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src Homology DomainsGRB2 Adaptor ProteinSequence Homology, Amino AcidGRB10 Adaptor ProteinMolecular Sequence DataAmino Acid SequenceGRB7 Adaptor ProteinProtein BindingAdaptor Proteins, Signal TransducingRecombinant Fusion ProteinsBinding Sitescdc42 GTP-Binding ProteinCloning, MolecularBase SequencePhosphoproteinsPhosphorylationSequence Alignmentcdc25 PhosphatasesSequence Homology, Nucleic AcidProtein Structure, TertiarySignal TransductionRecombinant Proteinssrc-Family KinasesTyrosineCDC2 Protein KinaseAmino Acid MotifsCarrier ProteinsProtein-Tyrosine KinasesCell LineProtein Interaction Domains and MotifsProtein ConformationTransfectionMutagenesis, Site-DirectedModels, MolecularProtein Tyrosine Phosphatase, Non-Receptor Type 11DNA, ComplementaryBlood ProteinsProtein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesMembrane ProteinsIntracellular Signaling Peptides and ProteinsProtein Structure, SecondaryMutationProteinsPhosphotyrosineCdc20 ProteinsEnzyme ActivationDNA-Binding ProteinsTwo-Hybrid System TechniquesStructure-Activity RelationshipStructural Homology, ProteinGuanine Nucleotide Exchange FactorsProto-Oncogene ProteinsSequence HomologyConserved SequencePhosphatidylinositol PhosphatesCrystallography, X-RayCell MembraneCOS CellsGlutathione TransferaseProto-Oncogene Proteins pp60(c-src)3T3 CellsSequence DeletionPhospholipase C deltaAdaptor Proteins, Vesicular TransportPeptide FragmentsEscherichia coliPrecipitin TestsDimerizationSH2 Domain-Containing Protein Tyrosine PhosphatasesDNA PrimersTranscription FactorsDNAKineticsPlasmidsSaccharomyces cerevisiaeNuclear ProteinsProtein TransportMutagenesisHeLa CellsProlinePhospholipase C gammaLigandsShc Signaling Adaptor ProteinsCell Cycle ProteinsMicrofilament ProteinsBacterial ProteinsAmino Acid SubstitutionGTPase-Activating ProteinsPeptidesPhosphatidylinositol 3-KinasesCells, CulturedTranscription, GeneticActinsDynaminsPhosphatidylinositol 4,5-DiphosphateRNA, MessengerPoint MutationModels, BiologicalType C Phospholipases
Catalytic domainCDC24AdaptorKinaseTyrosineProteinsStructuralYeastMotifSequenceCells
Catalytic domain2
  • A main feature of the catalytic domain is the protrusion of a helical hairpin important for the nucleotide-exchange mechanism. (embl.de)
  • This entry represents the catalytic domain of the Ras guanine-nucleotide exchange factors. (embl.de)
CDC243
  • It has also been identified in several other protein families such as: PI3 Kinase, Ras GTPase-activating protein, CDC24 and cdc25. (wikipedia.org)
  • Signal transducing adaptor proteins CDC24 Cdc25 PI3 kinase Phospholipase Ras GTPase-activating protein Vav proto-oncogene GRB2 p54 S6 kinase 2 (S6K2) SH3D21 ARMH3 (potentially) STAC3 Some myosins SH3 and multiple ankyrin repeat domains: SHANK1, SHANK2, SHANK3 YAP1 ARHGAP12 vexin (VXN) TANGO1 Integrase Focal Adhesion Kinase (FAK, PTK2) Proline-rich tyrosine kinase (Pyk2, CADTK, PTK2beta) TRIP10 (cip4) Src homology 2 domain-containing Structural domain Pawson T, Schlessingert J (July 1993). (wikipedia.org)
  • This protein possesses both a domain belonging to the CDC25 family and one belonging to the CDC24 family. (embl.de)
Adaptor1
Kinase2
  • SH3 domains are found in proteins of signaling pathways regulating the cytoskeleton, the Ras protein, and the Src kinase and many others. (wikipedia.org)
  • Ras-mediated activation of DH-PH-Sos did not require activation of mitogen-activated protein kinase but it was dependent on activation of phosphoinositide 3-kinase. (embl.de)
Tyrosine1
  • This domain is also present in the molecules of phospholipase and several cytoplasmic tyrosine kinases such as Abl and Src. (wikipedia.org)
Proteins10
  • Approximately 300 SH3 domains are found in proteins encoded in the human genome. (wikipedia.org)
  • In addition to that, the SH3 domain was responsible for controlling protein-protein interactions in the signal transduction pathways and regulating the interactions of proteins involved in the cytoplasmic signaling. (wikipedia.org)
  • The classical SH3 domain is usually found in proteins that interact with other proteins and mediate assembly of specific protein complexes, typically via binding to proline-rich peptides in their respective binding partner. (wikipedia.org)
  • Classical SH3 domains are restricted in humans to intracellular proteins, although the small human MIA family of extracellular proteins also contain a domain with an SH3-like fold. (wikipedia.org)
  • Many SH3-binding epitopes of proteins have a consensus sequence that can be represented as a regular expression or Short linear motif: -X-P-p-X-P- 1 2 3 4 5 with 1 and 4 being aliphatic amino acids, 2 and 5 always and 3 sometimes being proline. (wikipedia.org)
  • There are 18332 RasGEF domains in 18317 proteins in SMART's nrdb database. (embl.de)
  • Taxonomic distribution of proteins containing RasGEF domain. (embl.de)
  • The complete taxonomic breakdown of all proteins with RasGEF domain is also avaliable . (embl.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing RasGEF domain in the selected taxonomic class. (embl.de)
  • Efficient cellular transformation by the Met oncoprotein requires a functional Grb2 binding site and correlates with phosphorylation of the Grb2-associated proteins, Cbl and Gab1. (wikidata.org)
Structural1
  • The structure consists of two distinct alpha helical structural domains: the N-terminal domain which seems to have a purely structural role and the C-terminal domain which is sufficient for catalytic activity and contains all residues that interact with Ras. (embl.de)
Yeast2
  • Nevertheless, orthologous SH3 domain-mediated interactions are highly rewired between worm and yeast. (wikipedia.org)
  • Cdc25 from yeast. (embl.de)
Motif1
  • More recently, SH3 domains that bind to a core consensus motif R-x-x-K have been described. (wikipedia.org)
Sequence1
  • The sequence binds to the hydrophobic pocket of the SH3 domain. (wikipedia.org)
Cells1
  • In COS-1 cells, the DH domain of Sos stimulated guanine nucleotide exchange on Rac but not Cdc42 in vitro and in vivo. (embl.de)