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http://purl.uniprot.org/citations/17679095http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17679095http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17679095http://www.w3.org/2000/01/rdf-schema#comment"Cbl proteins are E3 ubiquitin ligases that are negative regulators of many receptor tyrosine kinases. Cbl-b and c-Cbl contain a ubiquitin-associated (UBA) domain, which is present in a variety of proteins involved in ubiquitin-mediated processes. Despite high sequence identity, Cbl UBA domains display remarkably different ubiquitin-binding properties. Here, we report the crystal structure of the UBA domain of Cbl-b in complex with ubiquitin at 1.9 A resolution. The structure reveals an atypical mechanism of ubiquitin recognition by the first helix of the UBA. Helices 2 and 3 of the UBA domain form a second binding surface, which mediates UBA dimerization in the crystal and in solution. Site-directed mutagenesis demonstrates that Cbl-b dimerization is regulated by ubiquitin binding and required for tyrosine phosphorylation of Cbl-b and ubiquitination of Cbl-b substrates. These studies demonstrate a role for ubiquitin in regulating biological activity by promoting protein dimerization."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2007.06.023"xsd:string
http://purl.uniprot.org/citations/17679095http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2007.06.023"xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Berghuis A.M."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Berghuis A.M."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Lin T."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Lin T."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Park M."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Park M."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Gehring K."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Gehring K."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Kozlov G."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Kozlov G."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Mirza I.A."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Mirza I.A."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Lipkowitz S."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Lipkowitz S."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Peschard P."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/author"Peschard P."xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/17679095http://purl.uniprot.org/core/name"Mol. Cell"xsd:string