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• W1963880360 abstract "Early region 1A (E1A) of human adenovirus type 5 (Ad5) produces five mRNAs that encode proteins of 55, 171, 217, 243, and 289 residues. We have shown previously that the major products of 289 and 243 residues are phosphorylated at a minimum of three sites of which one, Ser-89, is located in the amino terminal half of the protein. In the present report we show that these E1A proteins are also phosphorylated at a second site in this region located at Ser-96. The 171 and 217 residue E1A species were also tentatively identified and, as predicted, neither contained the Ser-89 or Ser-96 sites but both appeared to be phosphorylated at the same sites as 289R and 243R toward the carboxy terminus. Studies with mutants in which Ser-89 or Ser-96 were converted to alanine residues indicated that phosphorylation of Ser-89 but not Ser-96 induces the major shift in gel mobility of E1A products. However, neither site appears to be of major importance in the regulation of E1A-mediated transactivation or transformation." @default.
• W1963880360 created "2016-06-24" @default.
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• W1963880360 date "1989-04-01" @default.
• W1963880360 modified "2023-09-23" @default.
• W1963880360 title "Analysis of phosphorylation sites in the exon 1 region of E1A proteins of human adenovirus type 5" @default.
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• W1963880360 doi "https://doi.org/10.1016/0042-6822(89)90165-7" @default.
• W1963880360 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2523179" @default.
• W1963880360 hasPublicationYear "1989" @default.
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