Multifuntional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells. Plays a role in the late stages of cytokinesis and is required for the abscission of the bridge joining the sister cells emerging from mitosis. Required for suppression of apoptosis. Interacts with EXOC2 and EXOC8. Interacts with RALBP1 via its effector domain. Alternate 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). Belongs to the small GTPase superfamily. Ras family. Note: This description may include information from UniProtKB.
Protein type: G protein, monomeric, Ras; G protein, monomeric; G protein
Molecular Function: GTPase activity; protein binding; GDP binding; GTP binding; ubiquitin protein ligase binding; ATPase binding
Biological Process: regulation of exocyst localization; nerve growth factor receptor signaling pathway; positive regulation of protein binding; apoptosis; metabolic process; regulation of exocyst assembly; Ras protein signal transduction; cytokinesis; positive regulation of protein amino acid phosphorylation; cellular response to starvation; signal transduction; negative regulation of protein binding
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.