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http://purl.uniprot.org/citations/8386367http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8386367http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8386367http://www.w3.org/2000/01/rdf-schema#comment"The product of the human c-myc protooncogene (Myc) is a sequence-specific DNA binding protein. Here, we demonstrate that the placement of the specific Myc DNA binding site CACGTG upstream of a luciferase reporter gene conferred Myc-stimulated expression that was inhibited by the overexpression of the basic-helix-loop-helix/leucine zipper protein Max. It was observed that Myc was phosphorylated in vivo within the NH2-terminal domain at Thr-58 and Ser-62. Replacement of these phosphorylation sites with Ala residues caused a marked decrease in Myc-stimulated reporter gene expression. In contrast, the replacement of Thr-58 or Ser-62 with an acidic residue (Glu) caused only a small inhibition of transactivation. Together, these data demonstrate that the NH2-terminal phosphorylation sites Thr-58 and Ser-62 are required for high levels of transactivation of gene expression by Myc."xsd:string
http://purl.uniprot.org/citations/8386367http://purl.org/dc/terms/identifier"doi:10.1073/pnas.90.8.3216"xsd:string
http://purl.uniprot.org/citations/8386367http://purl.org/dc/terms/identifier"doi:10.1073/pnas.90.8.3216"xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/author"Gupta S."xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/author"Gupta S."xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/author"Davis R.J."xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/author"Davis R.J."xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/author"Seth A."xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/author"Seth A."xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/pages"3216-3220"xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/pages"3216-3220"xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/title"Transactivation of gene expression by Myc is inhibited by mutation at the phosphorylation sites Thr-73 and Ser-77."xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/title"Transactivation of gene expression by Myc is inhibited by mutation at the phosphorylation sites Thr-73 and Ser-77."xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/volume"90"xsd:string
http://purl.uniprot.org/citations/8386367http://purl.uniprot.org/core/volume"90"xsd:string
http://purl.uniprot.org/citations/8386367http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8386367
http://purl.uniprot.org/citations/8386367http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8386367
http://purl.uniprot.org/citations/8386367http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8386367
http://purl.uniprot.org/citations/8386367http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8386367