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Similar findings have been reported for H-Ras, K-Ras, and N-Ras isoforms, which share over 90% sequence identity in their G-domains yet exhibit distinct biochemical properties, including differential interactions with effectors like Raf-RBD and for Rap1A and Rap1B proteins that are regulated by specific GAPs like RapGAP, with profound differences in effector engagement due to hypervariable regions and conformational preferences 56,57,58