Curated Information
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Curated Information Page
PubMed Id: 18097023 
Pei Y, et al. (2008) Nuclear export of NF90 to stabilize IL-2 mRNA is mediated by AKT-dependent phosphorylation at Ser647 in response to CD28 costimulation. J Immunol 180, 222-9 18097023
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.
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S647-p - NFAT90 (human)
Orthologous residues
NFAT90 (human): S647‑p, NFAT90 iso2 (human): S647‑p, NFAT90 iso4 (human): S651‑p, NFAT90 iso5 (human): S647‑p, NFAT90 (mouse): N647‑p, NFAT90 (rat): N647‑p
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  CHO (fibroblast), Jurkat (T lymphocyte), T lymphocyte-blood
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) pharmacological inhibitor of upstream enzyme, transfection of inactive enzyme, transfection of constitutively active enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
anti-CD3/CD28 increase
LY294002 anti-CD3/CD28 inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  translation, altered
 Comments:  required for NFAT90 export; stabilizes IL-2 mRNA

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