gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

OTU domain containing 5

This gene encodes a member of the OTU (ovarian tumor) domain-containing cysteine protease superfamily. The OTU domain confers deubiquitinase activity and the encoded protein has been shown to suppress the type I interferon-dependent innate immune response by cleaving the polyubiquitin chain from an essential type I interferon adaptor protein. Cleavage results in disassociation of the adaptor protein from a downstream signaling complex and disruption of the type I interferon signaling cascade. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Oct 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, A20, SIGIRR, SBS, IL-1ra
Papers on Duba
A Structural View of Negative Regulation of the Toll-like Receptor-Mediated Inflammatory Pathway.
Nussinov et al., İstanbul, Turkey. In Biophys J, Oct 2015
Structural data suggest that 1) Toll/IL-1R (TIR) domain-containing regulators (BCAP, SIGIRR, and ST2) interfere with TIR domain signalosome formation; 2) major deubiquitinases such as A20, CYLD, and DUBA prevent association of TRAF6 and TRAF3 with their partners, in addition to removing K63-linked ubiquitin chains that serve as a docking platform for downstream effectors; 3) alternative downstream pathways of TLRs also restrict signaling by competing to bind common partners through shared binding sites.
The Preclinical Profile of the Duocarmycin-Based HER2-Targeting ADC SYD985 Predicts for Clinical Benefit in Low HER2-Expressing Breast Cancers.
Dokter et al., Nijmegen, Netherlands. In Mol Cancer Ther, Mar 2015
SYD985 is a HER2-targeting antibody-drug conjugate (ADC) based on trastuzumab and vc-seco-DUBA, a cleavable linker-duocarmycin payload.
DUBA-UBR5 axis: other than transactivation.
Kuchroo et al., Boston, United States. In Cell Res, Mar 2015
A recent publication by Rutz et al. in Nature describes a novel deubiquitylating enzyme DUBA as a negative regulator for IL-17 by regulating stability of RORγt, the master transcription factor that induces Th17 cells.
A putative OTU domain-containing protein 1 deubiquitinating enzyme is differentially expressed in thyroid cancer and identifies less-aggressive tumours.
Ward et al., Campinas, Brazil. In Br J Cancer, 2014
We have further identified an OTU domain-containing protein 1, DUBA-7 deubiquitinating enzyme as the scFv-binding antigen using two-dimensional polyacrylamide gel electrophoresis and mass spectrometry.
Pattern-recognition receptor signaling regulator mRNA expression in humans and mice, and in transient inflammation or progressive fibrosis.
Lech et al., München, Germany. In Int J Mol Sci, 2012
We therefore determined the mRNA expression levels of A20, CYLD, DUBA, ST2, CD180, SIGIRR, TANK, SOCS1, SOCS3, SHIP, IRAK-M, DOK1, DOK2, SHP1, SHP2, TOLLIP, IRF4, SIKE, NLRX1, ERBIN, CENTB1, and Clec4a2 in human and mouse solid organs.
Phosphorylation meets proteolysis.
Farady et al., Basel, Switzerland. In Structure, 2012
Huang and colleagues and Velázquez-Delgado and Hardy (this issue of Structure) describe how phosphorylation activates the protease activity of the deubiquitinating enzyme DUBA and how it inhibits caspase-6, respectively.
Phosphorylation-dependent activity of the deubiquitinase DUBA.
Cochran et al., San Francisco, United States. In Nat Struct Mol Biol, 2012
Here the authors show that phosphorylation of the human deubiquitinase DUBA (OTUD5) at a single residue, Ser177, is both necessary and sufficient to activate the enzyme.
Interleukin 1 receptor signaling regulates DUBA expression and facilitates Toll-like receptor 9-driven antiinflammatory cytokine production.
Raz et al., San Diego, United States. In J Exp Med, 2011
Deubiquitinating enzyme A (DUBA), which selectively cleaves K63-linked ubiquitin chains from TRAF3, was up-regulated in the absence of IL-1R1 signaling.
DUBA: a deubiquitinase that regulates type I interferon production.
Dixit et al., San Francisco, United States. In Science, 2008
data identify DUBA as a negative regulator of innate immune responses
share on facebooktweetadd +1mail to friends