Literature summary extracted from

Maezawa, S.; Fukushima, R.; Matsushita, T.; Kato, T.; Takagaki, Y.; Nishiyama, Y.; Ando, S.; Matsumoto, T.; Kouda, K.; Hayano, T.; Suzuki, M.; Koiwai, K.; Koiwai, O.
Ubiquitylation of terminal deoxynucleotidyltransferase inhibits its activity (2012), PLoS ONE, 7, e39511.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.7.7.31	expression in Escherichia coli and in 293T cell	Bos taurus

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.7.7.31	Bos taurus	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
2.7.7.31	thymus	-	Bos taurus	-

General Information

EC Number	General Information	Comment	Organism
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	Bos taurus

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Release 2023.1 (January 2023)