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In general, SUMO modifications may function to modulate protein subcellular localization, protein-protein interactions, or affect other secondary protein modifications.
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The attachment of SUMO moieties to their substrate targets regulates many relevant physiological processes by modulating enzyme activity, activating transcription factors (TFs), shifting protein subcellular localizations, and eventually, determining their substrate fate.
The diversity of structure within the phosphoprotein phosphatase (PPP) and the protein phosphatase, Mg2+/Mn2+-dependent (PPM) families is generated by regulatory subunits and domains that function to modulate protein specificity and to localize the phosphatase to particular subcellular locations.
Protein phosphorylation often leads to structural changes in proteins, and such changes can directly modulate protein activity and reflect changes in interaction partners or subcellular localization [ 14].
(C) Protein subcellular localization.
Fortunately, many computational methods are available for predicting protein subcellular localization.
There are many reliable bioinformatics tools available to predict protein subcellular localization.
Upon molecular recognition a ligand can modulate protein function, thereby enhancing, inhibiting or modulating its activity.
This modification can modulate protein function [24].
Protein subcellular localization was predicted by WoLF PSORT [ 46].
Knowing accurate protein subcellular localization is important for this study.
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