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http://purl.uniprot.org/citations/9501187http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9501187http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9501187http://www.w3.org/2000/01/rdf-schema#comment"Tyrosine O-sulfation is a common posttranslational modification of proteins in all multicellular organisms. This reaction is mediated by a Golgi enzyme activity called tyrosylprotein sulfotransferase (TPST) that catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate to tyrosine residues within acidic motifs of polypeptides. Tyrosine O-sulfation has been shown to be important in protein-protein interactions in several systems. For example, sulfation of tyrosine residues in the leukocyte adhesion molecule P-selectin glycoprotein ligand 1 (PSGL-1) is required for binding to P-selectin on activated endothelium. In this report we describe the purification of TPST from rat liver microsomes based on its affinity for the N-terminal 15 amino acids of PSGL-1. We have isolated human and mouse TPST cDNAs that predict type II transmembrane proteins of 370 amino acid residues with almost identical primary structure. The human cDNA encodes a fully functional N-glycosylated enzyme with an apparent molecular mass of approximately 54 kDa when expressed in mammalian cells. This enzyme defines a new class of Golgi sulfotransferases that may catalyze tyrosine O-sulfation of PSGL-1 and other protein substrates involved in diverse physiologic functions including inflammation and hemostasis."xsd:string
http://purl.uniprot.org/citations/9501187http://purl.org/dc/terms/identifier"doi:10.1073/pnas.95.6.2896"xsd:string
http://purl.uniprot.org/citations/9501187http://purl.org/dc/terms/identifier"doi:10.1073/pnas.95.6.2896"xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/author"Lane W.S."xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/author"Lane W.S."xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/author"Ouyang Y.-B."xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/author"Ouyang Y.-B."xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/author"Moore K.L."xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/author"Moore K.L."xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/pages"2896-2901"xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/pages"2896-2901"xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/title"Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins."xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/title"Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins."xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/volume"95"xsd:string
http://purl.uniprot.org/citations/9501187http://purl.uniprot.org/core/volume"95"xsd:string
http://purl.uniprot.org/citations/9501187http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9501187
http://purl.uniprot.org/citations/9501187http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9501187
http://purl.uniprot.org/citations/9501187http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9501187
http://purl.uniprot.org/citations/9501187http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9501187