Ubiquitin Specific Peptidase 1 (USP1)

UBP; Ubiquitin Carboxyl-Terminal Hydrolase 1; Ubiquitin Specific Protease 1; Deubiquitinating enzyme 1; Ubiquitin thioesterase 1; Ubiquitin-specific-processing protease 1

SPN	U259
HGNC	12607
MGI	2385198
PubMed	19217432
RGD	1306461
UniProt	O94782
Wiki	USP1

Deubiquitinating enzymes (DUBs) are capable of producing a free ubiquitin moiety from ubiquitin-fused precursors and ubiquitylated proteins in cells. DUBs possess conserved catalytic regions known as the 'cys domain' and the 'his domain.'

Ubiquitin carboxyl-terminal hydrolase 1 is 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.

Reference

"Identification and chromosomal assignment of USP1, a novel gene encoding a human ubiquitin-specific protease."
Genomics 54:155-158(1998) [PubMed] [Europe PMC] [Abstract]

"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"The deubiquitinating enzyme USP1 regulates the Fanconi Anemia pathway."
Mol. Cell 17:331-339(2005) [PubMed] [Europe PMC] [Abstract]

"Regulation of monoubiquitinated PCNA by DUB autocleavage."
Nat. Cell Biol. 8:339-347(2006) [PubMed] [Europe PMC] [Abstract]

"A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway."
Mol. Cell 28:786-797(2007) [PubMed] [Europe PMC] [Abstract]

"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]

"A quantitative atlas of mitotic phosphorylation."
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]

"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]

"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]