RABGEF1

RAB guanine nucleotide exchange factor (GEF) 1
PDB rendering based on 1txu.
Available structures PDB 1TXU, 2C7M, 2C7N, 2OT3
Identifiers
Symbols	RABGEF1; FLJ32302; RABEX5; rabex-5
External IDs	OMIM: 609700 MGI: 1929459 HomoloGene: 8720 GeneCards: RABGEF1 Gene
Gene Ontology Molecular function • DNA binding • protein binding • zinc ion binding • metal ion binding Cellular component • cytoplasm • early endosome • recycling endosome Biological process • endocytosis • protein transport
Orthologs
Species	Human	Mouse
Entrez	27342	56715
Ensembl	n/a	ENSMUSG00000025340
UniProt	n/a	Q9JM13
RefSeq (mRNA)	NM_014504	NM_019983
RefSeq (protein)	NP_055319	NP_064367
Location (UCSC)	n/a	Chr 5: 130.65 – 130.69 Mb
PubMed search	[1]	[2]

Rab5 GDP/GTP exchange factor is a protein that in humans is encoded by the RABGEF1 gene.

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]

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. doi:10.1016/0378-1119(94)90802-8. 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. doi:10.1016/S0092-8674(00)80380-3. 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. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• 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. PMC 55678. PMID 11452015. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=55678. 
• 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129. 
• 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. PMC 1890836. PMID 17341663. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1890836. 
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948. 
• 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. PMC 2254184. PMID 17450153. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2254184.