Bioinformatic analysis of Cacybp-associated proteins using human glioma databases.
Chengmin XuanYong GaoMingwei JinShumei XuLei WangYuan WangRui HanKunpeng ShiXincheng ChenQi AnPublished in: IUBMB life (2019)
The ubiquitin-proteasome system is the primary cellular pathway for protein degradation, mediating 80% of intracellular protein degradation. Because of the widespread presence of ubiquitin-modified protein substrates, ubiquitination can regulate a variety of cellular activities including cell proliferation, apoptosis, autophagy, endocytosis, DNA damage repair, and immune responses. With the continuous generation of genomics data in recent years it has become particularly important to analyze these data effectively and reasonably. Cacybp forms a complex with the E3 ubiquitinated ligase Siah1 to participate in ubiquitination. We analyzed Cacybp-associated genes using the Gene Expression Omnibus (GEO) and CGGA (Chinese Glioma Genome Atlas) databases and identified 121 differentially expressed genes (DEGs), of which 46 were downregulated and 75 were upregulated. The biological processes, molecular functions, and protein-protein interaction (PPI) network of differential genes were analyzed by Cytoscape software and STRING software. We found no difference in Cacybp expression among different grades of gliomas and there was no significant association between the expression level of Cacybp and the prognosis of patients with glioma in LGG and GBM. © 2019 IUBMB Life, 1-8, 2019.
Keyphrases
- protein protein
- small molecule
- genome wide
- gene expression
- dna damage
- oxidative stress
- bioinformatics analysis
- cell proliferation
- big data
- poor prognosis
- immune response
- binding protein
- endoplasmic reticulum stress
- electronic health record
- cell death
- single cell
- dna methylation
- endothelial cells
- genome wide identification
- data analysis
- signaling pathway
- genome wide analysis
- amino acid
- high grade
- dna repair
- dendritic cells
- pluripotent stem cells
- pi k akt