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Basic Characteristics of Mutations
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Mutation Site
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K102I |
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Mutation Site Sentence
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PME-BGLF4-K102I was constructed by amplifying the entire coding sequence of BGLF4-K102I, in which the invariant lysine at position 102 was substituted with isoleucine, from pAcGHLT-BGLF4-K102I (Kato et al., 2003) and cloning the DNA fragments into pME18S. |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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BGLF4 |
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Standardized Encoding Gene
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BGLF4
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Genotype/Subtype
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- |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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Cell line
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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- |
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Literature Information
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PMID
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19321754
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Title
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Epstein-Barr virus protein kinase BGLF4 interacts with viral transactivator BZLF1 and regulates its transactivation activity
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Author
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Asai R,Kato A,Kawaguchi Y
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Journal
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The Journal of general virology
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Journal Info
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2009 Jul;90(Pt 7):1575-1581
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Abstract
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BGLF4 is a serine/threonine protein kinase encoded by Epstein-Barr virus. One of the physiological substrates of BGLF4 is viral transactivator BZLF1. In the present study, it was demonstrated that alanine substitution of the serine residue at position 209 (S209A) in BZLF1 eliminated phosphorylation of the protein by BGLF4 in vitro. The S209A mutation in BZLF1, as well as a K102I mutation in BGLF4, which inactivated catalytic activity of the viral kinase, also inhibited formation of a stable BGLF4-BZLF1 complex and downregulation of BZLF1 autotransactivation activity mediated by BGLF4. These results indicate that formation of a stable complex of BGLF4-BZLF1 enables downregulation of BZLF1 autoregulation activity and it appears that BGLF4 phosphorylation of BZLF1 may be involved in these processes.
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Sequence Data
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-
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