TRIM35: A Potential Drug Target and Biomarker for Ubiquitin-Protein Ligase

Target Name: TRIM35

NCBI ID: G23087

TRIM35

TRIM35: A Potential Drug Target and Biomarker for Ubiquitin-Protein Ligase

Ubiquitin (Uv) is a protein that plays a central role in the regulation of various cellular processes, including DNA replication, RNA translation, and protein degradation. One of the critical mechanisms by which Uv regulates these processes is through its role as a protein ligase, where it links and disrupts protein-protein interactions. The protein TRIM35 is a member of the UV-dependent ubiquitin ligase family and has been shown to play a critical role in cellular processes such as DNA replication, cell growth, and the regulation of cell-cell adhesion.

TRIM35 is a 21-kDa protein that is expressed in various tissues, including muscle, liver, and brain. It is composed of an N-terminal transmembrane domain, a catalytic domain, and a C-terminal tail that is involved in its stability and interactions with other proteins. The transmembrane domain of TRIM35 is composed of a single copy of the protein transmembrane domain (3), which is known for its role in the regulation of protein trafficking and localization to the plasma membrane.

The catalytic domain of TRIM35 contains a unique ubiquitin-like domain (5) that is responsible for the protein-protein ligation reaction. This domain is composed of a series of conserved amino acid residues that are involved in the formation of a disulfide bond, which is the hallmark of a protein-protein ligase. The catalytic domain of TRIM35 contains a number of conserved acidic residues that are important for its catalytic activity.

The C-terminal tail of TRIM35 is involved in its stability and interactions with other proteins. This region contains a number of conserved acidic residues that are important for its stability and for its interactions with the protein Co-factor psori.

TRIM35 is involved in a number of cellular processes that are important for cell survival and growth. For example, it has been shown to be involved in the regulation of DNA replication (10), cell growth (11), and cell-cell adhesion. In addition, TRIM35 has also been shown to play a role in the regulation of various signaling pathways, including the TGF-β pathway.

Due to its involvement in these cellular processes, TRIM35 has been identified as a potential drug target. The development of inhibitors of TRIM35 has been shown to be effective in a variety of cancer models, including breast, ovarian, and colorectal cancer. In addition, TRIM35 has also been shown to be involved in the regulation of the efficacy of certain chemotherapy drugs, including taxanes.

In addition to its potential as a drug target, TRIM35 has also been identified as a potential biomarker for a variety of diseases. For example, TRIM35 has been shown to be overexpressed in a variety of cancer tissues, including breast, ovarian, and colorectal cancer. In addition, TRIM35 has also been shown to be involved in the regulation of cellular processes that are important for disease progression, such as the regulation of cell-cell adhesion.

Conclusion

In conclusion, TRIM35 is a protein that is involved in a variety of cellular processes that are important for cell survival and growth. Its role as a protein ligase and its expression in various tissues make it a potential drug target. In addition, TRIM35 has also been shown to be involved in the regulation of various signaling pathways and has been identified as a potential biomarker for a variety of diseases. Further research is needed to fully understand the role of TRIM35 in cellular processes and its potential as a drug

Protein Name: Tripartite Motif Containing 35

Functions: E3 ubiquitin-protein ligase that participates in multiple biological processes including cell death, glucose metabolism, and in particular, the innate immune response. Mediates 'Lys-63'-linked polyubiquitination of TRAF3 thereby promoting type I interferon production via RIG-I signaling pathway (PubMed:32562145). Can also catalyze 'Lys-48'-linked polyubiquitination and proteasomal degradation of viral proteins such as influenza virus PB2 (PubMed:32562145). Acts as a negative feedback regulator of TLR7- and TLR9-triggered signaling. Mechanistically, promotes the 'Lys-48'-linked ubiquitination of IRF7 and induces its degradation via a proteasome-dependent pathway (PubMed:25907537). Reduces FGFR1-dependent tyrosine phosphorylation of PKM, inhibiting PKM-dependent lactate production, glucose metabolism, and cell growth (PubMed:25263439)

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