IndraLab

Statements


USP1 affects PCNA
1 | 1 49
USP1 deubiquitinates PCNA. 10 / 44
1 | 1 42

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"Recently, PCNA deubiquitylation by the USP1 and UAF1 complex in conjunction with ELG1, which directs the USP1-UAF1 to ubiquitin-PCNA, has emerged as an important regulatory mechanism of damage bypass."

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"For example, USP1 deubiquitylates mono-ubiquitylated PCNA, which inhibits recruitment of DNA polymerases in the absence of DNA damage, and thereby leads to regulated DNA repair."

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"Significantly, we report that PCNA polyubiquitination is negatively regulated by USP1."

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"Whereas Rad6/Rad18 E2 conjugate/E3 ligase cause PCNA monoubiquitination, Usp1 and Usp7 cause PCNA deubiquitination with some difference in case of HU (Niimi et al, 2008; Fox et al, 2011)."

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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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"USP1 combined with USP1-associated factor 1 (UAF1) deubiquitinates PCNA or FANCD2 during DNA repair process such as interstrand cross-link (ICL) repair, homologous recombination (HR) repair, and translesion DNA synthesis (TLS) [87]."
| PMC

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"PCNA polyubiquitination, similar to PCNA monoubiquitination, is negatively regulated by USP1 [138,141]."

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"Thus, deubiquitination of PCNA, normally deubiquitinated by cellular USP1, by the viral DUB can disrupt repair of DNA damage by compromising recruitment of TLS polymerase to stalled replication forks."

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"S4A, USP1 inhibited PCNA ubiquitination but not affected PCNA NEDDylation."
USP1 deubiquitinates ubiquitinated PCNA. 4 / 4
| 4

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

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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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"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]"
Unubiquitinated USP1 leads to the deubiquitination of PCNA. 1 / 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."
Modified mutated USP1 leads to the deubiquitination of PCNA. 1 / 1
| 1

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"Importantly, expression of a USP1 mutant that can not be degraded via APC/C (Cdh1) inhibited PCNA monoubiquitination during G1, likely compromising the recruitment of trans-lesion synthesis polymerase to UV repair sites."
Modified USP1 leads to the deubiquitination of PCNA. 1 / 1
| 1

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"Conversely, overexpression of USP1 when cells are treated with hydroxyurea inhibits monoubiquitination of PCNA."
USP1 affects FANCD2
1 | 1 48
USP1 deubiquitinates FANCD2. 10 / 47
1 | 1 45

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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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"Surprisingly, depletion of UBE2M did not reduce the FANCD2 monoubiquitination that is up-regulated by USP1 depletion (XREF_SUPPLEMENTARY), suggesting that the Nedd8 inhibition specifically abrogates FANCD2 monoubiquitination that is induced by exogenous DNA damage."

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"We propose that USP1 deubiquitinates FANCD2 when cells exit S phase or recommence cycling after a DNA damage insult and may play a critical role in the FA pathway by recycling FANCD2."

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"The exact role of deubiquitination of PCNA and FANCD2 by USP1 and UAF1 in human DNA damage response remains to be elucidated."

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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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"Deubiquitination of FANCD2 and FANCI by USP1 in complex with UAF1 is also important for FA pathway function."

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

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"Deubiquitination of FANCD2 and FANCI proteins by the multisubunit protein complex USP1 and UAF1 is required for the completion of the FA pathway."

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"FANCD2 is deubiquitinated by USP1 once DNA repair is complete."

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"The USP1 and UAF1 complex deubiquitylates the Fanconi anemia protein FANCD2, which promotes homologous recombination (HR) and DNA cross-link repair."
USP1 deubiquitinates ubiquitinated FANCD2. 2 / 2
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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 [165]."

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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]."
Unubiquitinated USP1 leads to the deubiquitination of FANCD2. 1 / 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 | 20
USP1 deubiquitinates FANCI. 10 / 21
1 | 20

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"Usp1 deubiquitinates FANCD2 and FANCI in the Falconi anemia pathway, promoting DNA repair."

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"Deubiquitination of FANCD2 and FANCI by USP1 in complex with UAF1 is also important for FA pathway function."

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"However, in addition to this opposition to activate and monoubiquitinate FANCD2/I, USP1 deubiquitination of FANCI has also been associated with promoting core complex recruitment to the site of DNA da[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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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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"We showed that deubiquitination of FANCI by USP1 is an important step to recruit the FA core complex at sites of DNA damage."

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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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"When the repair process is completed, the FANCD2 and FANCI complex is deubiquitylated and dissociated from the repaired ICL site by the USP1 and UAF1 complex and is then released from the DNA [XREF_BIBR]."

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"The deubiquitination of FANCD2 and FANCI by the UAF1 and USP1 deubiquitinating enzyme complex appears to be required for the completion of the repair process [XREF_BIBR - XREF_BIBR]."

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"Indeed, USP1 knockdown delayed but did not abolish FANCI deubiquitination, as previously observed with similar timing (Nijman et al., 2005)."

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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 EZH2
| 14
USP1 deubiquitinates EZH2. 10 / 14
| 14

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

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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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"USP1 and EZH2 interact with each other and overexpression of USP1 diminishes the ubiquitination of EZH2, which is further enhanced by the overexpression of USP1 binding partner, WDR48."

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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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"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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"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 USP1/WDR48 decreased EZH2 ubiquitination, and the efficiency was increased with the amount of USP1/WDR48 proteins that were added to the reactions (Fig.3E)."

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"In vitro deubiquitylation of EZH2 by USP1 was performed as described previously."

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

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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 ID1
1 | 11
USP1 deubiquitinates ID1. 10 / 12
1 | 11

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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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"Williams et al. also recently reported that USP1 and UAF1 deubiquitinates and prevents proteasomal degradation of ID (inhibitor of DNA binding) proteins, 13 which have been shown to activate multiple pathways involved in tumor progression, including preservation of the cancer stem cell phenotype."

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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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"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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"To identify a biological context in which USP1 deubiquitinates ID proteins, we examined USP1 expression patterns."

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

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

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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)."
USP1 affects ID2
1 | 6
USP1 deubiquitinates ID2. 5 / 5
1 | 4

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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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"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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"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 also deubiquitinates and stabilizes the transcriptional regulators ID1, ID2 and ID3 [XREF_BIBR - XREF_BIBR]."
USP1 deubiquitinates ubiquitinated ID2. 1 / 1
| 1

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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."
Modified USP1 leads to the deubiquitination of ID2. 1 / 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 hsFANCI-Ub
| 4
USP1 deubiquitinates hsFANCI-Ub. 4 / 4
| 4

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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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"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)."

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

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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)."
USP1 affects hsPCNA-Ub
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USP1 deubiquitinates hsPCNA-Ub. 3 / 3
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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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"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 KDM4A
| 3
USP1 deubiquitinates KDM4A. 3 / 3
| 3

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"3.4 USP1 deubiquitinates KDM4A."

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"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."

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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."
USP1 affects ID3
1 | 2
USP1 deubiquitinates ID3. 3 / 3
1 | 2

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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 also deubiquitinates and stabilizes the transcriptional regulators ID1, ID2 and ID3 [XREF_BIBR - XREF_BIBR]."
USP1 affects AKT
| 1 2
USP1 deubiquitinates AKT. 3 / 3
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"USP1 deubiquitinates Akt to inhibit PI3K-Akt-FoxO signaling in muscle during prolonged starvation."

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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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"USP1 deubiquitinates Akt to inhibit PI3K-Akt-FoxO signaling in muscle during prolonged starvation."
USP1 affects monoubiquitinated-PCNA
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USP1 deubiquitinates monoubiquitinated-PCNA. 2 / 2
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"Recent studies have shown that monoubiquitinated-PCNA is deubiquitinated by the deubiquitinating enzyme USP1 [10] ."

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"Recent studies have shown that monoubiquitinated-PCNA is deubiquitinated by the deubiquitinating enzyme USP1 [XREF_BIBR]."
USP1 affects mUb-PCNA
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USP1 deubiquitinates mUb-PCNA. 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."

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"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 PHLPP1
1 | 1
USP1 deubiquitinates PHLPP1. 2 / 2
1 | 1

"USP1 [137] and USP46 [138] are other DUBs known to deubiquitinate PHLPP1, with a similar outcome in other cancers as well."

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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 xlFANCD2-Ub
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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)."
USP1 affects lane 3
| 1
USP1 leads to the deubiquitination of lane 3. 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 TRAF6
| 1
USP1 deubiquitinates TRAF6. 1 / 1
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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]."
USP1 affects TRAF2
| 1
USP1 deubiquitinates TRAF2. 1 / 1
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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]."
USP1 affects TBK1
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USP1 leads to the deubiquitination of TBK1. 1 / 1
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"USP1 greatly inhibited TBK1 ubiquitination, whereas USP12 and USP46 had no effects on TBK1 ubiquitination."
USP1 affects TAFAZZIN
| 1
USP1 deubiquitinates TAFAZZIN. 1 / 1
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"USP1-regulated reciprocal differentiation of Th17 cells and Treg cells by deubiquitinating and stabilizing TAZ."
USP1 affects PLK1
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USP1 deubiquitinates PLK1. 1 / 1
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"Moreover, USP1 interacted with and deubiquitinated PLK1, a critical regulator of glycolysis."
USP1 affects PHLPP2
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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 PCNA-mUb
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USP1 deubiquitinates PCNA-mUb. 1 / 1
| 1

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"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 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 IDS
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USP1 deubiquitinates IDS. 1 / 1
| 1

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"Deubiquitination of IDs by USP1 promotes ID protein stability and prevents stem cell differentiation."
USP1 affects Fig.S2B
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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 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

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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."
USP1 affects FANCI-FANCD2
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USP1 leads to the deubiquitination of FANCI-FANCD2. 1 / 1
| 1

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"Monoubiquitination of FANCI-FANCD2 is reversed by the deubiquitinating enzyme (DUB) USP1."
USP1 affects DNA-binding proteins 1–4
| 1
USP1 deubiquitinates DNA-binding proteins 1–4. 1 / 1
| 1

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"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 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 BCAT2
| 1
USP1 deubiquitinates BCAT2 on K229. 1 / 1
| 1

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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."