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http://purl.uniprot.org/citations/16778074http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16778074http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16778074http://www.w3.org/2000/01/rdf-schema#comment"The transcription factor Stp1 is endoproteolytically processed in response to extracellular amino acids by the plasma membrane SPS (Ssy1-Ptr3-Ssy5)-sensor. Processed Stp1, lacking a cytoplasmic retention motif, enters the nucleus and induces amino acid transporter gene expression. The SPS-sensor component Ssy5 is a chymotrypsin-like protease with a Pro-domain and a catalytic domain. The Pro-domain, required for protease maturation, is autolytically cleaved from the catalytic domain but remains associated, forming an inactive protease complex that binds Stp1. Stp1 is processed only after amino acid-induced signals cause the dissociation of the inhibitory Pro-domain. Our findings demonstrate that gene expression can be controlled by regulating the enzymatic activity of an intracellular endoprotease."xsd:string
http://purl.uniprot.org/citations/16778074http://purl.org/dc/terms/identifier"doi:10.1101/gad.374206"xsd:string
http://purl.uniprot.org/citations/16778074http://purl.org/dc/terms/identifier"doi:10.1101/gad.374206"xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/author"Ljungdahl P.O."xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/author"Ljungdahl P.O."xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/author"Andreasson C."xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/author"Andreasson C."xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/author"Heessen S."xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/author"Heessen S."xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/pages"1563-1568"xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/pages"1563-1568"xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/title"Regulation of transcription factor latency by receptor-activated proteolysis."xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/title"Regulation of transcription factor latency by receptor-activated proteolysis."xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/16778074http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/16778074http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16778074
http://purl.uniprot.org/citations/16778074http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16778074
http://purl.uniprot.org/citations/16778074http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16778074
http://purl.uniprot.org/citations/16778074http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16778074