http://purl.uniprot.org/citations/20966198 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20966198 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20966198 | http://www.w3.org/2000/01/rdf-schema#comment | "RNPS1, Acinus, and SAP18 form the apoptosis- and splicing-associated protein (ASAP) complex, which is also part of the exon junction complex. Whereas RNPS1 was originally identified as a general activator of mRNA processing, all three proteins have been found within functional spliceosomes. Both RNPS1 and Acinus contain typical motifs of splicing regulatory proteins including arginine/serine-rich domains. Due to the absence of such structural features, however, a function of SAP18 in splicing regulation is completely unknown. Here we have investigated splicing regulatory activities of the ASAP components. Whereas a full-length Acinus isoform displayed only limited splicing regulatory activity, both RNPS1 and, surprisingly, SAP18 strongly modulated splicing regulation. Detailed mutational analysis and three-dimensional modeling data revealed that the ubiquitin-like fold of SAP18 was required for efficient splicing regulatory activity. Coimmunoprecipitation and immunofluorescence experiments demonstrated that SAP18 assembles a nuclear speckle-localized splicing regulatory multiprotein complex including RNPS1 and Acinus via its ubiquitin-like fold. Our results therefore suggest a novel function of SAP18 in splicing regulation."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.org/dc/terms/identifier | "doi:10.1261/rna.2304410"xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.org/dc/terms/identifier | "doi:10.1261/rna.2304410"xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Dehof A.K."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Dehof A.K."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Erkelenz S."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Erkelenz S."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Hildebrandt A."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Hildebrandt A."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Rattay S."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Rattay S."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Schaal H."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Schaal H."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Schulze-Osthoff K."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Schulze-Osthoff K."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Schwerk C."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Schwerk C."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Singh K.K."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/author | "Singh K.K."xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/name | "RNA"xsd:string |
http://purl.uniprot.org/citations/20966198 | http://purl.uniprot.org/core/name | "RNA"xsd:string |