3.3.4 ǀ Post-translational modifications (PTMs)
C-mannosylation sites and N-terminal acetylation sites were not found in
the cpOAS1 protein (FIGURE 9S). cpOAS1 is a non-GPI-anchor protein
(FIGURE 9S). Based on the analysis of the NetNglyc server, a potential
N-linked glycosylation site was not found in the cpOAS1 protein (FIGURE
9S). Potentially two predicted mucin type GalNAc O-glycosylation sites
were found in the cpOAS1 (FIGURE 6A). Nine glycation sites at amino
groups of lysine residue were present in the cpOAS1 protein and these
sites are shown in Figure 6B. Various predicted phosphorylation sites in
the cpOAS1 protein sequence are shown in Table 6 and Figure 9S. In the
cpOAS1,14-serine, 8- threonine and 1-tyrosine residues were found. One
potential arginine and lysine propeptide cleavage site was predicted in
the cpOAS1 (Data not shown). Different 10 internal acetylation sites by
PAIL software were predicted in the cpOAS1 (Table 7). Sumoylation sites
in the cpOAS1 protein under the medium threshold were presented in Table
8. In the cpOAS1, two sumoylation sites at 62 and 280 positions were
found. and eight cysteines are found at positions: 53, 122, 134, 164,
190, 215, 240 and 277. The two most probable pattern of pairs 134-277,
164-190, were found using the CYS_REC tool.