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UBC7 Ubc7p

UBC7, Ubc7p, UBE2G2
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. The encoded protein shares 100% sequence identity with the mouse counterpart. This gene is ubiquitously expressed, with high expression seen in adult muscle. Three alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jan 2011] (from NCBI)
Top mentioned proteins: Ubiquitin, gp78, CAN, V1a, UBC6
Papers on UBC7
Analysis of antibody production in Saccharomyces cerevisiae: effects of ER protein quality control disruption.
Frey et al., Espoo, Finland. In Appl Microbiol Biotechnol, Nov 2015
In order to analyze the influence of ERAD on production of a human IgG, we disrupted ERAD at different stages by deletion of the HTM1, YOS9, HRD1, HRD3, or UBC7 gene, with or without a disruption of the UPR by deletion of the IRE1 gene.
A CRISPR-Based Screen Identifies Genes Essential for West-Nile-Virus-Induced Cell Death.
Wu et al., El Paso, United States. In Cell Rep, Aug 2015
Among the genes identified, seven genes, EMC2, EMC3, SEL1L, DERL2, UBE2G2, UBE2J1, and HRD1, stood out as having the strongest phenotype, whose knockout conferred strong protection against WNV-induced cell death with two different WNV strains and in three cell lines.
Human liver cytochrome P450 3A4 ubiquitination: molecular recognition by UBC7-gp78 autocrine motility factor receptor and UbcH5a-CHIP-Hsc70-Hsp40 E2-E3 ubiquitin ligase complexes.
Correia et al., San Francisco, United States. In J Biol Chem, Mar 2015
This CYP3A4 turnover involves endoplasmic reticulum-associated degradation via the ubiquitin (Ub)-dependent 26 S proteasomal system that relies on two highly complementary E2 Ub-conjugating-E3 Ub-ligase (UBC7-gp78 and UbcH5a-C terminus of Hsc70-interacting protein (CHIP)-Hsc70-Hsp40) complexes, as well as protein kinases (PK) A and C. We have documented that CYP3A4 Ser/Thr phosphorylation (Ser(P)/Thr(P)) by PKA and/or PKC accelerates/enhances its Lys ubiquitination by either of these E2-E3 systems.
Mulan E3 ubiquitin ligase interacts with multiple E2 conjugating enzymes and participates in mitophagy by recruiting GABARAP.
Zervos et al., Orlando, United States. In Cell Signal, 2014
Our studies identified four different E2 conjugating enzymes (Ube2E2, Ube2E3, Ube2G2 and Ube2L3) as specific interactors of Mulan.
The human ubiquitin conjugating enzyme UBE2J2 (Ubc6) is a substrate for proteasomal degradation.
Fleming et al., Cork, Ireland. In Biochem Biophys Res Commun, 2014
Here we demonstrate that it, and a second ubiquitin conjugating (Ubc) enzyme Ube2G2, are unstable, and incubation of transfected cells with proteasome inhibitors increased steady-state protein levels.
Ube2g2-gp78-mediated HERP polyubiquitylation is involved in ER stress recovery.
Li et al., Beijing, China. In J Cell Sci, 2014
Here we show that, after ER stress induction, HERP is rapidly degraded by Ube2g2-gp78-mediated ubiquitylation and proteasomal degradation.
Exome sequencing reveals novel and recurrent mutations with clinical impact in blastic plasmacytoid dendritic cell neoplasm.
Cigudosa et al., Madrid, Spain. In Leukemia, 2014
We identified for the first time deleterious mutations in IKZF3, HOXB9, UBE2G2 and ZEB2 in human leukemia.
Hepatic cytochrome P450 ubiquitination: conformational phosphodegrons for E2/E3 recognition?
Guan et al., San Francisco, United States. In Iubmb Life, 2014
Indeed, we have shown that both CYP3A4 and CYP2E1 incur ERAD-C, during which they are first phosphorylated by protein kinases A and C, which greatly enhance/accelerate their ubiquitination by UBC7/gp78 and UbcH5a/CHIP/Hsp70/Hsp40 E2/E3 ubiquitin ligase complexes.
Dimeric Ube2g2 simultaneously engages donor and acceptor ubiquitins to form Lys48-linked ubiquitin chains.
Li et al., Beijing, China. In Embo J, 2014
The ER-associated E3 gp78 ubiquitinates misfolded proteins by transferring preformed Lys48-linked ubiquitin chains from the cognate E2 Ube2g2 to substrates.
gp78 is specifically expressed in human prostate cancer rather than normal prostate tissue.
Zhu et al., Tianjin, China. In J Mol Histol, 2013
For gp78 is a ubiquitin E3 ligase, we then investigated the expression pattern of its cognate E2 (ubiquitin conjugating enzyme)-Ube2g2 in prostate cancers.
gp78 elongates of polyubiquitin chains from the distal end through the cooperation of its G2BR and CUE domains.
Li et al., Beijing, China. In Sci Rep, 2013
The ER quality control protein E3 gp78 catalyzes Lys48-linked polyubiquitin-chain- assembly on the Ube2g2 active site and is capable of transferring preassembled ubiquitin chains to its substrates.
Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine.
Byrd et al., Frederick, United States. In Embo J, 2013
gp78 includes a high-affinity secondary binding region for its cognate E2, Ube2g2, the G2BR.
Positive genetic interactors of HMG2 identify a new set of genetic perturbations for improving sesquiterpene production in Saccharomyces cerevisiae.
Makris et al., ChaniĆ”, Greece. In Microb Cell Fact, 2011
Tandem heterozygous deletion of a set of three genes, the ubiquitin ligases ubc7 and ssm4/doa10, and the ER resident protein pho86, led to an 11-fold increase in caryophyllene yields (125 mg/L in shake flasks) compared to cells lacking these modifications.
Selective ubiquitylation of p21 and Cdt1 by UBCH8 and UBE2G ubiquitin-conjugating enzymes via the CRL4Cdt2 ubiquitin ligase complex.
Dutta et al., Charlottesville, United States. In Mol Cell Biol, 2011
study reports that UBCH8 and UBE2G1 and UBE2G2 cooperate with CRL4Cdt2 in promoting the polyubiquitylation and subsequent degradation of p21 and Cdt1, respectively
Ancient ubiquitous protein 1 (AUP1) localizes to lipid droplets and binds the E2 ubiquitin conjugase G2 (Ube2g2) via its G2 binding region.
Thiele et al., Bonn, Germany. In J Biol Chem, 2011
The presence of the AUP1-Ube2g2 complex at LDs provides a direct molecular link between LDs and the cellular ubiquitination machinery.
Mechanism of polyubiquitin chain recognition by the human ubiquitin conjugating enzyme Ube2g2.
Tolman et al., Baltimore, United States. In J Biol Chem, 2011
Lys-48-linked polyubiquitin chains may be designed to bind certain proteins like Ube2g2 such that the terminal ubiquitin subunit carrying the reactive Lys-48 side chain can be positioned properly for chain elongation regardless of chain length.
Solution structure and dynamics of human ubiquitin conjugating enzyme Ube2g2.
Tolman et al., Baltimore, United States. In Proteins, 2010
Results report the solution structure and backbone dynamics of Ube2g2 solved by nuclear magnetic resonance spectroscopy.
A Ubc7p-binding domain in Cue1p activates ER-associated protein degradation.
Weissman et al., Frederick, United States. In J Cell Sci, 2009
Data show that a discrete C-terminal Ubc7p binding region of Cue1p is required for ER-associated degradation and for Ubc7p-dependent ubiquitylation by Hrd1p in vitro.
A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate.
Ye et al., Bethesda, United States. In Nature, 2007
Ube2g2/gp78-mediated polyubiquitination involves preassembly of Lys 48-linked ubiquitin chains at the catalytic cysteine of Ube2g2
Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MAT alpha 2 repressor.
Hochstrasser et al., Chicago, United States. In Cell, 1993
Here we show that four UBC proteins (UBC4, UBC5, UBC6, and UBC7) target the yeast MAT alpha 2 transcriptional regulator for intracellular degradation by two distinct ubiquitination pathways.
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