Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.5.9.3
Powered by Cell Signaling Technology
Home > Curated Information Page > PubMed Id: 14504289
Fujita N, Sato S, Tsuruo T (2003) Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein S6 kinases promotes its binding to 14-3-3 and cytoplasmic localization. J Biol Chem 278, 49254-60 14504289
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
Download

S10-p - p27Kip1 (human)
Modsite: NVRVSNGsPsLErMD SwissProt Entrez-Gene
Orthologous residues
p27Kip1 (human): S10‑p, p27Kip1 (mouse): S10‑p, p27Kip1 (rat): S10‑p

T198-p - p27Kip1 (human)
Modsite: PGLRRRQt_______ SwissProt Entrez-Gene
Orthologous residues
p27Kip1 (human): T198‑p, p27Kip1 (mouse): T197‑p, p27Kip1 (rat): T197‑p
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE RSK2 (mouse) genetic transfer of dominant-negative enzyme, pharmacological inhibitor of upstream enzyme, genetic transfer of wild-type enzyme
KINASE p90RSK (rat) genetic transfer of dominant-negative enzyme, pharmacological inhibitor of upstream enzyme, genetic transfer of wild-type enzyme
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
14-3-3 sigma (human) Induces
14-3-3 theta (human) Induces
14-3-3 eta (human) Induces
14-3-3 epsilon (human) Induces