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Literature summary for 2.7.7.31 extracted from
- Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity (2012), PLoS ONE, 7, e39511.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli and in 293T cell | Bos taurus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| thymus | - |
Bos taurus | - |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Bos taurus |
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Release 2023.1 (January 2023)
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