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http://purl.uniprot.org/citations/10635561http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10635561http://www.w3.org/2000/01/rdf-schema#comment"Saccharomyces cerevisiae Mnn9 protein is a type II Golgi membrane protein which concerns in protein mannosylation. When solubilized by Triton X-100, it was recovered in two distinct complexes both having mannosyltransferase activity; one with Van1 protein (V-complex) and the other with Anp1, Hoc1, Mnn10, and Mnn11 proteins (A-complex). Characterization of the null mutants suggested that A-complex is also concerned in protein O-glycosylation. A-complex was more resistant than V-complex to dissociating conditions. Interaction between the lumenal domains of Van1 and Mnn9 was detected by a two-hybrid experiment. The anchor domain of Mnn9 protein could be replaced with other membrane anchors without losing the ability to form complexes similar to V- and A-complexes. Thus the lumenal domains are important to assemble these distinct complexes."xsd:string
http://purl.uniprot.org/citations/10635561http://purl.org/dc/terms/identifier"doi:10.1271/bbb.63.1970"xsd:string
http://purl.uniprot.org/citations/10635561http://purl.uniprot.org/core/author"Kojima H."xsd:string
http://purl.uniprot.org/citations/10635561http://purl.uniprot.org/core/author"Hashimoto H."xsd:string
http://purl.uniprot.org/citations/10635561http://purl.uniprot.org/core/author"Yoda K."xsd:string
http://purl.uniprot.org/citations/10635561http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10635561http://purl.uniprot.org/core/name"Biosci Biotechnol Biochem"xsd:string
http://purl.uniprot.org/citations/10635561http://purl.uniprot.org/core/pages"1970-1976"xsd:string
http://purl.uniprot.org/citations/10635561http://purl.uniprot.org/core/title"Interaction among the subunits of Golgi membrane mannosyltransferase complexes of the yeast Saccharomyces cerevisiae."xsd:string
http://purl.uniprot.org/citations/10635561http://purl.uniprot.org/core/volume"63"xsd:string
http://purl.uniprot.org/citations/10635561http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10635561
http://purl.uniprot.org/citations/10635561http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10635561
http://purl.uniprot.org/uniprot/P46985#attribution-254336FD94416AF172991A55151C2A76http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10635561
http://purl.uniprot.org/uniprot/#_P39107-mappedCitation-10635561http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10635561
http://purl.uniprot.org/uniprot/#_P50108-mappedCitation-10635561http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10635561
http://purl.uniprot.org/uniprot/#_P46985-mappedCitation-10635561http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10635561
http://purl.uniprot.org/uniprot/#_P47124-mappedCitation-10635561http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10635561
http://purl.uniprot.org/uniprot/#_P23642-mappedCitation-10635561http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10635561
http://purl.uniprot.org/uniprot/#_P32629-mappedCitation-10635561http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10635561
http://purl.uniprot.org/uniprot/P23642http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10635561
http://purl.uniprot.org/uniprot/P39107http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10635561
http://purl.uniprot.org/uniprot/P50108http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10635561
http://purl.uniprot.org/uniprot/P47124http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10635561
http://purl.uniprot.org/uniprot/P46985http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10635561