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Ubiquitin-conjugating enzyme E2D 2

UBC4, UbcH5B, Ubc4p
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. This enzyme functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. Two alternatively spliced transcript variants have been found for this gene and they encode distinct isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, CAN, ACID, V1a, SFT
Papers on UBC4
Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B.
Weissman et al., Bethesda, United States. In J Biol Chem, Jan 2016
Unlike most RINGs, AO7 (RNF25) binds the E2 ubiquitin-conjugating enzyme, UbcH5B (UBE2D2), with strikingly high affinity.
Endocytosis of Ubiquitylation-Deficient EGFR Mutants via Clathrin-Coated Pits is Mediated by Ubiquitylation.
Sorkin et al., Pittsburgh, United States. In Traffic, Nov 2015
RNA interference analysis revealed that this residual internalization is strongly inhibited by depletion of Grb2 and the E2 ubiquitin-conjugating enzyme UbcH5b/c, and partially affected by depletion of the E3 ubiquitin ligase Cbl and ubiquitin-binding adaptors, indicating that an ubiquitylation process is involved.
Validation of reference genes for quantitative real-time PCR during latex regeneration in rubber tree.
Tang et al., Taiwan. In Gene, Jul 2015
Three softwares (comparative delta Ct method, NormFinder and GeNorm) exported similar results that identify UBC4, ADF, UBC2a, eIF2 and ADF4 as the top five suitable references, and 18S as the least suitable one.
Phosphomimetic mutation of the N-terminal lid of MDM2 enhances the polyubiquitination of p53 through stimulation of E2-ubiquitin thioester hydrolysis.
Hupp et al., Edinburgh, United Kingdom. In J Mol Biol, May 2015
However, the Asp17 mutation in MDM2 stimulated its discharge of the UBCH5a-ubiquitin thioester adduct (UBCH5a is a ubiquitin-conjugating enzyme E2D 1 UBC4/5 homolog yeast).
Activation of a primed RING E3-E2-ubiquitin complex by non-covalent ubiquitin.
Huang et al., Glasgow, United Kingdom. In Mol Cell, May 2015
Here, we show that backside bound Ub (Ub(B)) enhances both RING-independent and RING-dependent UbcH5B-catalyzed donor Ub (Ub(D)) transfer, but with a more prominent effect in RING-dependent transfer.
Structural basis for the inhibition of host protein ubiquitination by Shigella effector kinase OspG.
Cygler et al., Saskatoon, Canada. In Structure, 2014
The OspG effector kinase binds ubiquitin and ubiquitin-loaded E2-conjugating enzymes, including UbcH5b and UbcH7, and attenuates the host innate immune NF-kB signaling.
E3 ubiquitin ligase Pub1 is implicated in endocytosis of a GPI-anchored protein Ecm33 in fission yeast.
Kuno et al., Shenyang, China. In Plos One, 2013
Here, we further identified two multicopy suppressor genes, ubi1 (+) and ubc4 (+), encoding ubiquitin-ribosomal fusion protein and ubiquitin conjugating enzyme E2, respectively.
Distinct ubiquitination cascades act on the peroxisomal targeting signal type 2 co-receptor Pex18p.
Platta et al., Bochum, Germany. In Traffic, 2013
Using in vivo and in vitro approaches, we demonstrate that the polyubiquitination of Pex18p requires the ubiquitin-conjugating enzyme (E2) Ubc4p, which cooperates with the RING (really interesting new gene)-type ubiquitin-protein ligases (E3) Pex2p as well as Pex10p.
Structural model of ubiquitin transfer onto an artificial RING finger as an E3 ligase.
Miyamoto, Himeji, Japan. In Sci Rep, 2013
The docking poses of the WSTF PHD_EL5 RING finger with the UbcH5b-ubiquitin conjugate provided insight into its functional E2 interaction and development of ubiquitination at the atomic level.
BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer.
Huang et al., Glasgow, United Kingdom. In Nat Struct Mol Biol, 2012
Presented is the structure of the human dimeric RING domain from BIRC7 in complex with the E2 UbcH5B covalently linked to Ub.
APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1.
King et al., Boston, United States. In Nat Cell Biol, 2012
Here we demonstrate that multiple monoubiquitylation of cyclin B1, catalysed by UBCH10 or UBC4/5, is sufficient to target cyclin B1 for destruction by the proteasome.
The essential Ubc4/Ubc5 function in yeast is HECT E3-dependent, and RING E3-dependent pathways require only monoubiquitin transfer by Ubc4.
Klevit et al., Seattle, United States. In J Biol Chem, 2011
Ubc4 and Ubc5 are 1) the primary E2s for Rsp5 in yeast and 2) act as monoubiquitinating E2s in RING E3-catalyzed pathways
Nuclear protein quality is regulated by the ubiquitin-proteasome system through the activity of Ubc4 and San1 in fission yeast.
Kawamukai et al., Matsue, Japan. In J Biol Chem, 2011
Nuclear protein quality is regulated by the ubiquitin-proteasome system through the activity of Ubc4 and San1 in fission yeast.
Ubc4 and Not4 regulate steady-state levels of DNA polymerase-α to promote efficient and accurate DNA replication.
Bielinsky et al., Minneapolis, United States. In Mol Biol Cell, 2010
Data suggest that regular turnover of Cdc17 via Ubc4 and Not4 is required for proper cell proliferation.
Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate.
Pan et al., New York City, United States. In Mol Cell, 2010
Whereas UbcH5(A, B and C) is highly efficient in converting IkBa into monoubiquitinated forms, Cdc34 drives ubiquitin (Ub)-Ub conjugation
Ubiquitin-dependent proteolysis in mammalian spermatogenesis, fertilization, and sperm quality control: killing three birds with one stone.
Sutovsky, Columbia, United States. In Microsc Res Tech, 2003
Ubiquitin ligases E1, E2, E3, and UBC4 are active in the testis.
A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B.
Kirschner et al., Boston, United States. In Cell, 1995
We find that UBC4 and at least one other ubiquitin-conjugating enzyme can support cyclin B ubiquitination.
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.
Genetic analysis of ubiquitin-dependent protein degradation.
Seufert et al., Tübingen, Germany. In Experientia, 1992
This pathway involves substrate recognition by components of a ubiquitin-protein ligase system, covalent attachment of ubiquitin moieties to proteolytic substrates, and subsequent degradation of these conjugates by a multicatalytic protease complex.
Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability.
Jentsch et al., Tübingen, Germany. In Acta Biol Hung, 1990
UBC1, UBC4 and UBC5 enzymes were found to mediate selective degradation of short-lived and abnormal proteins.
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