### UBE3C Gene Summary

The **UBE3C** gene (Ubiquitin Protein Ligase E3C) encodes an E3 ubiquitin-protein ligase, which plays a critical role in the ubiquitin-proteasome system, responsible for the selective degradation of proteins. As detailed in the NCBI and UniProt summaries, UBE3C facilitates the polyubiquitination process primarily through 'Lys-29'- and 'Lys-48'-linked ubiquitin chains, impacting various biological processes, including proteasome function and autophagy.

### 1. Associated Genes

In addition to the substrates mentioned, other gene products associated with UBE3C include:

- **UBE2D1**: Ubiquitin-conjugating enzyme essential for transferring ubiquitin to UBE3C.
- **IRF3 (Interferon Regulatory Factor 3)**: Target for degradation via UBE3C-mediated ubiquitination, critical for type I interferon signaling.
- **IRF7 (Interferon Regulatory Factor 7)**: Another target for degradation by UBE3C, with roles in antiviral responses.
- **PIK3C3 (VPS34)**: Involved in autophagy regulation, targeted by UBE3C leading to its degradation.
- **CAND2**: Involved in the control of the ubiquitin-proteasome system.

### 2. Aging and Age-Related Diseases

While specific studies directly linking UBE3C to aging or age-related diseases may be limited, the ubiquitin-proteasome system is known to play a key role in protein homeostasis, which is critically involved in aging. Accumulation of damaged proteins and dysregulation of cellular signaling pathways can contribute to age-related conditions, including neurodegenerative diseases (e.g., Alzheimer's Disease, Parkinson's Disease). Alterations in ubiquitination patterns mediated by UBE3C may influence these pathological processes.

Some studies indicate that improper regulation of ubiquitin ligases, including UBE3C, can lead to cellular senescence and contribute to the development of age-related disorders by impairing the degradation of misfolded proteins.

### 3. Drug Interactions

Currently, no specific drugs target UBE3C directly; however, drugs that affect the ubiquitin-proteasome system, such as proteasome inhibitors (e.g., bortezomib, carfilzomib), may indirectly influence UBE3C activity and function. Additionally, compounds used for modulating autophagy may intersect with the functional pathways influenced by UBE3C, especially in the context of stress responses and cellular homeostasis.

### 4. Pathways and Biological Processes

UBE3C is involved in several key pathways and biological processes, including:

- **Ubiquitin-Proteasome Pathway**: The core process for protein degradation, maintaining protein turnover and cellular homeostasis.
- **Autophagy**: Regulation of autophagic processes by ubiquitination pathways, affecting the degradation of cellular components.
- **Cytokine Signaling**: Modulates responses to type I interferons through degradation of regulatory proteins (IRF3, IRF7).
- **Response to Stress**: Associated with proteotoxic stress by mediating the degradation of proteins involved in stress responses (e.g., ADRM1/RPN13).

UBE3C functions exhibit an influence on various diseases including cancer, where alteration in ubiquitin-mediated degradation can affect tumor suppression and growth, asserting its role as a significant entity in maintaining cellular integrity and mediating stress responses.