[1]高 晗,赵 贝.葡萄糖转运体8的生物信息学分析[J].医学信息,2022,35(12):26-31.[doi:10.3969/j.issn.1006-1959.2022.12.007]
 GAO Han,ZHAO Bei.Bioinformatics Analysis of Glucose Transporter 8[J].Medical Information,2022,35(12):26-31.[doi:10.3969/j.issn.1006-1959.2022.12.007]
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葡萄糖转运体8的生物信息学分析()
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医学信息[ISSN:1006-1959/CN:61-1278/R]

卷:
35卷
期数:
2022年12期
页码:
26-31
栏目:
生物信息学
出版日期:
2022-06-15

文章信息/Info

Title:
Bioinformatics Analysis of Glucose Transporter 8
文章编号:
1006-1959(2022)12-0026-06
作者:
高 晗赵 贝
(大理大学基础医学院,云南 大理 671000)
Author(s):
GAO HanZHAO Bei
(School of Basic Medicine,Dali University,Dali 671000,Yunnan,China)
关键词:
葡萄糖转运体氨基酸序列理化性质亲疏水性
Keywords:
Glucose transporterAmino acid sequencePhysical and chemical propertiesHydrophilicity
分类号:
R34
DOI:
10.3969/j.issn.1006-1959.2022.12.007
文献标志码:
A
摘要:
目的 利用生物信息学方法分析GLUT8蛋白的结构和功能。方法 从NCBI数据库中获取GLUT8的基因序列和氨基酸序列,通过ProtParam和ProtScale分析GLUT8的理化性质和亲疏水性;通过TMHMM、SignalP和ProtCrop-Version分析GLUT8的跨膜结构域、信号肽和亚细胞定位;通过YinOYang 1.2 Server和NecNGlyc 1.0 Server分析GLUT8的糖基化情况;通过NetPho 3.1分析GLUT8的磷酸化位点;通过SOPMA、SWISS-MEDOL分析GLUT8的二级和三级结构;通过Uiprot中的Inertation数据库分析GLUT8的二元相互作用;通过STRING分析GLUT8的蛋白相互作用分析。结果 GLUT8蛋白由SLC2A8编码,位于9q33.3,全长10 759 bp,包含11个外显子,共477个氨基酸,其中丙氨酸(Ala)占12.8%,亮氨酸(Leu)占13.8%,其他氨基酸的占比均小于10%。GLUT8蛋白共有12个跨膜结构域,其主要定位于细胞膜和细胞质内。GLUT8蛋白共有5个O-糖基化位点,分别在47、333、350、356、360位;有1个N-糖基化位点,在349位。GLUT8蛋白共有24个磷酸位点,其中丝氨酸(Ser)磷酸化位点12个,苏氨酸(Thr)磷酸化位点10个,酪氨酸(Tyr)磷酸化位点2个。GLUT8蛋白二级结构以α-螺旋为主,三级结构中GEMQ评分为0.63分,平均QMEAN评分为(0.66±0.05)分。GLUT8蛋白共与46个蛋白有二元相互作用,与10个蛋白有相互作用。结论 GLUT8为12次跨膜蛋白,有多个糖基化位点和磷酸化位点,与多个蛋白相互作用,参与多条信号通路。
Abstract:
Objective To analyze the structure and function of GLUT8 protein by bioinformatics methods.Methods The gene sequence and amino acid sequence of GLUT8 were obtained from NCBI database; the physicochemical properties and hydrophilicity of GLUT8 were analyzed by ProtParam and ProtScale; the transmembrane domain, signal peptide and subcellular localization of GLUT8 were analyzed by TMHMM, SignalP and ProtCrop-Version; the glycosylation of GLUT8 was analyzed by YinOYang 1.2 Server and NecNGlyc 1.0 Server; the phosphorylation sites of GLUT8 were analyzed by NetPho 3.1; the secondary and tertiary structures of GLUT8 were analyzed by SOPMA and SWISS-MEDOL; the binary interaction of GLUT8 was analyzed by Inertation database in Uiprot; the protein interaction of GLUT8 was analyzed by STRING.Results GLUT8 protein was encoded by SLC2A8, located at 9q33.3, with a full length of 10 759 bp, including 11 exons and 477 amino acids, while Ala accounted for 12.8 %, Leu accounted for 13.8%, and other amino acids accounted for less than 10%. GLUT8 protein had 12 transmembrane domains, mainly located in cell membrane and cytoplasm. GLUT8 protein had 5 O-glycosylation sites at 47, 333, 350, 356 and 360, respectively. There was a N-glycosylation site at 349. GLUT8 protein had 24 phosphorylation sites, including 12 Ser phosphorylation sites, 10 Thr phosphorylation sites and 2 Tyr phosphorylation sites. The secondary structure of GLUT8 protein was dominated by α-helix. In the tertiary structure, the GEMQ score was 0.63 scores, and the average QMEAN score was (0.66±0.05) scores. GLUT8 interacted with 46 proteins and 10 proteins.Conclusion GLUT8 is a 12-transmembrane protein with multiple glycosylation sites and phosphorylation sites. It interacts with multiple proteins and participates in multiple signaling pathways.

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更新日期/Last Update: 1900-01-01