Ser90
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Home > Phosphorylation Site Page: > Ser90  -  HSP27 (hamster)

Site Information
RALNRQLsSGVSEIR   SwissProt
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 448403

In vivo Characterization
Methods used to characterize site in vivo:
2D analysis ( 2 ) , mass spectrometry ( 2 ) , microscopy-colocalization with upstream kinase ( 2 ) , mutation of modification site ( 1 , 2 , 3 , 4 ) , phospho-antibody ( 1 , 2 ) , western blotting ( 1 , 2 )
Disease tissue studied:
colorectal cancer ( 1 ) , colorectal carcinoma ( 1 )
Relevant cell line - cell type - tissue:

Upstream Regulation
Regulatory protein:
FAT (human) ( 2 )
Treatments:
arsenite ( 4 ) , DCVC ( 2 ) , SB203580 ( 2 ) , SP600125 ( 2 )

Downstream Regulation
Effects of modification on HSP27:
activity, induced ( 3 ) , molecular association, regulation ( 1 , 4 )
Effects of modification on biological processes:
apoptosis, altered ( 2 )
Induce interaction with:
IKKA (human) ( 1 )
Inhibit interaction with:
HSP27 (hamster) ( 4 )

References 

1

Kammanadiminti SJ, Chadee K (2006) Suppression of NF-kappaB activation by Entamoeba histolytica in intestinal epithelial cells is mediated by heat shock protein 27. J Biol Chem 281, 26112-20
16840786   Curated Info

2

de Graauw M, et al. (2005) Heat shock protein 27 is the major differentially phosphorylated protein involved in renal epithelial cellular stress response and controls focal adhesion organization and apoptosis. J Biol Chem 280, 29885-98
15944157   Curated Info

3

Thériault JR, et al. (2004) Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27. J Biol Chem 279, 23463-71
15033973   Curated Info

4

Lambert H, et al. (1999) HSP27 multimerization mediated by phosphorylation-sensitive intermolecular interactions at the amino terminus. J Biol Chem 274, 9378-85
10092617   Curated Info