IndraLab
Statements
reach
"These observed differences in hydrolysis rates between those reported for individual chains and the ones we found in the mixture containing all linkages may indicate that the presence of certain diUb linkages can lead to a change in hydrolysis rates of other linkages.Another interesting finding is the high preference of the metallo-DUB RPN11/RPN8 complex for Lys11 diUb."
PSMD14 affects cell population proliferation
|
1
70
PSMD14 activates cell population proliferation.
|
1
63
PSMD14 inhibits cell population proliferation.
|
7
PSMD14 inhibits cell population proliferation. 7 / 7
|
7
reach
"They subsequently optimized the structure of 8TQ using the FBDD approach to summarize SARs and identified the first potent and specific Rpn11 chemical probe, capzimin (IC = ∼300 nmol/L), which inhibited the proliferation of bortezomib-resistant cancer cells by stabilizing the proteasome substrates and inducing an unfolded protein response."
reach
"Although POH1 overexpression caused the deubiqutination of E2F1, the approach did not have an appreciable impact on levels of total polyubiquitin modified proteins (XREF_SUPPLEMENTARY), suggesting that POH1 mediated deubiquitination of E2F1 can take place in cells in absence of a noticeable alteration in global proteasome activity."
reach
"Furthermore, we generated different siRNA resistant (siR-R) POH1 constructs for rescue assays, and the results showed that restoration of POH1 expression with the C120S-, H113Q- and DeltaJAMM POH1 mutants did not attenuate the inhibition of E2F1 caused by the deletion of endogenous POH1 (XREF_FIG)."
reach
"Furthermore, we generated different siRNA resistant (siR-R) POH1 constructs for rescue assays, and the results showed that restoration of POH1 expression with the C120S-, H113Q- and DeltaJAMM POH1 mutants did not attenuate the inhibition of E2F1 caused by the deletion of endogenous POH1 (XREF_FIG)."
PSMD14 affects apoptotic process
|
2
45
PSMD14 inhibits apoptotic process.
|
2
25
PSMD14 activates apoptotic process.
|
20
reach
"Deubiquitinases (DUBs) also play an important role in the regulation of Snail1 protein stability, including USP3, USP11, USP13, DUB3, USP18, USP26, USP27X, USP37, USP47, OTUB1, and PSMD14, that have been shown to facilitate deubiquitination and stabilization of nuclear Snail1 in promoting cell proliferation, migration, and invasion ."
reach
"Two new deubiquitinating enzymatic enzymes, PSMD14 with OTUB1, can inhibit the ubiquitination level of Snail and hinder its proteasomal degradation pathway, thus enabling the accumulation of Snail in cells, and activating the Snail-mediated epithelial-stromal transformation process to promote tumor progression and metastasis in esophageal squamous carcinoma (Jing et al., 2021; Zhou et al., 2018)."
PSMD14 affects Neoplasm Invasiveness
|
2
43
PSMD14 activates Neoplasm Invasiveness.
|
2
40
PSMD14 inhibits Neoplasm Invasiveness.
|
3
reach
"All together, these data revealed a previously undescribed mechanism by which RNF5 and POH1 mediate the ubiquitin modification of SARS-CoV-2 M for virion trafficking and release.As noted by previous studies, unlike with most enveloped viruses, in which M is necessary and sufficient to mediate VLP release, the E/M proteins of murine hepatitis virus (MHV) or the M/E/N proteins of SARS-CoV are necessary for efficient assembly, trafficking, and VLP release (7–9)."
sparser
"Notably, states E A1 and E A2 show ubiquitin densities near RPN10 and RPN11 and no substrate density inside the AAA ring, whereas state E B shows density features of both RPN11-bound ubiquitin and AAA-bound substrate with a visible isopeptide bond between the ubiquitin and substrate."
sparser
"In contrast, state E C1 shows densities of both RPN11-bound ubiquitin and AAA-bound substrate, with the isopeptide bond being completely absent in density, unambiguously verifying that this state is chemically post-deubiquitylation following state E B . Interestingly, state E C2 shows virtually identical ATPase conformation but lacks the RPN11-bound ubiquitin and the nucleotide density in RPT1, thus verifying that it represents the state immediately after state E C1 ."
sparser
"Around the scissile isopeptide bond between the RPN11-bound ubiquitin and the substrate lysine, a ternary interface is formed between RPN11, RPN8 and the N-loop of RPT5 which emanates from the top of its OB domain to efficiently carry out the deubiquitylation step ( xref b) [ xref ]."
PSMD14 affects Proteasome
|
3
20
2
PSMD14 activates Proteasome.
|
3
10
PSMD14 activates Proteasome. 10 / 13
|
3
10
reach
"The significantly upregulated genes encoding proteasome components (PSMC1, PSMD1, PSMD14, PSMD3, PSMD2, PSMD8) belong to multiple categories, indicating that numerous cellular processes in skeletal muscle from UCP1 KI pigs might be regulated by the degradation of ubiquitinated target proteins through coordinated functions of genes associated with these four GO terms (proteasome complex, endopeptidase complex, proteasome regulatory particle, proteasome accessory complex) (Figure 4C)."
eidos
"Additionally , in order to reduce proteasome activity , which was also elevated at baseline ( Figure 2B ) , we multiplexed with a guide RNA against Psmd14 ; this subunit of the proteasome is essential for proteasome assembly and function and upregulation of Psmd14 in invertebrates has been shown to increase proteasome activity ( Tonoki et al ., 2009 ) ."
PSMD14 inhibits Proteasome.
|
7
2
PSMD14 inhibits Proteasome. 9 / 10
|
7
2
reach
"Depending on the length and sequence of a substrate’s initiation region as well as the position and/or length of a ubiquitin chain, the Rpn11/ubiquitin-mediated attenuation of the proteasome conformational switching could become critical for successful substrate engagement, and substrate delivery through Rpn10’s UIM could therefore be more favorable compared to the Rpn1 or Rpn13 receptors."
PSMD14 binds Proteasome.
|
3
sparser
"In addition, we provide experimental evidence that BMP6 pathway regulated by ALK2-PSMD14 axis induces chemoresistance of human colorectal cancer cells through upregulating ABC transporter genes, and higher expressions of PSMD14 and ALK2 genes are clinically associated with poor prognosis of human colorectal cancer patients."
PSMD14 affects Neoplasm Metastasis
|
1
24
sparser
"In HeLa cells, high-glucose treatment facilitated chromatin binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to the negative-control locus GATA1 ( xref ), suggesting that NRF1 contributes to the activation of the proteasome subunit genes when it is accumulated in response to enhanced cellular O -GlcNAcylation."
sparser
"In HeLa cells transfected with control siRNA, as observed in the ChIP-seq analysis, MG132 treatment induced robust binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to a negative-control locus, GATA1 ( xref )."
reach
"In addition, while the treatment of the cells with lysosome inhibitor bafilomycin A1 (BFA1) rescued POH1 knockdown-mediated destabilization of the TGF-β receptors (Fig. 5d), the proteasome inhibitor Mg132 did not produce similar results (Fig. S4d), demonstrating the requirement of lysosomal activity in this process."
PSMD14 affects cell growth
|
10
1
PSMD14 activates cell growth.
|
8
PSMD14 inhibits cell growth.
|
2
1
reach
"Concurrently, gene set enrichment analyses of the TCGA and several GEO liver cancer datasets demonstrated a significant enrichment in the expression of a set of genes, which indicates poor survival of patients [32], in HCCs with high POH1 expression (Fig. S2b).3.2
POH1 promotes TGF-beta signaling in HCC cells."
Proteasome affects PSMD14
|
7
Proteasome binds PSMD14.
|
3
Proteasome deubiquitinates PSMD14.
|
3
Proteasome deubiquitinates PSMD14. 3 / 3
|
3
reach
"In line with this, knockdown of two components of the UPS, the ubiquitin ligase scaffolding protein Cul-1 and the proteasome-associated deubiquitinating protein Pad-1, leads to cell cycle reactivation and apoptosis in subsets of post-mitotic neurons (Staropoli and Abeliovich 2005)."
Proteasome activates PSMD14.
|
1
Proteasome activates PSMD14. 1 / 1
|
1
PSMD14 affects Osteosarcoma
|
11
PSMD14 activates Osteosarcoma.
|
9
PSMD14 activates Osteosarcoma. 9 / 9
|
9
reach
"Its function and mechanism in tumorigenesis and its potential significance in drug resistance remain unknown.In our work, we discovered that in vivo and in vitro overexpression of PSMD14 was adversely correlated with a poor prognosis in osteosarcoma; PSMD14 may induce malignant osteosarcoma characteristics by the PI3K/AKT/mTOR pathway, according to a preliminary study."
PSMD14 inhibits Osteosarcoma.
|
2
reach
"Further in vivo and clinical studies are required to verify the findings in the present study.In conclusion, the present study demonstrated that HEY1 can activate PSMD14 expression, thereby promoting trophoblast proliferation, invasion and migration, in addition to downstream endothelial angiogenesis."
sparser
"Notably, states E A1 and E A2 show ubiquitin densities near RPN10 and RPN11 and no substrate density inside the AAA ring, whereas state E B shows density features of both RPN11-bound ubiquitin and AAA-bound substrate with a visible isopeptide bond between the ubiquitin and substrate."
sparser
"In contrast, state E C1 shows densities of both RPN11-bound ubiquitin and AAA-bound substrate, with the isopeptide bond being completely absent in density, unambiguously verifying that this state is chemically post-deubiquitylation following state E B . Interestingly, state E C2 shows virtually identical ATPase conformation but lacks the RPN11-bound ubiquitin and the nucleotide density in RPT1, thus verifying that it represents the state immediately after state E C1 ."
sparser
"Around the scissile isopeptide bond between the RPN11-bound ubiquitin and the substrate lysine, a ternary interface is formed between RPN11, RPN8 and the N-loop of RPT5 which emanates from the top of its OB domain to efficiently carry out the deubiquitylation step ( xref b) [ xref ]."
PSMD14 affects Cell Survival
|
10
reach
"Finally, the rescue experiment demonstrated that PSMD14 knockdown reversed the function of ALKBH1 silencing in the hypoxia treated HTR-8/SVneo cells.In conclusion, this study demonstrated that ALKBH1 knockdown promoted the cell growth, migration, and invasion of hypoxia treated HTR-8/SVneo cells through enhancing the m5C levels of PSMD14."
PSMD14 affects cellular senescence
|
1
8
PSMD14 inhibits cellular senescence.
|
1
5
PSMD14 activates cellular senescence.
|
3
reach
"Concurrently, gene set enrichment analyses of the TCGA and several GEO liver cancer datasets demonstrated a significant enrichment in the expression of a set of genes, which indicates poor survival of patients [32], in HCCs with high POH1 expression (Fig. S2b).3.2
POH1 promotes TGF-beta signaling in HCC cells."
reach
"POH1 can remove the K63-polyubiqutin chains attached to CAV1 and compromise its activity in the lysosomal degradation of the TGF-β receptors.Regarding the functional consequences of POH1-mediated promotion of TGF-β signaling in HCC cells, we found that POH1 substantially increased the metastatic potential of HCC cells both in vitro and in vivo."
reach
"Collectively, these results strongly suggest that POH1 may promote TGF-β signaling in HCC.Consistently, Kaplan-Meier analyses from the HCC samples revealed that the patients with higher staining scores of POH1 and p-SMAD3 had lower overall survival (Fig. 2c) and more advanced progression (Fig. 2d)."
PSMD14 affects cell migration
|
8
sparser
"To further confirm these results, we examined the half-life of the ALK2 protein in the absence or presence of PSMD14 upon treatment of protein synthesis inhibitor cycloheximide (CHX) after a plasmid encoding HA-ALK2 protein was transfected into HCT116 cells together with or without Flag-PSMD14."
sparser
"To identify which polyubiquitination pattern of ALK2 is deubiquitinated by PSMD14, wild-type ubiquitin (HA-Ubi), the K48 ubiquitin mutant (HA-Ubi-K48) in which six lysine residues except for lysine 48 are substituted into arginines, and the K63 ubiquitin mutant (HA-Ubi-K63) in which only lysine 63 is left intact, were transfected into HCT116 cells with or without Flag-PSMD14."
sparser
"To further confirm these results, we examined the half-life of the ALK2 protein in the absence or presence of PSMD14 upon treatment of protein synthesis inhibitor cycloheximide (CHX) after a plasmid encoding HA-ALK2 protein was transfected into HCT116 cells together with or without Flag-PSMD14."
sparser
"To identify which polyubiquitination pattern of ALK2 is deubiquitinated by PSMD14, wild-type ubiquitin (HA-Ubi), the K48 ubiquitin mutant (HA-Ubi-K48) in which six lysine residues except for lysine 48 are substituted into arginines, and the K63 ubiquitin mutant (HA-Ubi-K63) in which only lysine 63 is left intact, were transfected into HCT116 cells with or without Flag-PSMD14."
MKO1 affects PSMD14
|
7
sparser
"Our results show that PSMD14-mKO1 accumulates in response to local UVC stimulation, but with slower kinetics than DDB2, XPC, and RAD23B. Notably in this regard, the proteasome is one of the most abundant protein factors in a cell, so even weak accumulation may indicate the presence of substantial numbers of molecules at damaged sites."
| PMC
PSMD14 affects proteolysis
|
7
PSMD14 inhibits proteolysis.
|
4
PSMD14 inhibits proteolysis. 4 / 4
|
4
reach
"POH1 knockdown could dramatically inhibit GFPu protein degradation in HEK-293 cells and induce ubiquitinated protein accumulation in HepG2 cancer cells, and this disassembly of 26S proteasome could mostly blocked the effects of CuPT on protein degradation and ubiquitinated protein accumulation, indicating that CuPT mediated proteasome malfunction did rely on the existence of intact 26S proteasome."
PSMD14 activates proteolysis.
|
3
PSMD14 affects mKO1
|
7
sparser
"Our results show that PSMD14-mKO1 accumulates in response to local UVC stimulation, but with slower kinetics than DDB2, XPC, and RAD23B. Notably in this regard, the proteasome is one of the most abundant protein factors in a cell, so even weak accumulation may indicate the presence of substantial numbers of molecules at damaged sites."
| PMC
|
7
PSMD14 activates epithelial to mesenchymal transition. 6 / 6
|
6
PSMD14 bound to SNAI1 activates epithelial to mesenchymal transition. 1 / 1
|
1
PSMD14 is modified
|
7
PSMD14 is ubiquitinated.
|
6
sparser
"Through our proteomic analysis, we understand that α-fodrin downregulation results in an increase in apoptotic pathway proteins such as 26S proteasome non-ATPase regulatory subunit 14 and polyubiquitin C and B. Ubiquitination and proteosome-based protein degradation are pathways that accompany apoptosis in cells."
PSMD14 is acetylated.
|
1
Capzimin affects PSMD14
|
6
Capzimin binds PSMD14.
|
5
reach
"They subsequently improved the potency of 8TQ by an approach based on structure–activity relationship and identified that capzimin, a molecule that binds the catalytic site of POH1 (Fig. 3), has greatly enhanced selectivity for POH1 over other JAMM metalloenzymes and sevenfold more potency towards POH1 (IC = 0.34 mM) [6]."
Capzimin activates PSMD14.
|
1
reach
"They subsequently improved the potency of 8TQ by an approach based on structure–activity relationship and identified that capzimin, a molecule that binds the catalytic site of POH1 (Fig. 3), has greatly enhanced selectivity for POH1 over other JAMM metalloenzymes and sevenfold more potency towards POH1 (IC = 0.34 mM) [6]."
5
|
1
PSMD14 affects cell cycle
|
2
4
reach
"Testing aspects of this model and how it has functionally evolved from yeast to humans will provide further mechanistic details of SNX3-retromer mediated sorting and elucidate the role of the MON2-PAD1 complex as an evolutionary conserved endosomal coat, and, more broadly, the role of flippases in carrier formation during membrane transport.In C. elegans, the retromer-dependent sorting of the bone morphogenetic protein (BMP) type I receptor, SMA-6, is also severely perturbed in mutants of Ce-snx-3 but not snx-1 or Ce-snx-27 ."
PSMD14 affects Carcinogenesis
|
6
PSMD14 activates Carcinogenesis. 6 / 6
|
6
reach
"A work from Qin et al. found cornification related protein, Peptidylargininedeiminase 1 or PAD1, could promote tumorigenesis by regulating MEK1-ERK1/2-MMP2 signaling in triple negative breast cancer.41 Another work from Fiskin revealed disrupted cornification could induce immune dysfunction state in human skin, which were consistent with our finding that TDERS high group with cornification activated state resulted with immune dysfunction."
PSMD14 affects CSN5i-3
|
6
reach
"Testing aspects of this model and how it has functionally evolved from yeast to humans will provide further mechanistic details of SNX3-retromer mediated sorting and elucidate the role of the MON2-PAD1 complex as an evolutionary conserved endosomal coat, and, more broadly, the role of flippases in carrier formation during membrane transport.In C. elegans, the retromer-dependent sorting of the bone morphogenetic protein (BMP) type I receptor, SMA-6, is also severely perturbed in mutants of Ce-snx-3 but not snx-1 or Ce-snx-27 ."
CSN5i-3 affects PSMD14
|
6
Mpr1 affects PSMD14
|
5
RPN8 affects PSMD14
|
5
sparser
"Some of the processes that are influenced by POH1 could be mediated by factors not affected by the main proteolytic activity of the 26S proteasome and involving the sole 19S regulatory particle or other POH1-containing subcomplexes (the proteasome lid or the POH1-Rpn8 dimer), although experimental proof of this concept is lacking due to the difficulty of separating proteasome binding from POH1 function."
PSMD14 affects signal transduction
|
5
PSMD14 activates signal transduction.
|
3
PSMD14 inhibits signal transduction.
|
2
PSMD14 affects mpr1
|
5
PSMD14 affects capzimin
|
5
reach
"They subsequently improved the potency of 8TQ by an approach based on structure–activity relationship and identified that capzimin, a molecule that binds the catalytic site of POH1 (Fig. 3), has greatly enhanced selectivity for POH1 over other JAMM metalloenzymes and sevenfold more potency towards POH1 (IC = 0.34 mM) [6]."
PSMD14 affects angiogenesis
|
5
PSMD14 activates angiogenesis. 5 / 5
|
5
reach
"PSMD14 overexpression was found to promote the proliferation, invasion, migration of HTR-8/SVneo cells and the angiogenesis of HUVECs following treatment with the HTR-8/SVneo cell culture supernatant, accompanied by enhanced expression of proliferation and migration-related proteins."
PSMD14 affects RPN8
|
5
sparser
"Some of the processes that are influenced by POH1 could be mediated by factors not affected by the main proteolytic activity of the 26S proteasome and involving the sole 19S regulatory particle or other POH1-containing subcomplexes (the proteasome lid or the POH1-Rpn8 dimer), although experimental proof of this concept is lacking due to the difficulty of separating proteasome binding from POH1 function."
reach
"CRISPR/Cas9-generated knockout mutations of HBP1, but not POH1 mutations, promoted earlier flowering time; conversely, HBP1 and POH1 overexpression delayed flowering time in rice under long-day and short-day conditions by activating the expression of Hd1 and suppressing the expression of Early heading date 1 (Ehd1), Heading date 3a (Hd3a), and Rice Flowering locus T 1 (RFT1), thus controlling flowering time in rice."
PSMD14 affects DNA-templated transcription
|
4
1
PSMD14 activates DNA-templated transcription.
|
3
PSMD14 inhibits DNA-templated transcription.
|
1
1
PSMD14 inhibits DNA-templated transcription. 2 / 2
|
1
1
reach
"Based on the studies in S. pombe, where the Pad1 and POH1 overexpression phenotype was dependent upon the expression of the pap1 gene, it was hypothesised that POH1 overexpression could decrease proteasome degradation of AP-1 transcription factors and lead to increased transactivation of AP-1-responsive genes."
PSMD14 affects AGR2
|
5
Capzimin affects PSMD14
|
5
AGR2 affects PSMD14
|
5
Phenanthroline affects PSMD14
|
2
2
PSMD14 affects TNBC
|
4
reach
"Herein, we found that PSMD14 promotes the progression of TNBC by regulating FADS1 through the m A modification pathway mediated by the HNRNPC and SF3B4 complex, which is achieved by deubiquitylation of SF3B4.HNRNPs, a family of multifunctional protein molecules, are the m A reader proteins that were identified to play a crucial role in the m A recognition process by selectively identifying m A-modified mRNA sites (33)."
PSMD14 affects Stomach Neoplasms
|
4
PSMD14 affects Carcinoma, Hepatocellular
|
4
sparser
"Consistent with the fluorescence of PSMD14-YFP, most of the endogenous proteasomes, likely membrane-bound, detected with antibodies against the 19S and 20S proteasomal subunits, also appeared in the middle fractions, with a lesser shift on proteasomal inhibition, in this case with the proteasome inhibitor bortezomib (Bz) ( xref F)."
sparser
"A proteasomal subunit linked to YFP, PSMD14-YFP, was also partially recruited to the ERQC region on proteasomal inhibition ( xref C), similarly to what we had seen with other cytosolic ERAD factors, p97 and SCF Fbs2 . xref , xref PSMD14-YFP even showed a higher presence in the ERQC region than H2a-RFP and CRT-GFP in untreated cells ( xref D and xref )."
reach
"Altogether it is questionable, whether gliotoxin directly inhibits the 20S proteasome or whether the observed inhibition is a secondary effect of for example unspecific protein damage.Only recently, gliotoxin and other ETPs were reported to inhibit Rpn11, a zinc‐dependent deubiquitinating enzyme and an essential component of the 19S regulatory particle of proteasomes responsible for ubiquitin‐mediated protein degradation in cells."
reach
"However, recent studies using the polyubiquitinated protein substrate Ub GST-Wbp2 (WW domain-binding protein 2, n > 30) to measure 26S proteasome-mediated protein degradation have revealed that gliotoxin and other ETPs inhibit proteasome activity in vitro and in cells by targeting the essential deubiquitinase Rpn11 [30,31] in the 19S regulatory complex of the 26S proteasome [111]."
| PMC
PSMD14 affects phospholipid translocation
|
3
PSMD14 inhibits phospholipid translocation.
|
2
PSMD14 inhibits phospholipid translocation. 2 / 2
|
2
reach
"Both single mutants are superficially wild-type and display essentially normal neuronal morphology, validating the approach of screening for suppression of non-neuronal phenotypes as a means to find rare mutations that may not be isolated based on their neuronal phenotypes.PAD-1/Dopey proteins have multiple functions in membrane trafficking: in C. elegans embryos, PAD-1 inhibits the release of ectosome-type EVs from the plasma membrane and promotes phagocytosis of cell corpses and debris by regulating the activity of TAT-5 flippase ."
PSMD14 activates phospholipid translocation.
|
1
PSMD14 activates phospholipid translocation. 1 / 1
|
1
PSMD14 affects osteoclast differentiation
|
1
2
PSMD14 activates osteoclast differentiation. 3 / 3
|
1
2
reach
"As an endopeptidase, RPN11 functions to cleave polyubiquitin chains from substrates [126] While CSN5/Jab1 hydrolyzes the ubiquitin-like modifier Nedd8 [127], POH1 enhances osteoclast differentiation and RANKL signaling via regulating Mitf, an important regulator of osteoclast differentiation which required gene expression [128]."
eidos
"As an endopeptidase , RPN11 functions to cleave polyubiquitin chains from substrates [ 126 ] While CSN5 / Jab1 hydrolyzes the ubiquitin-like modifier Nedd8 [ 127 ] , POH1 enhances osteoclast differentiation and RANKL signaling via regulating Mitf , an important regulator of osteoclast differentiation which required gene expression [ 128 ] ."
sparser
"Consistent with the fluorescence of PSMD14-YFP, most of the endogenous proteasomes, likely membrane-bound, detected with antibodies against the 19S and 20S proteasomal subunits, also appeared in the middle fractions, with a lesser shift on proteasomal inhibition, in this case with the proteasome inhibitor bortezomib (Bz) ( xref F)."
sparser
"A proteasomal subunit linked to YFP, PSMD14-YFP, was also partially recruited to the ERQC region on proteasomal inhibition ( xref C), similarly to what we had seen with other cytosolic ERAD factors, p97 and SCF Fbs2 . xref , xref PSMD14-YFP even showed a higher presence in the ERQC region than H2a-RFP and CRT-GFP in untreated cells ( xref D and xref )."
PSMD14 affects cell differentiation
|
3
PSMD14 deubiquitinates PSMD14.
|
2
PSMD14 increases the amount of PSMD14.
|
1
reach
"CRISPR/Cas9-generated knockout mutations of HBP1, but not POH1 mutations, promoted earlier flowering time; conversely, HBP1 and POH1 overexpression delayed flowering time in rice under long-day and short-day conditions by activating the expression of Hd1 and suppressing the expression of Early heading date 1 (Ehd1), Heading date 3a (Hd3a), and Rice Flowering locus T 1 (RFT1), thus controlling flowering time in rice."
PSMD14 affects HNSCC
|
3
Proteasome subunit affects PSMD14
|
2
sparser
"In HeLa cells, high-glucose treatment facilitated chromatin binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to the negative-control locus GATA1 ( xref ), suggesting that NRF1 contributes to the activation of the proteasome subunit genes when it is accumulated in response to enhanced cellular O -GlcNAcylation."
sparser
"In HeLa cells transfected with control siRNA, as observed in the ChIP-seq analysis, MG132 treatment induced robust binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to a negative-control locus, GATA1 ( xref )."
Cyclic peptide affects PSMD14
|
2
Cyclic peptide inhibits PSMD14. 2 / 2
|
2
reach
"Hence we concluded that among the other members of the UCH family, the cyclic β-sheet peptide 2 inhibits UCH-L5 most efficiently.To further investigate whether the cyclic peptide 2 inhibits the activity of Rpn11, the metalloprotease DUBs found in the 19S cap of the 26S proteasome, we carried out a standard fluorescence polarization assay using a Ubiquitin-Fluorescence Polarization (Ub-FP) substrate containing Ub linked by an isopeptide bond to a TAMRA-labelled Ub peptide, comprising residues 41 to 54 of Ub (Supplementary Figure S3A)."
reach
"We observed that the cyclic peptide, 2, was unable to inhibit Rpn11/Rpn8 activity (Supplementary Figure S3B), potentially suggesting that the Rpn11 activity remains unhindered in cells in the presence of 2.Next, we tested whether our cyclic peptide 2 can compete with the activity-based probe Cy5-UbVME in the labeling of UCH-L5."
Calcium(2+) affects PSMD14
|
2
PSMD14 affects ubiquitination degradation E2F1
|
2
PSMD14 affects translation
|
2
PSMD14 affects such DDB2 immobilization induced proteasome
|
2
|
2
PSMD14 activates response to xenobiotic stimulus. 2 / 2
|
2
reach
"The human POH1 gene encodes for a protein with a high degree of sequence similarity with fission yeast Pad1 (Fig. 2), is a fully functional homologue of Pad1 and induces by overexpression the same phenotype of pleiotropic drug resistance in S. pombe.To assess whether POH1 could be involved in resistance to cytotoxic insults and in particular to anticancer agents in mammalian cells, experiments of POH1 overexpression by transfection in mammalian cells were performed."
PSMD14 affects proteasome subunit
|
2
sparser
"In HeLa cells, high-glucose treatment facilitated chromatin binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to the negative-control locus GATA1 ( xref ), suggesting that NRF1 contributes to the activation of the proteasome subunit genes when it is accumulated in response to enhanced cellular O -GlcNAcylation."
sparser
"In HeLa cells transfected with control siRNA, as observed in the ChIP-seq analysis, MG132 treatment induced robust binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to a negative-control locus, GATA1 ( xref )."
PSMD14 affects proteasome complex disassembly
|
2
PSMD14 inhibits proteasome complex disassembly. 2 / 2
|
2
reach
"Based on the studies in S. pombe, where the Pad1 and POH1 overexpression phenotype was dependent upon the expression of the pap1 gene, it was hypothesised that POH1 overexpression could decrease proteasome degradation of AP-1 transcription factors and lead to increased transactivation of AP-1-responsive genes."
PSMD14 affects pathway
|
2
PSMD14 affects migration
|
2
PSMD14 affects imidazol-4-ylacetic acid
|
2
PSMD14 affects homologous recombination
|
2
PSMD14 affects homeostatic process
|
2
PSMD14 affects calcium(2+)
|
2
reach
"Based on the results obtained from RNAi screening targeting candidates that are present on the list derived from SARS-CoV-2 M IP/MS, we also attempted to identify the proteins that negatively regulate VLP release, especially the deubiquitinating enzyme POH1; knockdown of POH1 increased VLP release (Fig. S1A and Fig. 5A)."
PSMD14 affects SARS-CoV-2
|
2
PSMD14 activates SARS-CoV-2. 2 / 2
|
2
reach
"All together, these data revealed a previously undescribed mechanism by which RNF5 and POH1 mediate the ubiquitin modification of SARS-CoV-2 M for virion trafficking and release.As noted by previous studies, unlike with most enveloped viruses, in which M is necessary and sufficient to mediate VLP release, the E/M proteins of murine hepatitis virus (MHV) or the M/E/N proteins of SARS-CoV are necessary for efficient assembly, trafficking, and VLP release (7–9)."
sparser
"In HeLa cells, high-glucose treatment facilitated chromatin binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to the negative-control locus GATA1 ( xref ), suggesting that NRF1 contributes to the activation of the proteasome subunit genes when it is accumulated in response to enhanced cellular O -GlcNAcylation."
sparser
"In HeLa cells transfected with control siRNA, as observed in the ChIP-seq analysis, MG132 treatment induced robust binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to a negative-control locus, GATA1 ( xref )."
PSMD14 affects PI3K/AKT/mTOR
|
2
PSMD14 affects NSCLS
|
2
sparser
"In HeLa cells, high-glucose treatment facilitated chromatin binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to the negative-control locus GATA1 ( xref ), suggesting that NRF1 contributes to the activation of the proteasome subunit genes when it is accumulated in response to enhanced cellular O -GlcNAcylation."
sparser
"In HeLa cells transfected with control siRNA, as observed in the ChIP-seq analysis, MG132 treatment induced robust binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to a negative-control locus, GATA1 ( xref )."
PSMD14 affects Multiple Myeloma
|
2
reach
"PAD1 interacts with and citrullinates MEK1 to regulate extracellular signal– regulated kinase 1/2– matrix metallopeptidase 2 signaling, thus promoting tumorigenesis.25 Furthermore, accumulating evidences showing that overexpression of PAD2 and PAD4 were detected in a wide range of human malignant cancers,26 and that PAD inhibitors suppress the proliferation of cancer cell lines both in vitro and in vivo,25,27 supports the notion that PADs play important roles in tumorigenesis."
PSMD14 affects Hippo-YAP1
|
2
PSMD11 affects proteasome subunit
|
2
sparser
"In HeLa cells, high-glucose treatment facilitated chromatin binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to the negative-control locus GATA1 ( xref ), suggesting that NRF1 contributes to the activation of the proteasome subunit genes when it is accumulated in response to enhanced cellular O -GlcNAcylation."
sparser
"In HeLa cells transfected with control siRNA, as observed in the ChIP-seq analysis, MG132 treatment induced robust binding of NRF1 to the promoter regions of the representative proteasome subunit genes PSMA5 , PSMD11 , and PSMD14 but not to a negative-control locus, GATA1 ( xref )."
reach
"PAD1 interacts with and citrullinates MEK1 to regulate extracellular signal– regulated kinase 1/2– matrix metallopeptidase 2 signaling, thus promoting tumorigenesis.25 Furthermore, accumulating evidences showing that overexpression of PAD2 and PAD4 were detected in a wide range of human malignant cancers,26 and that PAD inhibitors suppress the proliferation of cancer cell lines both in vitro and in vivo,25,27 supports the notion that PADs play important roles in tumorigenesis."
Glutathione transferase activity affects RPN3
|
1
RPN11 binds PSMD14, glutathione transferase activity, and RPN3. 1 / 1
|
1
Ethionamide affects PSMD14
|
1
Ethionamide inhibits PSMD14. 1 / 1
|
1
reach
"CRISPR/Cas9-generated knockout mutations of HBP1, but not POH1 mutations, promoted earlier flowering time; conversely, HBP1 and POH1 overexpression delayed flowering time in rice under long-day and short-day conditions by activating the expression of Hd1 and suppressing the expression of Early heading date 1 (Ehd1), Heading date 3a (Hd3a), and Rice Flowering locus T 1 (RFT1), thus controlling flowering time in rice."
Arachidonic acid affects PSMD14
|
1
Arachidonic acid inhibits PSMD14. 1 / 1
|
1
TXNL1 affects 19S
|
1
TAT-5 affects PSMD14
|
1
reach
"PAD-1, a C. elegans DOPEY ortholog, also inhibits extracellular vesicles , suggesting a possible functional association between PAD-1 and TAT-5 in this process.Heterozygous mutations in the ATP9A gene have been identified in two families, causing a novel autosomal recessive neurodevelopmental disorder involving postnatal microcephaly , highlighting crucial role of ATP9A in brain development."
RTHF affects PSMD14
|
1
RPN3 affects glutathione transferase activity
|
1
RPN11 binds PSMD14, glutathione transferase activity, and RPN3. 1 / 1
|
1
PSMD7 affects Lys11
|
1
reach
"These observed differences in hydrolysis rates between those reported for individual chains and the ones we found in the mixture containing all linkages may indicate that the presence of certain diUb linkages can lead to a change in hydrolysis rates of other linkages.Another interesting finding is the high preference of the metallo-DUB RPN11/RPN8 complex for Lys11 diUb."
PSMD14 affects release polyubiquitin chain bloc
|
1
PSMD14 affects pro-IL-1β
|
1
|
1
PSMD14 activates post-translational protein modification. 1 / 1
|
1
PSMD14 affects pomalidomide
|
1
PSMD14 inhibits pomalidomide. 1 / 1
|
1
reach
"The first proof that POH1 could be targeted was provided by a group at the Dana Farber Cancer Institute that showed in 2017 that pharmacologic inhibition of POH1 with O-phenanthroline blocked proteasome function, had an anti-myeloma effect in human xenografts and, similarly to proteasome inhibitors in the clinic, was synergistic with the anti-myeloma activity of lenalidomide, pomalidomide and dexametasone [83]."
PSMD14 affects lipid metabolic process
|
1
PSMD14 activates lipid metabolic process. 1 / 1
|
1
reach
"RPN11 deubiquitinates and stabilizes methyltransferase-like 3 (METTL3), promotes m6A modification and the expression of cyl-CoA synthetase short-chain family member 3 (ACSS3), and upregulates lipid metabolism genes through histone propionylation to create propionyl coenzyme A (131)."
|
1
RPN11 binds PSMD14, glutathione transferase activity, and RPN3. 1 / 1
|
1
PSMD14 affects docetaxel anhydrous
|
1
PSMD14 activates docetaxel anhydrous. 1 / 1
|
1
PSMD14 affects decreased sensitivity cytotoxic drugs prognosis
|
1
PSMD14 affects cellular component biogenesis
|
1
PSMD14 inhibits cellular component biogenesis. 1 / 1
|
1
PSMD14 affects auxin homeostasis
|
1
PSMD14 inhibits auxin homeostasis. 1 / 1
|
1
PSMD14 affects autophagy of mitochondrion
|
1
PSMD14 inhibits autophagy of mitochondrion. 1 / 1
|
1
PSMD14 affects arachidonic acid
|
1
PSMD14 increases the amount of arachidonic acid. 1 / 1
|
1
PSMD14 affects apoptosis SCC15 UM1 cells treated CDDP
|
1
PSMD14 affects YAP1-Hippo
|
1
PSMD14 affects TAT-5
|
1
reach
"PAD-1, a C. elegans DOPEY ortholog, also inhibits extracellular vesicles , suggesting a possible functional association between PAD-1 and TAT-5 in this process.Heterozygous mutations in the ATP9A gene have been identified in two families, causing a novel autosomal recessive neurodevelopmental disorder involving postnatal microcephaly , highlighting crucial role of ATP9A in brain development."
PSMD14 affects RPN3
|
1
RPN11 binds PSMD14, glutathione transferase activity, and RPN3. 1 / 1
|
1
PSMD14 affects PABPN1-17ala
|
1
PSMD14 affects NSD2.We
|
1
PSMD14 affects Lys11
|
1
reach
"These observed differences in hydrolysis rates between those reported for individual chains and the ones we found in the mixture containing all linkages may indicate that the presence of certain diUb linkages can lead to a change in hydrolysis rates of other linkages.Another interesting finding is the high preference of the metallo-DUB RPN11/RPN8 complex for Lys11 diUb."
PSMD14 affects HNSCC initiation
|
1
PSMD14 affects E2F1/ERK/AKT
|
1
reach
"To verify the effects of both PSMD11 and PSMD14 in pancreatic cancer, we confirmed that the knockdown of PSMD11 and PSMD14 could inhibit the malignant biological behaviors of pancreatic cancer cells, such as their proliferation, migration, and invasion, via the MTT assay, cell scratch assay, and transwell assay, which suggested that these two proteins could be used as potential markers for pancreatic cancer progression and prognostic assessment."
PSMD14 affects 19S
|
1
NSD2.We affects PSMD14
|
1
Lys11 affects PSMD7
|
1
reach
"These observed differences in hydrolysis rates between those reported for individual chains and the ones we found in the mixture containing all linkages may indicate that the presence of certain diUb linkages can lead to a change in hydrolysis rates of other linkages.Another interesting finding is the high preference of the metallo-DUB RPN11/RPN8 complex for Lys11 diUb."
JAMM motif affects PSMD14
|
1
GSK484 affects PSMD14
|
1
E6 affects PSMA3, PSMB7, PSMB9, PSMC2, PSMC3, PSMC4, PSMD1, PSMD11, PSMD13, PSMD14, PSMD2, PSMD3, PSMD6, PSMD7, PSMD8, PSME4, and oncoprotein
|
1
E6 binds oncoprotein, PSMA3, PSMC2, PSMC3, PSMD1, PSMD2, PSMD3, PSMD14, PSMD11, PSMD7, PSMC4, PSMD13, PSMD6, PSMD8, PSMB7, PSMB9, and PSME4. 1 / 1
|
1
sparser
"These observations were supported by a series of analyses that demonstrated interactions between multiple α-HPV E6 oncoproteins and PSMA3, PSMC2, PSMC3, PSMD1, PSMD2, PSMD3, PSMD14, PSMD11, PSMD7, PSMC4, PSMD13, PSMD6, PSMD8, PSMB7, PSMB9 and PSME4 proteasomal subunits, while a panel of β-HPV E6 oncoproteins interacted only with a few proteasomal subunits, including PSMA3, PSMC2, PSMD1, PSMD2, PSMD3, PSMD11, and PSMD13 [ xref , xref , xref ]."
19S affects TXNL1
|
1