Curated Information
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Home > Curated Information Page > PubMed Id: 10961991
Minty A, Dumont X, Kaghad M, Caput D (2000) Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J Biol Chem 275, 36316-23 10961991
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, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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K627-sm - p73 (human)
Modsite: KARKQPIkEEFTEAE SwissProt Entrez-Gene
Orthologous residues
p73 (human): K627‑sm, p73 iso2 (human): , p73 iso8 (human): K578‑sm, p73 iso10 (human): , p73 (mouse): K622‑sm
Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site
Disease tissue studied:  soft tissue cancer
Relevant cell lines - cell types - tissues:  SK-N-MC (neural crest)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
SUMO LIGASE SUMO1 (human) modification site within consensus motif, transfection of wild-type enzyme
Downstream Regulation
Effect of modification (function):  intracellular localization, protein degradation