Ubiquitin carboxyl-terminal hydrolase 1 is an enzyme that in humans is encoded by the USP1gene.[5][6]
This gene encodes a member of the ubiquitin-specific processing (UBP) family of proteases that is a deubiquitinating enzyme (DUB) with His and Cys domains. This protein is located in the cytoplasm and cleaves the ubiquitin moiety from ubiquitin-fused precursors and ubiquitinylated proteins.
The protein specifically deubiquitinates a protein in the Fanconi anemia (FA) DNA repair pathway. Alternate transcriptional splice variants have been characterized.[6]
A 2024 paper by Li, et al indicates possible contribution to cancer progression. Apparently via stabilizing proteins that promote cell proliferation (in TNBC, UCHL1 deubiquitinates and stabilizes KLF5, as a consequence there is resistance to endocrine therapy).[8]
D'Andrea A, Pellman D (1999). "Deubiquitinating enzymes: a new class of biological regulators". Critical Reviews in Biochemistry and Molecular Biology. 33 (5): 337–352. doi:10.1080/10409239891204251. PMID9827704.
Fujiwara T, Saito A, Suzuki M, Shinomiya H, Suzuki T, Takahashi E, et al. (November 1998). "Identification and chromosomal assignment of USP1, a novel gene encoding a human ubiquitin-specific protease". Genomics. 54 (1): 155–158. doi:10.1006/geno.1998.5554. PMID9806842.