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OTU domain, ubiquitin aldehyde binding 1

otubain 1, OTUB1, Otubain, OTU-1, OTU-domain containing ubiquitin aldehyde binding protein 1, ubiquitin-specific protease otubain 1
The product of this gene is a member of the OTU (ovarian tumor) superfamily of predicted cysteine proteases. The encoded protein is a highly specific ubiquitin iso-peptidase, and cleaves ubiquitin from branched poly-ubiquitin chains but not from ubiquitinated substrates. It interacts with another ubiquitin protease and an E3 ubiquitin ligase that inhibits cytokine gene transcription in the immune system. It is proposed to function in specific ubiquitin-dependent pathways, possibly by providing an editing function for polyubiquitin chain growth. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, fibrillin-1, V1a, Flu, OTUB2
Papers on otubain 1
FIH Regulates Cellular Metabolism through Hydroxylation of the Deubiquitinase OTUB1.
Taylor et al., Dublin, Ireland. In Plos Biol, Jan 2016
Here, we demonstrate that the deubiquitinase ovarian tumor domain containing ubiquitin aldehyde binding protein 1 (OTUB1) is a substrate for hydroxylation by FIH on N22.
PTEN regulates RPA1 and protects DNA replication forks.
Yin et al., Beijing, China. In Cell Res, Nov 2015
PTEN recruits the deubiquitinase OTUB1 to mediate RPA1 deubiquitination.
Short-term exposure to benzo[a]pyrene disrupts reproductive endocrine status in the swimming crab Portunus trituberculatus.
Pan et al., Taiwan. In Comp Biochem Physiol C Toxicol Pharmacol, Aug 2015
The following were investigated: (1) Gonadosomatic Index (GSI) and oocyte diameter, (2) steroid concentrations in ovary and hemolymph, and (3) mRNA levels of genes involved in sex steroid synthesis (3β-HSD,17β-HSD) or reproduction (estrogen receptor (ER), OUT (Ovarian tumor gene) domain containing ubiquitin aldehyde-binding protein 1 (OTUB1), vitellogenin (VTG),vasa).
OTUB1 inhibits the ubiquitination and degradation of FOXM1 in breast cancer and epirubicin resistance.
Lam et al., London, United Kingdom. In Oncogene, Aug 2015
Initial co-immunoprecipitation studies verified previous proteomic analysis finding that the OTUB1 is a novel FOXM1-interacting protein.
Proteomic profiling of SupT1 cells reveal modulation of host proteins by HIV-1 Nef variants.
Tripathi et al., Lucknow, India. In Plos One, 2014
Proteins were identified as Cyclophilin A, EIF5A-1 isoform B, Rho GDI 1 isoform a, VDAC1, OTUB1 and α-enolase isoform 1 (ENO1) through LC-MS/MS.
Casein kinase 2 (CK2) phosphorylates the deubiquitylase OTUB1 at Ser16 to trigger its nuclear localization.
Sapkota et al., Padova, Italy. In Sci Signal, 2014
The deubiquitylating enzyme OTUB1 is present in all tissues and targets many substrates, in both the cytosol and nucleus.
OTUB1 de-ubiquitinating enzyme promotes prostate cancer cell invasion in vitro and tumorigenesis in vivo.
Flores-Morales et al., Copenhagen, Denmark. In Mol Cancer, 2014
RhoA activity was measured in relation with OTUB1 effects on prostate cancer cell invasion.
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.
Deubiquitinating enzyme regulation of the p53 pathway: A lesson from Otub1.
Dai et al., Portland, United States. In World J Biol Chem, 2014
We recently reported that Otub1, a DUB from the OTU-domain containing protease family, is a novel p53 regulator.
OTUB1 promotes metastasis and serves as a marker of poor prognosis in colorectal cancer.
Huang et al., Guangzhou, China. In Mol Cancer, 2013
BACKGROUND: OTUB1 (OTU deubiquitinase, ubiquitin aldehyde binding 1) is a deubiquitinating enzyme (DUB) that belongs to the OTU (ovarian tumor) superfamily.
Proteomic profile of pre - B2 lymphoblasts from children with acute lymphoblastic leukemia (ALL) in relation with the translocation (12; 21).
Vannier et al., Rouen, France. In Clin Proteomics, 2013
Level of expression of proteasome subunit beta type-2 (p ≤ 0.01) and protein casein kinase 2α (p ≤ 0.01) which both favored apoptosis, deubiquitinating enzyme OTUB1 (p ≤ 0.05) and MLL septin-like fusion protein MSF-B, septin 9 i4 (p ≤ 0.01) were in accord with a good prognosis related to t(12;21) lymphoblasts.
The biology of A20-like molecules.
Evans et al., In Adv Exp Med Biol, 2013
The human genome contains 15 members of the OTU family including the deubiquitinating enzymes Cezanne, VCIP135 and Otubain 1.
Molecular basis of Lys-63-linked polyubiquitination inhibition by the interaction between human deubiquitinating enzyme OTUB1 and ubiquitin-conjugating enzyme UBC13.
Fukai et al., Tokyo, Japan. In J Biol Chem, 2012
the crystal structure of human OTUB1 in complex with human UBC13 and MMS2
The mechanism of OTUB1-mediated inhibition of ubiquitination.
Wolberger et al., Baltimore, United States. In Nature, 2012
structural and biochemical studies elucidating how OTUB1 inhibits UBC13 and other E2 enzymes
OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function.
Durocher et al., Toronto, Canada. In Mol Cell, 2012
OTUB1 therefore co-opts Lys48-linked ubiquitin chain recognition to suppress ubiquitin conjugation and the DNA damage response
Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1.
Dai et al., Portland, United States. In Embo J, 2012
Overexpression of Otub1(D88A) or ablation of endogenous Otub1 by siRNA markedly impaired p53 stabilization and activation in response to DNA damage. Together, these results reveal a novel function for Otub1 in regulating p53 stability and activity
Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1.
Durocher et al., Tokyo, Japan. In Nature, 2010
OTUB1, a deubiquitinating enzyme, is an inhibitor of double-strand break-induced chromatin ubiquitination
Two isoforms of otubain 1 regulate T cell anergy via GRAIL.
Fathman et al., Stanford, United States. In Nat Immunol, 2004
Here we show that GRAIL is associated with and regulated by two isoforms of the ubiquitin-specific protease otubain 1.
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