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http://purl.uniprot.org/citations/11027579http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11027579http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11027579http://www.w3.org/2000/01/rdf-schema#comment"We report here molecular cloning and expression analysis of the gene for a novel human brain link protein-1 (BRAL1) which is predominantly expressed in brain. The predicted open reading frame of human brain link protein-1 encoded a polypeptide of 340 amino acids containing three protein modules, the immunoglobulin-like fold and proteoglycan tandem repeat 1 and 2 domains, with an estimated mass of 38 kDa. The brain link protein-1 mRNA was exclusively present in brain. When analyzed during mouse development, it was detected solely in the adult brain. Concomitant expression pattern of mRNAs for brain link protein-1 and various lectican proteoglycans in brain suggests a possibility that brain link protein-1 functions to stabilize the binding between hyaluronan and brevican. The human BRAL1 gene contained 7 exons and spanned approximately 6 kb. The entire immunoglobulin-like fold was encoded by a single exon and the proteoglycan tandem repeat 1 and 2 domains were encoded by a single and two exons, respectively. The deduced amino acid sequence of human brain link protein-1 exhibited 45% identity with human cartilage link protein-1 (CRTL1), previously reported as link protein to stabilize aggregates of aggrecan and hyaluronan in cartilage. These results suggest that brain link protein-1 may have distinct function from cartilage link protein-1 and play specific roles, especially in the adult brain."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.2000.3583"xsd:string
http://purl.uniprot.org/citations/11027579http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.2000.3583"xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Murakami T."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Murakami T."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Yoshioka H."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Yoshioka H."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Ninomiya Y."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Ninomiya Y."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Oohashi T."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Oohashi T."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Arata J."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Arata J."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Hirakawa S."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Hirakawa S."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Su W.-D."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/author"Su W.-D."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/pages"982-989"xsd:string
http://purl.uniprot.org/citations/11027579http://purl.uniprot.org/core/pages"982-989"xsd:string