Harrington KM, Clevenger CV (2016) Identification of NEK3 Kinase Threonine 165 as a Novel Regulatory Phosphorylation Site That Modulates Focal Adhesion Remodeling Necessary for Breast Cancer Cell Migration. J Biol Chem 291, 21388-21406 27489110

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T165-p - NEK3 (human) ▲

Modsite: FACTYVGtPYYVPPE SwissProt Entrez-Gene Orthologous residues NEK3 (human): T165‑p, NEK3 (mouse): T163‑p, NEK3 (rat): T165‑p Characterization Methods used to characterize site in vivo:  immunoprecipitation, mutation of modification site, phospho-antibody, western blotting Disease tissue studied:  breast cancer Relevant cell lines - cell types - tissues:  HEK293T (epithelial), MCF-7 (breast cell), T47D (breast cell) Cellular systems studied:  cell lines Species studied:  human Enzymes shown to modify site in vitro:  Type Enzyme KINASE NEK3 (human) Comments:  autophosphorylation Upstream Regulation Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes PRL increase U0126 PRL inhibit treatment-induced increase PRL ERK1 (human), ERK2 (human) increase ERK1/2 siRNA decrease Downstream Regulation Effect of modification (function):  enzymatic activity, induced Effect of modification (process):  cell adhesion, altered, cell motility, induced Comments:  focal adhesion maturation