UBE2L6
UBE2L6 (ubiquitin conjugating enzyme E2 L6, also known as UBCH8) is an E2 enzyme that catalyses the covalent attachment of ubiquitin or ISG15 to other proteins. It belongs to the ubiquitin-conjugating enzyme family and contributes to protein degradation pathways. Browse Assay Genie's current range of UBE2L6 research reagents below, or read on for the biology behind the target.
UBE2L6 catalyses the covalent attachment of ubiquitin or ISG15 to other proteins. Modification with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation, and it involves at least three classes of enzyme: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2L6 acts at the E2 step of this cascade. It functions in the E6/E6-AP-induced ubiquitination of p53/TP53, and it promotes the ubiquitination and subsequent proteasomal degradation of FLT3.
The UBE2L6 gene encodes a member of the E2 ubiquitin-conjugating enzyme family, listed by HGNC in the group of ubiquitin conjugating enzymes E2. The enzyme is highly similar in primary structure to the enzyme encoded by the UBE2L3 gene. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. Orthologous genes are present in mouse and rat, both named Ube2l6, which allows the enzyme to be studied in rodent models.
The protein is also known as UBCH8, and an earlier approved name was ubiquitin-conjugating enzyme E2L 6. The UniProt name, ubiquitin/ISG15-conjugating enzyme E2 L6, reflects its dual activity with both ubiquitin and the ubiquitin-like modifier ISG15. Researchers studying UBE2L6 often investigate how a single E2 enzyme can serve ubiquitination and ISG15 conjugation, and how it contributes to the turnover of specific substrates such as p53 and FLT3.
As an E2 enzyme, UBE2L6 supports the ubiquitination that targets abnormal or short-lived proteins for degradation.
UBE2L6 catalyses attachment of ISG15 as well as ubiquitin to target proteins, making it relevant to ISGylation research.
UBE2L6 functions in E6/E6-AP-induced ubiquitination of p53/TP53, linking this E2 enzyme to p53 turnover.
UBE2L6 promotes ubiquitination and proteasomal degradation of FLT3, so it is relevant to studies of FLT3 protein stability.
UBE2L6 is an E2 enzyme that catalyses the covalent attachment of ubiquitin or ISG15 to other proteins. It functions in E6/E6-AP-induced ubiquitination of p53/TP53 and promotes ubiquitination and proteasomal degradation of FLT3.
UBE2L6 is also called UBCH8, and its previous name was ubiquitin-conjugating enzyme E2L 6. UniProt names it ubiquitin/ISG15-conjugating enzyme E2 L6. Two alternatively spliced transcript variants encoding distinct isoforms have been reported for the gene.
UBE2L6 is highly similar in primary structure to the enzyme encoded by UBE2L3. Mouse and rat both have an ortholog named Ube2l6. Check the datasheet of any product for its validated reactivity.
Other ubiquitin-conjugating E2 enzymes and related ubiquitin ligase targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O14933; product specifications from Assay Genie datasheets.