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ras GTPase-Activating Proteinsras Proteinsp120 GTPase Activating ProteinGTPase-Activating ProteinsProto-Oncogene Proteins p21(ras)GTP PhosphohydrolasesNeurofibromin 1Genes, rasProteinsSignal TransductionMolecular Sequence DataAmino Acid SequenceOncogene Protein p21(ras)Guanosine Triphosphaterho GTP-Binding ProteinsMonomeric GTP-Binding Proteinsrab GTP-Binding ProteinsGTP-Binding ProteinsGuanine Nucleotide Exchange FactorsGuanosine Diphosphaterac1 GTP-Binding Proteinrac GTP-Binding ProteinsrhoA GTP-Binding ProteinDynaminsras Guanine Nucleotide Exchange Factorsrap GTP-Binding ProteinsMutationProto-Oncogene Proteins c-rafran GTP-Binding Proteinral GTP-Binding ProteinsEnzyme Activationrap1 GTP-Binding ProteinsGTP Phosphohydrolase-Linked Elongation FactorsProtein BindingDynamin IProtein Structure, TertiaryADP-Ribosylation FactorsCell LineProtein TransportRecombinant Fusion Proteinsrab1 GTP-Binding Proteinsral Guanine Nucleotide Exchange FactorActinsProtein-Serine-Threonine Kinasesras-GRF13T3 CellsGuanine Nucleotide Dissociation InhibitorsHydrolysisTransfectionPhosphorylationCell Transformation, NeoplasticDynamin IICell MembraneRGS ProteinsCytoskeletoncdc42 GTP-Binding Protein, Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSaccharomyces cerevisiaeMembrane ProteinsProto-Oncogene Proteins
RasGAPSYNapticKinaseGeneCharacterizationImportantSmallActivity
RasGAP1
  • A mouse homologue of the Drosophila tumor suppressor l(2)tid gene defines a novel Ras GTPase-activating protein (RasGAP)-binding protein. (embl.de)
SYNaptic3
  • SYNGAP1 is a gene that encodes the cytosolic protein SYNGAP1 ( SYNaptic GTPase Activating Protein ), an essential component of the postsynaptic density at excitatory glutamatergic neurons . (nih.gov)
  • The brain-specific synaptic guanosine triphosphatase (GTPase)-activating protein (SynGAP) is important in synaptic plasticity. (nih.gov)
  • Structural overview and comparative kinetic analysis of synaptic guanosine triphosphatase-activating proteins. (nih.gov)
Kinase3
  • It is known that the human Ras GTPase activating protein (GAP) p120-GAP can be phosphorylated by different members of the Src kinase family and recently phosphorylation of the GDP/GTP exchange factor (GEF) CDC25Mm/GRF1 by proteins of the Src kinase family has been revealed in vivo [Kiyono, M., Kaziro, Y. & Satoh, T. (2000) J. Biol. (embl.de)
  • In addition to its association with Ras, GAP has been shown to bind to several tyrosine-phosphorylated proteins in cells stimulated by growth factors or expressing transforming tyrosine kinase variants. (embl.de)
  • KRAS binds tightly to RAF kinase in vitro , but activates RAF kinase only at the plasma membrane in vivo . (nih.gov)
Gene1
  • Here we report the cloning and characterization of a novel GAP-binding protein, mTid-1, a DnaJ chaperone protein that represents the murine homolog of the Drosophila tumor suppressor l(2)tid gene. (embl.de)
Characterization1
  • Progress in the characterization of processed full length KRAS4B and its interaction with cellular membranes stands as a highlight of the RAS Initiative to date. (nih.gov)
Important1
  • Thus, it is important to understand the mechanics of RAS-membrane interaction not only to clarify RAS signal transduction, but also to facilitate future drug discovery efforts directed against RAS itself. (nih.gov)
Small3
  • It shows dual specificity for the small guanine nucleotide-binding proteins Rap and Ras. (nih.gov)
  • All known oncogenic mutants of Ras map to a small subset of amino acids. (embl.de)
  • Project 1 aimed to determine which effectors are engaged by each of the mutant proteins, solve the structures of mutant RAS proteins complexed with relevant effectors, and identify new opportunities for small-molecule therapeutics. (nih.gov)
Activity5
  • In contrast to the isolated GAP domain, which does not show any detectable RapGAP activity, a fragment comprising the C2 and GAP domains (C2-GAP) stimulates the intrinsic GTPase reaction of Rap by approximately 1 x 10(4). (nih.gov)
  • Despite its obvious importance for carcinogenesis, the role of Gln-61 in the GAP-stimulated GTPase activity of Ras has remained a mystery. (embl.de)
  • As it still remains unclear how these phosphorylations can influence the Ras pathway we have analyzed the ability of p60c-Src and Lck to phosphorylate these two Ras regulators and have compared the activity of the phosphorylated and unphosphorylated forms. (embl.de)
  • The phosphorylation of p120-GAP by p60c-Src inhibited its ability to stimulate the Ha-Ras-GTPase activity, whereas phosphorylation by Lck did not display any effect. (embl.de)
  • Our results suggest that phosphorylation by p60c-Src and Lck is a selective process that can modulate the activity of p120-GAP and CDC25Mm towards Ras proteins. (embl.de)