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http://purl.uniprot.org/citations/11439093http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11439093http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11439093http://www.w3.org/2000/01/rdf-schema#comment"A fraction of alpha2-Heremans-Schmid (alpha2-HS) glycoprotein (human fetuin) isolated from plasma was phosphorylated at serine-120 and serine-312 as shown by MS and peptide fragment sequencing after tryptic digestion. Serine-312-containing peptides were phosphorylated to 77% as determined from relative peak heights in the mass spectrum, which together with the phosphorylation of serine-120 implies a molar degree of phosphorylation of at least 1. Approximately 20% of the circulating fetuin plasma pool was phosphorylated to approx. 1 mol of phosphate/mol of protein. The remainder did not contain phosphate, resulting in an average phosphorylation degree for the protein in plasma of approx. 0.2 mol/mol. The isolated alpha2-HS glycoprotein was a heterodimer in which the entire C-terminal part of the connecting peptide including threonine-321 was present, but traces of C-terminally trimmed connecting peptide fragments were also found. The short B-chain was O-glycosylated to approx. 40%, whereas the N-glycosylation of asparagine-138 and asparagine-158 seemed to be 100%. This finding, for the first time, that circulating human plasma fetuin is partly phosphorylated, implies that the effects of phosphorylated alpha2-HS glycoprotein on insulin signal transduction seen in different cell systems could be relevant to its physiological function in vivo."xsd:string
http://purl.uniprot.org/citations/11439093http://purl.org/dc/terms/identifier"doi:10.1042/0264-6021:3570437"xsd:string
http://purl.uniprot.org/citations/11439093http://purl.org/dc/terms/identifier"doi:10.1042/0264-6021:3570437"xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/author"Ek B."xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/author"Ek B."xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/author"Ek P."xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/author"Ek P."xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/author"Haglund A.C."xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/author"Haglund A.C."xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/pages"437-445"xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/pages"437-445"xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/title"Phosphorylation of human plasma alpha2-Heremans-Schmid glycoprotein (human fetuin) in vivo."xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/title"Phosphorylation of human plasma alpha2-Heremans-Schmid glycoprotein (human fetuin) in vivo."xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/volume"357"xsd:string
http://purl.uniprot.org/citations/11439093http://purl.uniprot.org/core/volume"357"xsd:string
http://purl.uniprot.org/citations/11439093http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11439093
http://purl.uniprot.org/citations/11439093http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11439093
http://purl.uniprot.org/citations/11439093http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11439093
http://purl.uniprot.org/citations/11439093http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11439093