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Ubiquitin Thioesterase Otubain-1 Otubain-1 is also called ubiquitin thioesterase OTUB1, deubiquitinating enzyme OTUB1, OTU domain-containing ubiquitin aldehyde-binding protein 1, or ubiquitin-specific-processing protease OTUB1. It is a deubiquitylase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that can specifically remove 'Lys-48'-linked conjugated ubiquitin from protein substrates. It is also capable of cleaving NEDD8 (neural-precursor-cell-expressed developmentally down-regulated 8), but not SUMO (small ubiquitin-related modifier) 1/2/3 and ISG15 (interferon-stimulated gene 15) conjugates. In addition, OTUB1 inhibits the DNA damage response independently of its catalytic activity by blocking ubiquitin transfer onto protein substrates via sequestration of E2 ubiquitin-conjugating enzymes. It also regulates many cancer-associated signaling pathways including MAPK, ERa, epithelial-mesenchymal transition (EMT), RHOa, mTORC1, FOXM1 and P53 to promote tumor cell survival, proliferation, invasiveness and therapeutic resistance. OTUB1 belongs to the OTU family of cysteine proteases that use a conserved cysteine, histidine, and an aspartate, as the catalytic triad. It is classified as a family C65 cysteine protease by MEROPS. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",