Curated Information
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Home > Curated Information Page > PubMed Id: 10092617
Lambert H, et al. (1999) HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus. J Biol Chem 274, 9378-85 10092617
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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S15-p - HSP27 (hamster)
Modsite: FSLLRSPsWEPFRDW SwissProt
Orthologous residues
HSP27 (human): S15‑p, HSP27 (mouse): S15‑p, HSP27 (rat): S15‑p, HSP27 (pig): S15‑p, HSP27 (hamster): S15‑p, HSP27 (chicken): S15‑p, HSP27 (dog): S15‑p, HSP27 (cow): S15‑p
Characterization
Methods used to characterize site in vivo mutation of modification site
Relevant cell lines - cell types - tissues:  3T3 (fibroblast)
Cellular systems studied:  cell lines
Species studied:  mouse

S90-p - HSP27 (hamster)
Modsite: RALNRQLsSGVSEIR SwissProt
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
Characterization
Methods used to characterize site in vivo mutation of modification site
Relevant cell lines - cell types - tissues:  3T3 (fibroblast)
Cellular systems studied:  cell lines
Species studied:  mouse
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
arsenite increase
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
HSP27 (hamster) Disrupts yeast two-hybrid, in vitro, chemical cross-linking