Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 20026644 
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.
von Knethen A, Tzieply N, Jennewein C, BrĂ¼ne B (2010) Casein-kinase-II-dependent phosphorylation of PPARgamma provokes CRM1-mediated shuttling of PPARgamma from the nucleus to the cytosol. J Cell Sci 123, 192-201 20026644
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.
Download Sites

S16-p - PPAR-gamma iso2 (mouse)
Orthologous residues
PPAR‑gamma (human): S46‑p, PPAR‑gamma iso3 (human): S18‑p, PPAR‑gamma (mouse): S46‑p, PPAR‑gamma iso2 (mouse): S16‑p, PPAR‑gamma (rat): S46‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial), macrophage-peritoneum, RAW 264.7 (macrophage)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK2A1 (human) modification site within consensus motif, genetic knockout/knockin of upstream enzyme, 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
 Effect of modification (process):  transcription, altered

S21-p - PPAR-gamma iso2 (mouse)
Orthologous residues
PPAR‑gamma (human): S51‑p, PPAR‑gamma iso3 (human): S23‑p, PPAR‑gamma (mouse): S51‑p, PPAR‑gamma iso2 (mouse): S21‑p, PPAR‑gamma (rat): S51‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial), macrophage-peritoneum, RAW 264.7 (macrophage)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK2A1 (human) modification site within consensus motif, genetic knockout/knockin of upstream enzyme, 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
 Effect of modification (process):  transcription, altered

S58-p - RANBP3 (mouse)
Orthologous residues
RANBP3 (human): S126‑p, RANBP3 iso2 (human): S126‑p, RANBP3 iso3 (human): S58‑p, RANBP3 (mouse): S58‑p, RANBP3 (rat): S58‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  RAW 264.7 (macrophage)
 Cellular systems studied:  cell lines
 Species studied:  mouse
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK1 (mouse) genetic knockout/knockin of upstream enzyme, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
PD98059 decrease


Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.