Curated Information
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Home > Curated Information Page > PubMed Id: 15147269
Toji S, et al. (2004) The centrosomal protein Lats2 is a phosphorylation target of Aurora-A kinase. Genes Cells 9, 383-97 15147269
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.
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S83-p - LATS2 (human)
Modsite: ALREIRysLLPFANE SwissProt Entrez-Gene
Orthologous residues
LATS2 (human): S83‑p, LATS2 (mouse): S82‑p, LATS2 (rat): S83‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, phospho-antibody
Relevant cell lines - cell types - tissues:  HeLa (cervical)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE AurA (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE AurA (human) mutation in upstream enzyme recognition motif
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
nocodazole increase Cells arrested at M phase by nocodazole treatment showed higher levels of S83 phosphorylation than asynchronous cells.
Downstream Regulation
Effect of modification (function):  intracellular localization