RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/24311690http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24311690http://www.w3.org/2000/01/rdf-schema#comment"Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT). We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc. The conformation is similar to that of a glycosylation-competent peptide substrate. Cleavage occurs between cysteine and glutamate residues and results in a pyroglutamate product. Conversion of the cleavage site glutamate into serine converts an HCF-1 proteolytic repeat into a glycosylation substrate. Thus, protein glycosylation and HCF-1 cleavage occur in the same active site."xsd:string
http://purl.uniprot.org/citations/24311690http://purl.org/dc/terms/identifier"doi:10.1126/science.1243990"xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/author"Jiang J."xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/author"Walker S."xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/author"Herr W."xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/author"Vocadlo D.J."xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/author"Lazarus M.B."xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/author"Zandberg W.F."xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/author"Bhuiyan T."xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/author"Kapuria V."xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/author"Janetzko J."xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/pages"1235-1239"xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/title"HCF-1 is cleaved in the active site of O-GlcNAc transferase."xsd:string
http://purl.uniprot.org/citations/24311690http://purl.uniprot.org/core/volume"342"xsd:string
http://purl.uniprot.org/citations/24311690http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24311690
http://purl.uniprot.org/citations/24311690http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24311690
http://purl.uniprot.org/uniprot/#_A0A223PQH6-mappedCitation-24311690http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24311690
http://purl.uniprot.org/uniprot/#_O15294-mappedCitation-24311690http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24311690
http://purl.uniprot.org/uniprot/#_Q05C05-mappedCitation-24311690http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24311690
http://purl.uniprot.org/uniprot/#_P51610-mappedCitation-24311690http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24311690
http://purl.uniprot.org/uniprot/A0A223PQH6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24311690
http://purl.uniprot.org/uniprot/P51610http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/24311690