Curated Information
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Curated Information Page
PubMed Id: 15485924 
This page summarizes selected information from the article 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.
Schwartz EI, Intine RV, Maraia RJ (2004) CK2 is responsible for phosphorylation of human La protein serine-366 and can modulate rpL37 5'-terminal oligopyrimidine mRNA metabolism. Mol Cell Biol 24, 9580-91 15485924
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S366-p - SSB (human)
Orthologous residues
SSB (human): S366‑p, SSB (mouse): , SSB (rat):
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, electrophoretic mobility shift, mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (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) antisense inhibition of upstream 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


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