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http://purl.uniprot.org/citations/12496242http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12496242http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12496242http://www.w3.org/2000/01/rdf-schema#comment"Human filamins are 280-kDa proteins containing an N-terminal actin-binding domain followed by 24 characteristic repeats. They also interact with a number of other cellular proteins. All of those identified to date, with the exception of actin, bind to the C-terminal third of a filamin. In a yeast two-hybrid search of a human placental library, using as bait repeats 10-18 of filamin B, we isolated a cDNA coding for a novel 374 amino acid protein containing a proline-rich domain near its N terminus and two LIM domains at its C terminus. We term this protein filamin-binding LIM protein-1, FBLP-1. Yeast two-hybrid studies with deletion mutants localized the areas of interaction in FBLP-1 to its N-terminal domain and in filamin B to repeats 10-13. FBLP-1 mRNA was detected in a variety of tissues and cells including platelets and endothelial cells. We also have identified two FBLP-1 variants. Both contain three C-terminal LIM domains, but one lacks the N-terminal proline-rich domain. Transfection of FBLP-1 into 293A cells promoted stress fiber formation, and both FBLP-1 and filamin B localized to stress fibers in the transfected cells. The association between filamin B and FBLP-1 may play a hitherto unknown role in cytoskeletal function, cell adhesion, and cell motility."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m209339200"xsd:string
http://purl.uniprot.org/citations/12496242http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m209339200"xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/author"Fujimura K."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/author"Fujimura K."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/author"Saeki M."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/author"Saeki M."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/author"Fujimoto T.-T."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/author"Fujimoto T.-T."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/author"Shapiro S.S."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/author"Shapiro S.S."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/author"Takafuta T."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/author"Takafuta T."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/pages"12175-12181"xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/pages"12175-12181"xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/title"A new member of the LIM protein family binds to filamin B and localizes at stress fibers."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/title"A new member of the LIM protein family binds to filamin B and localizes at stress fibers."xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12496242http://purl.uniprot.org/core/volume"278"xsd:string