Curated Information
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Curated Information Page
PubMed Id: 16931761 
Dornan D, et al. (2006) ATM engages autodegradation of the E3 ubiquitin ligase COP1 after DNA damage. Science 313, 1122-6 16931761
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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S387-p - COP1 (human)
Orthologous residues
COP1 (human): S387‑p, COP1 (mouse): S389‑p, COP1 (rat): S89‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Disease tissue studied:  ataxia-telangiectasic cancer
 Relevant cell lines - cell types - tissues:  293T (epithelial), GM02052 (fibroblast), GM03490 (fibroblast), U2OS (bone cell) [GR (human)]
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ATM (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ATM (human) transfection of inactive enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
ionizing radiation increase
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation, protein degradation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
p53 (human) Disrupts protein degradation co-immunoprecipitation
 Comments:  phosphorylation of this site promotes COP1 autoubiquitination which prevents its interaction and stabilizes p53
Associated Diseases
Diseases: Alterations: Comments:
ataxia-telangiectasic cancer decreased alternation: mutation of ATM protein kinase


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