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OTU domain, ubiquitin aldehyde binding 2

This gene encodes one of several deubiquitylating enzymes. Ubiquitin modification of proteins is needed for their stability and function; to reverse the process, deubiquityling enzymes remove ubiquitin. This protein contains an OTU domain and binds Ubal (ubiquitin aldehyde); an active cysteine protease site is present in the OTU domain. [provided by RefSeq, Aug 2011] (from NCBI)
Top mentioned proteins: Ubiquitin, otubain 1, fibrillin-1, ISG15, NEDD8
Papers on OTUB2
The human otubain2-ubiquitin structure provides insights into the cleavage specificity of poly-ubiquitin-linkages.
Kessler et al., Oxford, United Kingdom. In Plos One, 2014
Here we report the crystal structure of human otubain 2 (OTUB2) in complex with a ubiquitin-based covalent inhibitor, Ub-Br2.
Fine-tuning of DNA damage-dependent ubiquitination by OTUB2 supports the DNA repair pathway choice.
Nakada et al., Suita, Japan. In Mol Cell, 2014
Here, we report that depletion of the deubiquitinating enzyme OTUB2 enhances RNF8-mediated ubiquitination in an early phase of the DDR and promotes faster DSB repair but suppresses homologous recombination.
Otubain 2 is a novel promoter of beta cell survival as revealed by siRNA high-throughput screens of human pancreatic islets.
Zick et al., Israel. In Diabetologia, 2013
One such hit was the de-ubiquitinating enzyme otubain 2 (OTUB2).
Integrative gene-tissue microarray-based approach for identification of human disease biomarkers: application to amyotrophic lateral sclerosis.
Karsten et al., Los Angeles, United States. In Hum Mol Genet, 2010
This large-scale gene and protein expression study pointing to distinct molecular mechanisms of TAU- and SOD1-induced motor neuron degeneration identified several new SALS-relevant proteins (CNGA3, CRB1, OTUB2, MMP14, SLK, DDX58, RSPO2) and putative blood biomarkers, including Nefh, Prph and Mgll.
Regulation of virus-triggered signaling by OTUB1- and OTUB2-mediated deubiquitination of TRAF3 and TRAF6.
Shu et al., Wuhan, China. In J Biol Chem, 2010
Findings suggest that OTUB1 and OTUB2 negatively regulate virus-triggered type I IFN induction and cellular antiviral response by deubiquitinating TRAF3 and -6.
Structural basis and specificity of human otubain 1-mediated deubiquitination.
Kessler et al., Oxford, United Kingdom. In Biochem J, 2009
A structural analysis of OTUB1 shows differences in accessibility to the active site and in surface properties of the substrate-binding regions when compared with its close homologue, OTUB2, suggesting variations in regulatory mechanisms and substrate specificity.
A novel Otubain-like cysteine protease gene is preferentially expressed during somatic embryogenesis in Pinus radiata.
Arce-Johnson et al., Santiago, Chile. In Mol Biol Rep, 2008
The 3-D model of PrOTUBAIN showed significant similarity to human OTUBAIN2, suggesting that the plant protein may possess functions similar to that of the human protein.
Crystal structure of human otubain 2.
Balakirev et al., Grenoble, France. In Embo Rep, 2004
Data report the first crystal structure of an OTU superfamily protein, otubain 2, at 2.1 A resolution and propose a model for otubain-ubiquitin binding.
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