Curated Information
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Curated Information Page
PubMed Id: 16636079 
Janji B, et al. (2006) Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells. J Cell Sci 119, 1947-60 16636079
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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S5-p - L-plastin (human)
Orthologous residues
L‑plastin (human): S5‑p, L‑plastin (mouse): S5‑p, L‑plastin (rat): S5‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  293T (epithelial), Jurkat (T lymphocyte), Vero (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  monkey
 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
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
8-Rp-cAMP increase
H-89 8-Rp-cAMP inhibit treatment-induced increase
forskolin increase
H-89 forskolin inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
ACTA1 (human) Induces in vitro, microscopy-colocalization
 Comments:  interaction with F-actin enhance cells migration and invasion


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