http://purl.uniprot.org/citations/28351617 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/28351617 | http://www.w3.org/2000/01/rdf-schema#comment | "N-glycosylation of proteins is important for protein folding and function. We have recently reported that FAM5C/BRINP3 contributes to the tumor necrosis factor-α-induced expression of leukocyte adhesion molecules in vascular endothelial cells (ECs). However, regulatory mechanism of the FAM5C biosynthesis is poorly understood. Co-immunoprecipitation assay revealed the interaction of FAM5C with UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), a glycoprotein folding-sensor enzyme. FAM5C ectopically expressed in HEK293 cells was localized to the endoplasmic reticulum and co-localized with endogenously expressed UGGT1. Molecular size of FAM5C was reduced by treatment with N-glycosidase F and in FAM5C-expressing cells cultured in the presence of the N-glycosylation inhibitor tunicamycin. FAM5C was secreted by the cells and the secretion of FAM5C was blocked by tunicamycin. Among six potential N-glycosylation sites, the potential site at Asn168 was not N-glycosylated, and Asn337, Asn456, Asn562, Asn609, and Asn641 mutants were poorly secreted by the cells. These results demonstrated that FAM5C is an N-glycosylated protein and N-glycosylation is necessary for the secretion of FAM5C."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2017.03.133"xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/author | "Kobayashi M."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/author | "Fujita H."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/author | "Sasaki N."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/author | "Hirata K.I."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/author | "Satomi-Kobayashi S."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/author | "Matsuoka I."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/author | "Sato J."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/author | "Terao Y."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/author | "Minami S."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/author | "Rikitake Y."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/author | "Horibe S."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/pages | "811-816"xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/title | "Interaction of FAM5C with UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1): Implication of N-glycosylation in FAM5C secretion."xsd:string |
http://purl.uniprot.org/citations/28351617 | http://purl.uniprot.org/core/volume | "486"xsd:string |
http://purl.uniprot.org/citations/28351617 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/28351617 |
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