Based on sequence homology, mammalian Gapex-5 has been shown to have an amino-terminal Ras GAP domain, a central polyproline (SH3 binding) region and a carboxy-terminal Rab GEF domain. The RabGEF domain has been suggested to activate Rab5[6] and Rab31.[7]
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↑Kitano M, Nakaya M, Nakamura T, Nagata S, Matsuda M (May 2008). "Imaging of Rab5 activity identifies essential regulators for phagosome maturation". Nature. 453 (7192): 241–5. doi:10.1038/nature06857. PMID18385674.
↑Su X, Kong C, Stahl PD (July 2007). "GAPex-5 mediates ubiquitination, trafficking, and degradation of epidermal growth factor receptor". J. Biol. Chem. 282 (29): 21278–84. doi:10.1074/jbc.M703725200. PMID17545148.
Su X, Kong C, Stahl PD (2007). "GAPex-5 mediates ubiquitination, trafficking, and degradation of epidermal growth factor receptor". J. Biol. Chem. 282 (29): 21278–84. doi:10.1074/jbc.M703725200. PMID17545148.
Hunker CM, Galvis A, Kruk I, et al. (2006). "Rab5-activating protein 6, a novel endosomal protein with a role in endocytosis". Biochem. Biophys. Res. Commun. 340 (3): 967–75. doi:10.1016/j.bbrc.2005.12.099. PMID16410077.
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. PMID15324660.
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. PMID14702039.
Nagase T, Kikuno R, Ishikawa K, et al. (2000). "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (2): 143–50. doi:10.1093/dnares/7.2.143. PMID10819331.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID8889548.