EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.5.4.38 | phosphoprotein |
515% of the enzyme expressed in activated B cells is phosphorylated at Ser38. The modified form contributes disproportionately to hypermutation. This form of activation-induced cytidine deaminase is enriched in the chromatin fraction in activated B cells |
720891 |
| 3.5.4.38 | phosphoprotein |
activation-induced cytidine deaminase that is phosphorylated on serine residue 38 interacts with replication protein A, a ssDNA binding protein, to promote deamination of transcribed double-stranded DNA in vitro. The Ser38 phosphorylation site is required for normal class switch recombination and Ig somatic hypermutation in mice |
720897 |
| 3.5.4.38 | phosphoprotein |
in addition to Ser38, the enzyme is also phosphorylated at position Thr140. Mutation of either Ser38 or Thr140 to Ala does not impact catalytic activity, but interfers with class switching and somatic hypermutation in vivo. Ser38 is equally important for both processes, Thr140 phosphorylation preferentially affects somatic mutation |
720141 |
| 3.5.4.38 | phosphoprotein |
phosphorylation at serine 38 and threonine 140 increases activity. Activation-induced cytidine deaminase activity and its oncogenic potential can be downregulated by phosphorylation of Ser3. This process is controlled by serine/threonine protein phosphatase 2A |
720456 |
| 3.5.4.38 | phosphoprotein |
phosphorylation of S38 is essential for activation-induced deaminase interaction with replication protein A (RPA). The residue S38 is a target for phosphorylation by protein kinase A. Phosphorylation of AID significantly increases its deaminase activity on duplexDNA, although the phosphorylated enzyme still retains its preference for single-stranded substrates |
719247 |
| 3.5.4.38 | phosphoprotein |
protein kinase A phosphorylates activation-induced cytidine deaminase and regulates its activity in GC B cells. Phosphorylation targets specifically Thr27 and Ser38 |
720890 |
| 3.5.4.38 | phosphoprotein |
protein kinase A phosphorylates the Ser38. This phosphorylation event activates the enzyme to enable interaction with replication protein A, thereby augmenting the ability of activation-induced cytidine deaminase to effect class switch recombination in vivo |
720538 |
| 3.5.4.38 | ubiquitination |
the enzyme is polyubiquitinated in the nucleus. Ubiquitin-mediated nuclear degradation of the enzyme is part of a multilayer control that contributes to the regulation of enzyme function during hypermutation and class switch recombination |
720140 |
