1H, 13C and 15N backbone and side-chain resonance assignments of the ZnF-UBP domain of USP20/VDU2

Deubiquitinase USP20/VDU2 has been identified as a regulator of multiple proteins including hypoxia-inducible factor (HIF)-1α, β2-adrenergic receptor, and tumor necrosis factor receptor associated factor 6 etc. It contains four structural domains, including an N-terminal zinc-finger ubiquitin binding domain (ZnF-UBP) that potentially helps USP20 to recruit its ubiquitin substrates. Here we report the ¹H, ¹³C and ¹⁵N backbone and side-chain resonance assignments of the ZnF-UBP domain of USP20/VDU2. The BMRB accession number is 26901. The secondary structural elements predicted from the NMR data reveal a global fold consisting of three α-helices and four β-strands. The complete assignments can be used to explore the protein dynamics of the USP20 ZnF-UBP and its interactions with monoubiquitin and ubiquitin chains.