Curated Information
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Curated Information Page
PubMed Id: 15324659 
Suzuki A, et al. (2004) aPKC acts upstream of PAR-1b in both the establishment and maintenance of mammalian epithelial polarity. Curr Biol 14, 1425-35 15324659
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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T596-p - MARK2 (human)
Orthologous residues
MARK2 (human): T596‑p, MARK2 iso4 (human): T542‑p, MARK2 iso10 (human): T509‑p, MARK2 iso11 (human): T596‑p, MARK2 iso13 (human): T516‑p, MARK2 iso14 (human): T562‑p, MARK2 (mouse): T593‑p, MARK2 iso3 (mouse): T539‑p, MARK2 (rat): T539‑p
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  MDCK (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
PHOSPHATASE PPP2CB (human) pharmacological inhibitor of upstream enzyme
KINASE PKCZ (human) pseudosubstrate inhibition
KINASE PKCI (human) siRNA inhibition of enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
okadaic acid increase
depolarization increase
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 beta (human) Induces co-immunoprecipitation, electrophoretic visualization

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