Cellular structures called proteasomes recognize and digest proteins tagged with ubiquitin.

[5][6] Further work is thus needed to delineate a complete map of UBE3A imprinting in humans and model organisms such as mice.

Silencing of Ube3a on the paternal allele is thought to occur through the Ube3a-ATS part of a lincRNA called "LNCAT"[7] (Large Non-Coding Antisense Transcript).

Like mutations within the gene, these chromosomal changes prevent any functional ubiquitin protein ligase E3A from being produced in the brain.

This interaction promotes the polyubiquitination and subsequent degradation of the tumor suppressor gene p53, thereby enabling the immortalization of infected cells.