Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (By similarity). Plays an important role in the regulation of cell proliferation (PubMed:3110778). Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner (By similarity). 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). Interaction with SOS1 promotes exchange of bound GDP by GTP. Interacts with SOS1 (By similarity). Interacts (when farnesylated) with PDE6D; this promotes dissociation from the cell membrane (By similarity). Interacts with PHLPP. Interacts (active GTP-bound form preferentially) with RGS14. Interacts with (when farnesylated) with GPR31 (By similarity). Interacts with RAP1GDS1 (By similarity). Interacts (when farnesylated) with GPR31. Isoforms differ in the C-terminal region which is encoded by two alternative exons (IVA and IVB). 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. Palmitoylated at Lys-182, Lys-184 and Lys-185. Lysine-depalmitoylation by SIRT2 promotes its localization to endomembranes in endocytic pathways. Belongs to the small GTPase superfamily. Ras family.