Curated Information
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Curated Information Page
PubMed Id: 23024368 
Spelat R, Ferro F, Curcio F (2012) Serine 111 phosphorylation regulates OCT4A protein subcellular distribution and degradation. J Biol Chem 287, 38279-88 23024368
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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S111-p - Oct4 (human)
Orthologous residues
Oct4 (human): S111‑p, Oct4 iso2 (human): , Oct4 (mouse): S106‑p, Oct4 iso2 (mouse):
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mass spectrometry, mutation of modification site, western blotting
 Disease tissue studied:  testicular cancer
 Relevant cell lines - cell types - tissues:  HeLa (cervical), NT2 (testicular)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (human) transfection of constitutively active enzyme, pharmacological inhibitor of upstream enzyme, co-immunoprecipitation
KINASE ERK1 (human) transfection of constitutively active enzyme, pharmacological inhibitor of upstream enzyme, co-immunoprecipitation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
PD98059 decrease
FGF2 increase
Downstream Regulation
 Effect of modification (function):  activity, inhibited, intracellular localization, protein degradation, ubiquitination
 Effect of modification (process):  transcription, altered
 Comments:  phosphorylation of this site downregulates Nanog, SOX2, REX1 and upregulates BMP4, GATA6, DDLX5


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