Curated Information
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Curated Information Page
PubMed Id: 11035045 
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.
Torres J, Pulido R (2001) The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation. J Biol Chem 276, 993-8 11035045
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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S370-p - PTEN (human)
Orthologous residues
PTEN (human): S370‑p, PTEN (mouse): S370‑p, PTEN (rat): S370‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  MCF-7 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Downstream Regulation
 Effect of modification (function):  protein stabilization
 Comments:  The authors present pulse-chase results that suggest that phosphorylation of this site contributes to the stability of the protein.

S380-p - PTEN (human)
Orthologous residues
PTEN (human): S380‑p, PTEN (mouse): S380‑p, PTEN (rat): S380‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  MCF-7 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Downstream Regulation
 Effect of modification (function):  protein stabilization
 Comments:  The authors present pulse-chase results that suggest that phosphorylation of this site contributes to the stability of the protein.

T382-p - PTEN (human)
Orthologous residues
PTEN (human): T382‑p, PTEN (mouse): T382‑p, PTEN (rat): T382‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  MCF-7 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Downstream Regulation
 Effect of modification (function):  protein stabilization
 Comments:  The authors present pulse-chase results that suggest that phosphorylation of this site contributes to the stability of the protein.

T383-p - PTEN (human)
Orthologous residues
PTEN (human): T383‑p, PTEN (mouse): T383‑p, PTEN (rat): T383‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  MCF-7 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Downstream Regulation
 Effect of modification (function):  protein stabilization
 Comments:  The authors present pulse-chase results that suggest that phosphorylation of this site contributes to the stability of the protein.

S385-p - PTEN (human)
Orthologous residues
PTEN (human): S385‑p, PTEN (mouse): S385‑p, PTEN (rat): S385‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  MCF-7 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Downstream Regulation
 Effect of modification (function):  protein stabilization
 Comments:  The authors present pulse-chase results that suggest that phosphorylation of this site contributes to the stability of the protein.


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