Curated Information
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Home > Curated Information Page > PubMed Id: 23219531
Wang Y, et al. (2013) Phosphorylation and Recruitment of BAF60c in Chromatin Remodeling for Lipogenesis in Response to Insulin. Mol Cell 49, 283-97 23219531
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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S247-p - SMARCD3 (human)
Modsite: VKRPGDLsVRCTLLL SwissProt Entrez-Gene
Orthologous residues
SMARCD3 (human): S247‑p, SMARCD3 (mouse): S247‑p, SMARCD3 (rat): S234‑p
Characterization
Methods used to characterize site in vivo immunoassay, immunoprecipitation, mass spectrometry, mutation of modification site, phospho-antibody, western blotting
Disease tissue studied:  liver cancer
Relevant cell lines - cell types - tissues:  293 (epithelial), HepG2 (hepatic), liver
Cellular systems studied:  cell lines, tissue
Species studied:  human, mouse
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKCZ (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCZ (human) transfection of dominant-negative enzyme, transfection of wild-type enzyme, competition with site-specific peptide, siRNA inhibition of enzyme, pharmacological inhibitor of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
meal feeding increase
insulin increase
siRNA decrease PKCZ-siRNA decreases phosphorylation
Downstream Regulation
Effect of modification (function):  intracellular localization, molecular association, regulation
Effect of modification (process):  chromatin organization, altered, transcription, induced
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
USF1 (human) Induces pull-down assay, co-immunoprecipitation

K235-ac - USF1 (human)
Modsite: DCSMESTkSGQSkGG SwissProt Entrez-Gene
Orthologous residues
USF1 (human): K235‑ac, USF1 (mouse): K235‑ac, USF1 (rat): K235‑ac
Characterization
Methods used to characterize site in vivo immunoprecipitation, modification-specific antibody, mutation of modification site, western blotting
Disease tissue studied:  liver cancer
Relevant cell lines - cell types - tissues:  293 (epithelial), HepG2 (hepatic)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
meal feeding increase
insulin increase
Downstream Regulation
Effect of modification (function):  intracellular localization, molecular association, regulation
Effect of modification (process):  transcription, induced
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
SMARCD3 (human) Induces co-immunoprecipitation
Comments:  K235 acetylation induces recruitment of SMARCD3 to the promoters of lipogenic genes

S262-p - USF1 (human)
Modsite: RQSNHRLsEELQGLD SwissProt Entrez-Gene
Orthologous residues
USF1 (human): S262‑p, USF1 (mouse): S262‑p, USF1 (rat): S262‑p
Characterization
Methods used to characterize site in vivo modification-specific antibody, western blotting
Disease tissue studied:  liver cancer
Relevant cell lines - cell types - tissues:  HepG2 (hepatic)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE DNAPK (human) genetic knockout/knockin of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
meal feeding increase
insulin increase
Downstream Regulation
Effect of modification (function):  acetylation, molecular association, regulation
Comments:  increases acetylation at USF1-K235