Curated Information
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Curated Information Page
PubMed Id: 12771378 
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.
Gerber SA, et al. (2003) Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci U S A 100, 6940-5 12771378
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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S1126-p - separase (human)
Orthologous residues
separase (human): S1126‑p, separase (mouse): S1121‑p
Characterization
 Methods used to characterize site in vivo mass spectrometry
 Relevant cell lines - cell types - tissues:  HeLa (cervical)
 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
nocodazole increase

S1501-p - separase (human)
Orthologous residues
separase (human): S1501‑p, separase (mouse): S1497‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CAMK2A (human)
KINASE PKACA (human)


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