Curated Information
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Curated Information Page
PubMed Id: 18223295 
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.
Gurel Z, et al. (2008) Recruitment of ikaros to pericentromeric heterochromatin is regulated by phosphorylation. J Biol Chem 283, 8291-300 18223295
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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S13-p - Ikaros (mouse) ▲
Orthologous residues
Ikaros (human): S13‑p, Ikaros iso12 (human): S13‑p, Ikaros (mouse): S13‑p, Ikaros iso9 (mouse): S13‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping
 Disease tissue studied:  thymic carcinoma
 Relevant cell lines - cell types - tissues:  293T (epithelial), 3T3 (fibroblast), thymocyte, VL3-3M2 (T lymphocyte)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE CK2-A1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK2-A1 (mouse) phosphopeptide analysis, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester, ionomycin decrease
DRB decrease
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
DNA Disrupts electrophoretic visualization

T23-p - Ikaros (mouse) ▲
Orthologous residues
Ikaros (human): T23‑p, Ikaros iso12 (human): ‑, Ikaros (mouse): T23‑p, Ikaros iso9 (mouse): T23‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping
 Disease tissue studied:  thymic carcinoma
 Relevant cell lines - cell types - tissues:  293T (epithelial), 3T3 (fibroblast), thymocyte, VL3-3M2 (T lymphocyte)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE CK2-A1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK2-A1 (mouse) phosphopeptide analysis, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
DRB decrease
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
DNA Disrupts electrophoretic visualization

S63-p - Ikaros (mouse) ▲
Orthologous residues
Ikaros (human): S63‑p, Ikaros iso12 (human): ‑, Ikaros (mouse): S63‑p, Ikaros iso9 (mouse): S83‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping
 Disease tissue studied:  thymic carcinoma
 Relevant cell lines - cell types - tissues:  293T (epithelial), 3T3 (fibroblast), thymocyte, VL3-3M2 (T lymphocyte)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE CK2-A1 (human)

S101-p - Ikaros (mouse) ▲
Orthologous residues
Ikaros (human): S101‑p, Ikaros iso12 (human): ‑, Ikaros (mouse): S101‑p, Ikaros iso9 (mouse): S121‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping
 Disease tissue studied:  thymic carcinoma
 Relevant cell lines - cell types - tissues:  293T (epithelial), 3T3 (fibroblast), thymocyte, VL3-3M2 (T lymphocyte)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE CK2-A1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK2-A1 (mouse) phosphopeptide analysis, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
DRB decrease

S293-p - Ikaros (mouse) ▲
Orthologous residues
Ikaros (human): S295‑p, Ikaros iso12 (human): S70‑p, Ikaros (mouse): S293‑p, Ikaros iso9 (mouse): S314‑p
Characterization
 Methods used to characterize site in vivo:  [32P] bio-synthetic labeling, mutation of modification site, phosphopeptide mapping
 Disease tissue studied:  thymic carcinoma
 Relevant cell lines - cell types - tissues:  293T (epithelial), 3T3 (fibroblast), thymocyte, VL3-3M2 (T lymphocyte)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE CK2-A1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK2-A1 (mouse) phosphopeptide analysis, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester, ionomycin decrease
DRB decrease
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
DNA Disrupts electrophoretic visualization


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