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, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E1 ubiquitin-activating enzyme family. The encoded enzyme is a retinoid target that triggers promyelocytic leukemia (PML)/retinoic acid receptor alpha (RARalpha) degradation and apoptosis in acute promyelocytic leukemia, where it is involved in the conjugation of the ubiquitin-like interferon-stimulated gene 15 protein. [provided by RefSeq, Jul 2008].
Kitareewan, Pitha-Rowe, Sekula, Lowrey, Nemeth, Golub, Freemantle, Dmitrovsky: "UBE1L is a retinoid target that triggers PML/RARalpha degradation and apoptosis in acute promyelocytic leukemia." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 6, pp. 3806-11, (2002) (PubMed).
Carritt, Kok, van den Berg, Osinga, Pilz, Hofstra, Davis, van der Veen, Rabbitts, Gulati: "A gene from human chromosome region 3p21 with reduced expression in small cell lung cancer." in: Cancer research, Vol. 52, Issue 6, pp. 1536-41, (1992) (PubMed).