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Abstract Angelman syndrome is a severe neurodevelopmental disorder caused by the loss of UBE3A, a gene that encodes an E3 ubiquitin ligase1,2. The mechanisms that underlie Angelman syndrome are not well understood, and in particular, the link between UBE3A substrates and disease phenotypes remains uncertain3. Here, using gain- and loss-of-function mutations in UBE3A4,5 along with unbiased proteomics, we show that asparagine synthetase (ASNS) is a target of UBE3A.
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