Curated Information
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Home > Curated Information Page > PubMed Id: 10931933
Gupta MP, Kogut P, Gupta M (2000) Protein kinase-A dependent phosphorylation of transcription enhancer factor-1 represses its DNA-binding activity but enhances its gene activation ability. Nucleic Acids Res 28, 3168-77 10931933
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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S102-p - TEAD1 (mouse)
Modsite: QVLARRKsRDFHSKL SwissProt Entrez-Gene
Orthologous residues
TEAD1 (human): S102‑p, TEAD1 iso2 (human): S87‑p, TEAD1 (mouse): S102‑p, TEAD1 (rat): S87‑p
Characterization
Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
Relevant cell lines - cell types - tissues:  Sol8 (myoblast)
Cellular systems studied:  cell lines
Species studied:  mouse
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKACA (mouse)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (mouse) transfection of wild-type enzyme
Downstream Regulation
Comments:  TEF1 phosphorylation at S102 reduces its DNA-binding activity; plays a role in the PKA-dependent activation of the alpha-MHC gene expression.