ArticleProtein science : a publication of the Protein Society2010
Solution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitin.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- UBTD1 Drives Ovarian Cancer Progression via Mutation-Associated Alterations, Stromal Microenvironment Remodeling, and TNF/AP-1 Signaling.Human mutation · 2026Article
- Increases in compulsivity, inflammation, and neural injury in HIV transgenic rats with escalated methamphetamine self-administration under extended-access conditions.Brain research · 2020Article
- A ubiquitin shuttle DC-UbP/UBTD2 reconciles protein ubiquitination and deubiquitination via linking UbE1 and USP5 enzymes.PloS one · 2014Article
- Ubiquitin and its binding domains.Frontiers in bioscience (Landmark edition) · 2012Review
- Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin.PloS one · 2011Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
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Abstract
DC-UbP/UBTD2 is a ubiquitin (Ub) domain-containing protein first identified from dendritic cells, and is implicated in ubiquitination pathway. The solution structure and backbone dynamics of the C-terminal Ub-like (UbL) domain were elucidated in our previous work. To further understand the biological function of DC-UbP, we then solved the solution structure of the N-terminal domain of DC-UbP (DC-UbP_N) and studied its Ub binding properties by NMR techniques. The results show that DC-UbP_N holds a novel structural fold and acts as a Ub-binding domain (UBD) but with low affinity. This implies that the DC-UbP protein, composing of a combination of both UbL and UBD domains, might play an important role in regulating protein ubiquitination and delivery of ubiquitinated substrates in eukaryotic cells.
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