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Ubiquitin carboxyl-terminal hydrolase 1 is an enzyme that in humans is encoded by the USP1gene.
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.
Therapy
USP1 expression is deregulated in certain types of human cancer. Recent findings indicated that USP1 inhibition may contribute to revert cisplatin resistance in an in vitro model of non-small cell lung cancer (NSCLC), which supports that USP1 can act as an effective target in cancer therapy.
D'Andrea A, Pellman D (1999). "Deubiquitinating enzymes: a new class of biological regulators". Crit. Rev. Biochem. Mol. Biol. 33 (5): 337–52. doi:10.1080/10409239891204251. PMID9827704.
Fujiwara T, Saito A, Suzuki M, et al. (1999). "Identification and chromosomal assignment of USP1, a novel gene encoding a human ubiquitin-specific protease". Genomics. 54 (1): 155–8. doi:10.1006/geno.1998.5554. PMID9806842.