Ubiquitin Specific Protease 25 (USP25), a member of the deubiquitinase family, 
is involved in several disease-related signal pathways including myogenesis, 
immunity and protein degradation. It specially catalyzes the hydrolysis of the 
K48-linked and K63-linked polyubiquitin chains. USP25 contains one 
ubiquitin-associated domain and two ubiquitin-interacting motifs (UIMs) in its 
N-terminal region, which interact with ubiquitin and play a role in substrate 
recognition. Besides, it has been shown that the catalysis activity of USP25 is 
either impaired by sumoylation or enhanced by ubiquitination within its UIM. To 
elucidate the structural basis of the cross-regulation of USP25 function by 
non-covalent binding and covalent modifications of ubiquitin and SUMO2/3, a 
systematic structural biology study of USP25 is required. Here, we report the 
(1)H, (13)C and (15)N backbone and side-chain resonance assignments of the 
N-terminal ubiquitin binding domains (UBDs) of USP25 with BMRB accession number 
of 19111, which is the first step of the systematic structural biology study of 
the enzyme.