title: ¹H, ¹³C and ¹⁵N backbone and side-chain resonance assignments of the N-terminal ubiquitin-binding domains of the human deubiquitinase Usp28.
abstract: Deubiquitinases (DUBs) reversibly remove ubiquitin tags from polypeptides and play crucial regulatory roles in multiple cellular processes. Ubiquitin-specific protease 28 (Usp28), a member of the DUB family, exerts its deubiquitination function on key protein molecules in a couple of cancer-associated pathways, likely acting as an oncogenic factor in vivo. The N-terminal ubiquitin-binding domains (UBDs) of Usp28 are potentially required for the full catalytic capacity of Usp28 toward ubiquitin chains. Here we report the expression, purification and (1)H, (13)C and (15)N backbone and side-chain resonance assignments of the N-terminal UBDs of Usp28. The BMRB accession number is 19077.
authors.affiliation: Department of Analytical Chemistry, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
authors.forename: Yi
authors.initials: Y
authors.lastname: Wen
authors.forename: Rong
authors.initials: R
authors.lastname: Cui
authors.forename: Huaqun
authors.initials: H
authors.lastname: Zhang
authors.forename: Naixia
authors.initials: N
authors.lastname: Zhang
mesh_terms: D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D025801:Ubiquitin / Q000378:metabolism*; D043222:Ubiquitin Thiolesterase / Q000737:chemistry* / Q000378:metabolism*
chemical_list: C442902:USP28 protein, human; D025801:Ubiquitin; D043222:Ubiquitin Thiolesterase