Curated Information
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Curated Information Page
PubMed Id: 15743772 
Caillaud A, Hovanessian AG, Levy DE, MariƩ IJ (2005) Regulatory serine residues mediate phosphorylation-dependent and phosphorylation-independent activation of interferon regulatory factor 7. J Biol Chem 280, 17671-7 15743772
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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S425-p - IRF7 (mouse)
Orthologous residues
IRF7 (human): S471‑p, IRF7 (mouse): S425‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, electrophoretic mobility shift, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial), 293 (epithelial) [IRF7 (mouse)], COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
 Comments:  Mutation of S437 and S438 to alanine resulted in high constitutive activity, while mutation of S429, S431 and S441 to alanine did not result in constituve activity. However when all 5 residues were mutated activity 5 times higher than WT resulted. This indicates that S437 and S438 are the primary phosphorylation targets, but other residues may act in concert.

S426-p - IRF7 (mouse)
Orthologous residues
IRF7 (human): S472‑p, IRF7 (mouse): S426‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, electrophoretic mobility shift, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial), 293 (epithelial) [IRF7 (mouse)], COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
 Comments:  Mutation of S437 and S438 to alanine resulted in high constitutive activity, while mutation of S429, S431 and S441 to alanine did not result in constituve activity. However when all 5 residues were mutated activity 5 times higher than WT resulted. This indicates that S437 and S438 are the primary phosphorylation targets, but other residues may act in concert.

S429-p - IRF7 (mouse)
Orthologous residues
IRF7 (human): S475‑p, IRF7 (mouse): S429‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, electrophoretic mobility shift, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial), 293 (epithelial) [IRF7 (mouse)], COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
 Comments:  Mutation of S437 and S438 to alanine resulted in high constitutive activity, while mutation of S429, S431 and S441 to alanine did not result in constituve activity. However when all 5 residues were mutated activity 5 times higher than WT resulted. This indicates that S437 and S438 are the primary phosphorylation targets, but other residues may act in concert.
Downstream Regulation
 Effect of modification (process):  transcription, induced
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
DNA Induces transcription, altered functional assay

S431-p - IRF7 (mouse)
Orthologous residues
IRF7 (human): S477‑p, IRF7 (mouse): S431‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, electrophoretic mobility shift, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial), 293 (epithelial) [IRF7 (mouse)], COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
 Comments:  Mutation of S437 and S438 to alanine resulted in high constitutive activity, while mutation of S429, S431 and S441 to alanine did not result in constituve activity. However when all 5 residues were mutated activity 5 times higher than WT resulted. This indicates that S437 and S438 are the primary phosphorylation targets, but other residues may act in concert.
Downstream Regulation
 Effect of modification (process):  transcription, induced
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
DNA Induces transcription, altered functional assay

S437-p - IRF7 (mouse)
Orthologous residues
IRF7 (human): S483‑p, IRF7 (mouse): S437‑p

S438-p - IRF7 (mouse)
Orthologous residues
IRF7 (human): S484‑p, IRF7 (mouse): S438‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, electrophoretic mobility shift, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  293 (epithelial), 293 (epithelial) [IRF7 (mouse)], COS (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey
 Comments:  Mutation of S437 and S438 to alanine resulted in high constitutive activity, while mutation of S429, S431 and S441 to alanine did not result in constituve activity. However when all 5 residues were mutated activity 5 times higher than WT resulted. This indicates that S437 and S438 are the primary phosphorylation targets, but other residues may act in concert.
Downstream Regulation
 Effect of modification (process):  transcription, induced
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
DNA Induces transcription, altered functional assay

S441-p - IRF7 (mouse)
Orthologous residues
IRF7 (human): S487‑p, IRF7 (mouse): S441‑p


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