Curated Information
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Curated Information Page
PubMed Id: 19696028 
Ban R, et al. (2009) Mitotic regulation of the stability of microtubule plus-end tracking protein EB3 by ubiquitin ligase SIAH-1 and Aurora mitotic kinases. J Biol Chem 284, 28367-81 19696028
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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S176-p - EB3 (human)
Orthologous residues
EB3 (human): S176‑p, EB3 iso2 (human): S161‑p, EB3 (mouse): S176‑p, EB3 iso2 (mouse): S161‑p, EB3 (rat): S176‑p
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  cervical cancer, cervical adenocarcinoma
 Relevant cell lines - cell types - tissues:  HeLa S3 (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Comments:  in mitotic cells
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE AurB (human)
KINASE AurA (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE AurA (human) pharmacological inhibitor of upstream enzyme
KINASE AurB (human) pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
nocodazole increase
VX-680 nocodazole inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation, protein stabilization, ubiquitination
 Effect of modification (process):  cell cycle regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
SIAH1 (human) Disrupts in vitro, pull-down assay

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