Ask about this productRelated genes to: UBE2K antibody
- Gene:
- UBE2K NIH gene
- Name:
- ubiquitin conjugating enzyme E2 K
- Previous symbol:
- HIP2
- Synonyms:
- HYPG, UBC1
- Chromosome:
- 4p14
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-28
- Date modifiied:
- 2016-03-14
Related products to: UBE2K antibody
Related articles to: UBE2K antibody
- Gastric cancer (GC) remains one of the leading causes of cancer-related mortality worldwide. Ubiquitin-conjugating enzyme E2 K (UBE2K), defined as an E2, is involved in various cellular processes. N6-methyladenosine (m6A) is one of the most abundant subtypes of RNA modifications. However, the systematic role of UBE2K and whether UBE2K undergoes an m6A modification in GC remain unknown. - Source: PubMed
Publication date: 2026/06/09
Guo JunweiZhang ZheSun YingsenYu ZhiweiZhu QingweiYuan ZiboHu SipinXia YongmingWu QiaoliangZhang GuibinLiu XinHu XiaogeCui DiHuang DongshengXu QiuranLi Shuangshuang - The Porcine Reproductive and Respiratory Syndrome Virus (PRRSV) has evolved sophisticated immune-evasion strategies to establish a productive infection in the host, primarily by counteracting the innate antiviral response. Here, we demonstrate for the first time that the PRRSV non-structural protein NSP8 suppresses NF-κB-dependent antiviral signalling by hijacking the host ubiquitin-conjugating enzyme UBE2K and inducing the degradation of IKKα, a pivotal kinase in the NF-κB pathway. PRRSV infection led to significant upregulation of host UBE2K, which in turn facilitated viral replication. Mechanistically, we found that NSP8 interacts directly with IKKα, triggering its degradation by the proteasome. Furthermore, we revealed that this process was facilitated by the host protein UBE2K, which acted as a crucial cofactor by directly interacting with NSP8 and thereby enhancing its activity against IKKα. This disruption blocked the activation of the NF-κB pathway and suppressed the expression of downstream antiviral factors, such as TNF-α, IL-6 and IFN-β, ultimately facilitating PRRSV replication. All of these findings showed that NSP8 is an important part of the process by which the host NF-κB pathway is blocked by viruses. This is a new way in which PRRSV avoids the immune system. - Source: PubMed
Publication date: 2026/05/18
Liu DaYan YanFu XuezhenQin LinglongMa JiayuZhou HuiSun ShipingLi HaiminDong WeirenZhou Jiyong - Aberrant alternative polyadenylation (APA) and alternative splicing (AS) contribute to numerous diseases, including cancer; however, their coordinated roles in ovarian cancer remain poorly understood. Here, we investigated CPSF7, an APA factor markedly upregulated in ovarian cancer and associated with poor prognosis. Silencing CPSF7 suppressed proliferation, migration, and invasion of ovarian cancer cells, while antisense oligonucleotides (ASOs) targeting CPSF7 reduced tumor growth in a patient‑derived xenograft (PDX) model. Mechanistically, knockdown of the splicing factor SNRPD2 induced exon 4 skipping in CPSF7 pre‑mRNA. Loss of exon 4 disrupted the RNA recognition motif (RRM) domain essential for CPSF7‑mediated pre‑mRNA cleavage and polyadenylation, and introduced premature termination codons (PTCs) that generated noncoding transcripts subject to nonsense‑mediated decay (NMD), thereby reducing CPSF7 expression. Thus, efficient splicing mediated by SNRPD2 is crucial for sustaining high CPSF7 levels in ovarian cancer cells. Functional assays showed that CPSF7 knockdown reduced proliferation and metastatic potential in cells with elevated SNRPD2, suggesting that CPSF7 is a key mediator of SNRPD2-driven oncogenesis. Moreover, CPSF7 governed specific APA events to maintain transcript stability, with UBE2K identified as a critical downstream target. CPSF7 preferentially bound distal polyadenylation signals (PASs) within the predominant UBE2K transcript (UBE2K-201), thereby increasing its mRNA stability and maintaining high functional UBE2K expression. Collectively, these findings reveal that AS and APA are interconnected in ovarian cancer via the SNRPD2-CPSF7-UBE2K axis, which drives disease progression and represents a promising target for therapeutic intervention. - Source: PubMed
Publication date: 2026/05/07
Li YingweiChen ZhongshaoDiao YuchaoGao QianqianGao YuehanPu YingyingYang Ning - Breast cancer (BC) remains one of the major threats to women's health in the 21st century, due to its high incidence and mortality rates. Ubiquitin-conjugating enzymes, as members of the ubiquitin-proteasome system, are responsible for numerous cellular physiological processes. However, ubiquitin-conjugating enzymes may also play unexpected roles in other physiological activities, such as phosphorylation, lactylation, and even methylation. The physiological function of the ubiquitin-conjugating E2 enzyme UBE2K in BC remains unknown. As a result, we looked into UBE2K's physiological role in the malignant development of BC. - Source: PubMed
Publication date: 2025/12/21
Mou JianchengTang HongchaoHu XiaogeYang ZhuotaoSu HaotianQian DaLi ChenhongLiu HaotianYe ZhihaoXu MingxingLiu ShuyanZheng QinghuiLiu XiaozhenZeng XinXu QiuranMeng Xuli - The heterotrimeric complex serine-threonine protein phosphatase 2 A (PP2A) is integral to the regulation of essential cellular processes. It is particularly crucial in spermatogenesis, where it is indispensable for meiosis, mitosis, sperm capacitation, and apoptosis. Previous research has concentrated on the knockdown of the catalytic subunit of PP2A, PPP2CA, in germ cells using Ddx4-Cre, resulting in male mouse sterility, disrupted meiotic recombination, and meiotic arrest of spermatocytes. To further elucidate the role of PP2A in spermatogenesis, we performed transcriptomic and proteomic sequencing analyses on the testes of knockout and control mice. A nine-quadrant map was developed to depict the differential expression of genes and proteins. Our analyses identified 1732 differentially expressed genes, which exhibited a strong positive correlation with the trends in differential protein expression. Gene Ontology (GO) enrichment analysis indicated a significant downregulation of genes involved in spermatogenesis, sperm cell development, and sperm cell differentiation. Furthermore, KEGG enrichment analysis revealed a notable enrichment of differentially expressed genes within the ubiquitin-mediated proteolysis pathway. In knockout mouse testicular tissue, testicular expression of the ubiquitin-related gene, UBE2K, was markedly downregulated, which was associated with the accumulation of histone H3, upregulation of the methyltransferase SETDB1, and increased levels of H3K9me3. Similarly, knockdown of Ppp2ca in GC2 cells resulted in decreased UBE2K expression, histone H3 accumulation, SETDB1 upregulation, and elevated H3K9me3 levels, consistent with mirroring the phenotype observed in the knockout mice. Notably, the ubiquitin-related gene UBE2K was identified as a significant outlier in the nine-quadrant map, and real-time quantitative PCR confirmed that UBE2K transcript levels were significantly reduced in knockout mice compared to wild-type controls. These findings suggest that PP2A may regulate histon. - Source: PubMed
Publication date: 2025/11/25
Ju HuameiGeng ZiliangChen BinyanShang YuweiChen XiaWang DanniWang WenbinSun HuitingShi YichaoYu Jiajun