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"The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues." |
Lees-Miller SP, Anderson CW |
Published Oct. 15, 1989 in J Biol Chem volume 264 .
Pubmed ID: 2507541
Abstract:
| The 90-kDa heat-shock protein, hsp90, is an abundant cytoplasmic protein that can be phosphorylated in vitro by a double-stranded (ds) DNA-activated protein kinase found in cells from several species. Here we show that the dsDNA-activated protein kinase from human HeLa cells phosphorylates 2 threonine residues in the sequence PEETQTQDQPME at the amino terminus of human hsp90 alpha. Hsp90 beta, which is 97% identical to hsp90 alpha but lacks both amino-terminal threonines, is not phosphorylated by the dsDNA-activated protein kinase. Mouse hsp86 and rabbit hsp90 alpha are homologous to human hsp90 alpha; both heterologous proteins are phosphorylated at the same amino-terminal threonines by the human dsDNA-activated protein kinase. |
This publication refers to following REPAIRtoire entries:
| Proteins |
Last modification of this entry: Oct. 6, 2010
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