Curated Information
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PubMed Id: 16135814 
Hergovich A, Bichsel SJ, Hemmings BA (2005) Human NDR kinases are rapidly activated by MOB proteins through recruitment to the plasma membrane and phosphorylation. Mol Cell Biol 25, 8259-72 16135814
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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S281-p - NDR1 (human)
Orthologous residues
NDR1 (human): S281‑p, NDR1 (mouse): S281‑p
 Methods used to characterize site in vivo microscopy-colocalization with upstream kinase, phospho-antibody, western blotting
 Disease tissue studied:  bone cancer
 Relevant cell lines - cell types - tissues:  COS (fibroblast), U2OS (bone cell)
 Cellular systems studied:  cell lines
 Species studied:  monkey
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced, intracellular localization, phosphorylation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
MOBP (human) Induces co-immunoprecipitation
 Comments:  Myristoylated palmitylated NDR1 is membrane targeted and constitutively active (mp-HA-NDR1). When hMOB1A was coexpressed T444, and S281 phosphorylation were greatly increased in wild-type. Association with hMOB1A induces autophosphorylation of NDR1 on S281. A chimera of PKB and and the C1 domain of PKCa fused to hMOB1A recruited this chimera protein to the membrane after TPA treatment. TPA induction further induced the phosphorylation of NDR1 S281 and T444. A NDR1 mutant deficient in hMOB1A binding did not show an increase in phosphorylation.

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