Curated Information
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Curated Information Page
PubMed Id: 12569090 
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.
Chikamori K, et al. (2003) Phosphorylation of serine 1106 in the catalytic domain of topoisomerase II alpha regulates enzymatic activity and drug sensitivity. J Biol Chem 278, 12696-702 12569090
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S1106-p - TOP2A (human)
Orthologous residues
TOP2A (human): S1106‑p, TOP2A iso2 (human): S1132‑p, TOP2A (mouse): S1105‑p, TOP2A (rat): N1104‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, mass spectrometry, mutation of modification site, peptide sequencing, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  HL60 (myeloid)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
BAPTA-AM decrease
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced


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