Ask about this productRelated genes to: FAM84A antibody
- Gene:
- LRATD1 NIH gene
- Name:
- LRAT domain containing 1
- Previous symbol:
- FAM84A
- Synonyms:
- NSE1, FLJ35392
- Chromosome:
- 2p24.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-07-28
- Date modifiied:
- 2019-03-01
Related products to: FAM84A antibody
Related articles to: FAM84A antibody
- Gestation length (GL) plays an important role in piglet maturation of major organs and development of body, while the genetic molecular markers of GL have not been extensively identified. In this study, according to the 5,662 effective records of 3,072 sows, the heritability and repeatability of GL were estimated through the dmuai of DMU Version 6.5.1 with a repeatability model, namely, = 0.1594 and = 0.2437. Among these sows, 906 individuals were genotyped with the GeneSeek Genomic Profiler (GGP) Porcine 50K Chip and imputed to the genome-wide level (9,212,179 SNPs) by the online software PHARP v1 for subsequent quality control and GWAS analyses. Further, the Fst was also performed to measure whether the actual frequency of genotypes in different GL phenotypes deviated from the theoretical proportion of genetic balance. We observed the highest degree of differentiation (average Fst value = 0.0376) in the group of 114 and 118 days, and identified a total of 1,002 SNPs strongly associated with GL. Through screening the genes located within a 500 kb distance on either side of the significant SNPs, we proposed 4,588 candidate genes. By the functional annotation, these candidates were found to be mainly involved in multicellular organism metabolism, early endosome, embryo implantation and development, and body and organ signaling pathway. Because of the simultaneous confirmation by GWAS and Fst analyses, there were 20 genes replied to be the most promising candidates including , , , , , , , , , , , , , , , , , , , and . This study provided effective molecular information for the genetic improvement of GL in pigs. - Source: PubMed
Publication date: 2023/01/05
Shi LijunLi HuihuiWang Lixian - Kinetic parameters ( and ) derived from the Michaelis-Menten equation are widely used to characterize enzymes. / is considered the catalytic efficiency or substrate specificity of an enzyme toward its substrate. N-Myristoyltransferases (NMTs) catalyze the N-terminal glycine myristoylation of numerous eukaryotic proteins. Surprisingly, we find that in vitro human NMT1 can accept acetyl-CoA and catalyze acetylation with and values similar to that of myristoylation. However, when both acetyl-CoA and myristoyl-CoA are present in the reaction, NMT1 catalyzes almost exclusively myristoylation. This phenomenon is caused by the dramatically different binding affinities of NMT1 for myristoyl-CoA and acetyl-CoA (estimated of 14.7 nM and 10.1 μM, respectively). When both are present, NMT1 is essentially entirely bound by myristoyl-CoA and thus catalyzes myristoylation exclusively. The NMT1 example highlights the crucial role of binding affinity in determining the substrate specificity of enzymes, which in contrast to the traditionally held view in enzymology that the substrate specificity is defined by / values. This understanding readily explains the vast biological literature showing the coimmunoprecipitation of enzyme-substrate pairs for enzymes that catalyzes protein post-translational modifications (PTM), including phosphorylation, acetylation, and ubiquitination. Furthermore, this understanding allows the discovery of substrate proteins by identifying the interacting proteins of PTM enzymes, which we demonstrate by identifying three previously unknown substrate proteins (LRATD1, LRATD2, and ERICH5) of human NMT1/2 by mining available interactome data. - Source: PubMed
Publication date: 2021/11/29
Su DanKosciuk TatsianaYang MinPrice Ian RLin Hening - With the improvement in diagnostic technology, the incidence of thyroid cancer (TC) is on the rise. Papillary thyroid carcinoma (PTC) is the most common pathological type of thyroid cancer; therefore, it is important to explore some valuable molecular targets to improve the treatment and prognosis of PTC. Studies have shown that family with sequence similarity 84, member A (FAM84A) is involved in the development of various tumors. However, the role of FAM84A in PTC remains unknown. Herein, we explored the biological function and specific molecular mechanism of FAM84A in PTC. Results indicated that FAM84A was upregulated in PTC tissues and cells. In addition, patients with higher FAM84A expression tended to possess larger tumor size, higher lymph node metastasis rate, and advanced TNM stage. Further studies indicated that downregulation of FAM84A could inhibit the development of PTC in vitro and in vivo by repressing the epithelial-mesenchymal transition (EMT) and Wnt/β-catenin signaling pathway. Moreover, FAM84A was confirmed to be negatively regulated by tumor suppressor miR-874-3p. In conclusion, our findings suggest that FAM84A may act as a potential diagnostic and therapeutic target for PTC. - Source: PubMed
Publication date: 2021/03/23
Ding YuWu LuyaoZhuang XiCai JingshengTong HouchaoSi YanZhang HaoWang XiaotingShen Meiping - Previous studies have suggested DNA methylation in blood is a potential epigenetic marker of cancer risk, but this has not been evaluated on a genome-wide scale in prospective studies for breast cancer. - Source: PubMed
Publication date: 2013/04/11
Xu ZongliBolick Sophia C EDeRoo Lisa AWeinberg Clarice RSandler Dale PTaylor Jack A - Using genome-wide cDNA microarray analysis, we identified a number of genes whose expression was up-regulated frequently in colorectal cancer. One of these was a gene termed FAM84A that was not expressed in any of the 23 normal tissues examined except the testis. Although immuno-cytochemical staining revealed localization of FAM84A protein in the subcellular membrane region, the staining was limited to the region lacking attachment with neighboring cells. In addition, we found that exogenous FAM84A expression increased cell motility in NIH3T3 cells, and that phosphorylation of serine 38 of FAM84A was associated with morphology of cells. Our results indicate a possibility that up-regulation of FAM84A plays a critical role in progression of colon cancer. - Source: PubMed
Kobayashi TakaakiMasaki TadahikoSugiyama MasanoriAtomi YutakaFurukawa YoichiNakamura Yusuke