gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Ubiquitin-conjugating enzyme E2W

Ube2w, ubiquitin-conjugating enzyme 16, UBC-16, hUBC16
Top mentioned proteins: Ubiquitin, Ubiquitin, Jos, CHIP, STEP
Papers on Ube2w
Molecular Characterization of LubX: Functional Divergence of the U-Box Fold by Legionella pneumophila.
New
Savchenko et al., Toronto, Canada. In Structure, Sep 2015
Here we show that the N terminus of LubX is able to activate an extended number of ubiquitin-conjugating (E2) enzymes including UBE2W, UBEL6, and all tested members of UBE2D and UBE2E families.
Intrinsic disorder drives N-terminal ubiquitination by Ube2w.
Klevit et al., Seattle, United States. In Nat Chem Biol, 2015
We show the Ub-conjugating enzyme (E2) Ube2w uses a unique mechanism to facilitate the specific ubiquitination of the α-amino group of its substrates that involves recognition of backbone atoms of intrinsically disordered N termini.
Biochemical and structural characterization of a novel ubiquitin-conjugating enzyme E2 from Agrocybe aegeria reveals Ube2w family-specific properties.
Liu et al., Beijing, China. In Sci Rep, 2014
The protein belongs to the Ube2w family and shows similar biochemical characteristics to human Ube2w, including monomer-dimer equilibrium in solution, α-NH2 ubiquitin-transfer activity and a mechanism to recognize backbone atoms of intrinsically disordered N-termini in substrates.
Biochemical and structural characterization of the ubiquitin-conjugating enzyme UBE2W reveals the formation of a noncovalent homodimer.
Klevit et al., Seattle, United States. In Cell Biochem Biophys, 2013
Here, we report that the mono-ubiquitinating E2 UBE2W forms a homodimer using two distinct protein surfaces.
The ubiquitin-conjugating enzyme (E2) Ube2w ubiquitinates the N terminus of substrates.
Paulson et al., Ann Arbor, United States. In J Biol Chem, 2013
In vitro, Ube2w is nonreactive with free lysine yet readily ubiquitinates substrate.
Activity-enhancing mutations in an E3 ubiquitin ligase identified by high-throughput mutagenesis.
Klevit et al., Seattle, United States. In Proc Natl Acad Sci U S A, 2013
The same mutations enhance E3 activity in the presence of another E2, Ube2w, implying a common allosteric mechanism, and therefore the general applicability of our observations to other E3s.
Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP.
Paulson et al., Ann Arbor, United States. In Mol Cell, 2011
Through their opposing activities, the initiator E2, Ube2w, and the specialized deubiquitinating enzyme (DUB), ataxin-3, participate in initiating, regulating, and terminating the CHIP ubiquitination cycle.
UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi anemia protein FANCD2.
GeneRIF
Huang et al., Beijing, China. In Mol Cells, 2011
UBE2W regulates FANCD2 monoubiquitination by mechanisms different from UBE2T and HRR6.
Candidate reference genes for gene expression studies in water lily.
Liu et al., Nanjing, China. In Anal Biochem, 2010
ACT11 and AP47 also stably expressed in roots subjected to various treatments, but in the leaves of the same plants the most stably expressed genes were ubiquitin-conjugating enzyme 16 (UBC16) and ACT11.
[Generation of mouse UBE2W antibody and analysis of UBE2W expression in mouse tissues].
Huang et al., Beijing, China. In Sheng Wu Gong Cheng Xue Bao, 2008
UBE2W, a newly described member of E2 family, was formerly reported probably involving in phototransduction or retinal degeneration in Drosophila.
E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages.
Klevit et al., Seattle, United States. In Nat Struct Mol Biol, 2007
Using a structure-based, yeast two-hybrid strategy, we discovered six previously unidentified interactions between the human heterodimeric RING E3 BRCA1-BARD1 and the human E2s UbcH6, Ube2e2, UbcM2, Ubc13, Ube2k and Ube2w.
Cloning, characterization and subcellular localization of a gene encoding a human Ubiquitin-conjugating enzyme (E2) homologous to the Arabidopsis thaliana UBC-16 gene product.
GeneRIF
Mao et al., Shanghai, China. In Front Biosci, 2005
human Ubiquitin-conjugating enzyme (E2) is homologous to the Arabidopsis thaliana UBC-16 gene product and contains 2 nuclear localization signals
share on facebooktweetadd +1mail to friends