Curated Information
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PubMed Id: 21952048 
Zhang K, et al. (2012) Lats2 kinase potentiates Snail1 activity by promoting nuclear retention upon phosphorylation. EMBO J 31, 29-43 21952048
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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T203-p - Snail1 (human)
Orthologous residues
Snail1 (human): T203‑p, Snail1 (mouse): T203‑p
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  breast cancer, breast cancer, triple negative, colorectal cancer, colorectal carcinoma
 Relevant cell lines - cell types - tissues:  293 (epithelial), BT-549 (breast cell), HCT116 (intestinal), MCF-10A (breast cell), MDA-MB231 (breast cell), MEF (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE LATS2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE LATS2 (human) siRNA inhibition of enzyme, transfection of wild-type enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
nocodazole increase
MST2 (human) increase
SAV1 (human) increase
high cell density increase
Downstream Regulation
 Effect of modification (function):  intracellular localization, protein stabilization
 Effect of modification (process):  carcinogenesis, induced, cell cycle regulation, cell motility, altered
 Comments:  contributes to Snail1 retention in the nucleus

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