Curated Information
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Home > Curated Information Page > PubMed Id: 16325853
Marchini A, et al. (2006) Phosphorylation on Ser106 modulates the cellular functions of the SHOX homeodomain protein. J Mol Biol 355, 590-603 16325853
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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S106-p - SHOX (human)
Modsite: EKREDVKsEDEDGQT SwissProt Entrez-Gene
Orthologous residues
SHOX (human): S106‑p, SHOX (dog): S105‑p
Characterization
Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, mass spectrometry, mutation of modification site, phosphopeptide mapping
Relevant cell lines - cell types - tissues:  U2OS (bone cell) [GR (human)]
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK2A1 (human) pharmacological inhibitor of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TBB decrease
apigenin decrease