EC Number   |
Natural Substrates |
|---|
   2.4.1.255 | more |
catalyses the O-linked attachment of single GlcNAc moieties to serine and threonine residues on many cytosolic or nuclear proteins |
| 2.4.1.255 | more |
catalyzes the attachment of GlcNAc monosaccharides to the hydroxyl group of serine or threonine residues of intracellular proteins and may play an important role in the hexosamine pathway |
| 2.4.1.255 | more |
catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to Ser/Thr residues of proteins |
| 2.4.1.255 | more |
catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders |
| 2.4.1.255 | more |
catalyzes the transfer of O-linked GlcNAc to serine/threonine residues of a variety of target proteins, many of which have been implicated in such diseases as diabetes and neurodegeneration |
| 2.4.1.255 | more |
enzyme catalyzes the abundant and dynamic posttranslational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) |
| 2.4.1.255 | more |
enzyme transfers N-acetylglucosamine from UDP-GlcNAc to selected serine and threonine residues |
| 2.4.1.255 | more |
O-GlcNAc transferase, the enzyme that adds O-GlcNAc to proteins, exists in stable and active complexes with the serine/threonine phosphatases PP1beta and PP1gamma, enzymes that remove phosphate from proteins |
| 2.4.1.255 | more |
p110 subunit of the enzyme forms both homo- and heterotrimers that appear to have different binding affinities for UDP-GlcNAc |
| 2.4.1.255 | more |
regulates breast cancer tumorigenesis through targeting of the oncogenic transcription factor FoxM1 |
