Curated Information
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Curated Information Page
PubMed Id: 1730670 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Landry J, et al. (1992) Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II. J Biol Chem 267, 794-803 1730670
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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S78-p - HSP27 (human) ▲
Orthologous residues
HSP27 (human): S78‑p, HSP27 (mouse): N82‑p, HSP27 (rat): N82‑p, HSP27 (pig): S80‑p, HSP27 (hamster): N86‑p, HSP27 (chicken): S77‑p, HSP27 (dog): S82‑p
Characterization
 Methods used to characterize site in vivo:  2D analysis, [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  CCL39 (fibroblast), HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  hamster, human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE p70S6Kb (human) mutation in upstream enzyme recognition motif, genetic transfer of inducible upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
heat shock increase
arsenite increase
phorbol ester increase
TNF increase
bFGF increase
serum increase
thrombin increase

S82-p - HSP27 (human) ▲
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
Characterization
 Methods used to characterize site in vivo:  2D analysis, [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phosphoamino acid analysis
 Relevant cell lines - cell types - tissues:  CCL39 (fibroblast), HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  hamster, human
 Comments:  S82 is the major site of phosphorylation of HSP27.
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE p70S6Kb (human) mutation in upstream enzyme recognition motif, genetic transfer of inducible upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
heat shock increase
arsenite increase
phorbol ester increase
TNF increase
bFGF increase
serum increase
thrombin increase


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