Ask about this productRelated genes to: SMYD3 antibody
- Gene:
- SMYD3 NIH gene
- Name:
- SET and MYND domain containing 3
- Previous symbol:
- ZNFN3A1, ZMYND1
- Synonyms:
- KMT3E
- Chromosome:
- 1q44
- Locus Type:
- gene with protein product
- Date approved:
- 2001-04-06
- Date modifiied:
- 2014-11-19
Related products to: SMYD3 antibody
Related articles to: SMYD3 antibody
- How adaptive and non-adaptive processes interact to shape urban-rural clines remains a fundamental question in urban evolution. Here, we integrate whole-genome sequencing, demographic modelling and forward-in-time simulations to test how natural selection in urban and rural environments interacts with non-adaptive forces to maintain a pigmentation cline in eastern grey squirrels (Sciurus carolinensis). Coat colour polymorphism (grey versus melanic) is determined by a 24 bp deletion in the melanocortin-1 receptor gene (Mc1R). In Syracuse, New York (USA), squirrel melanism decreases from 50% in the city to less than 10% in rural forests. Our analyses revealed a strong urban bottleneck, yet urban-rural divergence at Mc1R was far greater than the genomic background, suggesting the pigmentation cline is maintained by selection. To estimate habitat-specific selection coefficients at Mc1R, we used forward simulation models using data on individual fitness and allele frequencies. Both models produce a surprising, yet consistent finding: strong selection against the melanic morph in rural forests and near neutrality in the city. We also detected elevated divergence between colour morphs at SMYD3-a gene implicated in adaptive thermogenesis-raising a possible link between pigmentation and thermal performance. Overall, our findings demonstrate that selection outside the city can be sufficient to maintain urban-rural clines amid urban bottlenecks, suggesting cities can preserve genetic diversity that would otherwise be lost in rural landscapes. - Source: PubMed
Bonar MaegwinBlumenfeld Alexander JFusco Nicole ACampagna LeonardoTimpson AdrianThomas Mark GGibbs James PCaccone AdalgisaCosentino Bradley J - SMYD3 is a lysine methyltransferase involved in epigenetic regulation and oncogenic transcription, making it an attractive yet challenging therapeutic target. This study presents an integrated computational workflow combining machine learning based quantitative structure-activity relationship (QSAR) modelling, external bioactivity prediction, molecular docking, molecular dynamics (MD) simulations, and network analysis to prioritize potential SMYD3 inhibitors. ML-QSAR models were constructed using multiple molecular descriptor representations and regression algorithms. A MACCS fingerprint-based Random Forest model showed the most reliable external predictivity, supported by cross-validation, applicability domain assessment, and Y-randomization analysis. Feature interpretability using SHAP highlighted a small set of chemically meaningful structural patterns that consistently influenced activity prediction. The validated model was then applied to an external compound library, and bioactivity was predicted only for compounds lying within the defined applicability domain. This screening enabled the prioritization of in-domain candidates with moderate predicted potency and acceptable structural coverage relative to the training space. Structure-based evaluation using the crystallographic SMYD3 structure demonstrated that selected compounds bind within the experimentally validated active site and engage key residues observed in the co-crystal complex. Extended 250 ns MD simulations indicated that CHEMBL4472528 maintained stable binding, persistent polar and hydrophobic interactions, and favorable binding free energies compared with both the co-crystal ligand and other screened candidates. Network and pathway analysis further placed SMYD3 within a focused chromatin-associated and transcriptional regulatory context, supporting the biological relevance of the target. This work provides a reproducible computational framework for SMYD3 inhibitor prioritization and highlights CHEMBL4472528 as a promising scaffold for further investigation. - Source: PubMed
Publication date: 2026/04/10
Alzahrani Abdullah RRehman Zia UrJawaid TalhaKhan Abida - Thyroid cancer is the most common malignancy of the endocrine system. Tumor-associated macrophages (TAMs) play a pivotal role in modulating the tumor microenvironment and promoting tumor progression. However, the prognostic implications of macrophage heterogeneity in thyroid cancer remain unclear. - Source: PubMed
Publication date: 2026/01/09
Xu SufangZhang XinSun JingruQin ManDu HuarongLuo Bing - The histone methyltransferase SMYD3 (SET and MYND domain containing 3) is critical for vascular homeostasis and may be implicated in pathological angiogenesis. However, its mechanism remains elusive, and targeted inhibitors are in early-stage development. We aim to clarify whether SMYD3 regulates angiogenesis and develop novel molecules targeting SMYD3. - Source: PubMed
Publication date: 2026/02/24
Ye QingCai JianghongLu XiannengZhu QiLi QixiuRen MiDing QianMao YichengZhu Yi Zhun - Cancer metastasis is the leading cause of mortality associated with cancer, and the prognosis for patients diagnosed with colorectal cancer(CRC) largely depends on the occurrence of metastasis during the progression of the disease. A comprehensive understanding of the mechanisms underlying metastasis in CRC is essential for advancing treatment strategies. Through integrated bioinformatics analysis of mRNA expression profiles and epigenetic modifiers, we identified SMYD3 as the top differentially expressed histone modifier in CRC. Clinically, SMYD3 overexpression significantly associates with poor prognosis and enhances metastatic potential. Utilizing immunoprecipitation-mass spectrometry, we discovered RACK1 as a novel SMYD3-interacting protein. Subsequent mechanistic studies revealed a tripartite interaction network: SMYD3 recruits SMAD3 through RACK1-mediated scaffolding, facilitating transcriptional activation of the downstream effector TSKU. Notably, RACK1 depletion disrupts SMYD3-SMAD3 complex formation, establishing the critical role of this axis in metastasis regulation. Consequently, inhibiting the SMYD3-SMAD3 interaction may represent a promising therapeutic strategy for addressing CRC metastasis. In conclusion, targeting the SMYD3-RACK1-SMAD3 transcriptional complex presents a viable approach for the treatment of CRC metastasis. - Source: PubMed
Publication date: 2026/02/03
Bai XiaomingHan DongChen JieSheng SiqiFeng HaimeiWang HongyuXu KeHuang YadiHuang MengxiChu XiaoyuanChen YitianLei Zengjie