Curated Information
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Home > Curated Information Page > PubMed Id: 16174736
Nakamura T, et al. (2005) Regulation of SR-BI protein levels by phosphorylation of its associated protein, PDZK1. Proc Natl Acad Sci U S A 102, 13404-9 16174736
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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S509-p - PDZK1 (rat)
Modsite: PARDRTLsAAsHsss SwissProt Entrez-Gene
Orthologous residues
PDZK1 (human): S505‑p, PDZK1 (mouse): S505‑p, PDZK1 (rat): S509‑p
Characterization
Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
Cellular systems studied:  cell lines, tissue
Species studied:  hamster, rat
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKACA (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) pharmacological activator 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
colforsin increase
H-89 decrease
glucagon increase
Downstream Regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
SCARB1 (rat) Not reported electrophoretic visualization
Comments:  phosphorylation of this site upregulates expression of SCARB1 protein