| http://purl.uniprot.org/citations/20946353 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20946353 | http://www.w3.org/2000/01/rdf-schema#comment | "Major histocompatibility complex class I (MHC-I) molecules bind antigens in the endoplasmic reticulum (ER) and deliver them to the cell surface for immune surveillance of viruses and tumors. Whereas key steps of MHC-I assembly and its acquisition of peptides in the ER are relatively well defined, little is known about how MHC-I molecules leave the ER for cell surface expression. Here, we show that ER export of human classical MHC-I molecules (HLA-A/-B/-C) is regulated by their C-terminal single amino acid, valine or alanine. These amino acids, conserved in nearly all known human MHC-I alleles, serve as the ER export signal by binding to the Sec23/24 complex, a structural component of coat protein complex II (COPII) vesicles that mediate ER-to-Golgi trafficking. Together, our results strongly suggest that ER export of human classical MHC-I molecules can occur via a receptor-mediated process dictated by a highly conserved ER export signal."xsd:string |
| http://purl.uniprot.org/citations/20946353 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1600-0854.2010.01132.x"xsd:string |
| http://purl.uniprot.org/citations/20946353 | http://purl.uniprot.org/core/author | "Cho S."xsd:string |
| http://purl.uniprot.org/citations/20946353 | http://purl.uniprot.org/core/author | "Ahn K."xsd:string |
| http://purl.uniprot.org/citations/20946353 | http://purl.uniprot.org/core/author | "Jun Y."xsd:string |
| http://purl.uniprot.org/citations/20946353 | http://purl.uniprot.org/core/author | "Ryoo J."xsd:string |
| http://purl.uniprot.org/citations/20946353 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/20946353 | http://purl.uniprot.org/core/name | "Traffic"xsd:string |
| http://purl.uniprot.org/citations/20946353 | http://purl.uniprot.org/core/pages | "42-55"xsd:string |
| http://purl.uniprot.org/citations/20946353 | http://purl.uniprot.org/core/title | "Receptor-mediated ER export of human MHC class I molecules is regulated by the C-terminal single amino acid."xsd:string |
| http://purl.uniprot.org/citations/20946353 | http://purl.uniprot.org/core/volume | "12"xsd:string |
| http://purl.uniprot.org/citations/20946353 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20946353 |
| http://purl.uniprot.org/citations/20946353 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20946353 |
| http://purl.uniprot.org/uniprot/P04439#attribution-5855EFE76E4B072D99F4720AF2CBD19C | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/20946353 |
| http://purl.uniprot.org/uniprot/P10321#attribution-5855EFE76E4B072D99F4720AF2CBD19C | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/20946353 |
| http://purl.uniprot.org/uniprot/P01889#attribution-5855EFE76E4B072D99F4720AF2CBD19C | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/20946353 |