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.
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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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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