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The reversible protein phosphorylation on serine, threonine, and tyrosine (Ser/Thr/Tyr) is a key post-translational modification in eukaryotes with stunning regulatory and signalling potential [1].
In the quest for the origin and evolution of protein phosphorylation, the major regulatory post-translational modification in eukaryotes, the members of archaea, the "third domain of life", play a protagonistic role.
The ubiquitin signal is an important protein modification in eukaryotes.
DNA methylation is a stably inherited epigenetic modification in eukaryotes.
Asparagine N-Glycosylation is one of the most important forms of protein post-translational modification in eukaryotes.
Database URL: http://www.phosphogrid.org/ Protein phosphorylation is the most thoroughly documented and characterized post-translational protein modification in eukaryotes.
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Ubiquitination is a well-known post-transcriptional modification in eukaryote.
Asparagine-linked (N-linked) protein glycosylation is the most abundant of all posttranslational modifications in eukaryotes, with nearly 70% of all eukaryotic proteins predicted to be N-glycoproteins [ 18].
The great majority of modifications in eukaryotes and archaea are 2′-O-ribose methylated nucleosides and pseudouridines.
The ability to accomplish post-translational modifications in eukaryotes, ability to grow to very high cell densities and the ability of protein secretions into fermentation media are the additional benefits of yeast expression systems.
The well-developed methylation systems of certain heteroloboseans, stramenopiles, chlorophytes, and haptophyte indicate that these might be new model systems to explore the relevance of DNA modifications in eukaryotes.
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