Anti-hHR23A antibody [1E4D6]

Supplementary info

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

Activity summary

The human homolog of Rad23A or hHR23A is an important player in protein maintenance and degradation pathways. This protein is known for its involvement in DNA repair mechanisms and proteasome function. hHR23A weighs approximately 43 kDa and expresses in many tissues reflecting its diverse roles throughout the body. Scientists also refer to it as RAD23A giving insight into its function by linking with the well-known RAD proteins.

Biological function summary

HHR23A contributes significantly to the protein ubiquitination process an essential cellular mechanism for targeting proteins for degradation. It forms part of a complex with ubiquitin aiding in the recognition and delivery of ubiquitinated proteins to the proteasome for degradation. The protein's ability to bind to both ubiquitin and the proteasome enables its dual function in proteolytic pathways positioning hHR23A as an intermediary that regulates protein turnover and stability.

Pathways

HHR23A engages in the ubiquitin-proteasome pathway and the nucleotide excision repair (NER) pathway. It cooperates with other proteins like Rad4 (XPC in humans) in NER where it functions in DNA damage recognition and repair. In the ubiquitin-proteasome pathway hHR23A interacts with the proteasomal subunit Rpn10 and other ubiquitin-like proteins. These interactions facilitate effective proteolysis of damaged or unnecessary proteins emphasizing its central role in controlling intracellular protein levels.

Associated diseases and disorders

HHR23A has implications in neurodegenerative diseases and cancer. Impaired ubiquitin-proteasome system function involving hHR23A associates with neurodegenerative diseases such as Alzheimer's where protein aggregates accumulate. hHR23A's interaction with proteins like p53 known for its role in tumor suppression ties this protein to cancer biology highlighting its potential involvement in tumor suppression failure when its pathways are disrupted.