IndraLab

Statements


USP1 affects PCNA
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USP1 deubiquitinates PCNA. 10 / 79
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"Consistently, cells lacking Usp1, the enzyme that de-ubiquitinates PCNA exhibited increased TLS across a UV lesion and the cisplatin adduct."

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"Upon UV-light induced DNA damage, Usp1 is degraded so that PCNA becomes ubiquitylated XREF_BIBR, XREF_BIBR, suggesting that Usp1 deubiquitylates PCNA continuously in the absence of DNA damage XREF_BIBR."

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"Upon UV light induced DNA damage, Usp1 undergoes autocleavage, and PCNA therefore becomes ubiquitylated, suggesting that Usp1 continuously deubiquitylates PCNA in the absence of DNA damage."

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"USP1 also deubiquitinates Ub-PCNA, suggesting that it plays a role in regulating Ub-PCNA-mediated translesion synthesis (TLS) ( Huang et al., 2006 )."

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"Wild-type USP1 that is autocleavage-inactive (G670A, G671A) deubiquitinated Ub–PCNA subunits, whereas catalytically inactive USP1 (C90S) did not."

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"These findings demonstrate that ATAD5-N modulates Ub–PCNA deubiquitination process directly and is crucial for UAF1–USP1 to efficiently deubiquitinate Ub–PCNA."

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"PCNA polyubiquitination, similar to PCNA monoubiquitination, is negatively regulated by USP1 [XREF_BIBR, XREF_BIBR]."

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"During unperturbed replication, PCNA ubiquitination is limited by USP1, as evidenced by increased PCNA ubiquitination upon USP1 depletion (XREF_FIG)."

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"Deubiquitination of PCNA by USP1 was confirmed in vitro, and the specificity of the reaction was demonstrated by testing an irrelevant DUB enzyme and a catalytically inactive form of USP1.The investig[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"This is in contrast to UV mediated DNA damage whereby USP1 is degraded to enhance PCNA monoubiquitination, suggesting that alternate mechanisms inhibit USP1 activity in a time dependent manner (XREF_FIG)."
USP1 deubiquitinates ubiquitinated PCNA. 8 / 8
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"Ubiquitin-specific protease 1 (Usp1) is responsible for deubiquitinating monoubiquitinated PCNA [60] ."

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"Whether Usp1 is responsible for deubiquitinating polyubiquitinated PCNA remains to be determined, although one study did detect an elevated PCNA polyubiquitination upon Usp1 depletion [51] ."

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"Following DNA synthesis on damaged DNA templates by TLS polymerase (Mailand et al., 2013), the ubiquitinated PCNA is deubiquitinated by USP1, causing the release of TLS polymerases and re-association [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP1 (ubiquitin specific peptidase 1), which promotes de-ubiquitination of mono-ubiquitinated PCNA [57], forms a stable complex with UAF1 (USP1 associated factor 1), which stabilizes and activates USP[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"In vitro, the USP1 and UAF1 complex can de-ubiquitinate mono-ubiquitinated PCNA more efficiently than USP1 alone [59]."

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"USP1, an important negative regulator of the DNA damage tolerance pathway, deubiquitinates mono-ubiquitinated PCNA, (mUb-PCNA) [ 38 ]."

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"They observed an increased mutation frequency in cells in which USP1 was inactivated, a result expected if steady-state levels of monoubiquitinated PCNA are upregulated because of reduced deubiquitina[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Previous studies have shown that USP1 deubiquitylates mono-ubiquitinated PCNA (ub-PCNA) and mono-ubiquitinated FANCD2 (ub-FANCD2) in response to replication stress due to DNA damage during DNA replication (4, 5, 41)."
Unubiquitinated USP1 leads to the deubiquitination of PCNA. 1 / 1
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"These include the deubiquitylation of PCNA and FANCD2 catalysed by USP1, deubiquitylation and stabilisation of 53BP1 or claspin by USP28 and more recently is has been reported that USP3 catalyses the deubiquitylation of H2AX and gamma-H2AX."
USP1 deubiquitinates PCNA on K164. 1 / 1
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"47 USP1 deubiquitinates modified PCNA at residue K164 in vivo and in vitro ."
Modified USP1 leads to the deubiquitination of PCNA. 1 / 1
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"Conversely, overexpression of USP1 when cells are treated with hydroxyurea inhibits monoubiquitination of PCNA."
USP1 affects FANCD2
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USP1 deubiquitinates FANCD2. 10 / 60
1 1 | 1 57

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"USP1 influences accumulation of the Fanconi anaemia core complex at DNA damage sites and deubiquitylates FANCD2–FANCI in a cell cycle-dependent manner ."

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"Interestingly, the opposite effect (DNA promoting USP1‐UAF1‐mediated FANCD2 deubiquitination) has been reported in a study utilising a ~60% FANCD2‐ubiquitinated ID2 complex produced with the aid of a 64‐mer single‐stranded DNA (Liang et al, 2019)."

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"Interestingly, the recently identified deubiquitinating enzyme, USP1, negatively regulates both FANCD2 and PCNA monoubiquitination, suggesting an interaction between these seemingly parallel DNA damag[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP1 deubiquitinates both ub-FANCD2 [XREF_BIBR] and ub-FANCI [XREF_BIBR], thus reverting the critical event in the activation of the FA pathway."

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"The USP1 and UAF1 complex deubiquitylates FANCD2 and FANCI."

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"The UAF1 and USP1 complex deubiquitinates FANCD2 during execution of the Fanconi anemia DNA damage response pathway."

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"Finally, FANCD2 is deubiquitinated by the USP1 and UAF1 deubiquitinating enzyme complex [XREF_BIBR, XREF_BIBR]."

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"In addition to the monoubiquitination of FANCD2, deubiquitination of FANCD2 by deubiquitination enzyme USP1 is known to be required for ICL repair."

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"Finally, FANCD2-Ub and PCNA-Ub are coordinately deubiquitinated by the same deubiquitinating (DUB) enzyme complex, USP1 and UAF1 43."

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"However, after the overexpression of SERPINB3, the expression level of USP1 was increased, which could accelerate the deubiquitination of FANCD2–FANCI during ICLs repair."
USP1 deubiquitinates ubiquitinated FANCD2. 4 / 4
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"Furthermore, the USP1 and UAF1 complex can readily, and rapidly, de-ubiquitinate mono-ubiquitinated FANCD2 in an in vitro de-ubiquitination reaction [XREF_BIBR]."

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"Previous studies have shown that USP1 deubiquitylates mono-ubiquitinated PCNA (ub-PCNA) and mono-ubiquitinated FANCD2 (ub-FANCD2) in response to replication stress due to DNA damage during DNA replication (4, 5, 41)."

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"In addition, monoubiquitinated FANCD2/FANCI proteins are deubiquitinated by the USP1/UAF1 complex after DNA removal, completing the ICL repair procedure [42–45]."

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"USP1 is known to play a critical role in Fanconi anemia, complementation group A by deubiquitinating mono-ubiquitinated FANCD2 [19]."
Unubiquitinated USP1 leads to the deubiquitination of FANCD2. 1 / 1
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"These include the deubiquitylation of PCNA and FANCD2 catalysed by USP1, deubiquitylation and stabilisation of 53BP1 or claspin by USP28 and more recently is has been reported that USP3 catalyses the deubiquitylation of H2AX and gamma-H2AX."
USP1 affects FANCI
1 1 | 25
USP1 deubiquitinates FANCI. 10 / 27
1 1 | 25

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"Similarly, USP1, which plays an important role in DNA repair by specifically deubiquitylating FANCI/FANCD2 (I-D2), relies on UAF1 for allosteric activation and substrate recognition ( Cohn et al., 200[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"We have previously shown that USP1, in complex with its stimulatory binding partner, UAF1, deubiquitinates the Fanconi Anemia (FA) proteins, FANCD2 and FANCI."

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"USP1 influences accumulation of the Fanconi anaemia core complex at DNA damage sites and deubiquitylates FANCD2–FANCI in a cell cycle-dependent manner ."

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"The USP1 and UAF1 complex deubiquitylates FANCD2 and FANCI."

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"How USP1 eventually deubiquitinates the FANCD2 and FANCI complex following the completion of the DNA repair is still a question."

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"Inhibition of USP1 increases monoubiquitination of both FANCD2 and FANCI, indicating further coordinate regulation at this level as well."

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"More recent evidence suggests that a later deubiquitination of FANCD2 and FANCI by USP1 and UAF1 might be required for efficient foci assembly and HR mediated repair (J. Kim and A. D'Andrea, unpublished observation)."

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"Indeed, USP1 is required for DNA damage induced FANCD2 foci formation [58-60] and FANCI de-ubiquitinated by USP1 is needed for efficient foci formation of the core complex [51]."

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"In the Fanconi anemia pathway, USP1 deubiquitinates FANCD2 and FANCI, two components of the Fanconi anemia complex, in order to facilitate DNA repair."

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"Monoubiquitination or ATR dependent phosphorylation of FANCI were not required for the FA core complex recruitment, but FANCI deubiquitination by USP1 was."
USP1 affects ID1
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USP1 deubiquitinates ID1. 10 / 23
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"Recently, it has been shown that USP1, a ubiquitin specific protease, deubiquitinates ID1 and rescues it from proteasome degradation."

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"USP1 deubiquitinates and stabilizes the ID1, ID2, and ID3 proteins to preserve a mesenchymal stem cell (MSC) program in osteosarcoma [21] ."

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"USP1 deubiquitinates ID proteins to preserve a mesenchymal stem cell program in osteosarcoma."

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"Once the lesion has been repaired, the ID complex is deubiquitinated by the USP1 and UAF1 complex, which also acts on monoubiquitinated PCNA when associated to the RFC subunit ELG1."

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"By deubiquitinating ID proteins, USP1 contributes to prevent bHLH mediated differentiation, and thus maintain stem-cell characteristics in osteosarcoma cells [XREF_BIBR]."

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"USP1 deubiquitinates ID proteins to preserve a mesenchymal stem cell program in osteosarcoma."

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"One of the responsible mechanisms for OS pathogenesis is the deubiquitination of ID proteins by enzyme USP1, which helps maintain the OS cell stemness."

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"USP1 also deubiquitinates and stabilizes the transcriptional regulators ID1, ID2 and ID3 [XREF_BIBR - XREF_BIBR]."

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"Another piece of evidence for a tight coordination between the two pathways is the notion that the isopeptidase USP1 mediates deubiquitylation of both PCNA and the ID complex."

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"The FA ID complex is deubiquitinated by the UAF1 and USP1 complex."
USP1 affects ID2
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USP1 deubiquitinates ID2. 9 / 10
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"Mechanically, we demonstrated that USP1 promoted GC metastasis via upregulating ID2 expression and further confirmed that USP1 stabilized ID2 expression through deubiquitinating ID2 in GC."

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"USP1 also deubiquitinates and stabilizes the transcriptional regulators ID1, ID2 and ID3 [XREF_BIBR - XREF_BIBR]."

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"It is presently unclear how USP1 catalyses de-ubiquitination of the ID2 complex as monoubiquitinated FANCI occludes the USP1 interaction site in FANCD2 ."

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"For instance, USP1 slows osteosarcoma proliferation by deubiquitinating the inhibitors of DNA binding proteins (IDs) ID1, ID2, and ID3, in order to maintain a differentiated state in low-aggressive cells [111]."

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"Therefore, we sought a deubiquitinating enzyme that counters ID ubiquitination.We show that USP1 deubiquitinates and stabilizes ID1, ID2, and ID3, resulting in their increased abundance."

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"To address whether USP1 deubiquitinated ID2 directly, ubiquitinated ID2 purified from 293T cells was incubated in vitro with either wild-type USP1 or USP1 C90S purified separately from 293T cells."

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"After participating in the FA pathway, the ID2 complex needs to be immediately de-ubiquitinated, which is mediated by the ubiquitin-specific peptidase USP1."

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"Similarly, USP1, which plays an important role in DNA repair by specifically deubiquitylating FANCI/FANCD2 (I-D2), relies on UAF1 for allosteric activation and substrate recognition ( Cohn et al., 200[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP1 deubiquitinates and stabilizes the ID1, ID2, and ID3 proteins to preserve a mesenchymal stem cell (MSC) program in osteosarcoma [21] ."
USP1 deubiquitinates ubiquitinated ID2. 2 / 2
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"To address whether USP1 deubiquitinated ID2 directly, ubiquitinated ID2 purified from 293T cells was incubated in vitro with either wild-type USP1 or USP1 C90S purified separately from 293T cells."

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"Finally, the monoubiquitinated ID2 is deubiquitinated by USP1 (ubiquitin-specific protease-1) and UAF1 (USP1-associated factor-1), which releases ID2 from DNA ( Tan et al., 2020c ) to complete the DNA[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
Modified USP1 leads to the deubiquitination of ID2. 1 / 1
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"Both basal and USP1 induced ID2 deubiquitination was enhanced by coexpression of USP1 cofactor WDR48 (Cohn et al., 2007)."
USP1 affects EZH2
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USP1 deubiquitinates EZH2. 10 / 13
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"Accordingly, depletion of endogenous USP1 using two independent shRNAs promotes EZH2 ubiquitination in GSC11 and U87MG cells (Fig.3D and Fig.S3B)."

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"Overexpression of wild-type USP1 notably reduced the ubiquitination of EZH2 (lane 3, Fig.3C), and this effect was enhanced by further expressing WDR48, an USP1-binding partner enhancing the activity of USP1 (lane 4, Fig.3C)."

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"Of those four DUBs, only USP1 significantly reduced the ubiquitination of EZH2 protein (Fig.S2B), indicating that USP1 may act as a deubiquitinase of EZH2."

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"USP1 interacts with and deubiquitinates EZH2 directly.."

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"Moreover, EZH2 is deubiquitinated in vitro by USP1/WDR48."

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"Furthermore, β-catenin could transcriptionally activate USP1 which in turn deubiquitinates and stabilizes EZH2."

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"beta-catenin/TCF4 activated transcription of the deubiquitinase USP1, which then interacted with and deubiquitinated EZH2 directly."

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"To address the question whether USP1 deubiquitinates EZH2 directly, ubiquitinated EZH2 was purified from HEK293T cells and incubated with USP1 and WDR48 proteins."

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"We found that β-catenin induced the expression of USP1, which then interacted and deubiquitinated EZH2 directly to suppress the ubiquitin-proteasomal degradation of EZH2."

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"In vitro deubiquitylation of EZH2 by USP1 was performed as described previously."
USP1 affects PARP1
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USP1 deubiquitinates PARP1. 9 / 9
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"USP1 promotes cholangiocarcinoma progression by deubiquitinating PARP1 to prevent its proteasomal degradation."

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"Firstly, we identify the deubiquitination of PARP1 by USP1 as one of its major targets in CCA."

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"Together, these results confirm that USP1 directly deubiquitinates PARP1.To determine the lysine site of PARP1 targeted by USP1, we conducted a thorough analysis of the ubiquitination-specific mass spectrometry data and observed that Lys-197 may be an important site for USP1 deubiquitination of PARP1 (Fig. 3E)."

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"Together, these data suggested that USP1 deubiquitinates PARP1, but it is not involved in the regulation of its protein stability that, conversely, seems to be linked to the activity of USP15 in triple-negative breast cancer model (22)."

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"We confirmed that USP1 inhibition, alone and better in combination with niraparib, enhanced PARP1 ubiquitination (Fig. 4C and fig."

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"Overall, the data collected here indicated that USP1 activity is necessary to deubiquitinate PARP1 at the site of DNA damage thereby modulating PARP1 dynamic activity necessary for the repair of damaged DNA (Fig. 6I)."

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"USP1 deubiquitinates PARP1 to regulate its trapping and PARylation activity."

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"Moreover, the overexpression of USP1 but not of the inactive form USP1 (9) reduced PARP1 polyubiquitination (Fig. 4A)."

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"It suggests that K197 site is the primary USP1 deubiquitination target on PARP1 controlling its degradation.Poly-ubiquitination chains are generated primarily through two distinct types of bonds: Lys48 or Lys63 chains."
USP1 affects BCAT2
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USP1 deubiquitinates BCAT2 on K229. 5 / 5
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"USP1 deubiquitylates BCAT2 at the K229 site."

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"In addition, KRAS and USP1 can also regulate the expression of BCAT2 in PDAC through the ubiquitin-proteasome pathway: KRAS can stabilize the expression of BCAT2 in PDAC by inhibiting the ubiquitination of BCAT2 by spleen tyrosine kinase (SYK) and E3 ubiquitination ligase TRIM21, while USP1 deubiquitinates the K229 site of BCAT2, and BCAAs promote USP1 protein expression at the translation level through the GCN2-eIF2a pathway."

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"In turn, elevated USP1 deubiquitylates BCAT2 at the K229 site to stabilize BCAT2 protein."

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"Moreover, we screened with an available deubiquitylase library which contains 31 members of USP family and identified that USP1 deubiquitylates BCAT2 at the K229 site."

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"High concentrations of BCAA increase the translation of ubiquitin-specific peptidase 1 (USP1) by inhibiting the GCN2-eIF2α signalling pathway, and USP1 in turn deubiquitinates BCAT2 at the K229 site to stabilize its protein expression, leading to increased catabolism of BCAAs to promote PDAC cell proliferation [41]."
USP1 deubiquitinates BCAT2. 4 / 4
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"Next, we found that treatment with ML323, a specific inhibitor of USP1 [33], enhanced BCAT2 ubiquitylation (Fig. 2B) whereas USP1 wild-type but not enzyme-dead C90S mutant overexpression decreased BCAT2 ubiquitylation (Fig. 2C)."

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"Furthermore, USP1 knockdown enhanced ubiquitylation of the BCAT2 but not BCAT2 mutant (Fig. 3B)."

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"In contrast, ectopic USP1 expression decreased ubiquitylation of the BCAT2 but not BCAT2 mutant (Fig. 3C)."

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"BCAAs promote the expression of USP1 protein, and USP1 can deubiquitylate BCAT2."
USP1 affects AKT
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USP1 deubiquitinates AKT. 8 / 8
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"As an AKT regulator, USP1 deubiquitinates AKT."

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"USP1, similarly to USP12 and USP46, deubiquitinates AKT phosphatases PHLPP and PHLPPL [XREF_BIBR] and relies on UAF1 for its enzymatic activity, while it does not bind to WDR20 or any other additional proteins [XREF_BIBR]."

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"For example, the Ubiquitin carboxyl-terminal hydrolase 7 (Usp7) regulates the subcellular localization of PTEN 28 and Usp1 deubiquitinates Akt 29."

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"USP1 deubiquitinates Akt to inhibit PI3K-Akt-FoxO signaling in muscle during prolonged starvation."

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"USP1 deubiquitinates AKT in vivo and cuts the ubiquitin chain at the Lys63 site of AKT, thus inhibiting PI3K-Akt signal transduction in B-cell acute lymphoblastic leukemia [185]."

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"Interestingly, USP1 was reported to regulate glucose uptake and muscle atrophy via deubiquitination of AKT during fasting [23]."

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"The results of the study by Dana Goldbraikh et al. showed that USP1 promoted the deubiquitination of Akt and reduced its phosphorylation level, while inhibition of USP1 promoted the activation of PI3K/Akt pathway [24]."

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"USP1 deubiquitinates Akt to inhibit PI3K-Akt-FoxO signaling in muscle during prolonged starvation."
USP1 leads to the deubiquitination of AKT on K63. 1 / 1
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"Similarly, under prolonged starvation, ubiquitin specific peptidase 1 (USP1) inhibits polyubiquitination of Akt at K63, which inhibits PI3K/Akt/FoxO signaling events ( Goldbraikh et al., 2020 )."
USP1 affects hsFANCD2-Ub
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USP1 deubiquitinates hsFANCD2-Ub. 8 / 8
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"With the substrates purified (Fig 2C), we assessed whether hsFANCD2-Ub, hsFANCI-Ub, or hsPCNA-Ub is directly deubiquitinated by USP1–UAF1 in vitro."

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"The recombinant USP1 is able to fully deubiquitinate hsFANCD2-Ub, hsFANCI-Ub, and hsPCNA-Ub at sub-stoichiometric concentrations, in a UAF1-dependent manner (Fig 2D)."

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"As shown, USP1 –UAF1 readily deubiquitinates hsFANCD2-Ub, hsFANCI-Ub, and hsPCNA-Ub (Fig 3A)."

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"Surprisingly, USP1 –UAF1 is unable to deubiquitinate hsFANCD2-Ub and there is slower activity on hsPCNA-Ub at early time points (Fig 3A), indicating the catalytic domain is not sufficient despite the catalytic domain being active on other substrates including hsFANCI-Ub."

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"This is in contrast to USP1 , which is able to deubiquitinate hsFANCD2-Ub at sub-stoichiometric concentrations (Fig 3C)."

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"To determine whether the N-terminus dependence of hsFANCD2-Ub deubiquitination by USP1 was due to possible post-translational modifications in eukaryotic cells, we also expressed and purified USP1 and USP1 from E. coli and tested their activity (Fig S3)."

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"Whereas USP1 is able to deubiquitinate some of the hsFANCD2-Ub in the presence of both DNA and hsFANCI, a portion of hsFANCD2-Ub and hsFANCI-Ub remains resistant to deubiquitination (Fig 7A), consistent with the recent findings using frog substrates (32)."

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"Interestingly, when DNA is removed, all of the hsFANCD2-Ub and hsFANCI-Ub is deubiquitinated by USP1 –UAF1; in contrast, USP1 –UAF1 and USP1 –UAF1 do not deubiquitinate hsFANCD2-Ub (Fig 7A)."
USP1 affects TAFAZZIN
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USP1 deubiquitinates TAFAZZIN. 6 / 7
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"Regarding TAZ, ubiquitin-specific peptidase 1 (USP1), ubiquitin-specific peptidase 7 (USP7), ubiquitin-specific peptidase 26 (USP26), and ubiquitin-specific peptidase 36 (USP36) deubiquitinate TAZ [37–40]."

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"Recent reports have documented that TAZ can be directly deubiquitinated and stabilized by USP1 [46], USP10 [15], OTUB2 [16] and JOSD2 [47] in hepatocellular carcinoma, breast cancer and cholangiocarcinoma."

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"USP1 depletion promotes the ubiquitination of TAZ and results in dysfunctional Hippo signaling pathway."

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"By deubiquitinating and stabilizing the transcriptional co-activator with PDZ-binding motif (TAZ), USP1 leads to enhanced activity of RORγt, which is an important transcription factor for T helper type 17 (Th17) cell development."

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"USP19 and USP1 promote HCC progression by deubiquitinating YAP and TAZ, respectively [ 26 , 27 ]."

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"USP1-regulated reciprocal differentiation of Th17 cells and Treg cells by deubiquitinating and stabilizing TAZ."
USP1 affects MYC
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USP1 deubiquitinates MYC. 7 / 7
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"USP1 Deubiquitinates and Stabilizes c-MYC."

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"Our study showed that inhibition of USP1 by shRNA or pimozide treatment significantly increased the ubiquitination of MAX/MYC and reduced the protein levels of MAX/MYC in rituximab/chemotherapy resistant DLBCL cells, which led to the decrease of MYC target genes and the growth inhibition of lymphoma cells in the cell or patient-derived DLBCL mouse model."

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"In summary, these results suggested that USP1 deubiquitinates and stabilizes c-MYC."

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"Finally, we investigated whether USP1 could inhibit the ubiquitination of c-MYC and found that USP1, but not USP1 C90S, decreased the ubiquitination level of c-MYC, thus increasing its stability (Figure 5H)."

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"USP1 is an oncogene that deubiquitinates and stabilizes c-MYC, thereby promoting cancer progression in vitro and in vivo."

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"Together, these data demonstrated that USP1 deubiquitinated and stabilized MAX and MYC proteins in rituximab/chemotherapy resistant DLBCL cells."

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"Overexpression of USP1 prolonged the half-life of MAX/MYC protein and decreased the ubiquitination of MAX/MYC protein."
USP1 affects MAX
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USP1 deubiquitinates MAX. 5 / 5
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"Overexpression of USP1 prolonged the half-life of MAX/MYC protein and decreased the ubiquitination of MAX/MYC protein."

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"Our study showed that inhibition of USP1 by shRNA or pimozide treatment significantly increased the ubiquitination of MAX/MYC and reduced the protein levels of MAX/MYC in rituximab/chemotherapy resistant DLBCL cells, which led to the decrease of MYC target genes and the growth inhibition of lymphoma cells in the cell or patient-derived DLBCL mouse model."

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"USP1 deubiquitinates MAX, which is an important MYC-binding protein and promotes MYC gene transcription."

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"Furthermore, USP1 knockdown enhanced ubiquitylation of the MAX but not MAX mutant (Supplementary Fig. S4c)."

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"Together, these data demonstrated that USP1 deubiquitinated and stabilized MAX and MYC proteins in rituximab/chemotherapy resistant DLBCL cells."
USP1 deubiquitinates MAX on K24. 1 / 1
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"To determine which the lysine residues in MAX deubiquitinated by USP1, we mutated K24, K40 or K57, which were predicted as potential ubiquitylation sites of MAX [21]."
USP1 affects SNAI1
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USP1 deubiquitinates SNAI1. 3 / 4
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"Here, we demonstrate that, following platinum treatment of OC cells, USP1 is able to de-ubiquitinate and stabilize Snail, eventually resulting in platinum resistance and metastatic dissemination of OC cells.Our work highlights a novel function of USP1, acting as a key factor that links platinum response to tumor spreading through the stabilization of Snail protein."

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"Once phosphorylated, USP1 binds to and deubiquitinates Snail, resulting in resistance to cisplatin and an increased metastatic potential [61]."

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"USP1 de-ubiquitinates and stabilizes Snail protein."
Mutated USP1 leads to the deubiquitination of SNAI1. 1 / 1
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"Accordingly, compared to USP1 , expression of USP1 mutant did not lead to Snail de-ubiquitination (Fig. 4F), and from a biological point of view, it failed to protect OVCAR-8 cells from CDDP-induced cell death (Fig. 4G)."
USP1 affects ID3
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USP1 deubiquitinates ID3. 4 / 5
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"For instance, USP1 slows osteosarcoma proliferation by deubiquitinating the inhibitors of DNA binding proteins (IDs) ID1, ID2, and ID3, in order to maintain a differentiated state in low-aggressive cells [111]."

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"Therefore, we sought a deubiquitinating enzyme that counters ID ubiquitination.We show that USP1 deubiquitinates and stabilizes ID1, ID2, and ID3, resulting in their increased abundance."

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"USP1 deubiquitinates and stabilizes the ID1, ID2, and ID3 proteins to preserve a mesenchymal stem cell (MSC) program in osteosarcoma [21] ."

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"USP1 also deubiquitinates and stabilizes the transcriptional regulators ID1, ID2 and ID3 [XREF_BIBR - XREF_BIBR]."
USP1 affects hsFANCI-Ub
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USP1 deubiquitinates hsFANCI-Ub. 4 / 4
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"The recombinant USP1 is able to fully deubiquitinate hsFANCD2-Ub, hsFANCI-Ub, and hsPCNA-Ub at sub-stoichiometric concentrations, in a UAF1-dependent manner (Fig 2D)."

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"With the substrates purified (Fig 2C), we assessed whether hsFANCD2-Ub, hsFANCI-Ub, or hsPCNA-Ub is directly deubiquitinated by USP1–UAF1 in vitro."

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"As shown, USP1 –UAF1 readily deubiquitinates hsFANCD2-Ub, hsFANCI-Ub, and hsPCNA-Ub (Fig 3A)."

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"Interestingly, when DNA is removed, all of the hsFANCD2-Ub and hsFANCI-Ub is deubiquitinated by USP1 –UAF1; in contrast, USP1 –UAF1 and USP1 –UAF1 do not deubiquitinate hsFANCD2-Ub (Fig 7A)."
USP1 affects TBK1
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USP1 deubiquitinates TBK1. 4 / 4
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"Studiy have shown that in the antiviral response signaling pathway of type I interferon, the deubiquitinase USP1 interacts with TBK1 to deubiquitinate TBK1, enhance the expression of downstream type I interferon, and inhibits viral replication (Yu et al., 2017)."

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"USP1 greatly inhibited TBK1 ubiquitination, whereas USP12 and USP46 had no effects on TBK1 ubiquitination."

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"USP1 has been reported to enhance the activation of STAT1 (phosphorylation on tyrosine 701, pSTAT1) by deubiquitinating and stabilizing tank binding kinase 1 (TBK1) [34]."

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"Studies have shown that in the antiviral response signaling pathway of type I interferon, the deubiquitinase USP1 interacts with TBK1 to deubiquitinate TBK1, enhance the expression of downstream type I interferon, and inhibits viral replication (Yu et al., 2017)."
USP1 affects KDM4A
| 4
USP1 deubiquitinates KDM4A. 4 / 4
| 4

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"A significant decrease in polyubiquitylated KDM4A protein was observed in cells transfected with GST fusion USP1, whereas GST fusion USP1 (CS) was not able to reduce KDM4A ubiquitination."

reach
"9, 27, 28 As KDM4A plays a key role in human cancer development, it is possible that in human cancers USP1 promotes the deubiquitination and stabilization of KDM4A."

reach
"3.4 USP1 deubiquitinates KDM4A."

reach
"USP1 deubiquitinates and stabilizes KDM4A, thereby promoting the binding of AR to the c-MYC gene enhancer."
USP1 affects BRD4
| 4
USP1 deubiquitinates BRD4. 4 / 4
| 4

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"To examine whether USP1 deubiquitinated BRD4, we then set up in vivo and in vitro deubiquitination assay."

reach
"USP1 itself is also overexpressed in liver cancer and we show USP1 deubiquitinates BRD4 in vivo and in vitro, which increases BRD4 stability."

reach
"USP1 deubiquitinates and stabilizes BRD4."

reach
"IP-WB showed that USP1-KD indeed increased ubiquitination of BRD4 in different liver cancer cells (Fig. 3E)."
USP1 affects ATG14
| 4
USP1 deubiquitinates ATG14. 4 / 4
| 4

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"USP1 promotes pancreatic cancer progression and autophagy by deubiquitinating ATG14."

reach
"USP1 deubiquitinates and stabilizes ATG14 protein."

reach
"Intriguingly, USP1 inhibition by SJB3-019A increased the ubiquitin level of ATG14 (Fig. 5J), indicating that USP1 deubiquitinates and stabilizes ATG14 protein."

reach
"USP1 deubiquitinates and stabilizes ATG14, thus remarkably promoting malignant features, such as cell proliferation, migration, autophagy, and tumor growth in PDAC."
USP1 affects hsPCNA-Ub
| 3
USP1 deubiquitinates hsPCNA-Ub. 3 / 3
| 3

reach
"The recombinant USP1 is able to fully deubiquitinate hsFANCD2-Ub, hsFANCI-Ub, and hsPCNA-Ub at sub-stoichiometric concentrations, in a UAF1-dependent manner (Fig 2D)."

reach
"As shown, USP1 –UAF1 readily deubiquitinates hsFANCD2-Ub, hsFANCI-Ub, and hsPCNA-Ub (Fig 3A)."

reach
"With the substrates purified (Fig 2C), we assessed whether hsFANCD2-Ub, hsFANCI-Ub, or hsPCNA-Ub is directly deubiquitinated by USP1–UAF1 in vitro."
USP1 affects Ubiquitin
| 3
USP1 deubiquitinates Ubiquitin. 3 / 3
| 3

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"Upon the induction of DNA damage, a fragment of USP1, ending in gly-gly, is produced, suggesting that USP1 “deubiquitinates” itself at an internal Ub-like region."

reach
"Wild-type USP1 that is autocleavage-inactive (G670A, G671A) deubiquitinated Ub–PCNA subunits, whereas catalytically inactive USP1 (C90S) did not."

reach
"These findings demonstrate that ATAD5-N modulates Ub–PCNA deubiquitination process directly and is crucial for UAF1–USP1 to efficiently deubiquitinate Ub–PCNA."
USP1 affects TRAF6
| 3
USP1 deubiquitinates TRAF6. 3 / 3
| 3

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"USP1 function as an oncogene by interacting with DNA repair signal through PCNA and FANCD2 [35], USP4 promote cancer progression by deubiquitinating TRAF2 and TRAF6 and thereby regulating the TGFβ signaling pathway [36]."

reach
"Our result showed that overexpressing USP1 remarkably attenuated TRAF6 ubiquitination (Figure 4D), suggesting that USP1 stabilizes TRAF6 by decreasing TRAF6 ubiquitination, therefore regulating NF-κB signaling."

reach
"Our data show that USP1 decreases TRAF6 ubiquitination."
USP1 affects SHOX2
| 3
USP1 leads to the deubiquitination of SHOX2. 3 / 3
| 3

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"Taken together, these results suggest that m6A-modified KIF9-AS1 promotes HCC chemoresistance via the deubiquitination of SHOX2 mediated by USP1."

reach
"Accordingly, we observed that USP1 suppression induced an increase in SHOX2 ubiquitination, leading to the downregulation of SHOX2 expression in HCC cells."

reach
"While SHOX2 is subjected to ubiquitination medicated degradation, USP1 enhances the deubiquitination of SHOX2, leading to high level of SHOX2 in HCC cells."
USP1 affects CHEK1
| 3
USP1 deubiquitinates CHEK1. 3 / 3
| 3

reach
"Multiple ubiquitin ligases, including the SKP1-CUL1-F-box (SCF) complex, CUL4-DDB1, and HUWE1 [ 89–93 ] can target CHK1 for proteasomal degradation, whereas the deubiquitinases USP1, USP3, USP7, and A[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"Moreover, BRD7 knockdown specifically increased USP1 levels but had no effect on the levels of USP7 and ATXN3, suggesting that increased USP1 may deubiquitinate and stabilize CHK1 (Figs."

reach
"Interestingly, USP1 silencing only partially reversed the protein levels of CHK1 (Fig. 3B, lanes 3 versus 2 and 1) and totally reversed the protein half-life and ubiquitination of CHK1, which further indicates BRD7 could negatively regulate CHK1 transcription."
USP1 affects CEBPB
| 3
USP1 deubiquitinates CEBPB. 3 / 3
| 3

reach
"Overexpression of USP1 WT caused a decrease in C/EBPβ ubiquitination, leading to stabilized C/EBPβ protein levels, whereas USP1 C90S, a catalytically inactive form of USP1, did not (Fig. 5D, E)."

reach
"We confirmed that USP1 directly interacts with and deubiquitinates C/EBPβ, enhancing the stability of C/EBPβ in the regulation of adipogenesis."

reach
"USP1 directly interacts with and deubiquitinates C/EBPβ, enhancing its stability in the regulation of adipogenesis [15]."
USP1 affects BIRC5
| 3
USP1 leads to the deubiquitination of BIRC5. 2 / 2
| 2

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"Moreover, USP1 inhibited survivin ubiquitination level, which was recovered in Tan IIA-treated CRC cells (Fig. 4B)."

reach
"Recent research has shown that USP1 interacts with survivin and promotes survivin deubiquitination and stability [31]."
USP1-C90S leads to the deubiquitination of BIRC5. 1 / 1
| 1

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"We examined Survivin ubiquitylation in cells expressing USP1 and USP1 C90S catalytic dead mutant and found that USP1, but not USP1 C90S, was able to decrease Survivin ubiquitylation."
USP1 affects mUb-PCNA
| 2
USP1 deubiquitinates mUb-PCNA. 2 / 2
| 2

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"Moreover, deubiquitination of mUb-PCNA by USP1 29, USP10 30, or interferon stimulated gene 15 modification of PCNA has also been suggested to dictate TLS termination 30."

reach
"Although Poleta reduced affinity for the DNA beyond the CPD might contribute to its dissociation after TLS 28, deubiquitination of mUb-PCNA by USP1 29 or USP10 30 can promote Poleta displacement from replication forks."
USP1 affects USP1
| 2
USP1 deubiquitinates USP1. 1 / 1
| 1

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"Interestingly, whereas USP1 –UAF1 deubiquitinates both substrates K561-Ub and KX-Ub at similar rates, USP1 –UAF1 shows clear activity on KX-Ub but little detectable activity on K561-Ub (Fig 4C)."
Modified USP1 leads to the deubiquitination of USP1. 1 / 1
| 1

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"To further validate this point, experimental evidence has suggested that higher than normal levels of USP1 will inhibit the DNA damage induced monoubiquitination of USP1 targets, such as FANCD2, FANCI, and PCNA, whereas the loss of USP1 has been shown to cause chromosomal instability and elevated perinatal lethality in mice."
USP1 affects ULK1
1 | 1
USP1 deubiquitinates ULK1. 1 / 2
1 | 1

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"For robust post-initiation autophagy, ULK1 deubiquitination by USP1 is required after TRAF6-induced ULK1 ubiquitination, promoting breast cancer cell survival and proliferation."
USP1 affects STAT1
| 2
USP1 deubiquitinates STAT1. 2 / 2
| 2

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"Therefore, it is possible that the UAF1-USP1 complex might deubiquitinate STAT1 to promote its recruitment to and subsequent activation by IFNAR."

reach
"Therefore, it is possible that the UAF1-USP1 complex might deubiquitinate STAT1 to promote its interaction with and subsequent activation by IFNAR."
USP1 affects RPS16
1 | 1
USP1 leads to the deubiquitination of RPS16. 1 / 2
1 | 1

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"A recent study has shown that USP1 can mediate the deubiquitination and stabilization of RPS16 and that ML-323 can remarkably inhibit the growth and metastasis of HCC cells [32], which is in agreement with our results."
USP1 affects PHLPP1
1 | 1
USP1 deubiquitinates PHLPP1. 1 / 2
1 | 1

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"USP1, similarly to USP12 and USP46, deubiquitinates AKT phosphatases PHLPP and PHLPPL [XREF_BIBR] and relies on UAF1 for its enzymatic activity, while it does not bind to WDR20 or any other additional proteins [XREF_BIBR]."
USP1 affects KIF11
| 2
USP1 deubiquitinates KIF11. 2 / 2
| 2

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"The results revealed that USP1 overexpression reduces K48-linked polyubiquitination of KIF11, while the K77R mutant of KIF11 does not undergo K48-linked polyubiquitination (Fig. 6G)."

reach
"These results suggest that USP1 plays a critical role in stabilizing KIF11 protein levels in hepatocellular carcinoma cells by removing ubiquitin modifications and preventing its degradation via the ubiquitin–proteasome pathway.To clarify the molecular mechanism by which USP1 deubiquitinates KIF11, we identified the interaction site between these proteins within the Kinesin Motor domain, specifically at the K77 residue, using truncation and lysine mutation experiments."
USP1 affects IDs
| 2
USP1 deubiquitinates IDs. 2 / 2
| 2

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"Deubiquitination of IDs by USP1 promotes ID protein stability and prevents stem cell differentiation."

reach
"For instance, USP1 slows osteosarcoma proliferation by deubiquitinating the inhibitors of DNA binding proteins (IDs) ID1, ID2, and ID3, in order to maintain a differentiated state in low-aggressive cells [111]."
USP1 affects FUS
| 2
USP1 deubiquitinates FUS. 2 / 2
| 2

reach
"Notably, USP1, a deubiquitinating enzyme for PCNA-Ub is exclusively degraded upon UVC damage-dependent autocleavage to promote PCNA monoubiquitination and TLS, arguing for the presence of specific DDR signaling that is utilized to promote stalled fork recovery from UVC-induced DNA lesions (41)."

reach
"[88] USP1 deubiquitinates PCNA—an important component of the trans-lesions synthesis (TLS) repair pathway."
USP1 affects FANCD2/I
| 2
USP1 deubiquitinates ubiquitinated FANCD2/I. 2 / 2
| 2

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"USP1 deubiquitinates mono-ubiquitinated FANCD2/I, thereby reversing the critical step in the activation of the Fanconi anemia pathway [6–8]."

reach
"USP1 is an important regulator of the DNA damage response, deubiquitinating mono-ubiquitinated FANCD2/I and PCNA [6, 8, 9]."
USP1 affects AURKA
| 2
USP1 deubiquitinates AURKA. 2 / 2
| 2

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"The deubiquitination of AURKA by USP1 was investigated by Co-IP and Western blot."

reach
"USP1 increased AURKA stability by mediating AURKA deubiquitination."
USP1 affects xlFANCD2-Ub
| 1
USP1 deubiquitinates xlFANCD2-Ub. 1 / 1
| 1

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"In contrast to previous reports, we found that USP1 and USP1 are able to fully deubiquitinate xlFANCD2-Ub (Fig 3D)."
| 1

reach
"USP1 can deubiquitinate ID1 (inhibitor of DNA binding 1), a transcription regulator, which was identified to control leukemogenesis by us previously, and protected ID1 from proteasome-mediated degradation [13]."
USP1 affects polycomb repressive complex1
| 1
USP1 deubiquitinates polycomb repressive complex1. 1 / 1
| 1

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"USP1 deubiquitinates polycomb repressive complex1 (PRC1), an important epigenetic modifier in stem cell development and maintenance [19] ."
USP1 affects monoubiquitinated-PCNA
| 1
USP1 deubiquitinates monoubiquitinated-PCNA. 1 / 1
| 1

reach
"Recent studies have shown that monoubiquitinated-PCNA is deubiquitinated by the deubiquitinating enzyme USP1 [XREF_BIBR]."
USP1 affects lane 3
| 1
USP1 leads to the deubiquitination of lane 3. 1 / 1
| 1

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"Overexpression of wild-type USP1 notably reduced the ubiquitination of EZH2 (lane 3, Fig.3C), and this effect was enhanced by further expressing WDR48, an USP1-binding partner enhancing the activity of USP1 (lane 4, Fig.3C)."
USP1 affects hsFANCD2-Ub-FANCI
| 1
USP1 deubiquitinates hsFANCD2-Ub-FANCI. 1 / 1
| 1

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"Using this set-up, we observed that USP1 –UAF1 is able to deubiquitinate hsFANCD2-Ub-FANCI with and without benzonase treatment (Fig 7B)."
USP1 affects ZEB1
| 1
USP1 leads to the deubiquitination of ZEB1. 1 / 1
| 1

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"Ubiquitination of ZEB1 may also be decreased by USP1 in UV-induced skin photoaging."
USP1 affects YAP1
| 1
USP1 deubiquitinates YAP1. 1 / 1
| 1

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"USP19 and USP1 promote HCC progression by deubiquitinating YAP and TAZ, respectively [ 26 , 27 ]."
USP1 affects WDR48
| 1
USP1 deubiquitinates WDR48. 1 / 1
| 1

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"To test whether this extended interface is involved in protecting FANCI from deubiquitination, we mutated H209, V243 and P244 of FANCD2 to alanine residues, and assessed I ‐DNA deubiquitination by USP1UAF1 in the presence of wild‐type (D2 ) or H209A/V243A/P244A mutated (D2 ) FANCD2."
USP1 affects Taniguchi et al., 2002
| 1
USP1 deubiquitinates Taniguchi et al., 2002. 1 / 1
| 1

reach
"USP1 can involve in DNA interstrand crosslink repair by deubiquitinating the Fanconi anemia protein (Taniguchi et al., 2002; Kim and D'Andrea, 2012) and regulating DNA damage response pathways (Jang and Kim, 2021)."
USP1 affects TRAF2
| 1
USP1 deubiquitinates TRAF2. 1 / 1
| 1

reach
"USP1 function as an oncogene by interacting with DNA repair signal through PCNA and FANCD2 [35], USP4 promote cancer progression by deubiquitinating TRAF2 and TRAF6 and thereby regulating the TGFβ signaling pathway [36]."
USP1 affects SIX1
| 1
USP1 deubiquitinates SIX1. 1 / 1
| 1

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"In addition, a recent report has shown that USP1 regulates the expression of cyclinD1 by deubiquitinating SIX1, and pharmacological or genetic inhibition of USP1 by ML-323 or siRNA downregulates the expression of SIX1 and cyclinD1, whereas the upregulation of USP1 increased the protein levels of SIX1 and cyclin D1 [41]."
USP1 affects RAD51AP1
| 1
USP1 deubiquitinates RAD51AP1. 1 / 1
| 1

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"This implies that RAD51AP1 may be regulated by ubiquitination, and that USP1 deubiquitinates RAD51AP1."
USP1 affects PRC1
| 1
USP1 deubiquitinates PRC1. 1 / 1
| 1

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"USP1 deubiquitinates polycomb repressive complex1 (PRC1), an important epigenetic modifier in stem cell development and maintenance [19] ."
USP1 affects PLK1
| 1
USP1 deubiquitinates PLK1. 1 / 1
| 1

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"Further results demonstrate that USP1 interacts with and deubiquitinates PLK1, leading to PLK1 stabilization.15 Notably, USP1 expression positively correlated with PLK1 in pediatric primary T-ALL samples, verifying the regulation between USP1 and PLK1."
USP1 affects PHLPP2
| 1
USP1 deubiquitinates PHLPP2. 1 / 1
| 1

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"USP1, similarly to USP12 and USP46, deubiquitinates AKT phosphatases PHLPP and PHLPPL [XREF_BIBR] and relies on UAF1 for its enzymatic activity, while it does not bind to WDR20 or any other additional proteins [XREF_BIBR]."
USP1 affects PDZ
| 1
USP1 leads to the deubiquitination of PDZ. 1 / 1
| 1

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"By deubiquitinating and stabilizing the transcriptional co-activator with PDZ-binding motif (TAZ), USP1 leads to enhanced activity of RORγt, which is an important transcription factor for T helper type 17 (Th17) cell development."
USP1 affects PCNA.PCNA
| 1
USP1 deubiquitinates PCNA.PCNA. 1 / 1
| 1

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"Rad18, having a high affinity for ssDNA coated with RPA ( Davies et al., 2008 ), can bind the gaps and monoubiquitinates PCNA.PCNA is deubiquitinated by the protease USP1, and after UVC irradiation, U[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP1 affects PCNA-mUb
| 1
USP1 deubiquitinates PCNA-mUb. 1 / 1
| 1

reach
"In contrast to USP1, which can deubiquitinate PCNA-mUb, MSH2, BRCA1 and Parkin have been shown to facilitate UV induced PCNA-mUb through promoting ssDNA generation and RPA focus formation."
USP1 affects PARP1-K197R
| 1
USP1 deubiquitinates PARP1-K197R. 1 / 1
| 1

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"We also found that USP1 did not deubiquitinate PARP1-K197R (Fig. 3F)."
USP1 affects MAP3K7
| 1
USP1 leads to the deubiquitination of MAP3K7. 1 / 1
| 1

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"11 , 12 , 13 Recent studies have found that the USP1 complex can downregulate the polyubiquitination of TAK1 and mediate its stability in vitro."
USP1 affects KPNA251
| 1
USP1 deubiquitinates KPNA251. 1 / 1
| 1

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"For example, USP1 promotes breast cancer metastasis by deubiquitinating KPNA251."
USP1 affects Id1-3
| 1
USP1 deubiquitinates Id1-3. 1 / 1
| 1

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"Moreover, the deubiquitinase USP1 can associate with and deubiquitinate Id1-3 in mesenchymal stem cells, thus preserving their stem cell state [XREF_BIBR]."
USP1 affects Figs
| 1
USP1 deubiquitinates Figs. 1 / 1
| 1

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"Moreover, BRD7 knockdown specifically increased USP1 levels but had no effect on the levels of USP7 and ATXN3, suggesting that increased USP1 may deubiquitinate and stabilize CHK1 (Figs."
USP1 affects Fig.S2B
| 1
USP1 leads to the deubiquitination of Fig.S2B. 1 / 1
| 1

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"Of those four DUBs, only USP1 significantly reduced the ubiquitination of EZH2 protein (Fig.S2B), indicating that USP1 may act as a deubiquitinase of EZH2."
USP1 affects Fanconi anemia group
| 1
USP1 deubiquitinates Fanconi anemia group on D2. 1 / 1
| 1

reach
"USP1 plays an important role in DNA damage response (DDR) by deubiquitinating proliferating cell nuclear antigen and Fanconi anemia group D2 protein (35, 36)."
USP1 affects Fanconi anemia complementation group I
| 1
USP1 deubiquitinates Fanconi anemia complementation group I. 1 / 1
| 1

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"Later studies showed that USP1 also deubiquitinates proliferating cell nuclear antigen (PCNA) and Fanconi anemia complementation group I (FANCI)."
USP1 affects Fanconi Anemia
| 1
USP1 deubiquitinates Fanconi Anemia. 1 / 1
| 1

reach
"We have previously shown that USP1, in complex with its stimulatory binding partner, UAF1, deubiquitinates the Fanconi Anemia (FA) proteins, FANCD2 and FANCI."
USP1 affects FLT3-ITD
| 1
USP1 leads to the deubiquitination of FLT3-ITD. 1 / 1
| 1

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"Importantly, we identified increased polyubiquitination of FLT3-ITD following USP1 inhibition (Fig. 4O)."
USP1 affects FANCI-FANCD2
| 1
USP1 leads to the deubiquitination of FANCI-FANCD2. 1 / 1
| 1

reach
"Monoubiquitination of FANCI-FANCD2 is reversed by the deubiquitinating enzyme (DUB) USP1."
USP1 affects FANCD2-I proteins
| 1
USP1 deubiquitinates FANCD2-I proteins. 1 / 1
| 1

reach
"FANCD2-I proteins are then deubiquitinated by the USP1-UAF1 complex [91,92,93,94,95,96]."
USP1 affects DNA-binding proteins 1–4
| 1
USP1 deubiquitinates DNA-binding proteins 1–4. 1 / 1
| 1

reach
"In addition to these three substrates, USP1 deubiquitinates a number of other substrates, including the inhibitor of DNA-binding proteins 1–4 (ID1-4), which regulate cell differentiation (13), and TBK1, which is involved in viral infection (14)."
USP1 affects CTNNB1
| 1
USP1 deubiquitinates CTNNB1. 1 / 1
| 1

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"A growing number of substrate-specific mammalian DUBs involved in tumorigenesis are continually being revealed such as USP1 and USP9X, which deubiquitinate FANCD2 and β-catenin, respectively ( Nijman [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP1 affects CCP110
| 1
USP1 leads to the deubiquitination of CCP110. 1 / 1
| 1

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"In addition, over-expression of two unrelated DUBs, USP1 and USP37, did not promote CP110 de-ubiquitylation (XREF_FIG and data not shown)."
USP1 affects BMAL1
| 1
USP1 deubiquitinates BMAL1. 1 / 1
| 1

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"Mechanistically, USP1 was able to de-ubiquitinate BMAL1 and inhibit the proteasomal degradation of BMAL1."