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http://purl.uniprot.org/citations/11500040http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11500040http://www.w3.org/2000/01/rdf-schema#comment"Bloom Syndrome (BS) is a human autosomal genetic disorder characterized by a predisposition to a variety of malignant tumors. The gene responsible for BS encodes a protein (BLM) consisting of 1417 amino acids with a nuclear localization signal in the C-terminal region, which is a member of the RecQ helicase family. We previously showed, using a yeast two-hybrid system, that BLM interacted with Ubc9, which is the conjugating enzyme of SUMO-1 (small ubiquitin-related modifier-1). In the present study, we exogenously expressed a green fluorescent protein-tagged Bloom syndrome protein, GFP-BLM, in human 293EBNA cells and found that it formed dots/rod-like structures associated with SUMO-1 in the nucleus. Deletion experiments indicated that the region from amino acids 238 to 586 of BLM is required for the formation of dots/rod-like structures associated with SUMO-1, and the DNA helicase domain, but not the helicase activity itself, slightly affected the formation and/or stability of these structures. Expression of a GFP-BLM which contained the 238-586 region, but lacked the C-terminal nuclear localization signal, resulted in localization to the cytoplasm without the formation of dots/rod-like structures and association with SUMO-1, indicating that these events occur only in the nucleus."xsd:string
http://purl.uniprot.org/citations/11500040http://purl.org/dc/terms/identifier"doi:10.1006/bbrc.2001.5387"xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/author"Kobayashi T."xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/author"Seki M."xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/author"Suzuki H."xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/author"Kondo N."xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/author"Mizuno S."xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/author"Harata M."xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/author"Enomoto T."xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/author"Kaneko H."xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/author"Masuko T."xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/author"Kawabe Yi"xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/pages"322-327"xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/title"The N-terminal internal region of BLM is required for the formation of dots/rod-like structures which are associated with SUMO-1."xsd:string
http://purl.uniprot.org/citations/11500040http://purl.uniprot.org/core/volume"286"xsd:string
http://purl.uniprot.org/citations/11500040http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11500040
http://purl.uniprot.org/citations/11500040http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11500040
http://purl.uniprot.org/uniprot/P54132#attribution-41A1BA6ACB36881ADDEF418A14BF19A7http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/11500040