Curated Information
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Home > Curated Information Page > PubMed Id: 22789442
van Tiel CM, et al. (2012) Dual function of Pin1 in NR4A nuclear receptor activation: Enhanced activity of NR4As and increased Nur77 protein stability. Biochim Biophys Acta 1823, 1894-904 22789442
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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S152-p - Nur77 (human)
Modsite: SFQPPQLsPWDGSFG SwissProt Entrez-Gene
Orthologous residues
Nur77 (human): S152‑p, Nur77 iso2 (human): S165‑p, Nur77 (mouse): S154‑p, Nur77 (rat): S151‑p
Characterization
Methods used to characterize site in vivo immunoassay, mutation of modification site, western blotting
Relevant cell lines - cell types - tissues:  HEK293T (epithelial)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK2A1 (human) siRNA inhibition of enzyme, pharmacological inhibitor of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TBB decrease
siRNA decrease siRNA for CK2A decreases phosphorylation
Downstream Regulation
Effect of modification (function):  protein stabilization
Comments:  Pin1 increases stability by acting on CK2 phosphorylated S152