RABGEF1

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RAB guanine nucleotide exchange factor (GEF) 1
File:PBB Protein RABGEF1 image.jpg
PDB rendering based on 1txu.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols RABGEF1 ; FLJ32302; RABEX5; rabex-5
External IDs Template:OMIM5 Template:MGI HomoloGene8720
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

RAB guanine nucleotide exchange factor (GEF) 1, also known as RABGEF1, is a human gene.[1]

RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM 603616) that is required for endocytic membrane fusion, and it serves as a specific guanine nucleotide exchange factor for RAB5 (RAB5A; MIM 179512) (Horiuchi et al., 1997).[supplied by OMIM][1]

References

  1. 1.0 1.1 "Entrez Gene: RABGEF1 RAB guanine nucleotide exchange factor (GEF) 1".

Further reading

  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Horiuchi H, Lippé R, McBride HM; et al. (1997). "A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function". Cell. 90 (6): 1149–59. PMID 9323142.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
  • Nimmrich I, Erdmann S, Melchers U; et al. (2000). "Seven genes that are differentially transcribed in colorectal tumor cell lines". Cancer Lett. 160 (1): 37–43. PMID 11098082.
  • Lippé R, Miaczynska M, Rybin V; et al. (2001). "Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex". Mol. Biol. Cell. 12 (7): 2219–28. PMID 11452015.
  • de Renzis S, Sönnichsen B, Zerial M (2002). "Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes". Nat. Cell Biol. 4 (2): 124–33. doi:10.1038/ncb744. PMID 11788822.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Mattera R, Arighi CN, Lodge R; et al. (2003). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". EMBO J. 22 (1): 78–88. doi:10.1093/emboj/cdg015. PMID 12505986.
  • Hillier LW, Fulton RS, Fulton LA; et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. doi:10.1038/nature01782. PMID 12853948.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Jin J, Smith FD, Stark C; et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
  • Delprato A, Merithew E, Lambright DG (2004). "Structure, exchange determinants, and family-wide rab specificity of the tandem helical bundle and Vps9 domains of Rabex-5". Cell. 118 (5): 607–17. doi:10.1016/j.cell.2004.08.009. PMID 15339665.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  • Kimura K, Wakamatsu A, Suzuki Y; et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.
  • Penengo L, Mapelli M, Murachelli AG; et al. (2006). "Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin". Cell. 124 (6): 1183–95. doi:10.1016/j.cell.2006.02.020. PMID 16499958.
  • Kalesnikoff J, Rios EJ, Chen CC; et al. (2007). "Roles of RabGEF1/Rabex-5 domains in regulating Fc epsilon RI surface expression and Fc epsilon RI-dependent responses in mast cells". Blood. 109 (12): 5308–17. doi:10.1182/blood-2007-01-067363. PMID 17341663.
  • Ewing RM, Chu P, Elisma F; et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.
  • Delprato A, Lambright DG (2007). "Structural basis for Rab GTPase activation by VPS9 domain exchange factors". Nat. Struct. Mol. Biol. 14 (5): 406–12. doi:10.1038/nsmb1232. PMID 17450153.

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