Curated Information
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Curated Information Page
PubMed Id: 15923181 
This page summarizes selected information from the article 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.
Goyal P, Pandey D, Behring A, Siess W (2005) Inhibition of nuclear import of LIMK2 in endothelial cells by protein kinase C-dependent phosphorylation at Ser-283. J Biol Chem 280, 27569-77 15923181
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S283-p - LIMK2 (human)
Orthologous residues
LIMK2 (human): S283‑p, LIMK2 iso2 (human): S262‑p, LIMK2 (mouse): S283‑p, LIMK2 (rat): S283‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Relevant cell lines - cell types - tissues:  umbilical vein
 Cellular systems studied:  primary cells
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKCD (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCD (human) pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
Go 6976 phorbol ester inhibit treatment-induced increase
Go 6983 phorbol ester inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Comments:  its phosphorylation inhibits the nuclear import of LIMK2


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