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Ubiquitin-conjugating enzyme E2 variant 1

Uev1A, UEV1, CROC-1, UBE2V1
Ubiquitin-conjugating E2 enzyme variant proteins constitute a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes but lack the conserved cysteine residue that is critical for the catalytic activity of E2s. The protein encoded by this gene is located in the nucleus and can cause transcriptional activation of the human FOS proto-oncogene. It is thought to be involved in the control of differentiation by altering cell cycle behavior. Multiple alternatively spliced transcripts encoding different isoforms have been described for this gene. A pseudogene has been identified which is also located on chromosome 20. Co-transcription of this gene and the neighboring upstream gene generates a rare transcript (Kua-UEV), which encodes a fusion protein comprised of sequence sharing identity with each individual gene product. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, Flu, TRAF6, CAN, Mms2
Papers using Uev1A antibodies
Terminal cisternae of denervated rabbit skeletal muscle: alterations of functional properties of Ca2+ release channels
Goldberg Alfred L. et al., In The Journal of Cell Biology, 1988
... UbcH1 and UbcH13/Uev1 E2-conjugating enzymes were purchased from Boston Biochem.
Papers on Uev1A
Parkin Protects Against Misfolded SOD1 Toxicity by Promoting Its Aggresome Formation and Autophagic Clearance.
Chin et al., Atlanta, United States. In Mol Neurobiol, Dec 2015
We find that parkin mediates K63-linked polyubiquitination of SOD1 mutants in cooperation with the UbcH13/Uev1a E2 enzyme and promotes degradation of these misfolded SOD1 proteins by the autophagy-lysosome system.
HTLV-1 Tax Stimulates Ubiquitin E3 Ligase, Ring Finger Protein 8, to Assemble Lysine 63-Linked Polyubiquitin Chains for TAK1 and IKK Activation.
Giam et al., Bethesda, United States. In Plos Pathog, Aug 2015
Using cytosolic extracts of HeLa and Jurkat T cells supplemented with purified proteins we have identified ubiquitin E3 ligase, ring finger protein 8 (RNF8), and E2 conjugating enzymes, Ubc13:Uev1A and Ubc13:Uev2, to be the cellular factors utilized by Tax for TAK1 and IKK activation.
Emerging roles of Lys63-linked polyubiquitylation in immune responses.
Karin et al., San Diego, United States. In Immunol Rev, Jul 2015
Among all the E2 ubiquitin-conjugating enzymes, Ubc13, which heterodimerizes with Uev1a, specifically mediates lysine 63 (K63)-linked protein polyubiquitylation, a process that does not lead to proteasomal degradation of its substrates.
Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis.
Komander et al., Cambridge, United Kingdom. In Embo J, Mar 2015
Notably, UBE2R1- (CDC34), UBE2N/UBE2V1- (UBC13/UEV1A), TRAF6- and HOIP-mediated chain assembly is inhibited by phosphoUb.
Novel Lys63-linked ubiquitination of IKKβ induces STAT3 signaling.
Donoghue et al., San Diego, United States. In Cell Cycle, 2013
Specific inhibition of the UBC13-UEV1A complex responsible for K63-linked ubiquitination establishes Lys147 as the predominant site of K63-ubiquitin conjugation and responsible for STAT3 activation.
The tomato ubiquitin-conjugating enzyme variant Suv, but not SlUev1C and SlUev1D regulates Fen-mediated programmed cell death in Nicotiana benthamiana.
Zeng et al., Little Rock, United States. In Plant Signal Behav, 2013
Additionally, we identified 2 tomato Uev1 homologs, SlUev1C and SlUev1D, respectively and showed they are not required for Fen-mediated programmed cell death in Nicotiana benthamiana, suggesting Uev homologs play differential role in the cell.
Selective UBC 13 Inhibitors
Reed et al., Bethesda, United States. In Unknown Journal, 2012
The activity of the probe compound was assessed by its ability to suppress Ubc13-mediated formation of heteropolymeric poly-ubquitination chains comprised of a mix of terbium-labeled and fluorescein-labeled ubiquitin molecules, as monitored by a reduction of the time-resolved fluorescent resonance energy transfer (TR-FRET) signal arising from this chains when synthesized in vitro in collaboration with the Ubc13 cofactor UEV1a.
TRIM5 structure, HIV-1 capsid recognition, and innate immune signaling.
Luban et al., Zürich, Switzerland. In Curr Opin Virol, 2012
As an E3 ubiquitin ligase TRIM5 cooperates with the heterodimeric E2, UBC13/UEV1A, to activate the TAK1 (MAP3K7) kinase, NF-κB and AP-1 signaling, and the transcription of inflammatory cytokines and chemokines.
The mechanism of OTUB1-mediated inhibition of ubiquitination.
Wolberger et al., Baltimore, United States. In Nature, 2012
UBC13 (also known as UBE2N) is a ubiquitin-conjugating enzyme (E2) that heterodimerizes with UEV1A (also known as UBE2V1) and synthesizes K63-linked polyubiquitin (K63Ub) chains at DSB sites in concert with the ubiquitin ligase (E3), RNF168 (ref.
TRIM5 acts as more than a retroviral restriction factor.
Wu et al., Columbus, United States. In Viruses, 2011
This unique function of TRIM5 is dependent on its association with the E2 ubiquitin-conjugating enzyme complex UBC13-UEV1A and subsequent activation of the TAK1 kinase complex and downstream genes involved in innate immune responses.
TRIM5 is an innate immune sensor for the retrovirus capsid lattice.
Luban et al., Genève, Switzerland. In Nature, 2011
Acting with the heterodimeric, ubiquitin-conjugating enzyme UBC13-UEV1A (also known as UBE2N-UBE2V1), TRIM5 catalyses the synthesis of unattached K63-linked ubiquitin chains that activate the TAK1 (also known as MAP3K7) kinase complex and stimulate AP-1 and NFκB signalling.
[Study on natural products for drug development].
Tsukamoto, Kumamoto, Japan. In Yakugaku Zasshi, 2010
We succeeded in isolating various compounds with three distinct inhibitory activities against an E1 enzyme reaction, Ubc13 (E2)-Uev1A interaction, and p53-HDM2 (E3) interaction as well as the proteasome inhibitors.
Direct activation of protein kinases by unanchored polyubiquitin chains.
Chen et al., Dallas, United States. In Nature, 2009
TRAF6 functions together with a ubiquitin-conjugating enzyme complex consisting of UBC13 (also known as UBE2N) and UEV1A (UBE2V1) to catalyse Lys 63-linked polyubiquitination, which activates the TAK1 (also known as MAP3K7) kinase complex.
Substrate modification with lysine 63-linked ubiquitin chains through the UBC13-UEV1A ubiquitin-conjugating enzyme.
Huang et al., San Francisco, United States. In J Biol Chem, 2007
modification of proteins with Lys(63)-linked ubiquitin chains occurs through a UEV1A-independent substrate modification and UEV1A-dependent Lys(63)-linked ubiquitin chain synthesis mechanism
Uev1A, a ubiquitin conjugating enzyme variant, inhibits stress-induced apoptosis through NF-kappaB activation.
Xiao et al., Saskatoon, Canada. In Apoptosis, 2006
These data provide evidence that Uev1A is a critical regulatory component in the NF-kappaB signaling pathway in response to environmental stresses and identify UEV1A as a potential proto-oncogene.
Structure and interactions of the ubiquitin-conjugating enzyme variant human Uev1a: implications for enzymatic synthesis of polyubiquitin chains.
Spyracopoulos et al., Edmonton, Canada. In Biochemistry, 2006
A structural model for the Ub-hUev1a-hUbc13-Ub tetramer was developed to gain chemical insight into the synthesis of Lys(63)-linked Ubiquitin chains.
Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A.
Xiao et al., Saskatoon, Canada. In J Cell Biol, 2005
Data demonstrate that divergent activities of Ubc13 rely on its pairing with either of two Uevs, Uev1A or Mms2.
TAK1 is a ubiquitin-dependent kinase of MKK and IKK.
Chen et al., Dallas, United States. In Nature, 2001
TRIKA1 is a dimeric ubiquitin-conjugating enzyme complex composed of Ubc13 and Uev1A (or the functionally equivalent Mms2).
Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain.
Chen et al., Dallas, United States. In Cell, 2000
Peptide mass fingerprinting analysis reveals that this complex is composed of the ubiquitin conjugating enzyme Ubc13 and the Ubc-like protein Uev1A.
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