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Ubiquitin-conjugating enzyme E2D 3

UbcH5c, UBE2D3
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. Multiple spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, SFT, UBC4, CAN, UbcH7
Papers using UbcH5c antibodies
Pathologic complete remission rate after cisplatin-based primary chemotherapy in breast cancer: correlation with p63 expression
Ratanaphan Adisorn et al., In Breast Cancer : Basic and Clinical Research, 2007
... -UbcH5c proteins were purified using nickel beads (Qiagen), and then dialyzed against ...
Papers on UbcH5c
Ovarian steroids regulate gene expression related to DNA repair and neurodegenerative diseases in serotonin neurons of macaques.
Reddy et al., Beaverton, United States. In Mol Psychiatry, Dec 2015
Ubiquinase coding genes UBEA5, UBE2D3 and UBE3A (Parkin) increased with E or E+P (all ANOVA, P<0.003).
UBE2D3 is a positive prognostic factor and is negatively correlated with hTERT expression in esophageal cancer.
Zhou et al., Wuhan, China. In Oncol Lett, Apr 2015
Ubiquitin-conjugating enzyme E2D 3 (UBE2D3) is a member of the E2 family, and participates in the ubiquitin proteasome pathway to regulate basic cellular activities, such as cell cycle control, the DNA damage response, apoptosis, and tumorigenesis.
BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.
Cochran et al., San Francisco, United States. In Nat Commun, 2014
The structure of a high-activity variant in complex with E2 (PCGF5-RING1B-UbcH5c) reveals only subtle differences from an earlier PCGF4 complex structure.
Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome.
Tan et al., United States. In Nature, 2014
This group includes the Polycomb repressive complex 1 (PRC1), which ubiquitylates nucleosomal histone H2A Lys 119 using its E3 ubiquitin ligase subunits, Ring1B and Bmi1, together with an E2 ubiquitin-conjugating enzyme, UbcH5c.
The ubiquitin-conjugating enzymes UBE2N, UBE2L3 and UBE2D2/3 are essential for Parkin-dependent mitophagy.
Kahle et al., Tübingen, Germany. In J Cell Sci, 2014
Knockdown of the E2 enzymes UBE2N, UBE2L3 or UBE2D2 and UBE2D3 (UBE2D2/3) significantly reduced autophagic clearance of depolarized mitochondria.
Distinct modes of ubiquitination of peroxisome-targeting signal type 1 (PTS1) receptor Pex5p regulate PTS1 protein import.
Fujiki et al., Fukuoka, Japan. In J Biol Chem, 2014
Here, we establish an in vitro ubiquitination assay system and demonstrate that RING finger Pex10p functions as an E3 with an E2, UbcH5C.
Identification of TRAF6 as a ubiquitin ligase engaged in the ubiquitination of SopB, a virulence effector protein secreted by Salmonella typhimurium.
Zhao et al., Tianjin, China. In Biochem Biophys Res Commun, 2014
The analysis of E2 revealed that UbcH5c and not other E2 conjugating enzymes are required for TRAF6-mediated SopB ubiquitination both in vitro and in vivo.
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
To identify the molecular determinants within E3 ligases that modulate activity, we scored each member of a library of nearly 100,000 protein variants of the murine ubiquitination factor E4B (Ube4b) U-box domain for auto-ubiquitination activity in the presence of the E2 UbcH5c.
Identification of RNF8 as a ubiquitin ligase involved in targeting the p12 subunit of DNA polymerase δ for degradation in response to DNA damage.
Lee et al., Valhalla, United States. In J Biol Chem, 2013
Using UbcH5c as ubiquitin-conjugating enzyme, a ubiquitin ligase activity that polyubiquitinates p12 was purified from HeLa cells.
Inhibition of UBE2D3 expression attenuates radiosensitivity of MCF-7 human breast cancer cells by increasing hTERT expression and activity.
Zhou et al., Wuhan, China. In Plos One, 2012
We identified ubiquitin-conjugating enzyme E2D3 (UBE2D3) as a principle hTERT-interacting protein and validated this association biochemically.
Bortezomib reduces the tumorigenicity of multiple myeloma via downregulation of upregulated targets in clonogenic side population cells.
Tagawa et al., Akita, Japan. In Plos One, 2012
Gene expression analysis showed that SP cells from five MM cell lines (RPMI 8226, AMO1, KMS-12-BM, KMS-11, JJN3) express genes involved in the cell cycle and mitosis (e.g., CCNB1, CDC25C, CDC2, BIRC5, CENPE, SKA1, AURKB, KIFs, TOP2A, ASPM), polycomb (e.g., EZH2, EPC1) and ubiquitin-proteasome (e.g., UBE2D3, UBE3C, PSMA5) more strongly than do non-SP cells.
Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex.
Cochran et al., San Francisco, United States. In Embo J, 2011
The crystal structure of a complex of the Bmi1/Ring1b RING-RING heterodimer & UbcH5c shows that UbcH5c interacts with Ring1b only.
EPAS1 mRNA in plasma from colorectal cancer patients is associated with poor outcome in advanced stages.
Bonilla et al., Madrid, Spain. In Oncol Lett, 2011
In the present study, the mRNA levels of three genes (EPAS1, KIAA0101 and UBE2D3) in plasma from colorectal cancer patients were analyzed.
Ubiquitin in motion: structural studies of the ubiquitin-conjugating enzyme∼ubiquitin conjugate.
Klevit et al., Seattle, United States. In Biochemistry, 2011
UbcH5c approximately Ub conjugate populates an array of extended conformations, and the population of Ubc13 approximately Ub conjugates favors a closed conformation in which the hydrophobic surface of Ub faces helix 2 of Ubc13
Retinoids regulate stem cell differentiation.
Wagner et al., New York City, United States. In J Cell Physiol, 2011
Binding of RA: (1) initiates changes in interactions of RAR/RXRs with co-repressor and co-activator proteins, activating transcription of primary target genes; (2) alters interactions with proteins that induce epigenetic changes; (3) induces transcription of genes encoding transcription factors and signaling proteins that further modify gene expression (e.g., FOX03A, Hoxa1, Sox9, TRAIL, UBE2D3); and (4) results in alterations in estrogen receptor α signaling.
Molecular basis for the association of human E4B U box ubiquitin ligase with E2-conjugating enzymes UbcH5c and Ubc4.
Mer et al., Rochester, United States. In Structure, 2010
determined structures of E4B U box free and bound to UbcH5c and Ubc4 E2s; findings show E4B U box is a monomer stabilized by a network of hydrogen bonds; findings suggest allosteric regulation of UbcH5c and Ubc4 by E4B U box
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
Combined Actions of UbcH5c and Cdc34 Promote Rapid and Efficient Polyubiquitination of IkBa
Lysine 63-linked polyubiquitination of the dopamine transporter requires WW3 and WW4 domains of Nedd4-2 and UBE2D ubiquitin-conjugating enzymes.
Sorkin et al., Aurora, United States. In J Biol Chem, 2010
role of WW3 and WW4 domains of Nedd4-2 in dopamine transporter ubiquitination was demonstrated; siRNA analysis demonstrated that this polyubiquitination is mediated by Nedd4-2 cooperation with UBE2D and UBE2L3 E2 ubiquitin-conjugating enzymes
Inhibition of NF-kappaB signaling by A20 through disruption of ubiquitin enzyme complexes.
Harhaj et al., Miami, United States. In Science, 2010
We have shown that A20 inhibited the E3 ligase activities of TRAF6, TRAF2, and cIAP1 by antagonizing interactions with the E2 ubiquitin conjugating enzymes Ubc13 and UbcH5c.
Direct activation of protein kinases by unanchored polyubiquitin chains.
Chen et al., Dallas, United States. In Nature, 2009
Furthermore, we found that unanchored polyubiquitin chains synthesized by TRAF6 and UBCH5C (also known as UBE2D3) activate the IKK complex.
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