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http://purl.uniprot.org/citations/10559187http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10559187http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10559187http://www.w3.org/2000/01/rdf-schema#comment"Monomeric GTPases of the Ras superfamily have a very slow intrinsic GTPase activity which is accelerated by specific GTPase-activating proteins. In contrast to Ras- and Rho-specific GTPase-activating proteins (GAPs) that have been studied in great detail, little is known about the functioning of GAPs specific for Ypt/Rab transport GTPases. We have identified two novel Ypt/Rab-GAPs because of their sequence relatedness to the three known GAPs Gyp1p, Gyp6p, and Gyp7p. Mdr1/Gyp2p is an efficient GAP for Ypt6p and Sec4p, whereas Msb3/Gyp3p is a potent GAP for Sec4p, Ypt6p, Ypt51p, Ypt31/Ypt32p, and Ypt1p. Although the affinity of Msb3/Gyp3p for its preferred substrate Sec4p is low (K(m) = 154 microM), it accelerates the intrinsic GTPase activity of Sec4p 5 x 10(5)-fold. Msb3/Gyp3p appears to be functionally linked to Cdc42p-regulated pathway(s). The results demonstrate that in yeast there is a large family of Ypt/Rab-GAPs, members of which discriminate poorly between GTPases involved in regulating different steps of exo- and endocytic transport routes."xsd:string
http://purl.uniprot.org/citations/10559187http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.47.33186"xsd:string
http://purl.uniprot.org/citations/10559187http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.47.33186"xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/author"Gallwitz D."xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/author"Gallwitz D."xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/author"Albert S."xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/author"Albert S."xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/pages"33186-33189"xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/pages"33186-33189"xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/title"Two new members of a family of Ypt/Rab GTPase activating proteins. Promiscuity of substrate recognition."xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/title"Two new members of a family of Ypt/Rab GTPase activating proteins. Promiscuity of substrate recognition."xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10559187http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/10559187http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10559187
http://purl.uniprot.org/citations/10559187http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10559187
http://purl.uniprot.org/citations/10559187http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10559187
http://purl.uniprot.org/citations/10559187http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10559187
http://purl.uniprot.org/uniprot/P38555http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10559187
http://purl.uniprot.org/uniprot/P36017http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10559187