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http://purl.uniprot.org/citations/8223692http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8223692http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8223692http://www.w3.org/2000/01/rdf-schema#comment"Overlapping cDNAs encoding the entire human ERGIC-53, a 53 kDa membrane protein of the ER-Golgi intermediate compartment, have been isolated and their nucleotide sequence determined. The isolated cDNA is about 2.7 kb in length. The deduced polypeptide chain for ERGIC-53 consists of 510 amino acids (M(r) 54217) including an N-terminal signal sequence of 30 amino acids, a single putative transmembrane segment of 18 amino acids, and a short cytoplasmic domain of 12 amino acids. Surprisingly, the cytoplasmic segment contains two lysines positioned three and four residues from the C-terminus. Such a double lysine motif is known to function as a retention signal for a group of membrane proteins associated with the ER. Expression of a full-length cDNA of ERGIC-53 in Vero cells revealed intracellular localization similar but not always identical to the endogenously expressed ERGIC-53. The presence of an ER retention motif in a protein of the ER-Golgi intermediate compartment has important implications for the retention mechanism mediated by this signal."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/author"Lottspeich F."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/author"Lottspeich F."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/author"Zerial M."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/author"Zerial M."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/author"Hauri H.-P."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/author"Hauri H.-P."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/author"Schindler R."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/author"Schindler R."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/author"Itin C."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/author"Itin C."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/name"Eur. J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/name"Eur. J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/pages"1-9"xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/pages"1-9"xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/title"ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/title"ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif."xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/volume"61"xsd:string
http://purl.uniprot.org/citations/8223692http://purl.uniprot.org/core/volume"61"xsd:string
http://purl.uniprot.org/citations/8223692http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8223692
http://purl.uniprot.org/citations/8223692http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8223692