Anti-HTF9C/TRMT2A antibody [1G8]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

HTF9C also known as TRMT2A is a tRNA methyltransferase enzyme with a mass of approximately 57 kDa. Its primary function is to catalyze the methylation of tRNA specifically the modification of uridine at position 54 to 5-methyluridine. This modification is essential for maintaining the correct structure and function of tRNA which affects protein synthesis. The protein is ubiquitously expressed in various tissues suggesting it plays an important role in fundamental cellular processes.

Biological function summary

The enzyme influences accurate tRNA function affecting overall protein translation efficiency. HTF9C/TRMT2A contributes to the maturation of tRNA molecules an important step in the stability and proper functioning of the translation machinery. Although it functions largely as an independent enzyme it may transiently interact with other proteins in the tRNA modification pathway indicating its potential involvement in broader RNA processing complexes.

Pathways

HTF9C/TRMT2A plays a critical role in the tRNA modification pathway which is tightly linked to protein biosynthesis. Its function affects the fidelity of translation connecting it indirectly to the mTOR pathway which regulates cell growth and metabolism. The TRMT2A enzyme's activity is potentially interrelated with ribosomal proteins like RPLP0 which are important for the translation process reflecting its impact on cellular growth and proliferation.

Associated diseases and disorders

Improper function of HTF9C/TRMT2A can contribute to the development of cancer due to dysregulated protein synthesis. Aberrant methylation patterns affecting tRNA can result in translation anomalies contributing to oncogenic transformation. Additionally its malfunction is thought to be connected to neurological disorders where precise protein translation is important for neural function. In these contexts HTF9C may interact with dysregulated proteins such as p53 involved in cell cycle control and tumor suppression further illustrating its role in disease mechanisms.