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http://purl.uniprot.org/citations/8288572http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8288572http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8288572http://www.w3.org/2000/01/rdf-schema#comment"GTPase-activating proteins or GAPs play an important role in signal transduction pathways regulated by GTP-binding proteins. In addition to acting as down-regulators of GTPases, there is growing evidence that they also act as effector molecules required for downstream signaling. PLC-beta 1, the target protein regulated by the heterotrimeric GTPase Gq, has been shown to be a GAP, whereas rasGAP, a down-regulator of the small GTPase ras, may be required for the ras-mediated signals. We have purified a GAP specific for the rho subfamily of small GTPases. Partial sequence analysis of rhoGAP has led to the identification of a family of related proteins which now includes bcr, chimaerin, p190, p85, and 3BP-1. We report here the isolation of a cDNA clone encoding human rhoGAP and the expression of recombinant protein. The full-length protein is 50 kDa and is ubiquitously expressed in mammalian cells. At least three members of the rho family are substrates for rhoGAP, rho, rac, and G25K/CDC42, and they each bind equally well to the protein. In vitro GTPase assays, however, reveal that G25K/CDC42 is the preferred substrate. RhoGAP contains a proline-rich sequence, suggesting that it is an SH3-binding protein."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)42232-0"xsd:string
http://purl.uniprot.org/citations/8288572http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(17)42232-0"xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"Hall A."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"Hall A."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"Brill S."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"Brill S."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"van Erp H.E."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"van Erp H.E."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"Lancaster C.A."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"Lancaster C.A."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"Self A.J."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"Self A.J."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"Taylor-Harris P.M."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/author"Taylor-Harris P.M."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/pages"1137-1142"xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/pages"1137-1142"xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/title"Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases."xsd:string
http://purl.uniprot.org/citations/8288572http://purl.uniprot.org/core/title"Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases."xsd:string