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http://purl.uniprot.org/citations/12039952http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12039952http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12039952http://www.w3.org/2000/01/rdf-schema#comment"In an attempt to isolate cofactors capable of influencing estrogen receptor alpha (ERalpha) transcriptional activity, we used yeast two-hybrid screening and identified protein arginine methyltransferase 2 (PRMT2) as a new ERalpha-binding protein. PRMT2 interacted directly with three ERalpha regions including AF-1, DNA binding domain, and hormone binding domain in a ligand-independent fashion. The ERalpha-interacting region on PRMT2 has been mapped to a region encompassing amino acids 133-275. PRMT2 also binds to ERbeta, PR, TRbeta, RARalpha, PPARgamma, and RXRalpha in a ligand-independent manner. PRMT2 enhanced both ERalpha AF-1 and AF-2 transcriptional activity, and the potential methyltransferase activity of PRMT2 appeared pivotal for its coactivator function. In addition, PRMT2 enhanced PR, PPARgamma, and RARalpha-mediated transactivation. Although PRMT2 was found to interact with two other coactivators, the steroid receptor coactivator-1 (SRC-1) and the peroxisome proliferator-activated receptor-interacting protein (PRIP), no synergistic enhancement of ERalpha transcriptional activity was observed when PRMT2 was coexpressed with either PRIP or SRC-1. In this respect PRMT2 differs from coactivators PRMT1 and CARM1 (coactivator-associated arginine methyltransferase). These results suggest that PRMT2 is a novel ERalpha coactivator."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m201053200"xsd:string
http://purl.uniprot.org/citations/12039952http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m201053200"xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Chang J."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Chang J."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Zhu Y."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Zhu Y."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Qi C."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Qi C."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Rao S.M."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Rao S.M."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Yeldandi A.V."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Yeldandi A.V."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Zhu Y.-J."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/author"Zhu Y.-J."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/pages"28624-28630"xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/pages"28624-28630"xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/title"Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."xsd:string
http://purl.uniprot.org/citations/12039952http://purl.uniprot.org/core/title"Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."xsd:string