The SOX2 domain structures and the posttranslational modification sites. SOX2 protein consists of 317 amino acids with three functional domains: high mobility group (HMG) domain at the N-terminus, dimerization (DIM) domain at the center, and transactivation (TAD) domain at the C-terminus. SOX2 is subjected to modification at the posttranslational level by acetylation, phosphorylation, SUMOylation, ubiquitylation, methylation, O-Glycosylation, and PARPylation. Note that the PARPylation site has not been identified
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