Curated Information
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Home > Curated Information Page > PubMed Id: 12740362
Rane MJ, et al. (2003) Heat shock protein 27 controls apoptosis by regulating Akt activation. J Biol Chem 278, 27828-35 12740362
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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S82-p - HSP27 (human)
Modsite: RALsRQLssGVsEIr SwissProt Entrez-Gene
Orthologous residues
HSP27 (human): S82‑p, HSP27 (mouse): S86‑p, HSP27 (rat): S86‑p, HSP27 (pig): S84‑p, HSP27 (hamster): S90‑p, HSP27 (chicken): S80‑p, HSP27 (dog): S86‑p, HSP27 (cow): S78‑p
Methods used to characterize site in vivo mutation of modification site, phospho-antibody
Relevant cell lines - cell types - tissues:  293 (epithelial), neutrophil
Cellular systems studied:  cell lines, primary cells
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) transfection of constitutively active enzyme
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Effect of modification (process):  apoptosis, altered
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Akt1 (human) Disrupts activity, inhibited co-immunoprecipitation