Ask about this productRelated genes to: UBE2I Blocking Peptide
- Gene:
- UBE2I NIH gene
- Name:
- ubiquitin conjugating enzyme E2 I
- Previous symbol:
- -
- Synonyms:
- UBC9
- Chromosome:
- 16p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-07-11
- Date modifiied:
- 2017-12-15
Related products to: UBE2I Blocking Peptide
Related articles to: UBE2I Blocking Peptide
- The synaptonemal complex (SC) is a highly ordered proteinaceous structure that assembles between homologous chromosomes during the prophase I of meiosis. Conserved as a tripartite architecture across species, the SC plays a central role in chromosome synapsis, meiotic recombination, and faithful chromosome segregation. This review marks the 70th anniversary of the discovery of the synaptonemal complex by Montrose Moses in 1956. In mammals, the SC is composed of eight core (canonical) structural proteins: SYCP1, SYCP2, SYCP3, SYCE1, SYCE2, SYCE3, SIX6OS1, and TEX12. The archetypal SC consists of two lateral elements (SYCP2 and SYCP3), a central element (SYCE1/2/3, SIX6OS1, and TEX12), and numerous transverse filaments (SYCP1). A shared structural feature of SC components is the presence of coiled-coil domains. Although the tripartite organization of the SC is evolutionarily conserved, its constituent proteins exhibit little to no sequence homology across species. In addition to these core components, a number of proteins, including HORMAD1, HORMAD2, TRIP13, SKP1, CDCA5 (Sororin), UBE2I (UBC9), SYCP2L, HSPA2, PSMA8, and FKBP6, associate with the SC. Beyond serving as a structural scaffold essential for homolog synapsis, SC proteins interact with key recombination factors such as DMC1, RAD51, and TEX11, thereby regulating recombination progression and crossover formation. Genetic, biochemical, and structural analyses of SC components have provided important mechanistic insights into SC assembly and function, as well as their clinical relevance to non-obstructive azoospermia (NOA) and premature ovarian insufficiency (POI) in humans. - Source: PubMed
Publication date: 2026/04/30
Yang FangWang P Jeremy - Perturbation of macrophage homeostasis is a key mechanism of airway inflammation in asthma. Ubiquitin conjugating enzyme E2 I (UBE2I), a SUMO E2 conjugating enzyme involved in macrophage M2 polarization, has an unclear role in asthma. - Source: PubMed
Publication date: 2026/04/25
Lin HongYu SijiaLi XiaowenYu LianyuChen XinyanPang YunyaoLv RourouDai BingZhou QianlanShan Lishen - Coronary heart disease (CHD), a major cardiovascular disorder, involves myocardial injury, inflammation, and fibrosis. NLRP3 inflammasome-driven pyroptosis plays a critical role in CHD progression. Although the ubiquitin-conjugating enzyme E2I (UBE2I) regulates protein SUMOylation, its function in CHD remains poorly understood. This study explores the expression and role of UBE2I in CHD, specifically examining its potential to mitigate myocardial injury and fibrosis via regulation of NLRP3 SUMOylation and pyroptosis. - Source: PubMed
Publication date: 2026/04/03
Ding Sheng-Kai - The pathogenesis of acute kidney injury (AKI) is closely related to the senescence of renal tubular epithelial cells (RTECs). The role of small ubiquitin-like modification (SUMOylation) in cellular stress and senescence has been gradually elucidated. Recent evidence has demonstrated that SUMOylation of p53 promotes cellular senescence. In this study, we investigated whether p53 SUMOylation-mediated cellular senescence contributes to AKI. A mouse AKI model was established via intraperitoneal injections of cisplatin (20 mg/kg, i.p.). The mice were sacrificed 72 h after the injection, and both blood and kidney tissue were collected. We found that UBC9 (Ube2i), the sole E2-conjugating enzyme for SUMOylation, was significantly upregulated in injured kidneys and drove p53-mediated cellular senescence. Tubular-specific knockdown of Ube2i or administration of the small-molecule UBC9 inhibitor 2-D08 (10 mg/kg, i.p, twice prior to and post-cisplatin injection) markedly alleviated senescence-related marker expression, improved renal function, and attenuated tissue damage in AKI model mice. We demonstrated that UBC9 interacted with p53 and promoted its SUMOylation at lysine 386 (K386). Chromatin immunoprecipitation assays demonstrated that UBC9 enhanced p53 binding to the p21 promoter, whereas the K386R mutation abolished this interaction. These results establish UBC9-mediated p53 SUMOylation as a critical pathway in acute injury-related renal senescence in mice and suggest its potential as a therapeutic target. - Source: PubMed
Publication date: 2026/01/16
Wu Qi-MeiLiu JingMu Ying-SongLi JuanTian Ying-JieWang ZhiDeng MiaoQiu Yang-MeiZhou ShuZhang Zi-YangXu Xin-MeiMa LiangFu PingYan Xiao-YongTan Zhou-Ke - Parkinson's disease (PD) is a neurodegenerative disorder that is characterized by α-synuclein aggregation, mitochondrial dysfunction, and impaired proteostasis. The peripheral biomarkers that reflect these cellular perturbations remain incompletely defined. This study aimed to evaluate the enzymatic activity and gene expression of two key protein degradation enzymes, Acyl PEptide Hydrolase (APEH) and Proteasome Subunit Beta Type-5 (PSMB5), in the peripheral blood of PD patients and to relate these findings to the severity of the disease. Thirteen PD patients and 13 age-matched healthy controls (HLT) were recruited. APEH and PSMB5 chymotrypsin-like (CT-like) activity were measured in whole blood, erythrocytes and immune cell fractions. Gene expression analysis was performed for APEH and PSMB5 and their related genes, plus other genes typical of parkinsonism or indicative of metabolic alterations: N(alpha)-acetyltransferase (NAA10) Aminoacylase 1 (ACY1), Ubiquitin-activating enzyme 1 (UBA1), Ubiquitin conjugating enzyme E2 I (UBE2I), Parkin RBR E3 ubiquitin protein ligase (PRKN), Alpha-synuclein (SNCA), Parkinsonism associated deglycase DJ-1 (PARK7), and mitochondrial Mn-SOD (SOD2). APEH activity did not differ significantly between PD and HLT in whole blood cells or cellular fractions. Conversely, PSMB5 CT-like activity was reduced in lymphocytes from PD patients, whereas erythrocytes and whole blood exhibited elevated activity. No changes in APEH and PSMB5 expression were observed, while PARK7 significantly decreased in patients with PD. Correlation analysis showed that proteasomal changes correlated with disease severity, and cognitive impairment. Our findings revealed compartment-specific proteasomal dysregulation in the peripheral blood of PD patients, suggesting systemic proteostasis imbalance. These alterations appeared more pronounced in patients with more severe clinical progression. This study supports the potential of peripheral proteasomal activity profiles as biomarkers linked to PD progression, warranting further investigation in larger cohorts. - Source: PubMed
Publication date: 2025/12/24
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