RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/3301004http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3301004http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3301004http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/3301004http://www.w3.org/2000/01/rdf-schema#comment"The yeast KEX1 gene product has homology to yeast carboxypeptidase Y. A mutant replacing serine at the putative active site of the KEX1 protein abolished activity in vivo. A probable site of processing by the KEX1 product is the C-terminus of the alpha-subunit of killer toxin, where toxin is followed in the precursor by 2 basic residues. Processing involves endoproteolysis following these basic residues and trimming of their C-terminal by a carboxypeptidase. Consistent with the KEX1 product being this carboxypeptidase is its role in alpha-factor pheromone production. In wild-type yeast, KEX1 is not essential for alpha-factor production, as the final pheromone repeat needs no C-terminal processing. However, in a mutant in which alpha-factor production requires a carboxypeptidase, pheromone production is KEX1-dependent."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(87)90030-4"xsd:string
http://purl.uniprot.org/citations/3301004http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(87)90030-4"xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/author"Bussey H."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/author"Bussey H."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/author"Dignard D."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/author"Dignard D."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/author"Dmochowska A."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/author"Dmochowska A."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/author"Thomas D.Y."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/author"Thomas D.Y."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/author"Henning D."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/author"Henning D."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/pages"573-584"xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/pages"573-584"xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/title"Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and alpha-factor precursor processing."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/title"Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and alpha-factor precursor processing."xsd:string
http://purl.uniprot.org/citations/3301004http://purl.uniprot.org/core/volume"50"xsd:string