Curated Information
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PubMed Id: 22566623 
Rangasamy V, et al. (2012) Mixed-lineage kinase 3 phosphorylates prolyl-isomerase Pin1 to regulate its nuclear translocation and cellular function. Proc Natl Acad Sci U S A 109, 8149-54 22566623
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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S138-p - PIN1 (human)
Orthologous residues
PIN1 (human): S138‑p, PIN1 (mouse): S140‑p, PIN1 (rat): S140‑p
 Methods used to characterize site in vivo immunoprecipitation, mass spectrometry (in vitro), mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  breast cancer
 Relevant cell lines - cell types - tissues:  293 (epithelial), 3T3 (fibroblast), breast, HeLa (cervical), MEF (fibroblast)
 Cellular systems studied:  cell lines, tissue
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE MLK3 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE MLK3 (human) transfection of inactive enzyme, transfection of wild-type enzyme, co-immunoprecipitation
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  cell cycle regulation
Associated Diseases
Diseases: Alterations: Comments:
breast cancer increased

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