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http://purl.uniprot.org/citations/10753916http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10753916http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10753916http://www.w3.org/2000/01/rdf-schema#comment"Core 2 O-glycan branching catalyzed by UDP-N-acetyl-alpha-D-glucosamine: acceptor beta1, 6-N-acetylglucosaminyltransferases (beta6GlcNAc-Ts) is an important step in mucin-type biosynthesis. Core 2 complex-type O-glycans are involved in selectin-mediated adhesion events, and O-glycan branching appears to be highly regulated. Two homologous beta6GlcNAc-Ts functioning in O-glycan branching have previously been characterized, and here we report a third homologous beta6GlcNAc-T designated C2GnT3. C2GnT3 was identified by BLAST analysis of human genome survey sequences. The catalytic activity of C2GnT3 was evaluated by in vitro analysis of a secreted form of the protein expressed in insect cells. The results revealed exclusive core 2 beta6GlcNAc-T activity. The product formed with core 1-para-nitrophenyl was confirmed by (1)H NMR to be core 2-para-nitrophenyl. In vivo analysis of the function of C2GnT3 by coexpression of leukosialin (CD43) and a full coding construct of C2GnT3 in Chinese hamster ovary cells confirmed the core 2 activity and failed to reveal I activity. The C2GnT3 gene was located to 5q12, and the coding region was contained in a single exon. Northern analysis revealed selectively high levels of a 5.5-kilobase C2GnT3 transcript in thymus with only low levels in other organs. The unique expression pattern of C2GnT3 suggests that this enzyme serves a specific function different from other members of the beta6GlcNAc-T gene family."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.15.11106"xsd:string
http://purl.uniprot.org/citations/10753916http://purl.org/dc/terms/identifier"doi:10.1074/jbc.275.15.11106"xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Fukuda M."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Fukuda M."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Clausen H."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Clausen H."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Levery S.B."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Levery S.B."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Yeh J.-C."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Yeh J.-C."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Merkx G."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Merkx G."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"van Kessel A.G."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"van Kessel A.G."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Schwientek T."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Schwientek T."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Keck B."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/author"Keck B."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10753916http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string