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http://purl.uniprot.org/citations/11927593http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11927593http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11927593http://www.w3.org/2000/01/rdf-schema#comment"Using a monoclonal antibody that recognizes a nuclear matrix protein, we selected a cDNA clone from a lambdagt11 human placenta cDNA library. This cDNA encoded a 939-amino acid protein designated nuclear matrix protein NXP-2. Northern blot analysis indicated that NXP-2 was expressed in various tissues at different levels. Forcibly expressed green fluorescent protein-tagged NXP-2 as well as endogenous NXP-2 was localized in the nucleus and distributed to the nuclear matrix. NXP-2 was released from the nuclear matrix when RNase A was included in the buffer for nuclear matrix preparation. Mapping of functional domains was carried out using green fluorescent protein-tagged truncated mutants of NXP-2. The region of amino acids 326-353 was responsible for nuclear matrix binding and contained a cluster of hydrophobic amino acids that was similar to the nuclear matrix targeting signal of acute myeloleukemia protein. The central region (amino acids 500-591) was demonstrated to be required for RNA binding by Northwestern analysis, although NXP-2 lacked a known RNA binding motif. The region of amino acid residues 682-876 was predicted to have a coiled-coil structure. The RNA-binding, nuclear matrix-binding, and coiled-coil domains are structurally separated, suggesting that NXP-2 plays important roles in diverse nuclear functions, including RNA metabolism and maintenance of nuclear architecture."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m201440200"xsd:string
http://purl.uniprot.org/citations/11927593http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m201440200"xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Kimura Y."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Kimura Y."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Sugimoto H."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Sugimoto H."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Osumi T."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Osumi T."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Sakai F."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Sakai F."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Sadano H."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Sadano H."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Sawamura T."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Sawamura T."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Nakano O."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Nakano O."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Kisaki O."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/author"Kisaki O."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11927593http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string