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http://purl.uniprot.org/citations/25811241http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25811241http://www.w3.org/2000/01/rdf-schema#comment"FAM20C is a secretory kinase responsible for the phosphorylation of multiple secreted proteins in mammalian cells; it has been shown to phosphorylate serine residues within a variety of different bone proteins. In this work we demonstrate that FAM20C also phosphorylates threonines, specifically those within the N-terminal domain of the neuroendocrine chaperone 7B2. Analysis of the primary sequence of 7B2 revealed that three threonine residues in its N-terminal domain are located within FAM20C consensus motifs: Thr73, Thr99, and Thr111. The individual substitution of Thr73 and Thr111 residues by neutral alanines caused a marked decrease in the total phosphorylation of 7B2. Furthermore, the phosphomimetic substitution of Thr111 by Glu clearly diminished the ability of 7B2 to activate pro-prohormone convertase 2 (PC2) in 7B2-lacking SK-N-MC neuroblastoma cells, suggesting that the phosphorylation of this residue critically impacts the 7B2-proPC2 interaction. However, the phosphomimetic mutation did not alter 7B2's ability to function as an antiaggregant for human islet amyloid polypeptide. FAM20C-mediated phosphorylation of a common alternatively spliced variant of human 7B2 that lacks Ala100 (thus eliminating the Thr99 phosphorylation consensus site) was similar to the Ala-containing protein, but this variant did not activate proPC2 as efficiently as the Ala-containing protein. Although threonines within 7B2 were phosphorylated efficiently, FAM20C was incapable of performing the well-known regulatory threonine phosphorylation of the molecular chaperone binding immunoglobulin protein. Taken together, these results indicate that FAM20C plays a role in 7B2-mediated proPC2 activation by phosphorylating residue Thr111; and that 7B2 function is regulated by alternative splicing."xsd:string
http://purl.uniprot.org/citations/25811241http://purl.org/dc/terms/identifier"doi:10.1210/me.2014-1394"xsd:string
http://purl.uniprot.org/citations/25811241http://purl.uniprot.org/core/author"Lindberg I."xsd:string
http://purl.uniprot.org/citations/25811241http://purl.uniprot.org/core/author"Ramos-Molina B."xsd:string
http://purl.uniprot.org/citations/25811241http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/25811241http://purl.uniprot.org/core/name"Mol Endocrinol"xsd:string
http://purl.uniprot.org/citations/25811241http://purl.uniprot.org/core/pages"756-764"xsd:string
http://purl.uniprot.org/citations/25811241http://purl.uniprot.org/core/title"Phosphorylation and Alternative Splicing of 7B2 Reduce Prohormone Convertase 2 Activation."xsd:string
http://purl.uniprot.org/citations/25811241http://purl.uniprot.org/core/volume"29"xsd:string
http://purl.uniprot.org/citations/25811241http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25811241
http://purl.uniprot.org/citations/25811241http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25811241
http://purl.uniprot.org/uniprot/#_P16519-mappedCitation-25811241http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25811241
http://purl.uniprot.org/uniprot/#_P05408-mappedCitation-25811241http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25811241
http://purl.uniprot.org/uniprot/#_Q9UM69-mappedCitation-25811241http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25811241
http://purl.uniprot.org/uniprot/P16519http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25811241
http://purl.uniprot.org/uniprot/P05408http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25811241
http://purl.uniprot.org/uniprot/Q9UM69http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25811241