EC Number   |
General Information |
Reference |
|---|
   2.7.7.31 | metabolism |
enzyme is ubiquitylated by a BPOZ-2/Cul3 complex, as the ubiquitin ligase, and then degraded by the 26 S proteasome. Enzyme is ubiquitylated by the Cul3-based ubiquitylation system in vitro and may also be directly ubiquitylated by the E2 proteins UbcH5a/b/c and UbcH6, E3-independently. Ubiquitylation inhibits the nucleotidyltransferase activity |
723573 |
| 2.7.7.31 | physiological function |
in cells overexpressing terminal deoxynucleotidyltransferase, the enzyme suppresses DNA repair that is based on short (one- or two-base) homology regions, to efficiently add deoxynucleotides during VDJ recombination in lymphoid cells |
738253 |
| 2.7.7.31 | physiological function |
in Chinese hamster ovary cells, ectopic expression of the enzmye efficiently promotes N-additions at the junction of chromosomal double-strand breaks generated by the meganuclease I-SceI. The size of the N-additions is comparable with that at V(D)J junctions. No N-addition is observed in KU80- or XRCC4-deficient cells |
723297 |
| 2.7.7.31 | physiological function |
TdT also has a templated-polymerase activity, in the presence of higher concentrations of a downstream DNA duplex, and performs a micro-homology single base-pair search to align the DNA synapsis. Both templated and untemplated activities of TdT are needed to explain the distributions of lengths of N regions observed experimentally in T cell receptors and antibodies |
739723 |
| 2.7.7.31 | physiological function |
the genetic variations generated by the hTdT single-nucleotide polymorphisms will vary the human immune repertoire and thus its responses. In vitro, six natural variants of TdT differ from wild-type TdT in polymerization ability, with four having significantly lower activity. In vivo, the presence of TdT varies both the efficiency of recombination and N-addition, with two variants generating coding joints with significantly fewer N-additions |
738328 |
