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http://purl.uniprot.org/citations/23086935http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23086935http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23086935http://www.w3.org/2000/01/rdf-schema#comment"Polysumoylation is a crucial cellular response to stresses against genomic integrity or proteostasis. Like the small ubiquitin-like modifier (SUMO)-targeted ubiquitin ligase RNF4, proteins with clustered SUMO-interacting motifs (SIMs) can be important signal transducers downstream of polysumoylation. To identify novel polySUMO-binding proteins, we conducted a computational string search with a custom Python script. We found clustered SIMs in another RING domain protein Arkadia/RNF111. Detailed biochemical analysis of the Arkadia SIMs revealed that dominant SIMs in a SIM cluster often contain a pentameric VIDLT ((V/I/L/F/Y)(V/I)DLT) core sequence that is also found in the SIMs in PIAS family E3s and is likely the best-fitted structure for SUMO recognition. This idea led to the identification of additional novel SIM clusters in FLASH/CASP8AP2, C5orf25, and SOBP/JXC1. We suggest that the clustered SIMs in these proteins form distinct SUMO binding domains to recognize diverse forms of protein sumoylation."xsd:string
http://purl.uniprot.org/citations/23086935http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m112.410985"xsd:string
http://purl.uniprot.org/citations/23086935http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m112.410985"xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/author"Sun H."xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/author"Sun H."xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/author"Hunter T."xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/author"Hunter T."xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/pages"42071-42083"xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/pages"42071-42083"xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/title"PolySUMO-binding proteins identified through a string search."xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/title"PolySUMO-binding proteins identified through a string search."xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/volume"287"xsd:string
http://purl.uniprot.org/citations/23086935http://purl.uniprot.org/core/volume"287"xsd:string
http://purl.uniprot.org/citations/23086935http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23086935
http://purl.uniprot.org/citations/23086935http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23086935
http://purl.uniprot.org/citations/23086935http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23086935
http://purl.uniprot.org/citations/23086935http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23086935
http://purl.uniprot.org/uniprot/Q9UKL3http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/23086935
http://purl.uniprot.org/uniprot/P61956http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/23086935