Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. GTP + H2O = GDP + H(+) + phosphate Alternates between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP). Forms a signaling complex with RASGRP1 and DGKZ (By similarity). In its GTP-bound form interacts with PLCE1 (PubMed:11179219). Interacts with TBC1D10C (By similarity). Interacts with RGL3 and RASSF5 (By similarity). Interacts with HSPD1 (By similarity). Interacts with PDE6D (By similarity). Interacts with IKZF3 (By similarity). Interacts with RACK1 (By similarity). Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14 (PubMed:19319189). Interacts (active GTP-bound form) with RGS14 (via RBD 1 domain) (PubMed:19319189, PubMed:19878719). Interacts with PIK3CG; the interaction is required for membrane recruitment and beta-gamma G protein dimer-dependent activation of the PI3K gamma complex PIK3CG:PIK3R6 (By similarity). Interacts with RAPGEF2 (By similarity). Interacts (in GTP-bound form) with Oog1 (By similarity). Shuttles between the plasma membrane and the Golgi apparatus (By similarity). The active GTP-bound form is localized most strongly to membranes than the inactive GDP-bound form. Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi. S-nitrosylated; critical for redox regulation. Important for stimulating guanine nucleotide exchange. No structural perturbation on nitrosylation. The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation. Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes. Belongs to the small GTPase superfamily. Ras family. Extended N-terminus. Extended N-terminus.