Curated Information
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Home > Curated Information Page > PubMed Id: 16325270
Sato N, et al. (2006) Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines. Immunol Lett 103, 127-34 16325270
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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T265-p - DAPK3 (mouse)
Modsite: KDPKRRMtIAQSLEH SwissProt Entrez-Gene
Orthologous residues
DAPK3 (human): T265‑p, DAPK3 (mouse): T265‑p
Methods used to characterize site in vivo mutation of modification site, phospho-antibody
Relevant cell lines - cell types - tissues:  3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], HeLa (cervical)
Cellular systems studied:  cell lines
Species studied:  human, mouse
Enzymes shown to modify site in vitro
Type Enzyme
KINASE DAPK3 (mouse)
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
IL-6 increase
LIF increase
Downstream Regulation
Effect of modification (function):  enzymatic activity, induced
Effect of modification (process):  apoptosis, induced
Comments:  A T265A mutant is unable to activate STAT3 in response to IL-6 stimulation