IndraLab

Statements


USP22 affects Histone_H2B
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USP22 deubiquitinates Histone_H2B. 10 / 16
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"As we discussed previously, USP22 is a component of a transcriptional activator complex SAGA and can deubiquitinate histones H2A and H2B, as well as several other substrates (Zhang et al., 2008a, b)."

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"USP22 is a component of the SAGA transcriptional coactivator complex and can deubiquitinate H2A and H2B [XREF_BIBR - XREF_BIBR]."

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"USP22 deubiquitylates both, H2A and H2B."

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"Remarkably, USP22, the human ortholog of Ubp8, forms a similar SAGA DUB module and deubiquitinates both H2A and H2B."

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"However, de-ubiquitylation of H2B by Usp22, the human homolog of yeast Ubp8, inhibits heterochromatic silencing and promotes gene activation [XREF_BIBR, XREF_BIBR]."

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"USP22 was initially reported to promote deubiquitylation of histones H2A and H2B, leading to transcription activation."

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"As a subunit of hSAGA, USP22 participates in the deubiquitination of histones H2A and H2B and the acetylation of histone H4 to regulate gene transcription and expression."

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"USP22 might de-ubiquitinate H2A and H2B, subunits of the human SAGA complex that are intimately linked to the transcriptional activation of the MYC gene and increased cell proliferation in HCC [XREF_BIBR]."

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"The requirement of ATXN7L3 for H2B deubiquitination by USP22, USP27x, and USP51 suggests that the ATXN7L3 zinc finger plays a role analogous to that of the Sgf11 zinc finger in docking human SAGA DUB [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP22 may deubiquitinate H2A and H2B, subunits of the hSAGA complex that activate transcription factors and promote carcinogenesis [XREF_BIBR]."
USP22 deubiquitinates Histone_H2B on K119. 1 / 1
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"USP22 deubiquitinates both histones H2A (lysine 119) and H2B (lysine 120; ref."
USP22 deubiquitinates Histone_H2B on K120. 1 / 1
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"USP22 deubiquitinates both histones H2A (lysine 119) and H2B (lysine 120; ref."
USP22 deubiquitinates Histone_H2B on S2. 1 / 1
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"Deubiquitination of H2B by Ubp8 and USP22 results in the recruitment of Ctk1 leading to Ser2 phosphorylation, a modification associated with elongation."
USP22 affects SIRT1
1 | 1 8
USP22 deubiquitinates SIRT1. 9 / 9
1 | 1 7

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"For instance, HULC can upregulate the expression of the ubiquitin specific peptidase 22 (USP22) protein by suppressing miR-6825-5p, miR-6845-5p, and miR-6886-3p at the epigenetic or transcriptional level in HCC cells; USP22 enhances the HULC induced deubiquitination of Sirt1 and stabilizes it, and Sirt1 stability induces the autophagy of HCC cells, thus increasing the resistance of HCC cells to oxaliplatin [XREF_BIBR]."

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"In addition, USP22 knockdown prevented c-MYC-mediated reduction of SIRT1 ubiquitination (XREF_FIG) and increase in SIRT1 expression (XREF_SUPPLEMENTARY)."

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"Collectively, USP22 might deubiquitinate SIRT1 and subsequently activate the AKT pathway, increasing the expression of MRP1 to induce MDR in HCC cells."

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"Ubiquitin specific protease 22 (USP22) reduced Sirt1 ubiquitination and degradation and decreased FN and TGF-beta1 expression in GMCs under both basal and AGEs treated conditions."

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"Ubiquitin-specific peptidase USP22 negatively regulates the STAT signaling pathway by deubiquitinating SIRT1."

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"USP22 can deubiquitinate and stabilize the expression of Sirt1."

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"Given that SIRT1 is deubiquitinated by USP22 and stabilized at the protein level (Armour etal., 2013; Lin etal., 2012) and previous studies have reported that SIRT1 could negatively influence the chemosensitivity of HCC cells (Chen etal., 2012), our results supported the notion that USP22 increases SIRT1 protein levels in HCC cells."

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"USP22 can deubiquitinate Sirt1 and enhance its stability through c-MYC-related network, leading to FLT3 tyrosine kinase inhibitors (TKIs) resistance in acute myeloid leukemia (AML)."
Modified USP22 leads to the deubiquitination of SIRT1. 1 / 1
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"In diabetic nephropathy, the increased expression of USP22 reduced the Sirt1 ubiquitination and degradation, and decreased fibronectin and TGF-beta1 expression in glomerular mesangial cells under both[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP22 affects Histone
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USP22 deubiquitinates Histone-H2A. 4 / 4
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"As a subunit of hSAGA, USP22 participates in the deubiquitination of histones H2A and H2B and the acetylation of histone H4 to regulate gene transcription and expression."

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"USP22 was initially reported to promote deubiquitylation of histones H2A and H2B, leading to transcription activation."

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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]."

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"As we discussed previously, USP22 is a component of a transcriptional activator complex SAGA and can deubiquitinate histones H2A and H2B, as well as several other substrates (Zhang et al., 2008a, b)."
USP22 deubiquitinates Histone. 4 / 4
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"USP22 also deubiquitinates non histone proteins, including telomeric repeat binding factor 1 (TRF1), sirtuin 1 (SIRT1), cyclin B1 and others, leading to protein stabilization by preventing proteasome mediated degradation."

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"In addition, certain non histone proteins such as sirtuin 1 (Sirt1) and fructose-bisphosphatase 1 (FBP1) could be deubiquitinated by USP22."

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"USP22 deubiquitylates histone and non histone substrates and has been associated with cancer progression and spinocerebellar ataxia."

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"USP22 deubiquitinates histone H2Bub and H2Aub."
USP22 deubiquitinates Histone-H2A on K120. 1 / 1
| 1

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"USP22 deubiquitinates both histones H2A (lysine 119) and H2B (lysine 120; ref."
USP22 deubiquitinates Histone-H2A on K119. 1 / 1
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"USP22 deubiquitinates both histones H2A (lysine 119) and H2B (lysine 120; ref."
USP22 affects KDM1A
1 | 7
USP22 deubiquitinates KDM1A. 8 / 8
1 | 7

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"These results indicate that USP22 deubiquitinates and stabilizes KDM1A."

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"Moreover, using in vitro deubiquitination assay, we found that KDM1A ubiquitination was decreased by incubating with recombinant USP22, suggesting that USP22 deubiquitinates KDM1A directly (XREF_FIG)."

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"In addition, deubiquitination of KDM1A by USP22 was attenuated after GSK3beta knockdown (XREF_FIG)."

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"USP22 deubiquitinated LSD1 in RB."

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"A screen for DUBs that could stabilize KDM1 demonstrates USP15, USP21, USP22 and USP28 as potential hits, among which ectopic expression of USP22 reduced KDM1A ubiquitination levels strikingly."

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"However, of those four DUBs, only USP22 substantially decreased KDM1A ubiquitination (XREF_SUPPLEMENTARY)."

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"Furthermore, knockdown of USP22 in GSC11 cells increased KDM1A ubiquitination (XREF_FIG)."
USP22 affects TERF1
1 | 5
USP22 deubiquitinates TERF1. 6 / 6
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"For example, USP22 promotes TRF1 deubiquitylation to enhance TRF1 protein stability and maintain telomere integrity."

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"Additionally, Usp22 directly deubiquitinates TRF1 (TBP (TATA box binding protein)-related factor 1) to regulate the transcription of cell cycle and apoptosis genes [XREF_BIBR] and inhibits the transcriptional activity of p53 by deubiquitinating SIRT1 histone deacetylase [XREF_BIBR] and by regulating MDMX stability [XREF_BIBR]."

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"Given the known regulation of TRF1 by ubiquitination, we hypothesized that the SAGA complex might facilitate Usp22 dependent deubiquitination of TRF1 and that loss of Gcn5 might alter this activity by compromising complex integrity."

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"GCN5 and USP22 also protect telomeres from DNA damage response through the stabilization of a shelterin component called TRF1, and interestingly, this regulation is not transcriptional but involves USP22 mediated deubiquitination of TRF1 [XREF_BIBR]."

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"This dissociation leads to lowered USP22 activity, which in turn leads to increased ubiquitination and turnover of TRF1 (XREF_FIG)."
USP22 affects CD274
1 | 5
USP22 deubiquitinates CD274. 6 / 6
1 | 5

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"In addition, USP22 could inhibit the ubiquitination of PD-L1 protein."

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"USP22 deubiquitinated PD-L1 and inhibited its proteasome degradation."

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"USP22 deubiquitinates CD274 to suppress anti-cancer immunity."

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"However, our previous study demonstrated that USP22 induces the deubiquitination of PD-L1 and prevents PD-L1 degradation."

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"USP22 can deubiquitinate PD-L1 itself or CSN5 for their stabilization [233] (Figure 3)."
| PMC

"Here, we identified ubiquitin-specific protease 22 (USP22) as a novel deubiquitinase of CD274."
USP22 affects FASN
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USP22 deubiquitinates FASN. 5 / 5
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"Together, these results support that USP22 interacts with FASN and inhibits FASN ubiquitination in CRC cells."

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"In p53 wild-type colorectal cancer (CRC) cells, hydrogen peroxide (H 2 O 2 )-induced p53 expression represses the transcription of deubiquitinase USP22, which otherwise deubiquitinates and stabilizes Fatty Acid Synthase (FASN), and thus inhibits fatty acid synthesis."

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"Whereas, depletion of USP22 in RKO E6 cells promoted FASN ubiquitination (Fig. 2E)."

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"We have found H O -induced p53 expression inhibits the transcription of USP22, which otherwise deubiquitinates and stabilizes FASN."

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"Overexpression of USP22 decreased FASN ubiquitination in the presence of MG132 (Fig. 2D and Fig. S2D)."
USP22 affects BMI1
1 | 4
USP22 deubiquitinates BMI1. 4 / 4
1 | 3

"All these findings indicate USP22 as a novel deubiquitinase of BMI1 in glioma."

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"3.3 USP22 deubiquitinates BMI1 for protein stabilization."

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"USP22 interacts with and deubiquitinates BMI1 for post-translational stabilization."

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"To test whether the endogenous BMI1 is also deubiquitinated by USP22 in glioma cells, we knocked down endogenous USP22 in U251 cells pretreated with CHX and found that endogenous BMI1 also became unstable and degraded rapidly."
Modified USP22 leads to the deubiquitination of BMI1. 1 / 1
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"However, WT-USP22 coexpression (not CI-USP22) almost completely abolished BMI1 ubiquitination (lane 2 vs lane 3, Figure XREF_FIG B)."
USP22 affects STING1
1 | 3
USP22 leads to the deubiquitination of STING1. 4 / 4
1 | 3

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"USP22 negatively regulates STING activation and ubiquitination."
| DOI

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"We furthermore demonstrate for the first time that in the absence of viral 421 infections or exogenous IFN, loss of USP22 expression resulted in basal and 2'3'-422 cGAMP-induced STING ubiquitination in hIECs."
| DOI

"USP22 removes K27-linked ubiquitination on STING through cooperation with USP13"

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"288 289 USP22 negatively regulates STING activation and ubiquitination 290 The differential response to ISD, but not poly(I:C), and the reversal of the IFN signature 291 in USP22-STING dKO hIECs suggests an important role of USP22 in the control of 292 STING-induced type III IFN signaling."
| DOI
USP22 affects H2Bub1
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USP22 deubiquitinates H2Bub1. 4 / 4
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"Thus, ATXN7L3 is required for the full activity of the three related DUB modules to regulate global H2Bub1 levels, whereas USP22-containing DUB module is less involved in genome-wide deubiquitylation of H2Bub1."

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"Unlike the ATXN7L3 DUB complex, a USP22, ATXN7L3B, and ENY2 complex can not deubiquitinate H2Bub1 efficiently in vitro Moreover, ATXN7L3B knockdown inhibits migration of breast cancer cells in vitro and limits expression of ER target genes."

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"Along these lines it is interesting to note that neither free USP22 nor a stable recombinant subcomplex, composed of TAF5L, ATXN7L3, ENY2, and USP22, can deubiquitinate H2Aub1 or H2Bub1 in vitro, sugg[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Finally, USP22 and the 2A-DUB (KIAA1915), both target H2Aub1 (although USP22 can also deubiquitylate H2Bub1), and both were described as co-activators of androgen receptor (AR)-mediated transcription."
USP22 affects EGFR
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USP22 deubiquitinates EGFR. 4 / 4
1 | 3

"Additionally, USP22 sustained the activation of multiple EGFR downstream signaling pathways, including STAT3, AKT/mTOR and MEK/ERK pathways, in lung ADC cell lines H1975 and PC9."

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"In this model, late endosome localized USP22 deubiquitinates EGFR and impedes sorting of EGFR to the lysosome, thus sustaining the trafficking of EGFR to the plasma membrane (Figs. 6 and 9)."

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"Similarly, shRNA knockdown of USP22 resulted in accumulated Ubn-EGFR, which further confirmed that USP22 antagonizes EGFR ubiquitination."

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"Mechanistically, USP22 deubiquitinates EGFR localized on late endosomes, prevents ubiquitination mediated EGFR degradation and enhances recycling of EGFR after EGF stimulation."
USP22 affects CCNB1
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USP22 deubiquitinates CCNB1. 4 / 4
1 | 3

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"USP22 deubiquitinates cyclin B1, stabilizes cyclin B1 by antagonizing proteasome mediated degradation, and promotes itaccumulation in the nucleus (Lin etal., 2015; Melo-Cardenas etal., 2016)."

"Phosphorylation of USP22 by CDK1 enhances its activity in deubiquitinating CCNB1."

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"Indeed, USP22 inhibited CCNB1 ubiquitination both in vivo and in vitro (XREF_FIG and XREF_SUPPLEMENTARY)."

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"The deubiquitinase catalytic activity of USP22 is required for CCNB1 deubiquitination because the catalytically inactive USP22 (USP22 and C185A) mutant failed to suppress CCNB1 ubiquitination without affecting its interaction with CCNB1 (XREF_SUPPLEMENTARY)."
USP22 affects MYC
1 | 2
USP22 deubiquitinates MYC. 3 / 3
1 | 2

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"It could be through a direct mechanism where USP22 deubiquitylates c-MYC inducing its stabilization and activation, or indirectly through ubiquitin removal from histones at c-MYC target genes, recruitment of other transcriptional machinery or deubiquitylation of proteins important for c-MYC activity."

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"We found that USP22 promotes deubiquitination of c-Myc in several breast cancer cell lines, resulting in increased levels of c-Myc."
USP22 affects ubH2B
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USP22 deubiquitinates ubH2B. 2 / 2
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"Deubiquitination of ubH2B is catalyzed by the ubiquitin protease subunit of the Spt-Ada-Gcn5 Acetyltransferase (SAGA) transcriptional coactivator complex : Nonstop (FBgn0013717) in Drosophila melanogaster, Ubp8 in Saccharomyces cerevisiae, and USP22 in humans."

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"While other events, such as histone exchange or direct or indirect RNF20 inactivation, are also possible, studies in the lab are ongoing to determine if USP22 (the mammalian homolog to Ubp8) also deubiquitinates ubH2B."
USP22 affects NFATC2
1 | 1
USP22 deubiquitinates NFATC2. 2 / 2
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"Gao et al found that USP22 interacts with and deubiquitinates NFATc2, and also stabilizes NFATc2 protein and promotes NFATc2 function to facilitate IL-2 expression in T cells."
USP22 affects KPNA2
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USP22 leads to the deubiquitination of KPNA2. 2 / 2
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"USP22 promotes IRF3 nuclear translocation and antiviral responses by deubiquitinating the importin protein KPNA2."

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"USP22 promotes IRF3 nuclear translocation and antiviral responses by deubiquitinating the importin protein KPNA2."
USP22 affects H2BK120ub
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USP22 deubiquitinates H2BK120ub. 2 / 2
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"USP22 is involved in the deubiquitylation of H2BK120ub, a mark that is found at DSB sites, USP22 could be a “reader” for this mark and potentiate the recruitment of other DNA damage factors through this ubiquitin mark."

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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]."
USP22 affects H2Aub
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USP22 deubiquitinates H2Aub. 2 / 2
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"However, whether deubiquitination of H2Aub (monoubiquitinated histone) by USP22 reverses the phenotype is not yet clearly established ."

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"USP22 deubiquitinates histone H2Bub and H2Aub."
USP22 affects Cyclin
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USP22 deubiquitinates Cyclin. 1 / 1
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"USP22 deubiquitinates cyclin B1, stabilizes cyclin B1 by antagonizing proteasome mediated degradation, and promotes itaccumulation in the nucleus (Lin etal., 2015; Melo-Cardenas etal., 2016)."
USP22 leads to the deubiquitination of Cyclin on D1. 1 / 1
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"USP22 function reverses cyclin D1 ubiquitylation; overexpression of cyclin D1 can partially rescue cell cycle arrest in USP22 knockdown cells."
USP22 affects histones H2B
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USP22 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]."
USP22 affects TBP
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USP22 deubiquitinates TBP. 1 / 1
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"Additionally, Usp22 directly deubiquitinates TRF1 (TBP (TATA box binding protein)-related factor 1) to regulate the transcription of cell cycle and apoptosis genes [XREF_BIBR] and inhibits the transcriptional activity of p53 by deubiquitinating SIRT1 histone deacetylase [XREF_BIBR] and by regulating MDMX stability [XREF_BIBR]."
USP22 affects TATA box-binding protein)-related factor 1
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USP22 deubiquitinates TATA box-binding protein)-related factor 1. 1 / 1
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"Additionally, Usp22 directly deubiquitinates TRF1 (TBP (TATA box binding protein)-related factor 1) to regulate the transcription of cell cycle and apoptosis genes [XREF_BIBR] and inhibits the transcriptional activity of p53 by deubiquitinating SIRT1 histone deacetylase [XREF_BIBR] and by regulating MDMX stability [XREF_BIBR]."
USP22 affects SOX2
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USP22 deubiquitinates SOX2. 1 / 1
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USP22 affects SNAI1
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USP22 deubiquitinates SNAI1. 1 / 1
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"These results suggested that USP22 could accelerate renal EMT and promote the pathological progression of diabetic TIF by deubiquitinating Snail1, providing an experimental basis for using USP22 as a potential target for DKD."
USP22 affects REPRESSOR
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USP22 deubiquitinates REPRESSOR. 1 / 1
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"Deubiquitination of the repressor E2F6 by USP22 facilitates AKT activation and tumor growth in hepatocellular carcinoma."
USP22 affects RCAN1
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USP22 leads to the deubiquitination of RCAN1. 1 / 1
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"USP22 antagonized the actions of FBW7, NEDD4-2, and beta-TrCP E3 ligase on RCAN1 and promoted RCAN1 de-ubiquitination."
USP22 affects PTGS2
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USP22 deubiquitinates PTGS2. 1 / 1
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"In non-small cell lung cancer (NSCLC), aberrant expression of USP22 is a predictor of poor survival, as is high expression of cyclooxygenase-2 (COX-2)."
USP22 affects PPARG
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USP22 deubiquitinates PPARG. 1 / 1
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"Herein, we identify ubiquitin-specific protease 22 (USP22) as a key regulator for de novo fatty acid synthesis, which directly interacts with deubiquitinates and stabilizes peroxisome proliferator-activated receptor gamma (PPARγ) through K48-linked deubiquitination, and in turn, this stabilization increases acetyl-CoA carboxylase (ACC) and ATP citrate lyase (ACLY) expressions."
USP22 affects PALB2
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USP22 deubiquitinates PALB2. 1 / 1
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"Furthermore, the lysine residues on PALB2 that USP22 could be potentially deubiquitinating have not been mapped by this study or others and is an excellent future direction for further study on the USP22-PALB2 interaction."
USP22 affects MMP9
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USP22 deubiquitinates MMP9. 1 / 1
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USP22 affects Histone H2B
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USP22 deubiquitinates Histone H2B. 1 / 1
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"Histone H2B deubiquitylation by USP22 and Ubp8 has been shown to occur at the transcribed regions of target genes [XREF_BIBR, XREF_BIBR]."
USP22 affects HES1
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USP22 deubiquitinates HES1. 1 / 1
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"A recent study showed that USP22‐ mediated deubiquitination of Hairy and Enhancer of split 1 (Hes1) is important for neuronal differentiation in the developing brain"
USP22 affects H2Bub
| 1
USP22 deubiquitinates H2Bub. 1 / 1
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"The SAGA complex was also discussed by Vikki Weake from the Workman lab (Stowers Institute), whose work centered on Usp22 dependent deubiquitination of H2Bub."
USP22 affects H2BC21
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USP22 deubiquitinates H2BC21. 1 / 1
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No evidence text available
USP22 affects H2BC10
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USP22 deubiquitinates H2BC10. 1 / 1
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USP22 affects H2B
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USP22 deubiquitinates H2B. 1 / 1
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"Several studies demonstrating that USP22 can deubiquitinate uH2B in vitro and might affect the transcriptional elongation on the IRF1 gene (interferon regulatory factor 1) suggested a possible mechani[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP22 affects H2Aub1
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USP22 deubiquitinates H2Aub1. 1 / 1
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"Along these lines it is interesting to note that neither free USP22 nor a stable recombinant subcomplex, composed of TAF5L, ATXN7L3, ENY2, and USP22, can deubiquitinate H2Aub1 or H2Bub1 in vitro, sugg[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
USP22 affects H2AX
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USP22 deubiquitinates H2AX. 1 / 1
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"These findings confirm that USP22 could deubiquitinate H2AX and promote its phosphorylation, thus contributing to DNA damage repair and inducing cisplatin resistance."
USP22 affects H2AK119ub
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USP22 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]."
USP22 affects H2AC20
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USP22 deubiquitinates H2AC20. 1 / 1
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No evidence text available
USP22 affects H2AC17
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USP22 deubiquitinates H2AC17. 1 / 1
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"USP22 was found to hydrolyze monoubiquitin tagged to uH2A and to antagonize PcG or hydrolyze monoubiquitin from uH2B to regulate MLL-trithorax-mediated trimethylation of histone H3 lysine-4"
USP22 affects FOXP3
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USP22 leads to the deubiquitination of FOXP3. 1 / 1
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"Loss of Usp22 in Treg reduces Foxp3 transcript levels, increases FOXP3 ubiquitination and degradation, and reduces suppressive activity in vivo in mice."
USP22 affects FBP1
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USP22 deubiquitinates FBP1. 1 / 1
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USP22 affects EZH2
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USP22 leads to the deubiquitination of EZH2. 1 / 1
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"To determine whether the six EZH2 interacting DUBs affect EZH2 ubiquitination and protein levels, we transfected them individually into HEK293T cells, and we found that USP22 and ZRANB1 decreased the polyubiquitination of EZH2 (XREF_SUPPLEMENTARY); however, only ZRANB1 upregulated endogenous EZH2 protein (XREF_SUPPLEMENTARY)."
USP22 affects E2F6
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USP22 deubiquitinates E2F6. 1 / 1
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"Deubiquitination of the repressor E2F6 by USP22 facilitates AKT activation and tumor growth in hepatocellular carcinoma."
USP22 affects CTK1
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USP22 deubiquitinates CTK1 on S2. 1 / 1
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"Deubiquitination of H2B by Ubp8 and USP22 results in the recruitment of Ctk1 leading to Ser2 phosphorylation, a modification associated with elongation."
USP22 affects COPS5
| 1
USP22 deubiquitinates COPS5. 1 / 1
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"USP22 can deubiquitinate PD-L1 itself or CSN5 for their stabilization [233] (Figure 3)."
| PMC
USP22 affects ATXN7
| 1
USP22 deubiquitinates ATXN7. 1 / 1
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"While the role of altered STAGA and USP22 deubiquitination complex function in SCA7 disease pathogenesis is unclear, recent studies of the related polyQ disorder SCA1 indicate that the polyQ expansion in ataxin-1 attenuates the formation and function of the Capicua transcription factor complex, contributing to SCA1 disease pathogenesis through a partial loss-of-function mechanism."