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http://purl.uniprot.org/citations/12582153http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12582153http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12582153http://www.w3.org/2000/01/rdf-schema#comment"Kaposi's sarcoma associated-herpes virus encodes two proteins, MIR (modulator of immune recognition) 1 and 2, which are involved in the evasion of host immunity. MIR1 and 2 have been shown to function as an E3 ubiquitin ligase for immune recognition-related molecules (e.g. major histocompatibility complex class I, B7-2, and ICAM-1) through the BKS (bovine herpesvirus 4, Kaposi's sarcoma associated-herpes virus, and Swinepox virus) subclass of plant homeodomain (PHD) domain, termed the BKS-PHD domain. Here we show that the human genome also encodes a novel BKS-PHD domain-containing protein that functions as an E3 ubiquitin ligase and whose putative substrate is the B7-2 co-stimulatory molecule. This novel E3 ubiquitin ligase was designated as c-MIR (cellular MIR) based on its functional and structural similarity to MIR1 and 2. Forced expression of c-MIR induced specific down-regulation of B7-2 surface expression through ubiquitination, rapid endocytosis, and lysosomal degradation of the target molecule. This specific targeting was dependent upon the binding of c-MIR to B7-2. Replacing the BKS-PHD domain of MIR1 with the corresponding domain of c-MIR did not alter MIR1 function. The discovery of c-MIR, a novel E3 ubiquitin ligase, highlights the possibility that viral immune regulatory proteins originated in the host genome and presents unique functions of BKS-PHD domain-containing proteins in mammals."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m211285200"xsd:string
http://purl.uniprot.org/citations/12582153http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m211285200"xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Sato Y."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Sato Y."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Hotta H."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Hotta H."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Ohgimoto S."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Ohgimoto S."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Goto E."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Goto E."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Ishido S."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Ishido S."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Nagano-Fujii M."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Nagano-Fujii M."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Ohgimoto K."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/author"Ohgimoto K."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/pages"14657-14668"xsd:string
http://purl.uniprot.org/citations/12582153http://purl.uniprot.org/core/pages"14657-14668"xsd:string