAB7A and the maturation of these compartments to late endosomes.[3]

Interactions

RAB5A has been shown to interact with RABEP1,[4][5][6][7] SDCBP,[8] ZFYVE20[9] and CHML.[10][11]

References

  1. ↑ Rousseau-Merck MF, Zahraoui A, Touchot N, Tavitian A, Berger R (April 1991). "Chromosome assignment of four RAS-related RAB genes". Hum Genet 86 (4): 350–4. doi:10.1007/BF00201831. PMID 1999336.
  2. ↑ "Entrez Gene: RAB5A RAB5A, member RAS oncogene family".
  3. ↑ http://www.ncbi.nlm.nih.gov/pubmed/21878991?dopt=Citation
  4. ↑ Xiao, G H; Shoarinejad F; Jin F; Golemis E A; Yeung R S (March 1997). "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis". J. Biol. Chem. (UNITED STATES) 272 (10): 6097–100. doi:10.1074/jbc.272.10.6097. ISSN 0021-9258. PMID 9045618.
  5. ↑ Vitale, G; Rybin V; Christoforidis S; Thornqvist P; McCaffrey M; Stenmark H; Zerial M (April 1998). "Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5". EMBO J. (ENGLAND) 17 (7): 1941–51. doi:10.1093/emboj/17.7.1941. ISSN 0261-4189. PMC 1170540. PMID 9524117.
  6. ↑ Stenmark, H; Vitale G; Ullrich O; Zerial M (November 1995). "Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion". Cell (UNITED STATES) 83 (3): 423–32. doi:10.1016/0092-8674(95)90120-5. ISSN 0092-8674. PMID 8521472.
  7. ↑ Valsdottir, R; Hashimoto H; Ashman K; Koda T; Storrie B; Nilsson T (November 2001). "Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER". FEBS Lett. (Netherlands) 508 (2): 201–9. doi:10.1016/S0014-5793(01)02993-3. ISSN 0014-5793. PMID 11718716.
  8. ↑ Tomoda, Toshifumi; Kim Jee Hae; Zhan Caixin; Hatten Mary E (March 2004). "Role of Unc51.1 and its binding partners in CNS axon outgrowth". Genes Dev. (United States) 18 (5): 541–58. doi:10.1101/gad.1151204. ISSN 0890-9369. PMC 374236. PMID 15014045.
  9. ↑ Nielsen, E; Christoforidis S; Uttenweiler-Joseph S; Miaczynska M; Dewitte F; Wilm M; Hoflack B; Zerial M (October 2000). "Rabenosyn-5, a Novel Rab5 Effector, Is Complexed with Hvps45 and Recruited to Endosomes through a Fyve Finger Domain". J. Cell Biol. (UNITED STATES) 151 (3): 601–12. doi:10.1083/jcb.151.3.601. ISSN 0021-9525. PMC 2185588. PMID 11062261.
  10. ↑ Anant, J S; Desnoyers L; Machius M; Demeler B; Hansen J C; Westover K D; Deisenhofer J; Seabra M C (September 1998). "Mechanism of Rab geranylgeranylation: formation of the catalytic ternary complex". Biochemistry (UNITED STATES) 37 (36): 12559–68. doi:10.1021/bi980881a. ISSN 0006-2960. PMID 9730828.
  11. ↑ 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.

Further reading

  • Bucci C, Parton RG, Mather IH et al. (1992). "The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway". Cell 70 (5): 715–28. doi:10.1016/0092-8674(92)90306-W. PMID 1516130.
  • 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.
  • Cremers FP, Armstrong SA, Seabra MC et al. (1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". J. Biol. Chem. 269 (3): 2111–7. PMID 8294464.
  • Stenmark H, Vitale G, Ullrich O, Zerial M (1996). "Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion". Cell 83 (3): 423–32. doi:10.1016/0092-8674(95)90120-5. PMID 8521472.
  • Vita F, Soranzo MR, Borelli V et al. (1996). "Subcellular localization of the small GTPase Rab5a in resting and stimulated human neutrophils". Exp. Cell Res. 227 (2): 367–73. doi:10.1006/excr.1996.0286. PMID 8831575.
  • Xiao GH, Shoarinejad F, Jin F et al. (1997). "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis". J. Biol. Chem. 272 (10): 6097–100. doi:10.1074/jbc.272.10.6097. PMID 9045618.
  • Simonsen A, Lippé R, Christoforidis S et al. (1998). "EEA1 links PI(3)K function to Rab5 regulation of endosome fusion". Nature 394 (6692): 494–8. doi:10.1038/28879. PMID 9697774.
  • Anant JS, Desnoyers L, Machius M et al. (1999). "Mechanism of Rab geranylgeranylation: formation of the catalytic ternary complex". Biochemistry 37 (36): 12559–68. doi:10.1021/bi980881a. PMID 9730828.
  • Bucci C, Chiariello M, Lattero D et al. (1999). "Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1)". Biochem. Biophys. Res. Commun. 258 (3): 657–62. doi:10.1006/bbrc.1999.0651. PMID 10329441.
  • Callaghan J, Nixon S, Bucci C et al. (1999). "Direct interaction of EEA1 with Rab5b". Eur. J. Biochem. 265 (1): 361–6. doi:10.1046/j.1432-1327.1999.00743.x. PMID 10491193.
  • Shisheva A, Chinni SR, DeMarco C (1999). "General role of GDP dissociation inhibitor 2 in membrane release of Rab proteins: modulations of its functional interactions by in vitro and in vivo structural modifications". Biochemistry 38 (36): 11711–21. doi:10.1021/bi990200r. PMID 10512627.
  • Masuda ES, Luo Y, Young C et al. (2000). "Rab37 is a novel mast cell specific GTPase localized to secretory granules". FEBS Lett. 470 (1): 61–4. doi:10.1016/S0014-5793(00)01288-6. PMID 10722846.
  • Hoffenberg S, Liu X, Nikolova L et al. (2000). "A novel membrane-anchored Rab5 interacting protein required for homotypic endosome fusion". J. Biol. Chem. 275 (32): 24661–9. doi:10.1074/jbc.M909600199. PMID 10818110.
  • Nielsen E, Christoforidis S, Uttenweiler-Joseph S et al. (2000). "Rabenosyn-5, a Novel Rab5 Effector, Is Complexed with Hvps45 and Recruited to Endosomes through a Fyve Finger Domain". J. Cell Biol. 151 (3): 601–12. doi:10.1083/jcb.151.3.601. PMC 2185588. PMID 11062261.
  • Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
  • Lanzetti L, Rybin V, Malabarba MG et al. (2000). "The Eps8 protein coordinates EGF receptor signalling through Rac and trafficking through Rab5". Nature 408 (6810): 374–7. doi:10.1038/35042605. PMID 11099046.
  • Wolf RM, Wilkes JJ, Chao MV, Resh MD (2001). "Tyrosine phosphorylation of p190 RhoGAP by Fyn regulates oligodendrocyte differentiation". J. Neurobiol. 49 (1): 62–78. doi:10.1002/neu.1066. PMID 11536198.
  • Seachrist JL, Laporte SA, Dale LB et al. (2002). "Rab5 association with the angiotensin II type 1A receptor promotes Rab5 GTP binding and vesicular fusion". J. Biol. Chem. 277 (1): 679–85. doi:10.1074/jbc.M109022200. PMID 11682489.