IndraLab

Statements


USP3 affects Histone_H2B
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USP3 deubiquitinates Histone_H2B. 6 / 6
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"Usp3 can deubiquitinate both H2A and H2B in humans."

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"In the DDR, USP3 dynamically interacts with chromatin and deubiquitinates H2A and H2B."

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"In addition to USP22 and its yeast homolog, H2B can be deubiquitylated by USP3 and USP7 in humans."

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"USP3 that was found as chromatin associated DUB suppresses global mono-ubiquitylation of H2A (and also H2B)."

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"USP3 dynamically associates with chromatin and deubiquitinates H2A and H2B in vivo."

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"Deubiquitination of histones H2A and H2B by USP3 is required for progression through the S phase and for genomic stability."
USP3 affects Histone
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USP3 deubiquitinates Histone. 3 / 3
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"Notably, USP3 deletion increased the levels of histone ubiquitination in adult tissues, reduced the hematopoietic stem cell (HSC) reserves over time, and shortened animal life span."

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"Consistently, we found that USP3, which deubiquitylates H2A-type histones to prevent accumulation of RNF168 and downstream repair factors, but not RNF8, at DSB sites, also suppressed RNF169 recruitment in a manner requiring its catalytic activity (XREF_FIG)."

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"Overexpression of USP3 in HeLa cells reduced levels of both Ub-H2A and Ub-H2B, whereas knockdown of USP3 enhanced the ubiquitination of both histones."
USP3 deubiquitinates Histone-H2A. 3 / 3
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"RNF168 is an E3 ligase that ubiquitinates histones H2A and gammaH2AX during the DNA damage response [XREF_BIBR], this ubiquitination can be reversed by Usp3 [XREF_BIBR]."

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"Deubiquitination of histones H2A and H2B by USP3 is required for progression through the S phase and for genomic stability."

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"Several DUBs have been implicated in histone deubiquitination, including USP3, USP12, USP22, and USP46, which deubiquitinate both histones H2A and histones H2B [XREF_BIBR]."
USP3 affects DDX58
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USP3 deubiquitinates DDX58. 4 / 4
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"CYLD (cylindromatosis) deubiquitinates RIG-I and several downstream molecules to prevent premature RIG-I activation in uninfected cells [17], while USP3 deubiquitinates RIG-I specifically after viral infection, likely serving as a negative feedback regulator [18]."

"USP3 inhibits type I interferon signaling by deubiquitinating RIG-I-like receptors"

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"CYLD (cylindromatosis) deubiquitinates RIG-I and several downstream molecules to prevent premature RIG-I activation in uninfected cells [XREF_BIBR], while USP3 deubiquitinates RIG-I specifically after viral infection, likely serving as a negative feedback regulator [XREF_BIBR]."

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"USP3 is also a DUB that deubiquitinates K63-polyUb chain of both RIG-I and MDA5 and suppresses IFN-β activation [25]."
USP3 affects gammaH2AX
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Modified USP3 leads to the deubiquitination of gammaH2AX. 2 / 2
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"Here, we showed that ectopic expression of USP3 led to the deubiquitination of both H2A and gammaH2AX in response to UV induced DNA damage."

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"In addition, while USP3 depletion resulted in delayed disappearance of ubiquitylaed H2A and FK2 staining (poly-ubiquitylation marker) after IR, over-expression of USP3 suppressed ubiquitylation of gam[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP3 affects KLF5
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USP3 leads to the deubiquitination of KLF5. 2 / 2
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"USP3 promotes breast cancer cell proliferation by deubiquitinating KLF5."

"In this study, ubiquitin-specific protease 3 (USP3) was identified as a new KLF5 deubiquitinase by genome-wide siRNA library screening."
USP3 affects H2AX
1 | 1
USP3 deubiquitinates H2AX. 2 / 2
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"USP3, USP51 and USP16 de-ubiquitinate H2A/H2AX with varying degrees of specificity [47–49]."
USP3 affects snail
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USP3 leads to the deubiquitination of snail. 1 / 1
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"USP3 mediates the deubiquitination of snail family transcriptional repressor 1 (SNAIL1)."
USP3 affects histones H2B
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USP3 deubiquitinates histones H2B. 1 / 1
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"Several DUBs have been implicated in histone deubiquitination, including USP3, USP12, USP22, and USP46, which deubiquitinate both histones H2A and histones H2B [XREF_BIBR]."
USP3 affects Vif
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USP3 deubiquitinates Vif. 1 / 1
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"Further investigation found that USP3 stabilized 90% to 95% of A3G expression by deubiquitinating Vif-mediated polyubiquitination and blocking its degradation in an enzyme-dependent manner."
USP3 affects UIMC1
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USP3 deubiquitinates UIMC1. 1 / 1
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"K63-linked ubiquitin accumulates on Rap80 at the DSB foci with the concerted effect of RNF8, RNF168, and Ubc13, which are clipped off with the assistance of USP3 and BRCC36 to maintain the G2/M checkpoint."
USP3 affects TRAF6
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USP3 leads to the deubiquitination of TRAF6. 1 / 1
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"Moreover, USP3 can reverse the ubiquitination of TRAF6 (tumor necrosis factor-receptor-associated factor 6), which intermediates the signals from inflammatory cytokines to NF-κB activation, thus blocking IL-1β-induced chondrocyte apoptosis [27]."
USP3 affects TP53
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USP3 deubiquitinates TP53. 1 / 1
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"Depletion of USP3 lead to accelerated degradation of p53 in normal cells thereby enhanced cell proliferation and transformation."
USP3 affects SUZ12
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USP3 deubiquitinates SUZ12. 1 / 1
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"We observed that USP3 interacted with and stabilized SUZ12 via deubiquitination."
USP3 affects SEC23
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USP3 deubiquitinates SEC23. 1 / 1
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"Interestingly, other data show that Sec23 is ubiquitylated by Rsp5 and de-ubiquitylated by Usp3/Bre5, with the ubiquitylated form of Sec23 unable to interact with Sec24."
USP3 affects PYCARD
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USP3 deubiquitinates PYCARD. 1 / 1
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"USP3 deubiquitinates and stabilizes the adapter protein ASC to regulate inflammasome activation."
USP3 affects NANOG
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USP3 deubiquitinates NANOG. 1 / 1
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USP3 affects MYCN
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USP3 leads to the deubiquitination of MYCN. 1 / 1
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"The known role of ALYREF as a regulator of DNA binding guided further analyses that uncovered ALYREF-MYCN interaction in a nuclear coactivator complex which stimulates transcription of the ‘ubiquitin specific peptidase 3′ (USP3), consequently reducing MYCN ubiquitination and degradation."
| PMC
USP3 affects IFIH1
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USP3 deubiquitinates IFIH1. 1 / 1
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"USP3 is also a DUB that deubiquitinates K63-polyUb chain of both RIG-I and MDA5 and suppresses IFN-β activation [25]."
USP3 affects Histone_H2A
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USP3 deubiquitinates Histone_H2A on K13. 1 / 1
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trips
"USP3 counteracts RNF168 via deubiquitinating H2A and γH2AX at lysine 13 and 15."
USP3 affects H2BK120ub
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USP3 deubiquitinates H2BK120ub. 1 / 1
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"Other major DUBs with specificity for histone H2AK119ub over H2BK120ub are BAP1 and USP16, while USP3, USP12, USP22, and USP44 deubiquitinate both H2AK119ub and H2BK120ub, as well as different non histone substrates [XREF_BIBR]."
USP3 affects H2BC21
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USP3 deubiquitinates H2BC21. 1 / 1
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"USP3 dynamically associates with chromatin and deubiquitinates H2A/H2B in vivo."
USP3 affects H2BC10
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USP3 deubiquitinates H2BC10. 1 / 1
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"Here we identify the ubiquitin-specific protease 3 USP3 as a deubiquitinating enzyme for uH2A and uH2B."
USP3 affects H2AK13/15ub
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USP3 deubiquitinates H2AK13/15ub. 1 / 1
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"USP3 deubiquitinates H2AK13/15ub as well as H2A119ub in response to DNA damage and affects recruitment of 53BP1 in cells [19,46]."
USP3 affects H2AK119ub
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USP3 deubiquitinates H2AK119ub. 1 / 1
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"Other major DUBs with specificity for histone H2AK119ub over H2BK120ub are BAP1 and USP16, while USP3, USP12, USP22, and USP44 deubiquitinate both H2AK119ub and H2BK120ub, as well as different non histone substrates [XREF_BIBR]."
USP3 affects H2AC20
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USP3 deubiquitinates H2AC20. 1 / 1
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"USP3 counteracts RNF168 via deubiquitinating H2A and gammaH2AX at lysine 13 and 15."
USP3 affects H2AC17
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USP3 deubiquitinates H2AC17. 1 / 1
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"USP3 and USP16 function to remove ubiquitin from histone H2A during the DDR"
USP3 affects H2A119ub
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USP3 deubiquitinates H2A119ub. 1 / 1
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"USP3 deubiquitinates H2AK13/15ub as well as H2A119ub in response to DNA damage and affects recruitment of 53BP1 in cells [19,46]."
USP3 affects COL9A3
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USP3 deubiquitinates COL9A3. 1 / 1
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"These data suggest that USP3 promotes GC progression and metastasis by deubiquitinating COL9A3 and COL6A5."
USP3 affects COL6A5
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USP3 deubiquitinates COL6A5. 1 / 1
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"These data suggest that USP3 promotes GC progression and metastasis by deubiquitinating COL9A3 and COL6A5."
USP3 affects CHEK1
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USP3 deubiquitinates CHEK1. 1 / 1
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"Herein, we show that the K63-linked ubiquitin chain at CHK1's K132 residue has an inhibitory effect on the kinase activity. Furthermore, we demonstrate that this modification can be removed by ubiquitin-specific protease 3 (USP3), a deubiquitinating enzyme that targets K63-linked ubiquitin chains."