UBE2B
- Known as:
- UBE2B
- Catalog number:
- ENZ-340
- Product Quantity:
- 2µg
- Category:
- -
- Supplier:
- Prospecbio
- Gene target:
- UBE2B
Related genes to: UBE2B
- Gene:
- UBE2B NIH gene
- Name:
- ubiquitin conjugating enzyme E2 B
- Previous symbol:
- -
- Synonyms:
- UBC2, HHR6B, RAD6B
- Chromosome:
- 5q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 1992-12-02
- Date modifiied:
- 2016-03-14
Related products to: UBE2B
anti-Ube2Banti-Ube2Banti-Ube2Banti-Ube2Banti-Ube2B (1F11)anti-Ube2B (4C3)anti-Ube2B (1F11)anti-Ube2B (4C3)anti-Ube2B type: Primary antibodies host: Mouseanti-Ube2B type: Primary antibodies host: RabbitAntigens UBE2B, 1-152aa, Human, His tag, E.coli, RecombinantBovine Ubiquitin-conjugating enzyme E2 B(UBE2B) ELISA kitBovine Ubiquitin-conjugating enzyme E2 B(UBE2B) ELISA kit SpeciesBovineBovine ubiquitin-conjugating enzyme E2B (RAD6 homolog) (UBE2B) ELISA kit, Species Bovine, Sample Type serum, plasmaCLIA Bos taurus,Bovine,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-protein ligase B Related articles to: UBE2B
- Protein ubiquitination regulates diverse cellular processes, and its dysregulation contributes to human disease, including cancer. E2 ubiquitin‑conjugating enzymes share a conserved UBC fold in which surface loops fine‑tune catalysis and partner interactions, yet the roles of individual loops remain incompletely defined. Here, we identify loop 3-a component of the "backside" β2-β3 hairpin-as a conserved structural and allosteric element in Rad6‑family E2s. Structural and bioinformatic analyses of yeast Rad6 and its human homologs (UBE2A/UBE2B) reveal that loop 3 forms an overlapping triple β‑turns, with variable first turn and a highly conserved second/third turn that links catalytic regulation to E3 ligase engagement. Systematic mutagenesis of the yeast Rad6 backside β‑turn (residues 42-51) shows that this element is required in vivo for Bre1‑dependent histone H2B Lys123 monoubiquitination, Rad18‑dependent PCNA monoubiquitination, and Ubr1/Ubr2‑dependent polyubiquitination and degradation of Sml1 and N‑end rule substrates, and related biological processes. Charge‑reversal mutations at backside β‑turn Glu49 and Asp50 disrupt E3 binding, whereas cancer‑relevant substitutions in kink‑inducing prolines (Pro43/Pro47) impair mono‑ and polyubiquitination without abolishing E3 interactions. Certain backside β‑turn mutations, including cancer-relevant variants, compromise steady-state levels following DNA damage, revealing them as conditional null or loss-of-function alleles. NMR spectroscopy demonstrates that Pro43/Pro47 mutations induce long‑range structural perturbations from backside β‑turn into the front‑face catalytic pocket, correlating with reduced in vitro ubiquitination activity. Deletion or alanine replacement of the β‑turn destabilizes yeast Rad6 and human UBE2A/UBE2B. Together, these findings establish the loop 3/backside β‑turn as a critical structural element of Rad6‑family enzymes. - Source: PubMed
Publication date: 2026/05/07
Chandrasekharan Mahesh BShukla Prakash KLeng Andrew MChen Hui-HsuanGanguly RajarshiNewell Nicholas - Ubiquitin-conjugating enzymes (E2s) are essential mediators of ubiquitin-dependent signaling cascades, governing diverse cellular processes such as proteolysis and transcriptional regulation. Despite increasing evidence linking E2 enzymes to tumorigenesis, their precise roles in gastric cancer (GC) remain incompletely defined. Here, we identified UBE2B as a key oncogenic E2 enzyme significantly upregulated in GC tissues through integrative bioinformatics analysis and clinical validation. High UBE2B expression was associated with poor patient prognosis and aggressive clinicopathological features. Functional assays demonstrated that UBE2B promotes GC cell proliferation both in vitro and in vivo. Mechanistically, UBE2B interacts with the E3 ligase BIRC2 to catalyze K63-linked ubiquitination of TRAF1, thereby amplifying NF-κB signaling. Furthermore, chromatin immunoprecipitation and luciferase reporter assays revealed that NF-κB subunit P65 directly binds to the UBE2B promoter, enhancing its transcription and forming a feedforward regulatory loop. This UBE2B-BIRC2-TRAF1 axis, coupled with the UBE2B-TRAF1-P65 feedback circuitry, establishes a self-sustaining mechanism that drives NF-κB hyperactivation and tumor cell proliferation. Collectively, our findings highlight UBE2B as a critical modulator of GC progression and a potential target for therapeutic intervention. Implications: This study characterizes the UBE2B-BIRC2-TRAF1 axis as a driver of NF-κB hyperactivation, identifying UBE2B as a prognostic biomarker and a potential therapeutic target for disrupting this oncogenic feedback loop in gastric cancer. - Source: PubMed
Publication date: 2026/02/09
He JianchengHuang XinkunXing DanjieChen ShunChen YuXue WanjiangHu Yilin - More and more evidence indicates that type 2 diabetes mellitus (T2DM) can cause muscle lesions and lead to the occurrence of sarcopenia. The changes in the gastrocnemius muscle of T2DM rats were investigated by using tandem mass tag (TMT) proteomics technology, with the aim of discovering biomarkers of muscle lesions induced by T2DM and clarifying their potential biological relationships. - Source: PubMed
Publication date: 2026/01/05
Wang TianruiZhang LiangJiang YuZhao XiaHou KehaoZhang YingzeYu NingXu Kuishuai - Understanding the genetic basis of male reproduction in mammals remains challenging. Commercial pig populations offer a unique model for studying fertility, as semen traits are routinely recorded using high-throughput systems. - Source: PubMed
Publication date: 2025/12/15
Sá PedroGòdia MartaGodinho Rodrigo MSevillano Claudia AHarlizius BarbaraMadsen OleBovenhuis Henk - Renal ischemia-reperfusion injury (RIRI) is a major cause of acute kidney injury, with endothelial dysfunction playing a central role in its pathophysiology. However, the molecular mechanisms underlying endothelial damage during RIRI remain incompletely understood. - Source: PubMed
Publication date: 2025/11/04
Wang QianRen SuxiaJiao LijingZhu QiuxiaoWang TingWang JingZhang Lihui