http://purl.uniprot.org/citations/26150415 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/26150415 | http://www.w3.org/2000/01/rdf-schema#comment | "Yeast Bro1 and Rim20 belong to a family of proteins which possess a common architecture of Bro1 and V domains. Alix and His domain protein tyrosine phosphatase (HD-PTP), mammalian Bro1 family proteins, bind YP(X)nL (n = 1 to 3) motifs in their target proteins through their V domains. In Alix, the Phe residue, which is located in the hydrophobic groove of the V domain, is critical for binding to the YP(X)nL motif. Although the overall sequences are not highly conserved between mammalian and yeast V domains, we show that the conserved Phe residue in the yeast Bro1 V domain is important for binding to its YP(X)nL-containing target protein, Rfu1. Furthermore, we show that Rim20 binds to its target protein Rim101 through the interaction between the V domain of Rim20 and the YPIKL motif of Rim101. The mutation of either the critical Phe residue in the Rim20 V domain or the YPIKL motif of Rim101 affected the Rim20-mediated processing of Rim101. These results suggest that the interactions between V domains and YP(X)nL motif-containing proteins are conserved from yeast to mammalian cells. Moreover, the specificities of each V domain to their target protein suggest that unidentified elements determine the binding specificity."xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.org/dc/terms/identifier | "doi:10.1128/ec.00091-15"xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/author | "Tanaka K."xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/author | "Kimura Y."xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/author | "Mizushima T."xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/author | "Takagi K."xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/author | "Maeda T."xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/author | "Tanigawa M."xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/author | "Kawawaki J."xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/name | "Eukaryot Cell"xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/pages | "976-982"xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/title | "Conserved Mode of Interaction between Yeast Bro1 Family V Domains and YP(X)nL Motif-Containing Target Proteins."xsd:string |
http://purl.uniprot.org/citations/26150415 | http://purl.uniprot.org/core/volume | "14"xsd:string |
http://purl.uniprot.org/citations/26150415 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26150415 |
http://purl.uniprot.org/citations/26150415 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/26150415 |
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http://purl.uniprot.org/uniprot/#_Q12033-mappedCitation-26150415 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26150415 |
http://purl.uniprot.org/uniprot/#_P48582-mappedCitation-26150415 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26150415 |
http://purl.uniprot.org/uniprot/#_P33400-mappedCitation-26150415 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26150415 |
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http://purl.uniprot.org/uniprot/P33400 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/26150415 |
http://purl.uniprot.org/uniprot/P48582 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/26150415 |
http://purl.uniprot.org/uniprot/Q12033 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/26150415 |