Ubiquitin specific peptidase 29 (USP29)

Ubiquitin specific peptidase 29 (USP29) is a member of the ubiquitin-specific protease (USP) family of deubiquitinating enzymes, which remove ubiquitin from substrate proteins and thereby regulate their degradation, activity, and signaling roles[2][3][5]. It is located on human chromosome 19 and plays important regulatory roles in cellular processes such as protein stability, metabolic adaptation, and DNA damage response. USP29 deubiquitinates and stabilizes key proteins including MYC, HIF1α, Cdc25A, Snail, and TAK1, affecting tumor progression, chemoresistance, response to hypoxia, cell cycle, and apoptotic signaling[2][3][5]. Emerging evidence implicates USP29 as a potential therapeutic target in various cancers, hepatic injury, viral immune response, and neurodegenerative conditions, although drug development targeting USP29 remains in the early stages[2][3][5][7].

Other names

Ubiquitin carboxyl-terminal hydrolase 29Deubiquitinating enzyme 29Ubiquitin thioesterase 29Ubiquitin-specific-processing protease 29HOM-TES-84/86USP29

Inhibition of deubiquitinase activity, Modulation of substrate proteins’ stability such as MYC, HIF1α, Cdc25A, and TAK1[2][3]