Ask about this productRelated genes to: UBE2J2 antibody
- Gene:
- UBE2J2 NIH gene
- Name:
- ubiquitin conjugating enzyme E2 J2
- Previous symbol:
- -
- Synonyms:
- Ubc6p, NCUBE2
- Chromosome:
- 1p36.33
- Locus Type:
- gene with protein product
- Date approved:
- 2002-11-26
- Date modifiied:
- 2016-03-14
Related products to: UBE2J2 antibody
Related articles to: UBE2J2 antibody
- Rhabdomyosarcoma (RMS), the most common pediatric soft tissue sarcoma, exhibits marked clinical heterogeneity driven by poorly understood molecular mechanisms. Identifying the molecular characteristics of different RMS subtypes and the molecular pathways influencing the RMS treatment response and recurrence is an urgent clinical need. Here, we perform deep proteomic profiling of 19 RMS tumors (8 alveolar [ARMS], 11 embryonal [ERMS]) and matched normal tissues, integrating bioinformatics with functional validation to delineate subtype-specific pathways, therapy resistance drivers, and actionable targets. ARMS tumors are characterized by ubiquitination pathway activation (UBE2R2, UBE2J2), while ERMS exhibits spliceosome dysregulation. Chemo- and radio-resistant tumors both show significant enrichment in the ribosome pathway. Relapsed cases show phosphonate and phosphinate metabolism pathway enrichment, suggesting metabolism reliance. Unsupervised clustering reveals ribosome- and glycolysis-driven subtypes with distinct metabolic dependencies. Functional studies implicate MED18─a core component of the Mediator complex─in mediating therapy resistance possibly via promoting DNA damage repair. Our study establishes proteomics as a tool to decode RMS heterogeneity, proposing subtype-tailored strategies targeting ubiquitination, splicing, and metabolism. - Source: PubMed
Publication date: 2026/01/15
Zhou ZhiyuanYe YingGuan WenbinZhu ChuanyingWen Lu - The prevalence of Parkinson's disease (PD) is increasing markedly in Asia, highlighting the urgent need to understand the current practices and challenges in delivering comprehensive PD care in this region. - Source: PubMed
Publication date: 2025/11/26
Mohamed Ibrahim NorlinahPhuenpathom WarongpornJagota PriyaBhidayasiri RoongrojPal Pramod KumarLin Chin-HsienKukkle Prashanth LingappaHatano TakuLim Shen-YangMyrzayev ZhanybekShang HuiFangOng Jed NoelRosales Raymond LYoun JinyoungAldaajani ZakiyahMittal Shivam OmNawi Azmawati MohammedUgawa Yoshikazu - Protein-lipid crosstalk is fundamental to homeostasis in the endoplasmic reticulum (ER). The ER-associated degradation (ERAD) pathway, a branch of the ubiquitin-proteasome system, maintains ER membrane properties by degrading lipid metabolic enzymes. However, the ERAD components that sense membrane properties and their mechanisms remain poorly defined. Using reconstituted systems with purified ERAD factors, we show that membrane composition modulates the ubiquitination cascade at multiple levels. The membrane-anchored E2 UBE2J2 acts as a sensor for lipid packing: in loosely packed membranes, UBE2J2 becomes inactive due to membrane association that impedes ubiquitin loading, while tighter packing promotes its active conformation and interaction with E1. UBE2J2 activity directs ubiquitin transfer by the E3 ligases RNF145, MARCHF6, and RNF139, targeting both themselves and the substrate squalene monooxygenase. Additionally, RNF145 senses cholesterol, altering its oligomerization and activity. These findings reveal that ERAD integrates multiple lipid signals, with UBE2J2 relaying and extending the effect of lipid signals through its cooperation with multiple E3 ligases. - Source: PubMed
Publication date: 2025/10/09
Vrentzou AikateriniLeidner FlorianSchmidt Claudia CGrubmüller HelmutStein Alexander - The coordination of numerous proteins is necessary for spermatogenesis, including degradation through the ubiquitin-proteasome pathway. Ubiquitin binding enzyme E2 (UBE2J2) is involved in the degradation of endoplasmic reticulum-associated proteins, while its role in spermatogenesis remains unclear. We found that mice exhibit azoospermia and spermatocytes undergo meiotic arrest at the mid-pachytene stage. Examining homologous recombination (HR) markers indicated that HR intermediate complexes are unstable and fail to form crossovers in spermatocytes. Proteomics analysis uncovered an extensive suite of meiosis- and chromosome segregation-associated proteins unexpressed in mouse spermatocytes lacking functional UBE2J2. Our findings suggest that UBE2J2 could possibly play a key role in SC disassembly, ensuring meiosis can proceed in the late pachynema during male germline cell development in mice, and serves as an essential factor in meiotic recombination and spermatogenesis. - Source: PubMed
Publication date: 2025/06/11
Yu XiaochenCen JieZhang YaxuanLi TongtongZhang MingyuGao FeiLiu HongbinCao Yongzhi - The RING-type E3 ubiquitin-protein ligase MuRF1 (also known as TRIM63) plays an important role in skeletal muscle atrophy by targeting contractile proteins. In cellulo, MuRF1 can alternatively interact with four E2 enzymes (UBE2E1, UBE2J1, UBE2J2, or UBE2L3), suggesting different functions or targets for the four MuRF1-E2 complexes. In this article, we studied the interface of these MuRF1-UBE2 complexes based on AlphaFold2 and AlphaFold3 predictions. These predictions revealed the involvement of different residues at the interface of each complex. We confirmed this overall interface difference by the differential sensitivity of MuRF1-E2 complexes to regenerating solutions in surface plasmon resonance experiments. We further confirmed several predictions individually by affinity measurements with point-mutant E2 enzymes and truncated MuRF1. We used the interaction-induced fluorescence change approach with fluorescent MuRF1. Besides canonical E2-RING-type E3 interactions, we were able to identify selective contact points between MuRF1 and its UBE2 partners. Furthermore, in the case of the MuRF1-E2E1 pair, unlike the other MuRF1-E2 pairs, the interaction may also be governed by a domain outside the RING domain. Since the function of RING-type E3s is regulated by E2 enzymes, deciphering the mechanisms of selective recruitment of E2s by MuRF1 paves the way for the development of targeted therapeutics to fight muscle atrophy. - Source: PubMed
Publication date: 2025/02/10
Claustre AgnèsMalige MélodieMacheton MaëlysCombaret LydieLefai EtienneFafournoux PierreTaillandier DanielHenri JulienPolge Cécile