Curated Information
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Curated Information Page
PubMed Id: 18669639 
Zhang YY, Mei ZQ, Wu JW, Wang ZX (2008) Enzymatic activity and substrate specificity of mitogen-activated protein kinase p38alpha in different phosphorylation states. J Biol Chem 283, 26591-601 18669639
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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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T180-p - P38A (mouse)
Orthologous residues
P38A (human): T180‑p, P38A iso2 (human): T180‑p, P38A (mouse): T180‑p, P38A iso3 (mouse): T180‑p, P38A (rat): T180‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE MKK6 (human)
PHOSPHATASE PPPM1A (human)
PHOSPHATASE MKP-5 (human)
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced

Y182-p - P38A (mouse)
Orthologous residues
P38A (human): Y182‑p, P38A iso2 (human): Y182‑p, P38A (mouse): Y182‑p, P38A iso3 (mouse): Y182‑p, P38A (rat): Y182‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
PHOSPHATASE PTP-SL (human)
KINASE MKK6 (human)
PHOSPHATASE HePTP (human)
PHOSPHATASE MKP-5 (human)
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced


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