URI1蛋白生物信息学分析及在人体组织中的表达

发布时间：2019-01-03 13:21

【摘要】：目的分析人非经典前折叠素RPB5相互作用因子1(URI1)蛋白的特性、结构和变异体,观察URI1蛋白在人组织中的表达。方法通过多种网络分析工具,预测和分析URI1的基本特性及结构。用人组织微阵列免疫组化染色方法检测其在多种组织/细胞中的表达。结果 URI1编码1个535个氨基酸的蛋白质,该蛋白质性质不稳定,无跨膜片段,N末端无信号肽,非分泌型蛋白质,其mRNA在组织中广泛表达。URI1具有11个潜在的泛素化位点,其中6个为高度可信,5个为中度可信。有48个潜在的磷酸化位点(35个在丝氨酸位、11个在苏氨酸位、2个在酪氨酸位)。在第287氨基酸位有一糖基化位点,在第291、371氨基酸位也可能发生糖基化修饰,未发现乙酰化位点。蛋白质结构预测α螺旋(H)占39.63%,N端具有1个PFD功能域。URI1在多种组织/细胞广泛表达并存在明显差异表达,与基于高密度微阵列技术的BioGPS mRNA表达谱数据吻合。结论用生物信息学技术预测了URI1蛋白的结构和功能,为URI1蛋白的相关研究提供了信息。
[Abstract]:Objective to analyze the characteristics, structures and variants of human non-classical RPB5 interaction factor 1 (URI1) protein and to observe the expression of URI1 protein in human tissues. Methods the basic characteristics and structure of URI1 were predicted and analyzed by a variety of network analysis tools. Human microarray immunohistochemical staining was used to detect its expression in various tissues / cells. Results URI1 encodes a 535 amino acid protein with unstable properties, no transmembrane fragment, no signal peptide at the N-terminal, non-secretory protein, and its mRNA is widely expressed in tissues. URI1 has 11 potential ubiquitin sites. Among them, 6 were highly credible and 5 were moderately credible. There were 48 potential phosphorylation sites (35 at serine site, 11 at threonine site and 2 at tyrosine site). There was a glycosylation site at the 287th amino acid site and a glycosylation modification at the 291371 amino acid site. No acetylation site was found. The protein structure predicted that 伪 -helix (H) had a PFD functional domain at the N-terminal of 39.63 cells. URI1 was widely expressed in various tissues / cells and was significantly differentially expressed, which coincided with the data of BioGPS mRNA expression profile based on high-density microarray technique. Conclusion the structure and function of URI1 protein were predicted by bioinformatics, which provided information for the study of URI1 protein.
【作者单位】：江苏大学基础医学与医学技术学院血液学与血液学检验系;Rush大学医学中心解剖和细胞生物学系;
【分类号】：R341

【共引文献】