Curated Information
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Curated Information Page
PubMed Id: 19671522 
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.
Stephan H, et al. (2009) Ionizing radiation-dependent and independent phosphorylation of the 32-kDa subunit of replication protein A during mitosis. Nucleic Acids Res 37, 6028-41 19671522
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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S23-p - RFA2 (human)
Orthologous residues
RFA2 (human): S23‑p, RFA2 (mouse): S23‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody, western blotting
 Disease tissue studied:  ataxia-telangiectasia, cervical cancer, cervical adenocarcinoma, Seckel syndrome
 Relevant cell lines - cell types - tissues:  GM O1525 (lymphoblastoid), GM18366 (fibroblast), HeLa S3 (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CDK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ATM (human) pharmacological inhibitor of upstream enzyme
KINASE DNAPK (human) pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
ionizing radiation no change compared to control
nocodazole increase
ionizing radiation nocodazole augment treatment-induced increase
wortmannin ionizing radiation, nocodazole inhibit treatment-induced increase
KU-55933 ionizing radiation, nocodazole inhibit treatment-induced increase
NU7441 ionizing radiation, nocodazole inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization

S29-p - RFA2 (human)
Orthologous residues
RFA2 (human): S29‑p, RFA2 (mouse): S29‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody, western blotting
 Disease tissue studied:  ataxia-telangiectasia, cervical cancer, cervical adenocarcinoma, Seckel syndrome
 Relevant cell lines - cell types - tissues:  GM O1525 (lymphoblastoid), GM18366 (fibroblast), HeLa S3 (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CDK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ATM (human) pharmacological inhibitor of upstream enzyme
KINASE DNAPK (human) pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
ionizing radiation no change compared to control
nocodazole increase
ionizing radiation nocodazole augment treatment-induced increase
wortmannin ionizing radiation, nocodazole inhibit treatment-induced increase
KU-55933 ionizing radiation, nocodazole inhibit treatment-induced increase
NU7441 ionizing radiation, nocodazole inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization


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