Curated Information
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Curated Information Page
PubMed Id: 2507541 
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.
Lees-Miller SP, Anderson CW (1989) The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues. J Biol Chem 264, 17275-80 2507541
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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T5-p - HSP90A (human)
Orthologous residues
HSP90A (human): T5‑p, HSP90A iso2 (human): T127‑p, HSP90A (mouse): T5‑p, HSP90A (rat): T5‑p, HSP90A (hamster): T4‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE DNAPK (human)

T7-p - HSP90A (human)
Orthologous residues
HSP90A (human): T7‑p, HSP90A iso2 (human): T129‑p, HSP90A (mouse): T7‑p, HSP90A (rat): T7‑p, HSP90A (hamster): T6‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE DNAPK (human)


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