Curated Information
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Home > Curated Information Page > PubMed Id: 21822051
Yabuta N, et al. (2011) The tumor suppressor Lats2 is pivotal in Aurora A and Aurora B signaling during mitosis. Cell Cycle 10, 2724-36 21822051
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

S172-p - LATS2 (human)
Modsite: TPVtRRPsFEGTGDS SwissProt Entrez-Gene
Orthologous residues
LATS2 (human): S172‑p, LATS2 (mouse): S171‑p, LATS2 (rat): S172‑p

S380-p - LATS2 (human)
Modsite: ATLARRDsLQKPGLE SwissProt Entrez-Gene
Orthologous residues
LATS2 (human): S380‑p, LATS2 (mouse): S362‑p, LATS2 (rat): S361‑p
Methods used to characterize site in vivo immunoprecipitation, microscopy-colocalization with upstream kinase, mutation of modification site, phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  HEK293T (epithelial), HeLa (cervical), HeLa S3 (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, phospho-antibody, siRNA inhibition of enzyme, pharmacological inhibitor of upstream enzyme, microscopy-colocalization, co-immunoprecipitation
Downstream Regulation
Effect of modification (function):  intracellular localization
Comments:  translocation from the centrosome to the chromosome and spindle during mitosis; chromosome segregation and cytokinesis