Description
Product Characteristics:
The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
Subcellular location: Cytoplasm
Synonyms: GAP phospho Y460, p-GAP phospho Y460, Ras GAP, CM AVM, CMAVM, DKFZp434N071, GAP, GTPase activating protein, GTPase-activating protein, OTTHUMP00000222390, OTTHUMP00000222391, OTTHUMP00000222392, OTTHUMP00000222393, p120GAP, p120RASGAP, PKWS, Ras GTPase-activating protein 1, RAS p21 protein activator GTPase activating protein 1, Ras p21 protein activator, RASA, RASA1, RASA1_HUMAN, RasGAP, Triphosphatase activating protein.
Target Information: The protein encoded by this gene is located in the cytoplasm and is part of the GAP1 family of GTPase-activating proteins. The gene product stimulates the GTPase activity of normal RAS p21 but not its oncogenic counterpart. Acting as a suppressor of RAS function, the protein enhances the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, thereby allowing control of cellular proliferation and differentiation. Mutations leading to changes in the binding sites of either protein are associated with basal cell carcinomas. Mutations also have been associated with hereditary capillary malformations (CM) with or without arteriovenous malformations (AVM) and Parkes Weber syndrome. Alternative splicing results in two isoforms where the shorter isoform, lacking the N-terminal hydrophobic region but retaining the same activity, appears to be abundantly expressed in placental but not adult tissues. [provided by RefSeq, May 2012]