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Most modification sites are in the C-terminal domain, although a modification site at human topoIIα residue S29 that is a substrate for protein kinase C has also been identified [6].
Post-translational modification sites are frequently marked by short conserved motifs in a variety of protein matrices (e.g. [7], [8]), and sites of cuticular protein modification or cross-linking are likely to be similarly conserved.
Because PHB (as well as few other insulin signaling intermediates such as IRS, Akt, GLUT4 etc) undergoes both O-GlcNAc modification and tyrosine phosphorylation and these modification sites are either adjacent or in the close proximity to each other we hypothesize that O-GlcNAc modification and tyrosine phosphorylation may be a previously unidentified novel binary switch.
After chemical or enzymatic probing, modification sites are sought.
The possible posttranslational modification sites are predicted by PROSITE (http://prosite.expasy.org/).org/
Consistent with this notion, putative modification sites are spread widely within the length of a miRNA molecule (Fig. 3).
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The identification of protein modification sites is an important step toward understanding the biological role of covalent modifications.
A total of 1428 acetylated proteins with 3163 unique modification sites were identified, which is dramatically higher than those in other previously reported microorganisms (Table 1).
The results showed that 52% of proteins contained only one acetylation site, and the percentage of proteins with two, three, four and five or more modification sites were 21, 12, 6, and 9%, respectively (Fig. 4a).
Also, a few new DMS modification sites were found under such condition, suggesting changes in local structure due to protein binding.
Perhaps proximity of the two modification sites is important.
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