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http://purl.uniprot.org/citations/12480532http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12480532http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12480532http://www.w3.org/2000/01/rdf-schema#comment"The Polycomb-group (Pc-G) gene products form complexes via protein-protein interactions and maintain the transcriptional repression of genes involved in embryogenesis, cell cycle, and tumorigenesis. Previously, we have shown that mouse Mel-18, a Pc-G protein, has tumor suppressor gene-like activity and negatively regulates transcription. Here, we show in vitro by pull-down assays and in vivo in transiently transfected COS-7 cells that Mel-18 forms homodimers. Deletion analysis revealed that the N-terminal RING-finger and alpha-helix domains are required for homodimer formation. In addition, we demonstrated that Mel-18 homo-dimerization is regulated by protein kinase C (PKC) and protein phosphatases, such that dephosphorylated Mel-18 is able to homo-dimerize. These results suggest that the stoichiometry and/or equilibrium of subunits of the class II Polycomb complex containing Mel-18 might be regulated by changes in phosphorylation status via the PKC signaling pathway."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(02)02791-2"xsd:string
http://purl.uniprot.org/citations/12480532http://purl.org/dc/terms/identifier"doi:10.1016/s0006-291x(02)02791-2"xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Fujisaki S."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Fujisaki S."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Ishihara H."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Ishihara H."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Miyazaki M."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Miyazaki M."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Asahara T."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Asahara T."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Kanno M."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Kanno M."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Ninomiya Y."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Ninomiya Y."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Kanno R."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/author"Kanno R."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/pages"135-140"xsd:string
http://purl.uniprot.org/citations/12480532http://purl.uniprot.org/core/pages"135-140"xsd:string