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O-GlcNAc (b-O-linked N-acetylglucosamine) is a ubiquitous and dynamic post-translational modification present on numerous cytoplasmic and nuclear proteins and is thought to play a regulatory role in numerous cellular processes including homeostatic mechanisms and gene expression. OGT (O-linked N-acetylglucosamine (GlcNAc) transferase) catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residues whereas OGA / O-GlcNAcase (O-linked N-acetylglucosamine (GlcNAc)-ase) is a glycosidase that removes O-GlcNAc. O-GlcNAc modifications have been described to directly regulate the activities of a variety of transcription factors including Sp1, estrogen receptors, STAT5, NF-kB, p53, YY1, Elf-1, c-Myc, Rb, PDX-1, CREB, fork-head, and others. In addition, RNA polymerase II and the basal transcription factors are also extensively modified by O-GlcNAc. O-GlcNAc modification has been reported to suppress or enhance transcription, depending on the promoter and other associated proteins.