TRIM62: A Potential Drug Target and Biomarker (G55223)

Target Name: TRIM62

NCBI ID: G55223

TRIM62: A Potential Drug Target and Biomarker

TRIM62 (TRI62_HUMAN) is a protein that is expressed in human tissues and has been identified as a potential drug target or biomarker. TRIM62 is a key regulator of cell division and has been shown to play a role in the development and progression of various diseases, including cancer.

TRIM62 was identified as a potential drug target by its ability to interact with and inhibit the activity of the protein p21, which is a key regulator of the cell cycle. p21 is a negative regulator of the cell cycle that has been shown to play a role in the regulation of cell growth, apoptosis, and cancer progression. By inhibiting the activity of p21, TRIM62 has been shown to inhibit the growth and spread of cancer cells.

In addition to its potential as a drug target, TRIM62 has also been identified as a potential biomarker for the diagnosis and prognosis of various diseases. TRIM62 has been shown to be expressed in a variety of human tissues, including cancer, and has been shown to be associated with the development and progression of various diseases, including cancer.

TRIM62 has also been shown to have a role in the regulation of cell adhesion and migration. By regulating the activity of cells, TRIM62 has been shown to play a role in the development and progression of various diseases, including cancer.

In conclusion, TRIM62 is a protein that has the potential to be a drug target or biomarker. Its ability to interact with and inhibit the activity of p21, as well as its association with the regulation of cell division, adhesion and migration, make it a promising target for further research. Further studies are needed to fully understand the role of TRIM62 in the development and progression of various diseases.

Protein Name: Tripartite Motif Containing 62

Functions: E3 ubiquitin ligase that plays a role in antifungal immunity by mediating 'Lys-27'-linked ubiquitination of CARD9 downstream of C-type lectin receptors; leading to CARD9 activation, followed by activation of NF-kappa-B and MAP kinase p38 pathways (PubMed:26488816). E3 ubiquitin ligase activity is dependent on E2 ubiquitin-conjugating enzyme UBE2D2 (PubMed:23402750)

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