Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (By similarity). Plays an important role in the regulation of cell proliferation (PubMed:6474169, PubMed:1352876). 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 PHLPP. Interacts (active GTP-bound form preferentially) with RGS14 (By similarity). Interacts (when farnesylated) with PDE6D; this promotes dissociation from the cell membrane. Interacts with SOS1 (By similarity). Interacts (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. This gene is amplified in the mouse adrenal tumor Y1 cells, and is also directly linked to lung tumor susceptibility. Belongs to the small GTPase superfamily. Ras family.