UBE2L6 Human

Ubiquitin Conjugating Enzyme E2L 6 (UBE2L6), also known as UBCH8, is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme plays a crucial role in the ubiquitination process, which is a fundamental cellular mechanism for targeting abnormal or short-lived proteins for degradation. The UBE2L6 gene is located on chromosome 11 in humans and encodes a protein that is highly similar in primary structure to the enzyme encoded by the UBE2L3 gene .

Ubiquitination involves three main classes of enzymes:

1. Ubiquitin-activating enzymes (E1s): These enzymes activate ubiquitin in an ATP-dependent manner.
2. Ubiquitin-conjugating enzymes (E2s): These enzymes, including UBE2L6, transfer the activated ubiquitin from the E1 enzyme to the target protein.
3. Ubiquitin-protein ligases (E3s): These enzymes facilitate the transfer of ubiquitin from the E2 enzyme to the lysine residues on the target protein .

UBE2L6 is involved in the covalent attachment of ubiquitin or ISG15 to other proteins. This process is essential for various cellular functions, including protein degradation, DNA repair, cell cycle regulation, and response to stress and infection. UBE2L6 specifically functions in the E6/E6-AP-induced ubiquitination of p53/TP53 and promotes the ubiquitination and subsequent proteasomal degradation of FLT3 .

UBE2L6 is expressed in various tissues, including granulocytes, monocytes, and lymph nodes. It is predominantly localized in the cytosol and nucleoplasm, where it participates in the ubiquitin ligase complex .

Mutations or dysregulation of UBE2L6 have been associated with several diseases, including Alzheimer’s disease and Parkinson’s disease. The enzyme’s role in protein degradation pathways makes it a potential target for therapeutic interventions in these and other neurodegenerative disorders .