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http://purl.uniprot.org/citations/22549881http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22549881http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22549881http://www.w3.org/2000/01/rdf-schema#comment"SHARPIN (SHANK-associated RH domain interacting protein) is part of a large multi-protein E3 ubiquitin ligase complex called LUBAC (linear ubiquitin chain assembly complex), which catalyzes the formation of linear ubiquitin chains and regulates immune and apoptopic signaling pathways. The C-terminal half of SHARPIN contains ubiquitin-like domain and Npl4-zinc finger domains that mediate the interaction with the LUBAC subunit HOIP and ubiquitin, respectively. In contrast, the N-terminal region does not show any homology with known protein interaction domains but has been suggested to be responsible for self-association of SHARPIN, presumably via a coiled-coil region. We have determined the crystal structure of the N-terminal portion of SHARPIN, which adopts the highly conserved pleckstrin homology superfold that is often used as a scaffold to create protein interaction modules. We show that in SHARPIN, this domain does not appear to be used as a ligand recognition domain because it lacks many of the surface properties that are present in other pleckstrin homology fold-based interaction modules. Instead, it acts as a dimerization module extending the functional applications of this superfold."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m112.359547"xsd:string
http://purl.uniprot.org/citations/22549881http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m112.359547"xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/author"Rittinger K."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/author"Rittinger K."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/author"Haire L.F."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/author"Haire L.F."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/author"Dikic I."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/author"Dikic I."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/author"Stieglitz B."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/author"Stieglitz B."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/pages"20823-20829"xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/pages"20823-20829"xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/title"Structural analysis of SHARPIN, a subunit of a large multi-protein E3 ubiquitin ligase, reveals a novel dimerization function for the pleckstrin homology superfold."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/title"Structural analysis of SHARPIN, a subunit of a large multi-protein E3 ubiquitin ligase, reveals a novel dimerization function for the pleckstrin homology superfold."xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/volume"287"xsd:string
http://purl.uniprot.org/citations/22549881http://purl.uniprot.org/core/volume"287"xsd:string
http://purl.uniprot.org/citations/22549881http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22549881
http://purl.uniprot.org/citations/22549881http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22549881