Abstract
Ubiquitination is one of the main post-translational modification of proteins. It plays key roles in a broad range of cellular functions, including protein degradation, protein interactions, and subcellular location. In the ubiquitination system, different proteins are involved and their dysregulation can lead to various human diseases, including cancers. By using data available from the Cancer Genome Atlas (TCGA) and the Genotype-Tissue Expression (GTEx) databases, we here show that the ubiquitin conjugating enzyme, E2C (UBE2C), is overexpressed in all 27 cancers we investigated. UBE2C expression is significantly higher in late-stage tumors, which might indicate its involvement in tumor progression and invasion. This study also revealed that patients with higher UBE2C levels showed a shorter overall survival (OS) time and worse OS prognosis. Moreover, our data show that UBE2C higher-expression leads to worse disease-free survival prognosis (DFS), indicating that UBE2C overexpression correlates with poor clinical outcomes. We also identified genes with positive correlations with UBE2C in several cancers. We found a number of poorly studied genes (family with sequence similarity 72-member D, FAM72D; meiotic nuclear divisions 1, MND1; mitochondrial fission regulator 2, MTFR2; and POC1 centriolar protein A, POC1A) whose expression correlates with UBE2C. These genes might be considered as new targets for cancers therapies since they showed overexpression in several cancers and correlate with worse OS prognosis.
Highlights
Most proteins post-translational modifications are essential for proper cellular localization, substrate activity, and associations with other proteins
Data extracted from the Cancer Genome Atlas (TCGA) database revealed that UBE2C expression was notably higher in all 27 tumor types compared to matched TCGA normal tissues and Genotype-Tissue Expression (GTEx) data (Figure 1)
UBE2C is a member of the E2 ubiquitin-conjugating enzyme family, it plays a key role in the ubiquitination system in cooperation with anaphase promoting complex/cyclosome (APC/C)
Summary
Most proteins post-translational modifications are essential for proper cellular localization, substrate activity, and associations with other proteins. Ubiquitination is a post-translational modification mediated by a multi-step process which involves three different enzymes, including E1 ubiquitin-activating enzymes, E2 ubiquitin-conjugating enzymes, and E3 ubiquitin-ligating enzymes. This function leads to the proteasomal elimination of its substrate or alteration of the substrate activity, localization, and associations with other partners in its protein networks [2,4,5]. In the ubiquitin-proteasome pathway, anaphase promoting complex/cyclosome (APC/C) and the ubiquitin conjugating enzyme, E2C (UBE2C), are involved in the initiation of ubiquitin chain formation on APC/C substrates. UBE2C overexpression has been found in different human cancers, including hepatocellular carcinoma [8], thyroid [9], colon [10], breast [11], lung [12], brain [13], and cervical cancer [14]
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