Curated Information
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Home > Curated Information Page > PubMed Id: 22068056
Forcales SV, et al. (2012) Signal-dependent incorporation of MyoD-BAF60c into Brg1-based SWI/SNF chromatin-remodelling complex. EMBO J 31, 301-16 22068056
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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T229-p - SMARCD3 (mouse)
Modsite: HLVEWHRtPTTQETD SwissProt Entrez-Gene
Orthologous residues
SMARCD3 (human): T229‑p, SMARCD3 (mouse): T229‑p, SMARCD3 (rat): T216‑p
Characterization
Methods used to characterize site in vivo [32P] ATP in vitro, immunoassay, immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  C2C12 (myoblast)
Cellular systems studied:  cell lines
Species studied:  mouse
Enzymes shown to modify site in vitro
Type Enzyme
KINASE P38A (mouse)
KINASE P38B (mouse)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE P38B (human) activation of upstream enzyme, pharmacological inhibitor of upstream enzyme, modification site within consensus motif
KINASE P38A (human) activation of upstream enzyme, pharmacological inhibitor of upstream enzyme, modification site within consensus motif
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
SB203580 decrease
MKK6 (mouse) increase
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Effect of modification (process):  cell differentiation, induced, chromatin organization, altered, transcription, induced
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
SMARCA4 (mouse) Induces pull-down assay, co-immunoprecipitation