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http://purl.uniprot.org/citations/22250200http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22250200http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22250200http://www.w3.org/2000/01/rdf-schema#comment"Membrane contact sites (MCSs), where the membranes of two organelles are closely apposed, are regions where small molecules such as lipids or calcium are exchanged between organelles. We have identified a conserved membrane-binding domain found exclusively in proteins at MCSs in Saccharomyces cerevisiae. The synaptotagmin-like-mitochondrial-lipid binding protein (SMP) domain is conserved across species. We show that all seven proteins that contain this domain in yeast localize to one of three MCSs. Human proteins with SMP domains also localize to MCSs when expressed in yeast. The SMP domain binds membranes and is necessary for protein targeting to MCSs. Proteins containing this domain could be involved in lipid metabolism. This is the first protein domain found exclusively in proteins at MCSs."xsd:string
http://purl.uniprot.org/citations/22250200http://purl.org/dc/terms/identifier"doi:10.1242/jcs.085118"xsd:string
http://purl.uniprot.org/citations/22250200http://purl.org/dc/terms/identifier"doi:10.1242/jcs.085118"xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/author"Prinz W.A."xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/author"Prinz W.A."xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/author"Toulmay A."xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/author"Toulmay A."xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/name"J. Cell Sci."xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/pages"49-58"xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/pages"49-58"xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/title"A conserved membrane-binding domain targets proteins to organelle contact sites."xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/title"A conserved membrane-binding domain targets proteins to organelle contact sites."xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/volume"125"xsd:string
http://purl.uniprot.org/citations/22250200http://purl.uniprot.org/core/volume"125"xsd:string
http://purl.uniprot.org/citations/22250200http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22250200
http://purl.uniprot.org/citations/22250200http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22250200
http://purl.uniprot.org/citations/22250200http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22250200
http://purl.uniprot.org/citations/22250200http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22250200
http://purl.uniprot.org/uniprot/Q8IWB9http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/22250200
http://purl.uniprot.org/uniprot/Q12466http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/22250200