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Ubiquitin specific peptidase 25

Ubiquitin (MIM 191339) is a highly conserved 76-amino acid protein involved in regulation of intracellular protein breakdown, cell cycle regulation, and stress response. Ubiquitin is released from degraded proteins by disassembly of the polyubiquitin chains, which is mediated by ubiquitin-specific proteases (USPs), such as USP25 (Valero et al., 1999 [PubMed 10644437]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, TRAF6, OUT, SUMO-2, Smt3
Papers on USP25
Induction of USP25 by viral infection promotes innate antiviral responses by mediating the stabilization of TRAF3 and TRAF6.
Zhong et al., Wuhan, China. In Proc Natl Acad Sci U S A, Oct 2015
Here, we found that a viral infection-induced deubiquitinase (DUB), ubiquitin-specific protease 25 (USP25) was required for host defense against RNA and DNA viruses.
Parkinson's Disease Genetic Loci in Rapid Eye Movement Sleep Behavior Disorder.
Rouleau et al., Montréal, Canada. In J Mol Neurosci, Jul 2015
Kaplan-Meier survival analysis in a subset of RBD patients (n = 56), demonstrated that homozygous carriers of the USP25 rs2823357 SNP had progressed to synucleinopathies faster than others (log-rank p = 0.003, Breslow p = 0.005, Tarone-Ware p = 0.004).
[Research progress on ubiquitin-specific protease in antiviral immunity].
Wei-Lin et al., Hangzhou, China. In Zhejiang Da Xue Xue Bao Yi Xue Ban, Jun 2015
USP2b, USP3, USP18, USP25, UL36USP and HAUSP play a role of antivirus; while USP4, USP13, USP15 and USP17 negatively regulate antiviral immune response.
Vaccinia-Related Kinase 2 Controls the Stability of the Eukaryotic Chaperonin TRiC/CCT by Inhibiting the Deubiquitinating Enzyme USP25.
Kim et al., South Korea. In Mol Cell Biol, May 2015
Here, we report that USP25 is a novel TRiC interacting protein that is also phosphorylated by VRK2.
Immunochip analysis identification of 6 additional susceptibility loci for Crohn's disease in Koreans.
Song et al., Seoul, South Korea. In Inflamm Bowel Dis, 2015
PTPN2 at 18p11 (rs514000; P = 9.00 × 10, OR = 1.33), and USP25 at 21q11 (rs2823256; P = 2.49 × 10, OR = 1.35), bringing the number of known CD loci (including 3 in the HLA) in Koreans to 15.
Acute ER stress regulates amyloid precursor protein processing through ubiquitin-dependent degradation.
Mook-Jung et al., Seoul, South Korea. In Sci Rep, 2014
Furthermore, an increase in levels of the endoplasmic reticulum-associated degradation (ERAD) marker, E3 ubiquitin ligase HRD1, proteasome activity, and decreased levels of the deubiquitinating enzyme USP25 were observed during ER stress.
¹H, ¹³C and ¹⁵N backbone and side-chain resonance assignments of the N-terminal ubiquitin-binding domains of USP25.
Zhang et al., Shanghai, China. In Biomol Nmr Assign, 2014
Ubiquitin Specific Protease 25 (USP25), a member of the deubiquitinase family, is involved in several disease-related signal pathways including myogenesis, immunity and protein degradation.
miRNA-200c inhibits invasion and metastasis of human non-small cell lung cancer by directly targeting ubiquitin specific peptidase 25.
Yao et al., Shanghai, China. In Mol Cancer, 2013
METHODS: The functions of miR-200c and USP25 in migration/invasion and lung metastasis formation were determined by transwell and tail vein injection assays, respectively.
Ubiquitin-specific protease 25 regulates TLR4-dependent innate immune responses through deubiquitination of the adaptor protein TRAF3.
Dong et al., Houston, United States. In Sci Signal, 2013
We identified ubiquitin-specific protease 25 (USP25) as a regulator of TLR signaling.
Ubiquitin-specific proteases 25 negatively regulates virus-induced type I interferon signaling.
Xiao et al., Wuhan, China. In Plos One, 2012
In this study, we carried out a targeted siRNA screen of 54 ubiquitin-specific proteases (USPs) and identified USP25 as a negative regulator of the virus-triggered type I IFN signaling pathway.
Negative regulation of IL-17-mediated signaling and inflammation by the ubiquitin-specific protease USP25.
Dong et al., Houston, United States. In Nat Immunol, 2012
In this study, we identified the ubiquitin-specific protease USP25 as a negative regulator of IL-17-mediated signaling and inflammation.
Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation.
Todi et al., Detroit, United States. In Plos One, 2011
a model where USP25 counteracts ubiquitination of ERAD substrates by the ubiquitin ligase HRD1, rescuing them from degradation by the proteasome.
PTMs in conversation: activity and function of deubiquitinating enzymes regulated via post-translational modifications.
Edelmann et al., Oxford, United Kingdom. In Cell Biochem Biophys, 2011
Studies indicate that DUBs recycle ubiquitin by processing polyubiquitin chains to generate free ubiquitin, and can be regulated by ubiquitination or phosphorylation.
Hepatic gene networks in morbidly obese patients with nonalcoholic fatty liver disease.
Olivier et al., Milwaukee, United States. In Obes Surg, 2010
Canonical pathway analysis in the NAFLD-associated gene clusters showed that the hepatic fibrosis signaling was the most significant pathway in the up-regulated NAFLD gene cluster containing three (COL1A1, IL10, IGFBP3) significantly altered genes, whereas the endoplasmic reticulum stress and protein ubiquitination pathways were the most significant pathways in the down-regulated NAFLD gene cluster, with the first pathway containing one (HSPA5) and the second containing two (HSPA5, USP25) significantly altered genes.
Functional interaction between the ubiquitin-specific protease 25 and the SYK tyrosine kinase.
Daviet et al., Paris, France. In Exp Cell Res, 2010
the second SH2 domain of SYK physically interacts with a tyrosine-rich, C-terminal region of USP25 independently of tyrosine phosphorylation
Genome-wide loss-of-function analysis of deubiquitylating enzymes for zebrafish development.
Jiang et al., Singapore, Singapore. In Bmc Genomics, 2008
Based on the huC neuronal marker expression, we grouped them into five sets (groups I to V). Group I DUBs (otud7b, uchl3 and bap1) appear to be involved in the Notch signaling pathway based on the neuronal hyperplasia, while group IV DUBs (otud4, usp5, usp15 and usp25) play a critical role in dorsoventral patterning through the BMP pathway.
The UBA-UIM domains of the USP25 regulate the enzyme ubiquitination state and modulate substrate recognition.
Marfany et al., Barcelona, Spain. In Plos One, 2008
Data show that USP25m is regulated through alternative conjugation of ubiquitin (activating) or SUMO (inhibiting) to the same lysine residue (K99), which may promote the interaction with distinct intramolecular regulatory domains.
Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25.
Melchior et al., Göttingen, Germany. In Mol Cell, 2008
Seven amino acids in the SIM of USP25 are sufficient for SUMO2/3-specific binding and conjugation
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