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- Table of Contents
Facts about Ubiquitin carboxyl-terminal hydrolase 1.
Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high action (PubMed:18082604, PubMed:26388029). .
Human | |
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Gene Name: | USP1 |
Uniprot: | O94782 |
Entrez: | 7398 |
Belongs to: |
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peptidase C19 family |
Deubiquitinating Enzyme 1; EC 3.1.2.15; EC 3.4.19.12; hUBP; ubiquitin carboxyl terminal hydrolase 1; Ubiquitin Carboxyl-Terminal Hydrolase 1; ubiquitin specific peptidase 1; ubiquitin specific processing protease 1; ubiquitin specific protease 1; Ubiquitin Thioesterase 1; Ubiquitin thiolesterase 1; Ubiquitin-specific-processing protease 1; UBP; USP1
Mass (kDA):
88.207 kDA
Human | |
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Location: | 1p31.3 |
Sequence: | 1; NC_000001.11 (62436304..62451804) |
Nucleus.
There are many options when designing flow procedures. This article will help you to make the right choice. In addition to the best flow procedures for your experiments, you'll also find tips for optimisation. Also included are tips for targeted inhibition, as well as references and targets. You can find all these resources on Boster Bio's website. This article will provide an overview on Boster Bio's flow protocols and help you select the best one to suit your experiment.
The USP1 gene is a new player in DNA repair. It reduces the activity of FANCD2 but is believed to play a key role in FA. The USP1 gene has many functions in cell biology. It regulates homologous replication and limiting mutations. It can also be used to predict disease-associated gene expression. Multiple studies have shown the USP1 marker's function in cancer.
The USP1 gene is essential for the regulation of PI3K-Akt signaling during fasting. It limits Akt protein synthesis, thereby suppressing PI3K-Akt signaling. This suppresses the expression of the atrogene program, which results in muscle wasting. USP1 has also been shown to suppress PI3K/Akt signaling. It is important for maintaining cell equilibrium and maintaining the protein levels.
Recent research has shown that USP1 is crucial for the regulation of FANCD2 function in cancer cells. It is also linked to the spread and growth of 4T1 murine BC cell lines. USP1 could be a therapeutic target because of its involvement in DNA repair and cell metastatic ability. However, more research is needed to confirm this conclusion. However, USP1 expression could be an important biomarker in ovarian cancer research.
USP1 has been implicated in the regulation CDDP sensitivity in OC cells. It is also an important target for differentiation therapy and plays a critical role in osteogenesis. USP1 also plays a key role in the transcription of the osteogenic differentiate program. It has been shown, that USP1 is a transcriptional regulator of the osteogenic differentiation program.
Scientists are currently studying how the USP1 marker is linked to cancer. This gene is vital for the survival, and invasion of surrounding tissues, of cancer cells. USP1 may also play a key role in the promotion of the Wnt pathway. Targeting the USP1 gene could be a new strategy for anticancer treatment. However, these studies only include mice and not humans.
In human breast cancer, USP1 controls CDDP sensitivity and the stem cell-like nature of OC cells. It also controls the ability of cells invade the mesothelium. USP1 is crucial for the treatment and prevention of ovarian and melanoma. CDDP's downstream target is USP1. Targeted therapies for melanoma may be possible by molecular targeting the USP1 gene.
MAP1LC3B lipidation in rapamycin treated and lysosome inhibit-treated cells was similar, which suggests a role for USP1 within canonical self-phagy. USP1 depletion can also affect the function of USP1 and identify a parallel pathway. SQSTM1, a proteasome that inhibits USP1 within the autophagic processes, is likely target of MAP1LC3B.
The CDDP sensitivity to the USP1 mutant protein was significantly reduced in 293T/17 Cells. The CDDP half-life of phosphorylated USP1 mutant cells was also longer, suggesting that USP1's de-ubiquitinase activity is required for increased Snail expression. This suggests that USP1 might be a promising target for cancer therapy. Although the gene has been identified to be a tumor suppressor and further research is required to understand its role in cancer cells.
Researchers were able use high-throughput genomics to identify pathways in HCC that are controlled USP1. These pathways may regulate cancer stem cell formation, EMT, and stem cell state regulation. USP1 activation decreased expression of cancer stem cells genes, such as Sox2 or c-Myc. USP1 knockout cells showed decreased spheroid formation.
USP1 inhibitors increase ubiquitinated TBLR1 proteins, thereby enhancing TBLR1 stability. They also sustain CTC survival. These inhibitors also inhibit HR activation, which may have other anti-cancer functions. By disrupting the FA/BRCA pathway, USP1 inhibitors could act as cisplatin sensitizers. These results suggest a potentially new therapeutic strategy to treat cancer.
The clinical characteristics of HCC patients are directly related to their USP1 levels. Patients with high levels of USP1 have a shorter overall survival (OS), which may be explained by the tumors' ability to metastasize to other parts of the body. These results suggest that USP1 may be a promising target for HCC treatment. These studies must be replicated to determine the clinical benefits and efficacy of USP1 inhibitors in cancer therapy.
To evaluate the effects on USP1 receptors, another study looked at inhibitors of USP1. USP1 levels were measured in cells that had been treated with platinum or pimozide. This result was statistically significant, at P0.05. When USP1 inhibitors are used in a clinical trial, the effects of the drug can be evaluated more quickly. This new treatment strategy will allow clinicians to determine the role of USP inhibitors.
The current study shows that USP1 inhibitor SJB2-043 inhibits Ub/VS labeling in cells. This compound blocks USP1-related conjugation in a dose-dependent way and is therefore useful for drug discovery. It also inhibits native USP1/UAF1 compounds. SJB2-043 is also known to inhibit the formation of USP1/Ub-VS conjugates.
The USP1 Gene is a new gene with many clinical uses. It regulates cells' response to DNA damage and the Fanconi pathway. Its function may also be involved in cell differentiation, but the exact mechanism is not yet known. It is found in a heterodimeric combination with its cofactor UAF1.
This gene is a part of the proteasome, and it is associated with the 19S regulatory subunit. It plays a crucial role in the process of ubiquitin recycling and also trims ubiquitin molecules from protein substrates. In melanoma, non-small cell lung carcinoma and other forms of cancer, the USP1 gene is increased. It is also linked to many signalling pathways.
USP1 deubiquitinates the ID proteins, which act as negative regulators of bHLH transcript factors. BHLH transcription factor binds to DNA to promote differentiation. USP1 prevents the recruitment and deubiquitination of low-fidelity monomerases by deubiquitinating ID Proteins. USP1 also contributes towards the maintenance of osteosarcoma by promoting the degradation of ID proteins Uaf1 which negatively regulates bHLH transcription factor.
One of the most widely studied human DUBs is USP1. USP1 is a potential anticancer target because it participates in DDR pathways. USP1 encodes an amino acid protein of 785 with a predicted mass of 88.2 KDa. It contains a USP domain conserved and catalytic residues. The p53 protein contains the USP gene.
USP1 is a key tumor suppressor in colon carcinoma. It inhibits Akt signaling by leukemic and regulates apoptosis. USP1 can also be used in gene therapy. The USP1 gene can be a useful diagnostic tool in the early detection of colon cancer. It can be used in the diagnosis of patients with aggressive cancer. In the meantime, it may also be used in the treatment of patients with various conditions.
PMID: 9806842 by Fjiwara T., et al. Identification and chromosomal assignment of USP1, a novel gene encoding a human ubiquitin-specific protease.
PMID: 15694335 by Nijman S.M.B., et al. The deubiquitinating enzyme USP1 regulates the Fanconi Anemia pathway.