Curated Information
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Curated Information Page
PubMed Id: 19174562 
Zimnik S, Gaestel M, Niedenthal R (2009) Mutually exclusive STAT1 modifications identified by Ubc9/substrate dimerization-dependent SUMOylation. Nucleic Acids Res 37, e30 19174562
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.
Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
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K386-sm - p53 (human)
Orthologous residues
p53 (human): K386‑sm, p53 (mouse): K380‑sm, p53 iso2 (mouse): K375‑sm, p53 (rat): K384‑sm, p53 (rabbit): K384‑sm, p53 (monkey): K386‑sm

Y701-p - STAT1 (human)
Orthologous residues
STAT1 (human): Y701‑p, STAT1 iso2 (human): Y701‑p, STAT1 (mouse): Y701‑p, STAT1 (rat): Y701‑p
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
IFN-beta increase
Downstream Regulation
 Effect of modification (function):  sumoylation
 Comments:  inhibits K703 sumoylation

K703-sm - STAT1 (human)
Orthologous residues
STAT1 (human): K703‑sm, STAT1 iso2 (human): K703‑sm, STAT1 (mouse): K703‑sm, STAT1 (rat): K703‑sm

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