Curated Information
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Curated Information Page
PubMed Id: 19901077 
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.
Lim KH, et al. (2010) Aurora-A phosphorylates, activates, and relocalizes the small GTPase RalA. Mol Cell Biol 30, 508-23 19901077
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S194-p - RalA (human)
Orthologous residues
RalA (human): S194‑p, RalA (mouse): S194‑p, RalA (rat): S194‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, microscopy-colocalization with upstream kinase, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  293T (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE AurA (human) transfection of constitutively active enzyme, transfection of wild-type enzyme, siRNA inhibition of enzyme, mutation in upstream enzyme recognition motif, transfection of dominant-negative enzyme
Downstream Regulation
 Effect of modification (function):  intracellular localization, molecular association, regulation
 Effect of modification (process):  cell growth, altered, cytoskeletal reorganization
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
RALBP1 (human) Not reported activity, induced cytoskeletal reorganization co-immunoprecipitation
 Comments:  localization to plasma membrane
Associated Diseases
Diseases: Alterations: Comments:
pancreatic cancer


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