Ask about this productRelated genes to: TRIM42 antibody
- Gene:
- TRIM42 NIH gene
- Name:
- tripartite motif containing 42
- Previous symbol:
- -
- Synonyms:
- FLJ40097, PPP1R40, T4A1
- Chromosome:
- 3q23
- Locus Type:
- gene with protein product
- Date approved:
- 2003-01-03
- Date modifiied:
- 2015-08-26
Related products to: TRIM42 antibody
Related articles to: TRIM42 antibody
- Previous studies have illuminated a significant genetic component in motor neuron disease (MND) pathogenesis, with several causative genes identified. However, a substantial proportion of MND cases remain genetically unexplained, particularly regarding the comprehensive contribution of rare, high-impact variants across the exome. - Source: PubMed
Publication date: 2026/01/09
Hu ZhenWan Jing-JinYan Qin-QinFan YuLiu Jun - The Parma and Piacenza turkey is among the few surviving Italian native turkey breeds, representing an important genetic resource currently at risk with roughly 100 animals alive. We performed a genome-wide characterization of this population using the Axiom® Turkey Genotyping Array (634 K SNPs) and compared it with a Commercial line. After quality control, 134 individuals and 398,401 SNPs were retained for analysis. Principal component and Discriminant analyses revealed strong differentiation between the local and Commercial populations, while also detecting farm-level substructure within the Parma and Piacenza breed. Runs of homozygosity (ROH) indicated markedly higher genomic inbreeding in the local breed (mean FROH = 0.34) compared to the Commercial one (mean FROH = 0.14), reflecting both long-term drift and recent inbreeding. Genomic differentiation analysis (FST) identified multiple highly divergent regions, and penalized regression (LASSO) selected a sparse panel of 22 SNPs capable of fully discriminating between local and Commercial turkeys, providing a potential tool for breed authentication and traceability. Overlapping results from ROH, FST, and LASSO highlighted candidate genomic regions under selection in the local population, including interesting loci overlapping TRIM42 and CLSTN2 genes, which have a known function towards immunity and reproduction, respectively. These findings reveal unique genomic features of the Parma and Piacenza turkey, provide tools for conservation and traceability, and emphasize the urgent need to preserve this highly endangered heritage population. - Source: PubMed
Publication date: 2025/12/13
Ablondi MichelaSummer AndreaAsti VittoriaMalacarne MassimoStrillacci Maria GiuseppinaBernini FrancescaSabbioni Alberto - To better understand different molecular mechanisms by which mutations lead to various human diseases, we classified 82,833 disease-associated mutations according to their inheritance modes (recessive versus dominant) and molecular types (in-frame [missense point mutations and in-frame indels] versus truncating [nonsense mutations and frameshift indels]) and systematically examined the effects of different classes of disease mutations in a three-dimensional protein interactome network with the atomic-resolution interface resolved for each interaction. We found that although recessive mutations affecting the interaction interface of two interacting proteins tend to cause the same disease, this widely accepted "guilt-by-association" principle does not apply to dominant mutations. Furthermore, recessive truncating mutations in regions encoding the same interface are much more likely to cause the same disease, even for interfaces close to the N terminus of the protein. Conversely, dominant truncating mutations tend to be enriched in regions encoding areas between interfaces. These results suggest that a significant fraction of truncating mutations can generate functional protein products. For example, TRIM27, a known cancer-associated protein, interacts with three proteins (MID2, TRIM42, and SIRPA) through two different interfaces. A dominant truncating mutation (c.1024delT [p.Tyr342Thrfs*30]) associated with ovarian carcinoma is located between the regions encoding the two interfaces; the altered protein retains its interaction with MID2 and TRIM42 through the first interface but loses its interaction with SIRPA through the second interface. Our findings will help clarify the molecular mechanisms of thousands of disease-associated genes and their tens of thousands of mutations, especially for those carrying truncating mutations, often erroneously considered "knockout" alleles. - Source: PubMed
Publication date: 2013/06/20
Guo YuWei XiaomuDas JishnuGrimson AndrewLipkin Steven MClark Andrew GYu Haiyuan