IndraLab
Statements
USP39 affects cell population proliferation
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USP39 activates cell population proliferation.
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USP39 inhibits cell population proliferation.
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USP39 affects apoptotic process
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63
USP39 inhibits apoptotic process.
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47
USP39 activates apoptotic process.
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16
USP39 affects cell cycle
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33
USP39 activates cell cycle.
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17
USP39 inhibits cell cycle.
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16
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"Mainly, in the first group, we have genes with a suggested novel anti-cancer role in the testis (Fetub, Hoxd10, Slc45a3, Ube2l6), with increased expression levels inhibiting cancer cell development, supported by the protective role of Mt3; while the Usp39 gene, with elevated expression levels (the most of all the observed changes), should lead to some tumor-like changes within the testis tissue."
reach
"To delve into the contribution of GLI1 in the tumor-promoting effects of USP39, we generated A549 and H1299 cell lines with stable GLI1 knockdown in conjunction with USP39 overexpression (Fig. 6C), and then performed MTT, colony formation, and transwell assays to examine the influence on cell growth and migration."
sparser
"To identify the domains responsible for the interaction between ETS2 and USP39, we created several deletion mutants of ETS2:ΔETS (ETS domain-deleted, aa 1–362), PNT-only (Pointed domain-containing, aa 1–170), ΔPNT (Pointed domain-deleted, aa 1–84 & 171–469) and 171–362 (containing aa 171–362) ( xref A)."
reach
"To identify the domains responsible for the interaction between ETS2 and USP39, we created several deletion mutants of ETS2:ΔETS (ETS domain-deleted, aa 1–362), PNT-only (Pointed domain-containing, aa 1–170), ΔPNT (Pointed domain-deleted, aa 1–84 & 171–469) and 171–362 (containing aa 171–362) (Figure 3A)."
reach
"Surprisingly, the increased USP39 dramatically and statistically significantly reduced ETS2 protein levels in the nucleus (from 1.00 in GFP control to approximately 0.04 in USP39), while causing only marginal changes in the cytoplasmic fraction (from 1.00 in GFP control to approximately 0.99 in USP39) (Figure 5A,B)."
USP39 affects Neoplasm Invasiveness
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USP39 activates Neoplasm Invasiveness.
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USP39 activates Neoplasm Invasiveness. 10 / 24
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"In glioma, USP39 acts as a splicing factor by altering the 3ʹ splice site to increase the expression of high mobility group protein A2 (HMGA2) and promotes the maturation of migratory invasion-associated proteins and TAZ mRNA, a key protein in the ADAM9 and Hippo signaling pathways."
USP39 inhibits Neoplasm Invasiveness.
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USP39 is modified
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USP39 is phosphorylated.
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USP39 is acetylated.
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USP39 is sumoylated.
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sparser
"Furthermore, inhibition of the SUMOylation of USP39 can enhance the proliferation of cancer cells including breast and hepatocellular cancer via affecting the recruitment of tri-snRNP, suggesting that SUMOylation of USP39 has an essential role in cancer therapy ( xref ; xref ; xref ) ( xref )."
USP39 is deacetylated.
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1
reach
"It is interesting to speculate that whether E3 ligase TRIM26 with ubiquitin function has a common foothold with USP39, that is, TRIM26 affects the stability of ZEB1 through ubiquitination, while USP39 promotes the abnormality of ZEB1 level through deubiquitination, which orchestrates the occurrence of EMT and determines the progression of HCC.This study uncovers the elaborate ubiquitination and deubiquitination modifications of ZEB1 in HCC."
reach
"Collectively, these results revealed a functional significance of USP39 on the ZEB1 induced EMT progression in HCC at protein levels.Interestingly, the ZEB1 mRNA level showed no significant difference in HepG2 cells transduced with shUSP39 (Fig. S2), which indicated that USP39 may mediate ZEB1 expression via posttranslational regulation (i.e., protein deubiquitination)."
reach
"Since ubiquitination and stability play important roles in ZEB1 regulation, hypothetically, USP39 with the function of deubiquitination could promote HCC progression through regulating the level of ZEB1 ubiquitination.The tripartite motif (TRIM) family proteins possess one or two B-boxes along with its domain structure, and a more diverse domain at the C terminus [20, 21], which are considered key regulators of protein degradation through ubiquitylation."
reach
"Collectively, our findings suggest that the balanced deubiquitination and ubiquitination of ZEB1 by USP39 and TRIM26 represent a novel mechanism for the progression of HCC, and this discovery provides a promising strategy for targeting USP39 or TRIM26 in the treatment of HCC cases with aberrant ZEB1 expression levels."
"Deubiquitinase <span class="match term0">USP39</span> and E3 ligase TRIM26 balance the level of <span class="match term1">ZEB1</span> ubiquitination and thereby determine the progression of hepatocellular carcinoma"
reach
"Since ubiquitination and stability play important roles in ZEB1 regulation, hypothetically, USP39 with the function of deubiquitination could promote HCC progression through regulating the level of ZEB1 ubiquitination.The tripartite motif (TRIM) family proteins possess one or two B-boxes along with its domain structure, and a more diverse domain at the C terminus [20, 21], which are considered key regulators of protein degradation through ubiquitylation."
reach
"The zinc finger E-box binding homology cassette (ZEB1) is a key inducer of epithelial–mesenchymal transition (EMT), promoting cancer cell metastasis; USP39 inhibits the degradation of ZEB1 and promotes the development of EMT through deubiquitylation, further accelerating the invasion and metastasis of HCC cells [38]."
reach
"Collectively, we believe that USP39 reduces the degradation of ZEB1 protein through direct deubiquitination, which promotes EMT progression and the development of HCC.Ubiquitination and deubiquitination are two contrasting posttranslational processes that involve in the conjugation and removing of ubiquitin from targeted proteins, respectively."
USP39 affects Neoplasm Metastasis
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USP39 activates Neoplasm Metastasis.
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USP39 inhibits Neoplasm Metastasis.
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sparser
"Given the importance of the p53 pathway in the tumor promotor function of USP39, further investigations should address these key questions: (1) How does USP39 regulate p53 and what is the interaction between USP39 and p53? (2) is the oncogenic function of USP39 solely dependent on the p53 pathway, or is another signaling pathway involved?"
reach
"In summary, our data reveal a novel mechanism in the progress of HCC that USP39 promotes the proliferation and migration of HCC through increasing beta-catenin level via both direct deubiquitination and reducing TRIM26 pre-mRNA maturation and splicing, which may provide a new idea and target for clinical treatment of HCC."
USP39 affects cell growth
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USP39 activates cell growth.
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10
USP39 inhibits cell growth.
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5
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"The results demonstrated that the level of the 3 '-end of EGFR decreased (P = 0.0015) more sharply than that of the 5 '-end (P = 0.0069), and the ratio ofthe 3 '-end to 5 '-end levels was significant decreased (P = 0.0297), implying that knockdown of USP39 might inhibit the transcription elongation of EGFR, and might produce unstable EGFR mRNA fragments lacking the 3 '-UTR."
reach
"We hypothesize that these nuclear membrane proteins may form a synergistic network to create a microenvironment to benefit heterochromatin organization and maintenance at the nuclear periphery, which requires further investigation.Fission yeast Sad1 binds both canonical histone H2A-H2B and histone variant H2A.Z-H2B, whereas the budding yeast SUN-family protein, Mps3, specifically recognizes H2A.Z ."
sparser
"To identify the domains responsible for the interaction between ETS2 and USP39, we created several deletion mutants of ETS2:ΔETS (ETS domain-deleted, aa 1–362), PNT-only (Pointed domain-containing, aa 1–170), ΔPNT (Pointed domain-deleted, aa 1–84 & 171–469) and 171–362 (containing aa 171–362) ( xref A)."
reach
"To identify the domains responsible for the interaction between ETS2 and USP39, we created several deletion mutants of ETS2:ΔETS (ETS domain-deleted, aa 1–362), PNT-only (Pointed domain-containing, aa 1–170), ΔPNT (Pointed domain-deleted, aa 1–84 & 171–469) and 171–362 (containing aa 171–362) (Figure 3A)."
reach
"Fortuitously, a SYD-2 phosphopeptide was a top hit present in all 3 biological replicates (Fig 3A), indicating SAD-1 may be responsible for SYD-2 phosphoregulation.To test if SAD-1 was directly responsible for phosphorylating SYD-2 and determine if additional sites may be present that were not found in the phosphoproteomics screen, we performed in vitro kinase assays between SAD-1 and SYD-2 (Figs 3B, S4A, and S4B and S2 Table)."
reach
"Fortuitously, a SYD-2 phosphopeptide was a top hit present in all 3 biological replicates (Figure 3A), indicating SAD-1 may be responsible for SYD-2 phosphoregulation.To test if SAD-1 was directly responsible for phosphorylating SYD-2 and determine if additional sites may be present not found in the phosphoproteomics screen, we performed in vitro kinase assays between SAD-1 and SYD-2 (Figure 3B and S3A-B)."
USP39 affects Carcinogenesis
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sparser
"Histone lactylation can also enhance USP39 expression, which interacts with the key glycolytic enzyme phosphoglycerate kinase 1 (PGK1) to promote its stability and deubiquitination, thereby increasing PGK1’s biological activity and potentially accelerating the glycolytic pathway."
sparser
"For example, in bladder cancer, H3K18 lactylation promotes tumorigenesis by enhancing the expression of the oncogene Lipocalin-2 (LCN2) ( xref ); in endometrial cancer, histone lactylation upregulates USP39 expression, which further interacts with PGK1 to activate the PI3K/AKT/HIF-1α signaling pathway, accelerating tumor progression ( xref ); in colorectal cancer, the activation of G-protein coupled receptor 37 (GPR37) promotes the expression of LDHA by activating the Hippo pathway, thereby intervening in tumor progression ( xref )."
sparser
"Our previous studies have shown that the deubiquitin ligase Ubiquitin‐specific Peptidase 39 (USP39) directly interacts with NAT10 in a molecule‐specific manner to enhance the stability of NAT10. [ xref ] The results from co‐immunoprecipitation demonstrated a strong interaction between exogenous expression of NAT10 and USP39, whereas the interaction was weakened by G‐749 (Figure xref )."
USP39 affects signal transduction
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9
USP39 activates signal transduction.
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7
USP39 inhibits signal transduction.
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2
reach
"We hypothesize that these nuclear membrane proteins may form a synergistic network to create a microenvironment to benefit heterochromatin organization and maintenance at the nuclear periphery, which requires further investigation.Fission yeast Sad1 binds both canonical histone H2A-H2B and histone variant H2A.Z-H2B, whereas the budding yeast SUN-family protein, Mps3, specifically recognizes H2A.Z ."
Bisphenol A affects USP39
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Bisphenol A increases the amount of USP39.
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Bisphenol A decreases the amount of USP39.
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sparser
"USP39 binds SRPK1 (Serine/arginine-rich splicing factor kinase 1) through its 101–565 fragment, promoting SRPK1-SRSF1 (Serine and arginine-rich splicing factor 1) phosphorylation and interaction, which subsequently regulates VEGF-A165b alternative splicing to drive RCC proliferation and angiogenesis ( xref )."
reach
"In particular, USP39 de-ubiquitinates and stabilizes CHK2 to regulate the DNA damage response and chemical radiation resistance [43], de-ubiquitinates and stabilizes the SP1 protein to promote hepatocellular carcinoma progression [44], and inhibits VEGF-A165b-selective splicing by regulating SRSF1 and SRPK1 to promote malignant proliferation and angiogenesis of renal cell carcinoma [45]."
USP39 affects Pancreatic Neoplasms
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8
USP39 activates Pancreatic Neoplasms.
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5
USP39 inhibits Pancreatic Neoplasms.
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3
USP39 affects Circulin-C
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USP39 binds Circulin-C. 8 / 8
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sparser
"After confirming the circular characteristics of circ-USP39, we further found that the circ-USP39 expression was upregulated in hypoxia-induced cardiomyocytes and the circ-USP39 knockdown facilitated the viability of hypoxia-induced AC16, while suppressing cardiomyocyte apoptosis and injury."
sparser
"Histone lactylation can also enhance USP39 expression, which interacts with the key glycolytic enzyme phosphoglycerate kinase 1 (PGK1) to promote its stability and deubiquitination, thereby increasing PGK1’s biological activity and potentially accelerating the glycolytic pathway."
sparser
"For example, in bladder cancer, H3K18 lactylation promotes tumorigenesis by enhancing the expression of the oncogene Lipocalin-2 (LCN2) ( xref ); in endometrial cancer, histone lactylation upregulates USP39 expression, which further interacts with PGK1 to activate the PI3K/AKT/HIF-1α signaling pathway, accelerating tumor progression ( xref ); in colorectal cancer, the activation of G-protein coupled receptor 37 (GPR37) promotes the expression of LDHA by activating the Hippo pathway, thereby intervening in tumor progression ( xref )."
reach
"Together, these data demonstrate that H2A-H2B promotes Sad1 phase separation to enrich Sad1-interaction partners, such as HDACs, in the same condensates.Collectively, we propose the following model for Sad1’s role in heterochromatin positioning and formation: H2A-H2B interacts with Sad1 and facilitates the otherwise-dispersed Sad1 clustering into condensates, forming discrete Sad1 puncta distributed on the NE as observed in Fig. 3; liquid droplet-like condensates formed by Sad1-H2A-H2B help recruit heterochromatin factors, such as Clr3 and Sir2, to the condensates, which promotes spatial organization and heterochromatin silencing at the nuclear envelope (Fig. 7c)."
H2AB affects USP39
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H2AB binds USP39.
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H2AB activates USP39.
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Circulin-C affects USP39
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USP39 binds Circulin-C. 8 / 8
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sparser
"After confirming the circular characteristics of circ-USP39, we further found that the circ-USP39 expression was upregulated in hypoxia-induced cardiomyocytes and the circ-USP39 knockdown facilitated the viability of hypoxia-induced AC16, while suppressing cardiomyocyte apoptosis and injury."
sparser
"Given the importance of the p53 pathway in the tumor promotor function of USP39, further investigations should address these key questions: (1) How does USP39 regulate p53 and what is the interaction between USP39 and p53? (2) is the oncogenic function of USP39 solely dependent on the p53 pathway, or is another signaling pathway involved?"
Doxycycline affects USP39
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Doxycycline inhibits USP39.
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3
Doxycycline activates USP39.
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3
USP39 affects homologous recombination
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USP39 activates homologous recombination.
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USP39 inhibits homologous recombination.
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USP39 inhibits homologous recombination. 2 / 2
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"To rule out that a decrease in transcript levels of USP39-linked factors causes HR or NHEJ defects in USP39 depleted cells, we performed qPCR for USP39-linked HR or NHEJ factors and found that none of the NHEJ factors identified in this study were downregulated by USP39 depletion (Supplementary Figure S13D)."
USP39 affects cell death
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USP39 inhibits cell death.
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USP39 activates cell death.
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USP39 activates cell death. 3 / 3
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3
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"Future studies should employ Annexin V/PI double staining flow cytometry to characterize the specific mode of cell death, complemented by Western blot analysis of apoptotic markers such as cleaved PARP and activated Caspase-3, thereby elucidating the molecular pathways involved in USP39-mediated cell death."
reach
"The expression of such markers demonstrated that Usp39 was essential to start the formation of a primitive streak correctly, but dispensable for the formation of a visceral endoderm, including anterior determination.As shown above, considering that USP39 may activate non-canonical Wnt signaling in LM-epidermal cells in vitro (Fig. 3g–p), we examined whether molecular markers for PCP components were affected in Usp39 embryos at E6.5 (Fig. 4l–m′)."
reach
"Taken together, these findings demonstrate that Usp39 genetically interacts with Vangl2 in terms of axial elongation, supporting the notion that USP39 contributes to modulation of non-canonical Wnt signaling.Next, to exclude the possibility of any involvement of USP39 in canonical Wnt signaling, we tested for any genetic interaction between β-catenin and Usp39 (Fig. S9)."
reach
"This potentially originating from the iUSP domain cannot bind ubiquitin either, and the ZnF of USP39 could interact with the splicing independent on ubiquitin [64], which provides the opportunity for SRSF1 binding to USP39 , though further exploration is required to confirm the conclusion.Firstly, one remaining limitation is how USP39 drives the changes in VEGF-A , which needs further research to elucidate the specific mechanisms."
reach
"This potentially originating from the iUSP domain cannot bind ubiquitin either, and the ZnF of USP39 could interact with the splicing independent on ubiquitin [64], which provides the opportunity for SRSF1 binding to USP39 , though further exploration is required to confirm the conclusion.Firstly, one remaining limitation is how USP39 drives the changes in VEGF-A , which needs further research to elucidate the specific mechanisms."
USP39 affects H2AB
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USP39 affects Cell Survival
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USP39 activates Cell Survival. 6 / 6
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"Based on a study conducted by Xing et al., (2018) on colorectal cancer cell lines SW1116 and HCT116, it was found that knockdown of USP39 could inhibit cell viability and colony formation of cell lines significantly in the group of cells treated with USP39 knockdown compared to the negative control group (<0.001)."
sparser
"USP39 binds SRPK1 (Serine/arginine-rich splicing factor kinase 1) through its 101–565 fragment, promoting SRPK1-SRSF1 (Serine and arginine-rich splicing factor 1) phosphorylation and interaction, which subsequently regulates VEGF-A165b alternative splicing to drive RCC proliferation and angiogenesis ( xref )."
USP39 affects localization
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USP39 inhibits localization.
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USP39 activates localization.
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USP39 affects cell migration
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USP39 affects angiogenesis
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USP39 affects Carcinoma, Hepatocellular
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USP39 activates Carcinoma, Hepatocellular. 3 / 5
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"In particular, USP39 de-ubiquitinates and stabilizes CHK2 to regulate the DNA damage response and chemical radiation resistance [43], de-ubiquitinates and stabilizes the SP1 protein to promote hepatocellular carcinoma progression [44], and inhibits VEGF-A165b-selective splicing by regulating SRSF1 and SRPK1 to promote malignant proliferation and angiogenesis of renal cell carcinoma [45]."
reach
"Furthermore, silencing of USP39, a target of miR-1281 in human osteosarcoma cells, inhibits survival under endoplasmic reticulum stress and slows the metastasis of malignant bone tumors to other tissues and organs by increasing the expression of Cyclin A2 and p21, leading to cell cycle arrest in the G2/M phase and promoting apoptosis [43, 92, 93]."
reach
"Although the aforementioned study showing the DUB activity of USP39 is controversial compared to that in previous studies (59,60), it is possible that USP39 modulates BRCA1-coupled HR in a PAR-independent fashion in various ways.Lastly, a recent study showed that the recruitment of 53BP1 to DNA lesions was not impaired after PARP inhibition (91)."
sparser
"Furthermore, to determine whether USP39 could interact with ADAM9 and regulate the ubiquitination of ADAM9, we co‐transfected Myc‐tagged USP39, Flag‐tagged ADAM9 with or without HA tagged Ub plasmids into HEK293T cells; co‐immunoprecipitation experiments revealed that USP39 failed to interact with ADAM9 at the protein level (Fig. xref ) and overexpressing USP39 had no effect on the polyubiquitination of ADAM9 (Fig. S9B)."
reach
"This potentially originating from the iUSP domain cannot bind ubiquitin either, and the ZnF of USP39 could interact with the splicing independent on ubiquitin [64], which provides the opportunity for SRSF1 binding to USP39 , though further exploration is required to confirm the conclusion.Firstly, one remaining limitation is how USP39 drives the changes in VEGF-A , which needs further research to elucidate the specific mechanisms."
Small interfering RNA affects USP39
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USP39 inhibits epithelial to mesenchymal transition.
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USP39 inhibits epithelial to mesenchymal transition. 2 / 2
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"The zinc finger E-box binding homology cassette (ZEB1) is a key inducer of epithelial–mesenchymal transition (EMT), promoting cancer cell metastasis; USP39 inhibits the degradation of ZEB1 and promotes the development of EMT through deubiquitylation, further accelerating the invasion and metastasis of HCC cells [38]."
USP39 activates epithelial to mesenchymal transition.
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USP39 activates epithelial to mesenchymal transition. 2 / 2
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USP39 binds PRPF4 bound to SART1, SNRNP200, PRPF6, LSM8, SNRPA, SNRPB, SNU13, SNRPE, SNRPF, SNRPG, LSM3, LSM6, SNRPD1, SNRPD2, SNRPD3, TXNL4A, EFTUD2, USP39, PRPF8, SNRNP27, PRPF31, SNRNP40, RBM42, DDX23, LSM7, LSM2, LSM5, and LSM4. 1 / 1
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"The major spliceosomal building blocks are the U1, U2, U4/U6, and U5 small nuclear ribonucleoproteins (snRNPs). Each consists of a small nuclear RNA (snRNA) (or two, in the case of U4/U6), seven Sm proteins that form a ring (or seven Lsm proteins in the case of U6), and a variable number of snRNP-specific proteins (Fig. 1F) (Will and Lührmann 2011). Under splicing conditions, the U4/U6 and U5 snRNPs form a 25S U4/U6.U5 tri-snRNP, in which the U4 and U6 snRNAs are base-paired, forming a three-way junction."
USP39 affects E protein
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USP39 affects DNA-templated transcription
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USP39 inhibits DNA-templated transcription.
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USP39 activates DNA-templated transcription.
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USP39 activates DNA-templated transcription. 2 / 2
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"The results demonstrated that the level of the 3 '-end of EGFR decreased (P = 0.0015) more sharply than that of the 5 '-end (P = 0.0069), and the ratio ofthe 3 '-end to 5 '-end levels was significant decreased (P = 0.0297), implying that knockdown of USP39 might inhibit the transcription elongation of EGFR, and might produce unstable EGFR mRNA fragments lacking the 3 '-UTR."
USP39 binds PRPF4 bound to SART1, SNRNP200, PRPF6, LSM8, SNRPA, SNRPB, SNU13, SNRPE, SNRPF, SNRPG, LSM3, LSM6, SNRPD1, SNRPD2, SNRPD3, TXNL4A, EFTUD2, USP39, PRPF8, SNRNP27, PRPF31, SNRNP40, RBM42, DDX23, LSM7, LSM2, LSM5, and LSM4. 1 / 1
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"The major spliceosomal building blocks are the U1, U2, U4/U6, and U5 small nuclear ribonucleoproteins (snRNPs). Each consists of a small nuclear RNA (snRNA) (or two, in the case of U4/U6), seven Sm proteins that form a ring (or seven Lsm proteins in the case of U6), and a variable number of snRNP-specific proteins (Fig. 1F) (Will and Lührmann 2011). Under splicing conditions, the U4/U6 and U5 snRNPs form a 25S U4/U6.U5 tri-snRNP, in which the U4 and U6 snRNAs are base-paired, forming a three-way junction."
USP39 affects regulation of cell cycle
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USP39 affects SARS-CoV-2
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3
reach
"We then performed an rb1 mRNA overexpression experiment in usp39 mutants and observed partial rescue of the adenohypophysis phenotype (XREF_FIG, mutant N = 34, ~ 50% showed rescue), validating the importance of usp39 mediated rb1 mRNA splicing in controlling pituitary lineage expansion during development."
USP39 affects Interferon
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USP39 activates Interferon. 3 / 3
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reach
"Unlike USP2A, the deubiquitinating enzymes BRCC36, USP13, and USP39 positively regulate IFN activities by attenuating the polyubiquitination level of STAT1, and this process is independent of IFN treatment, which suggests divergent functional roles of these DUBs under differential contexts.Additionally, ATXN3 does not affect IFN-I production during viral infection but positively regulates IFNAR1-mediated downstream signaling by targeting HDAC3 (108)."
USP39 affects HDACs
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USP39 affects Carcinoma, Endometrioid
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HDACs affects USP39
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E protein affects USP39
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3
Tetrachloromethane affects USP39
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Sodium arsenite affects USP39
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Sodium arsenite increases the amount of USP39.
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Sodium arsenite decreases the amount of USP39.
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MiR-133a affects USP39
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Methyl methanesulfonate affects USP39
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Citric acid affects USP39
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Beta-lapachone affects USP39
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Beta-lapachone increases the amount of USP39.
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Beta-lapachone decreases the amount of USP39.
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All-trans-retinoic acid affects USP39
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USP39 affects splicing efficiency HMGA2
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USP39 affects nuclear envelope
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USP39 affects miR-133a
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USP39 affects mRNA processing
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USP39 affects invasion potential ovarian cancer cells
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USP39 affects invasion ovarian cancer cells
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USP39 affects heterochromatin organization
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USP39 affects glycolytic process
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USP39 activates glycolytic process. 2 / 2
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USP39 affects carboplatin
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USP39 activates Squamous Cell Carcinoma of Head and Neck. 2 / 2
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USP39 affects RFP
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USP39 affects PI3K/AKT/HIF-1alpha
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USP39 affects LINC00623
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USP39 affects Genomic Instability
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USP39 inhibits Genomic Instability.
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USP39 inhibits Genomic Instability. 1 / 1
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USP39 activates Genomic Instability.
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USP39 activates Genomic Instability. 1 / 1
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USP39 affects DNA repair
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USP39 affects DNA Breaks, Double-Stranded
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USP39 affects DAP
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USP39 affects Carcinoma, Squamous Cell
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USP39 inhibits Carcinoma, Squamous Cell.
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USP39 inhibits Carcinoma, Squamous Cell. 1 / 1
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USP39 activates Carcinoma, Squamous Cell.
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USP39 activates Carcinoma, Squamous Cell. 1 / 1
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reach
"This enhanced Treg cell function is partially mediated by lactate-dependent ubiquitin-specific peptidase 39 (USP39), a component of the RNA splicing machinery, to augment cytotoxic T-lymphocyte antigen 4 (CTLA-4) expression in a FOXP3-dependent manner and, thus, to prevent cytotoxic T cell function [128]."
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USP39 affects Adenocarcinoma of Lung
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2
RFP affects USP39
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LINC00623 affects USP39
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Gentamicins affects USP39
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reach
"In addition, we performed quantitative RT-PCR analysis on the rb1 mRNA injected usp39 embryos and observed a 30% reduction of e2f4 expression compared to control uninjected usp39 mutants (XREF_SUPPLEMENTARY), indicating that e2f4 upregulation in usp39 mutant is secondary to Rb1 loss of function."
DAP affects USP39
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Acrylamide affects USP39
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sparser
"Furthermore, to determine whether USP39 could interact with ADAM9 and regulate the ubiquitination of ADAM9, we co‐transfected Myc‐tagged USP39, Flag‐tagged ADAM9 with or without HA tagged Ub plasmids into HEK293T cells; co‐immunoprecipitation experiments revealed that USP39 failed to interact with ADAM9 at the protein level (Fig. xref ) and overexpressing USP39 had no effect on the polyubiquitination of ADAM9 (Fig. S9B)."
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Type SIRT7 affects USP39
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1
Trovafloxacin affects USP39
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Trimellitic anhydride affects USP39
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Sodium arsenate affects USP39
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Short hairpin RNA affects USP39
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Short hairpin RNA inhibits USP39. 1 / 1
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Resveratrol affects USP39
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Oncogene protein c-MYC ovarian cancer cells affects USP39
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Nimesulide affects USP39
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MiR-370-3p affects USP39
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Methamphetamine affects USP39
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Mercury(0) affects USP39
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Ivermectin affects USP39
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Hydrogen peroxide affects USP39
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Hsa-miR-193b-3p affects USP39
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Diafenthiuron affects USP39
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Diafenthiuron activates USP39. 1 / 1
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1
Deoxynivalenol affects USP39
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Astaxanthin affects USP39
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Astaxanthin inhibits USP39. 1 / 1
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Arsenic disulfide affects USP39
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YP_009227196 affects USP39
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Vehicle Emissions affects USP39
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Ualcan databases affects USP39
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USP39 affects β-amyrin
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USP39 affects wound healing
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USP39 activates wound healing. 1 / 1
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USP39 affects stability p53 protein
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USP39 affects splicing
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USP39 affects splicing exon-exon minigene transcripts
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USP39 affects sad2 mutants
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USP39 affects proteolysis
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USP39 inhibits proteolysis. 1 / 1
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USP39 affects primitive streak formation
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USP39 inhibits primitive streak formation. 1 / 1
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USP39 affects phenazine-1-carboxylate
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USP39 inhibits phenazine-1-carboxylate. 1 / 1
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USP39 affects pathogenesis
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USP39 inhibits pathogenesis. 1 / 1
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USP39 affects overall survival mice
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USP39 affects non-homologous end-joining repair
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USP39 affects metastasis lung cancer cells
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USP39 affects metabolic process
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USP39 activates metabolic process. 1 / 1
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USP39 affects mesendoderm migration
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USP39 activates mesendoderm migration. 1 / 1
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USP39 affects immune response
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USP39 activates immune response. 1 / 1
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USP39 affects human glioma cells migration
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USP39 affects glioma25
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1
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USP39 increases the amount of cytotoxic T-lymphocyte antigen 4. 1 / 1
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"This enhanced Treg cell function is partially mediated by lactate-dependent ubiquitin-specific peptidase 39 (USP39), a component of the RNA splicing machinery, to augment cytotoxic T-lymphocyte antigen 4 (CTLA-4) expression in a FOXP3-dependent manner and, thus, to prevent cytotoxic T cell function [128]."
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USP39 affects cytokinesis
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USP39 activates cytokinesis. 1 / 1
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USP39 affects colony A549 cells
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USP39 affects centromere clustering
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USP39 activates centromere clustering. 1 / 1
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USP39 affects cell migration A549 HCC827 cells
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USP39 affects cell cycle phase transition
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USP39 activates cell cycle phase transition. 1 / 1
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USP39 affects antitumor cisplatin colon cancer cells dependent p53
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USP39 activates anatomical structure morphogenesis. 1 / 1
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"Since both canonical and non-canonical Wnt pathway signaling is necessary for the formation of LM-epidermal cells , and USP39 was able to induce LM-epidermal cells when canonical Wnt signaling alone was activated (Fig. 3g–p), these findings indicate that USP39 can direct epithelial morphogenesis by enhancing the enrichment of actomyosin networks via activation of non-canonical Wnt signaling."
USP39 affects activation p53 pathway
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USP39 affects abnormal cell cycle distribution
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eidos
"First , we observed that depletion of USP39 contributes to abnormal cell cycle distribution by inducing cell cycle arrest at G2 / M. Moreover , the underlying mechanism of action of USP39 is partly dependent on activation of the p53 pathway , upregulation of p53 and p21 , and downregulation of CDC2 and CyclinB1 [ 29 ] in A549 cells ."
USP39 affects YP_009227196
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USP39 affects Wnt/β-catenin
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USP39 affects UNC-84 homology) protein
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"The LINC complex functions as a nuclear envelope-spanning physical bridge connecting the nucleus and cytoskeleton and comprises two protein families: KASH (Klarsicht/ANC-1/Syne-1 homology) domain proteins that interact with the cytoskeleton on the outer nuclear envelope and SUN (Sad1/UNC-84 homology) protein complexes that are bound to the nuclear lamina and chromatin at the inner nuclear envelope ."
USP39 affects UBL domain
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USP39 affects TAZ mRNA
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USP39 affects Syne homology proteins
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reach
"In analogy to Klarsicht, Anc-1, and Syne homology proteins that accumulate at the ONM by binding to INM Sad1 and Unc-84 proteins (Sosa et al., 2013), we propose that Atg39 accumulates at the ONM by forming a translumenal bridge through direct or indirect interactions with the INM.We next asked whether the lumenal domain (with its transmembrane [TM] anchor) was sufficient to confer NE targeting and NE blebbing by making sequential N-terminal deletions."
USP39 affects Spliceosomes
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USP39 activates Spliceosomes. 1 / 1
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USP39 affects SUMOylation specific protein
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USP39 affects RNA-binding
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USP39 inhibits RNA-binding. 1 / 1
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USP39 affects RNA splicing
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USP39 activates RNA splicing. 1 / 1
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USP39 affects Osteosarcoma
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USP39 activates Osteosarcoma. 1 / 1
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USP39 affects Mis18C
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USP39 affects Metastatic Cells Vitro potential contribution USP39 metastatic capacity A549 HCC827 cells performed Matrigel non-coated Transwell migration coated Transwell invasion assays
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USP39 activates Metastatic Cells Vitro potential contribution USP39 metastatic capacity A549 HCC827 cells performed Matrigel non-coated Transwell migration coated Transwell invasion assays. 1 / 1
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eidos
"Knockdown of USP39 Inhibits Metastatic of Lung Cancer Cells In Vivo and In Vitro To test the potential contribution of USP39 to the metastatic capacity of A549 and HCC827 cells , in vitro , we performed Matrigel non-coated Transwell migration and Matrigel coated Transwell invasion assays ."
USP39 affects MAPK cascade
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USP39 activates MAPK cascade. 1 / 1
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"Complementary pathway activity analysis using the GSCA database demonstrated that USP39 predominantly activated the cell cycle (47% activation vs. 0% inhibition), DNA damage response (34% activation vs. 0% inhibition), and apoptosis (25% activation vs. 3% inhibition) pathways, while inhibiting RAS/MAPK signaling (0% activation vs. 34% inhibition) (Fig. 2B)."
USP39 affects KO mice
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USP39 affects Histone_H2B
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USP39 binds Histone_H2B. 1 / 1
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USP39 affects H2AB.Notably
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reach
"Thus, our mutagenesis analyzes supported the importance of hydrophobic and electrostatic interactions in coordinating the interaction between Sad1 and H2AB.Notably, the core histone-binding fragment of Sad1 contains a DEF/Y motif commonly identified in H2A-H2B or H2A.Z-H2B-binding proteins, including Chz1, Anp32e, Swr1, and the suppressor of Ty16 (Spt16) (Fig. 2e), and showed a conserved histone recognition mode (Supplementary Fig. 5)."
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USP39 activates Esophageal Squamous Cell Carcinoma. 1 / 1
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USP39 affects E3_Ub_ligase
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E3_Ub_ligase binds USP39. 1 / 1
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USP39 affects Deubiquitinase
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USP39 inhibits Deubiquitinase. 1 / 1
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"Further studies are warranted to investigate the precise mechanism by which the USP39-mediated inhibition of ETS2’s nuclear localization occurs and subsequently leads to the transcriptional suppression of ETS2.USP39 has been traditionally considered an inactive DUB due to the substitution of the conserved cysteine residue at amino acid 234 in its USP domain with aspartate [30,31,32]."
USP39 affects CyclinB1
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USP39 affects Colonic Neoplasms
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USP39 activates Colonic Neoplasms. 1 / 1
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USP39 affects Cell Polarity
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USP39 increases the amount of Cell Polarity. 1 / 1
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USP39 affects Carcinoma, Renal Cell
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USP39 activates Carcinoma, Renal Cell. 1 / 1
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USP39 affects CDC2 cyclinB1
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USP39 affects 5-fluorouracil
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USP39 activates 5-fluorouracil. 1 / 1
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USP39 affects 3,3'-diaminobenzidine
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USP39 activates 3,3'-diaminobenzidine. 1 / 1
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UNC-84 homology) protein affects USP39
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reach
"The LINC complex functions as a nuclear envelope-spanning physical bridge connecting the nucleus and cytoskeleton and comprises two protein families: KASH (Klarsicht/ANC-1/Syne-1 homology) domain proteins that interact with the cytoskeleton on the outer nuclear envelope and SUN (Sad1/UNC-84 homology) protein complexes that are bound to the nuclear lamina and chromatin at the inner nuclear envelope ."
UBL domain affects USP4
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Syne homology proteins affects USP39
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reach
"In analogy to Klarsicht, Anc-1, and Syne homology proteins that accumulate at the ONM by binding to INM Sad1 and Unc-84 proteins (Sosa et al., 2013), we propose that Atg39 accumulates at the ONM by forming a translumenal bridge through direct or indirect interactions with the INM.We next asked whether the lumenal domain (with its transmembrane [TM] anchor) was sufficient to confer NE targeting and NE blebbing by making sequential N-terminal deletions."
Plant Extracts affects USP39
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Mis18C affects USP39
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Long non-coding RNA LINC00623 affects USP39
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Histone_H2B affects USP39
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USP39 binds Histone_H2B. 1 / 1
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H2AB.Notably affects USP39
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reach
"Thus, our mutagenesis analyzes supported the importance of hydrophobic and electrostatic interactions in coordinating the interaction between Sad1 and H2AB.Notably, the core histone-binding fragment of Sad1 contains a DEF/Y motif commonly identified in H2A-H2B or H2A.Z-H2B-binding proteins, including Chz1, Anp32e, Swr1, and the suppressor of Ty16 (Spt16) (Fig. 2e), and showed a conserved histone recognition mode (Supplementary Fig. 5)."
H2AB-RFP affects USP39
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Glyphosate affects USP39
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E3_Ub_ligase affects USP39
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E3_Ub_ligase binds USP39. 1 / 1
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Clr3.To affects USP39
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Carcinoma, Endometrioid affects USP39
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Carcinoma, Endometrioid decreases the amount of USP39. 1 / 1
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Air Pollutants affects USP39
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3-isobutyl-1-methyl-7H-xanthine affects USP39
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17alpha-ethynylestradiol affects USP39
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1,2-dimethylhydrazine affects USP39
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4,4'-sulfonyldiphenol affects USP39
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