Curated Information
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Home > Curated Information Page > PubMed Id: 27489110
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
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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T165-p - NEK3 (human)
Modsite: FACTYVGtPYYVPPE SwissProt Entrez-Gene
Orthologous residues
NEK3 (human): T165‑p, NEK3 (mouse): T163‑p, NEK3 (rat): T165‑p
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