RABGEF1

Rab5 GDP/GTP exchange factor is a protein that in humans is encoded by the RABGEF1 gene.[5][6][7]

RABGEF1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1TXU, 2C7M, 2C7N, 2OT3, 4N3X, 4N3Y, 4N3Z, 4Q9U
Identifiers
Aliases	RABGEF1, RABEX5, RAP1, rabex-5, RAB guanine nucleotide exchange factor 1
External IDs	OMIM: 609700 MGI: 1929459 HomoloGene: 8720 GeneCards: RABGEF1
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7q11.21 Start 66,682,164 bp[1] End 66,811,464 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 G1.3 Start 130,171,798 bp[2] End 130,214,342 bp[2]
Gene ontology Molecular function • DNA binding • zinc ion binding • metal ion binding • Rab GTPase binding • GO:0001948 protein binding • Rab guanyl-nucleotide exchange factor activity • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity Cellular component • cytoplasm • recycling endosome • endosome • early endosome • nucleolus • cytosol • early endosome membrane • vesicle Biological process • endocytosis • protein targeting to membrane • protein transport • negative regulation of protein phosphorylation • negative regulation of leukocyte migration • protein ubiquitination • negative regulation of mast cell activation • negative regulation of mast cell degranulation • negative regulation of Ras protein signal transduction • negative regulation of receptor-mediated endocytosis • negative regulation of inflammatory response • regulation of Fc receptor mediated stimulatory signaling pathway • negative regulation of interleukin-6 secretion • negative regulation of Kit signaling pathway Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	27342	56715
Ensembl	ENSG00000154710	ENSMUSG00000025340
UniProt	Q9UJ41 Q3HKR1	Q9JM13
RefSeq (mRNA)	NM_001287060 NM_001287061 NM_001287062 NM_014504	NM_001199059 NM_019983 NM_001359233 NM_001378873
RefSeq (protein)	NP_001273989 NP_001273990 NP_001273991 NP_055319 NP_001354651 NP_001354652 NP_001354653 NP_001354654 NP_001354655 NP_001354656 NP_001354657 NP_001354658 NP_001354659 NP_001354660 NP_001354661 NP_001354662 NP_001354663 NP_001354664 NP_001354665 NP_001354666 NP_001354667 NP_001354668 NP_001354669 NP_001354670 NP_001354671 NP_001354672 NP_001354673 NP_001354674 NP_001354675 NP_001354676 NP_001354677 NP_001354678 NP_001354679 NP_001354680 NP_001354681 NP_001354682 NP_001354683 NP_001354684 NP_001354685	NP_001185988 NP_064367 NP_001346162 NP_001365802
Location (UCSC)	Chr 7: 66.68 – 66.81 Mb	Chr 5: 130.17 – 130.21 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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].[7]

References

1. GRCh38: Ensembl release 89: ENSG00000154710 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025340 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Mattera R, Arighi CN, Lodge R, Zerial M, Bonifacino JS (Dec 2002). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". EMBO J. 22 (1): 78–88. doi:10.1093/emboj/cdg015. PMC 140067. PMID 12505986.
6. Nimmrich I, Erdmann S, Melchers U, Finke U, Hentsch S, Moyer MP, Hoffmann I, Muller O (Dec 2000). "Seven genes that are differentially transcribed in colorectal tumor cell lines". Cancer Lett. 160 (1): 37–43. doi:10.1016/S0304-3835(00)00553-X. PMID 11098082.
7. "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. 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. doi:10.1091/mbc.12.7.2219. PMC 55678. 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. PMC 139241. PMID 12477932.
• 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.
• 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.
• 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.
• 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.
• 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.