The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2L3 is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-kB precursor p105 in vitro.
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Protein Aliases: E2 ubiquitin-conjugating enzyme L3; L-UBC; UbcH7; UbcM4; Ubiquitin carrier protein L3; ubiquitin conjugating enzyme E2L 3; ubiquitin-conjugating enzyme 7; Ubiquitin-conjugating enzyme E2 L3; Ubiquitin-conjugating enzyme E2-F1; ubiquitin-conjugating enzyme E2L 3; ubiquitin-conjugating enzyme UBCH7; Ubiquitin-protein ligase L3
Gene Aliases: C79827; E2-F1; L-UBC; UBCE7; UBCH7; UbcM4; UBE2L3
Molecular Function: ligase