IndraLab
Statements
sparser
"Cys282 is next to the active site, and in fact it makes a van der Waals contact with Leu73 of the distal ubiquitin in the structure of AMSH-LP DUB domain bound to Lys63-linked ubiquitin dimer. xref In the disulfide orientation, however, as seen in the model of AMSH244 bound to Lys63-linked diubiquitin (please see below), the contact is lost."
sparser
"Interestingly, in the structure of AMSH-LP DUB domain bound to Lys63-linked ubiquitin dimer, the corresponding residue pair is still seen in a similar position as the substrate-free form, xref suggesting that these residues close the active site during catalysis as well, perhaps to help position the scissile peptide bond or stabilize the transition state or both."
sparser
"Using the AMSH-LP E292A -ubiquitin complex (PDB ID: 2ZNV) from Homo sapiens as an example, the C-terminal tail of the distal ubiquitin moiety binds the active site cleft and is stabilized with the Ins-1 segment by extensive hydrophobic interactions and hydrogen bonds, thus facilitating a scissile isopeptide bond for hydrolysis ( xref A,C) [ xref ]."
sparser
"The
structure was determined by molecular replacement using a model of
Sst2–K63-Ub 2 generated by superimposition of Sst2 cat with the structure of AMSH-LP bound to K63-Ub 2 (PDB entry 2ZNV( xref )) and refined yielding satisfactory
crystallographic, free R factors and good stereochemistry
(Table xref )."
reach
"Interestingly, Wang et al. reported that gastric cancer and colorectal cancer downregulate an E3 ubiquitin ligase RING finger protein 167 (RNF167) and upregulate a deubiquitinase STAMBPL1 that can prevent the ubiquitination of Sestrin2, decrease Sestrin2-GATOR2 interaction and increase mTORC1 signaling [119]."
sparser
"Cys282 is next to the active site, and in fact it makes a van der Waals contact with Leu73 of the distal ubiquitin in the structure of AMSH-LP DUB domain bound to Lys63-linked ubiquitin dimer. xref In the disulfide orientation, however, as seen in the model of AMSH244 bound to Lys63-linked diubiquitin (please see below), the contact is lost."
sparser
"Interestingly, in the structure of AMSH-LP DUB domain bound to Lys63-linked ubiquitin dimer, the corresponding residue pair is still seen in a similar position as the substrate-free form, xref suggesting that these residues close the active site during catalysis as well, perhaps to help position the scissile peptide bond or stabilize the transition state or both."
sparser
"Using the AMSH-LP E292A -ubiquitin complex (PDB ID: 2ZNV) from Homo sapiens as an example, the C-terminal tail of the distal ubiquitin moiety binds the active site cleft and is stabilized with the Ins-1 segment by extensive hydrophobic interactions and hydrogen bonds, thus facilitating a scissile isopeptide bond for hydrolysis ( xref A,C) [ xref ]."
sparser
"The
structure was determined by molecular replacement using a model of
Sst2–K63-Ub 2 generated by superimposition of Sst2 cat with the structure of AMSH-LP bound to K63-Ub 2 (PDB entry 2ZNV( xref )) and refined yielding satisfactory
crystallographic, free R factors and good stereochemistry
(Table xref )."
STAMBPL1 affects apoptotic process
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STAMBPL1 inhibits apoptotic process.
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STAMBPL1 inhibits apoptotic process. 10 / 16
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reach
"We designed experiments to show that the percentage of apoptotic cells in A549 STAMBPL1 SI group (4.89% ± 0.33%, p<0.05) and H1299 STAMBPL1 SI (9.18% ± 0.51%, p<0.001) group increased significantly compared with A549 STAMBPL1 NC group (3.33% ± 0.41%) and H1299 STAMBPL1 NC group (2.91% ± 0.24%) (Fig. 2G, p<0.05, p<0.001), which proved that STAMBPL1 could reduce apoptosis of LUAD cells."
STAMBPL1 activates apoptotic process.
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STAMBPL1 activates apoptotic process. 4 / 4
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reach
"Recent studies have shown that excessive ROS generated in H. pylori infection induces direct degradation of STAMBPL1 by cullin 1-RING ubiquitin ligase and the 26S proteasome, while STAMBPL1 can lead to cell apoptosis by reducing the anti-apoptotic protein survivin (Chaithongyot and Naumann, 2022)."
reach
"Recent studies have shown that excessive ROS generated in H. pylori infection induces direct degradation of STAMBPL1 by cullin 1-RING ubiquitin ligase and the 26S proteasome, while STAMBPL1 can lead to cell apoptosis by reducing the anti-apoptotic protein survivin (Chaithongyot and Naumann, 2022)."
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STAMBPL1 activates cell population proliferation.
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STAMBPL1 activates cell population proliferation. 10 / 10
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reach
"These findings highlight the diverse roles that deubiquitinases play in HCC, either by promoting or suppressing the disease, and suggest that they could be potential targets for therapeutic intervention in HCC.In the study, we identified one oncogene gene (STAMBPL1) which promote the proliferation and metastasis of HCC."
reach
"Following STAMBPL1 knockdown by short hairpin RNA (sh)STAMBPL1, cell proliferation was significantly suppressed, the cell apoptosis rate was significantly upregulated, and the numbers of invasive AGS cells and the AGS wound healing rate were significantly decreased (P<0.01 and P<0.001, respectively), compared with those in the shControl group."
STAMBPL1 inhibits cell population proliferation.
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reach
"Our study reveals for the first time that GRHL3 promotes transcriptional activity by binding to the promoter of the HIF1A gene.In this study, we utilized two TNBC cell lines, HCC1806 and HCC1937, along with human primary umbilical vein endothelial cells (HUVECs) and a nude mouse breast orthotopic transplantation tumor model to investigate the regulatory mechanism by which STAMBPL1 activates the GRHL3/HIF1α/VEGFA signaling pathway through its interaction with FOXO1, thereby promoting angiogenesis in TNBC."
sparser
"How JAMM/MPNDUBs cleave ubiquitin chains with K63-linkage specificity has been explained by the crystal structure of AMSH-LP bound to K63-linked di-ubiquitin: Two insertion loops orient the distal and proximal ubiquitin in order to place the isopeptide bond at lysine 63 in direct proximity to the active site [ xref ]."
sparser
"Only recently was Lys63-linkage specificity understood from the structural analysis of the DUB domain of AMSH-LP bound Lys63-linked diubiquitin. xref This structure reveals interactions between the enzyme and both the distal and proximal ubiquitins, but the basis for specificity arises from residues in the proximal site of the enzyme interacting with the proximal ubiquitin, despite a more extensive interaction with the distal ubiquitin (a significantly more accessible surface area is buried upon interaction with distal than proximal ubiquitin). xref Overall, AMSH adopts very similar interactions when modeled according to the ubiquitin-bound structure of AMSH-LP."
sparser
"However, this
residue, in fact, the two-residue turn segment, Leu402-Phe403, needs
to move apart relative to Thr316 to make room for the diubiquitin
substrate to position itself correctly in the active site. (These
observations are also true in the structure of AMSH-LP bound to diubiquitin.)
It seems likely that the β-turn segment is dynamic, fluctuating
between open and closed forms; the substrate binds to the open form,
perhaps by conformational selection."
sparser
"Modeling of the catalytic domain of AMSH onto the structure of AMSH-LP bound to Lys63-linked diubiquitin revealed four residues within AMSH (Thr341, Phe343, Ser346, and Phe395) that could determine its specificity for Lys63-linked polyubiquitin chains by recognizing the tri-peptide sequence motif Gln62-Lys63-Glu64 within the proximal ubiquitin, which encompasses the acceptor Lys63 and its two immediate flanking residues."
reach
"X-ray crystal structures of the DUB domains of both AMSH-LP and Sst2 bound to diubiquitin shows Phe403 collapsed onto the Lys63 side chain of the proximal ubiquitin; however, the flap residues appear to retain their mobility even in presence of bound substrate or product (indicated by relatively weak electron density enveloping these residues and higher B-factors than internal residues)."
TBMS-1 affects STAMBPL1
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reach
"Interestingly, Wang et al. reported that gastric cancer and colorectal cancer downregulate an E3 ubiquitin ligase RING finger protein 167 (RNF167) and upregulate a deubiquitinase STAMBPL1 that can prevent the ubiquitination of Sestrin2, decrease Sestrin2-GATOR2 interaction and increase mTORC1 signaling [119]."
reach
"Our study reveals for the first time that GRHL3 promotes transcriptional activity by binding to the promoter of the HIF1A gene.In this study, we utilized two TNBC cell lines, HCC1806 and HCC1937, along with human primary umbilical vein endothelial cells (HUVECs) and a nude mouse breast orthotopic transplantation tumor model to investigate the regulatory mechanism by which STAMBPL1 activates the GRHL3/HIF1α/VEGFA signaling pathway through its interaction with FOXO1, thereby promoting angiogenesis in TNBC."
reach
"By downregulating the level of Ubiquitin using RNA interference-mediated knockdown of Ubb and Ubc, we found that knockdown of UbC that instructs tandem units of ubiquitin with nine repeats resulted in more efficient attenuation of both K48 and total and mono-Ub levels without affecting STAMBPL1 levels (Supplementary Fig. S3e) and that downregulation of UbC effectively hindered STAMBPL1-mediated Snail protein reduction (Fig. 4i)."
STAMBPL1 affects angiogenesis
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sparser
"DUBs employ diverse mechanisms and modes of interaction with their substrates to mediate the removal of mono‐ubiquitin or poly‐ubiquitin chains from the target protein. [ xref ] To ascertain the direct interaction between STAMBPL1 and AXL, Immunoprecipitation (IP) and in vitro pull‐down assays were performed."
sparser
"The
structure was determined by molecular replacement using a model of
Sst2–K63-Ub 2 generated by superimposition of Sst2 cat with the structure of AMSH-LP bound to K63-Ub 2 (PDB entry 2ZNV( xref )) and refined yielding satisfactory
crystallographic, free R factors and good stereochemistry
(Table xref )."
STAMBPL1 affects cell growth
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STAMBPL1 activates cell growth.
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STAMBPL1 inhibits cell growth.
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STAMBPL1 inhibits cell growth. 1 / 1
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STAMBPL1 affects K63-Ub 2
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sparser
"The
structure was determined by molecular replacement using a model of
Sst2–K63-Ub 2 generated by superimposition of Sst2 cat with the structure of AMSH-LP bound to K63-Ub 2 (PDB entry 2ZNV( xref )) and refined yielding satisfactory
crystallographic, free R factors and good stereochemistry
(Table xref )."
reach
"These findings highlight the diverse roles that deubiquitinases play in HCC, either by promoting or suppressing the disease, and suggest that they could be potential targets for therapeutic intervention in HCC.In the study, we identified one oncogene gene (STAMBPL1) which promote the proliferation and metastasis of HCC."
sparser
"The Fisher exact test showed that seven fusion genes— MAN2A1–FER ( P = 1.4 × 10 −19 ), CCNH–C5orf30 ( P = 1.1 × 10 −5 ), SLC45A2–AMACR ( P = 2.8 × 10 −9 ), ZMPSTE24–ZMYM4 ( P = 9.3 × 10 −6 ), PTEN–NOLC1 ( P = 1.8 × 10 −6 ), PCMTD1–SNTG1 ( P = 0.006), and STAMBPL1–FAS ( P = 0.01)—had significantly greater frequencies of expression in the serum samples of patients with HCC, suggesting that the detection of these fusion transcripts in the serum samples of patients with HCC likely predicts the risk for HCC."
sparser
"DUBs employ diverse mechanisms and modes of interaction with their substrates to mediate the removal of mono‐ubiquitin or poly‐ubiquitin chains from the target protein. [ xref ] To ascertain the direct interaction between STAMBPL1 and AXL, Immunoprecipitation (IP) and in vitro pull‐down assays were performed."
K63-Ub 2 affects STAMBPL1
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sparser
"The
structure was determined by molecular replacement using a model of
Sst2–K63-Ub 2 generated by superimposition of Sst2 cat with the structure of AMSH-LP bound to K63-Ub 2 (PDB entry 2ZNV( xref )) and refined yielding satisfactory
crystallographic, free R factors and good stereochemistry
(Table xref )."
sparser
"The Fisher exact test showed that seven fusion genes— MAN2A1–FER ( P = 1.4 × 10 −19 ), CCNH–C5orf30 ( P = 1.1 × 10 −5 ), SLC45A2–AMACR ( P = 2.8 × 10 −9 ), ZMPSTE24–ZMYM4 ( P = 9.3 × 10 −6 ), PTEN–NOLC1 ( P = 1.8 × 10 −6 ), PCMTD1–SNTG1 ( P = 0.006), and STAMBPL1–FAS ( P = 0.01)—had significantly greater frequencies of expression in the serum samples of patients with HCC, suggesting that the detection of these fusion transcripts in the serum samples of patients with HCC likely predicts the risk for HCC."
STAMBPL1 affects cell death
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STAMBPL1 inhibits cell death.
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STAMBPL1 activates cell death.
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STAMBPL1 affects Neoplasm Metastasis
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STAMBPL1 activates Neoplasm Metastasis. 4 / 4
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"These findings highlight the diverse roles that deubiquitinases play in HCC, either by promoting or suppressing the disease, and suggest that they could be potential targets for therapeutic intervention in HCC.In the study, we identified one oncogene gene (STAMBPL1) which promote the proliferation and metastasis of HCC."
STAMBPL1 affects Neoplasm Invasiveness
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STAMBPL1 activates Neoplasm Invasiveness.
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STAMBPL1 inhibits Neoplasm Invasiveness.
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STAMBPL1 inhibits Neoplasm Invasiveness. 1 / 1
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reach
"Besides, we found that the expression of DHRS2 in the primary tumor was lower than in normal samples in the TCGA-LUAD database (Fig. 3E), while the expression of STAMBPL1 in the primary tumor was higher than in normal samples (Fig. 3F), so we carried out the hypothesis that STAMBPL1 promotes the progression of lung adenocarcinoma by inhibiting DHRS2 expression."
sparser
"The
structure was determined by molecular replacement using a model of
Sst2–K63-Ub 2 generated by superimposition of Sst2 cat with the structure of AMSH-LP bound to K63-Ub 2 (PDB entry 2ZNV( xref )) and refined yielding satisfactory
crystallographic, free R factors and good stereochemistry
(Table xref )."
sparser
"Thus, the mechanism by which mutant p53 might activate STAMBPL1 is therefore likely through its interaction with these TFs, which possess responsive to mutant p53. xref – xref Although future studies are needed to delineate whether other DUBs are involved in mutant p53-induced EMT or to other mutant p53-mediated oncogenic pro-survival benefits (ref. xref , xref ), our findings suggest an involvement of mutant p53 in driving the expression of STAMBPL1 as a novel pro-EMT GOF, providing further rationale to investigate DUB expression by other oncoproteins."
reach
"While ChIP assay revealed p53 enrichment on MDM2 and CDKN1A promoters in p53 -expressing cells (up to ~4% and ~10% of input), no significant (>1%) occupancy on any of the six predicted was detected for either WT or p53 (Supplementary Fig. S5c), indicating that the expression of STAMBPL1 gene is not directly regulated by p53 ."
sparser
"Indeed, endogenous binding between STAMBPL1 and AXL was observed in multiple KIRC cell lines (786‐O, 769‐P and Caki‐1), and the glutathione S‐transferase (GST) pull‐down experiments showed that AXL interacted with purified GST‐STAMBPL1, but not GST alone ( Figure xref ; Figure xref , Supporting Information)."
sparser
"Indeed, endogenous binding between STAMBPL1 and AXL was observed in multiple KIRC cell lines (786‐O, 769‐P and Caki‐1), and the glutathione S‐transferase (GST) pull‐down experiments showed that AXL interacted with purified GST‐STAMBPL1, but not GST alone ( Figure xref ; Figure xref , Supporting Information)."
STAMBPL1 affects signal transduction
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STAMBPL1 activates signal transduction. 2 / 2
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reach
"Our study reveals for the first time that GRHL3 promotes transcriptional activity by binding to the promoter of the HIF1A gene.In this study, we utilized two TNBC cell lines, HCC1806 and HCC1937, along with human primary umbilical vein endothelial cells (HUVECs) and a nude mouse breast orthotopic transplantation tumor model to investigate the regulatory mechanism by which STAMBPL1 activates the GRHL3/HIF1α/VEGFA signaling pathway through its interaction with FOXO1, thereby promoting angiogenesis in TNBC."
STAMBPL1 affects cell migration
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STAMBPL1 affects TNBC
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STAMBPL1 affects Cell Survival
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STAMBPL1 activates Cell Survival. 2 / 2
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STAMBPL1 affects Carcinoma, Hepatocellular
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STAMBPL1 inhibits Carcinoma, Hepatocellular.
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STAMBPL1 inhibits Carcinoma, Hepatocellular. 1 / 1
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STAMBPL1 activates Carcinoma, Hepatocellular.
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STAMBPL1 activates Carcinoma, Hepatocellular. 1 / 1
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Reactive Oxygen Species affects STAMBPL1
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Reactive Oxygen Species inhibits STAMBPL1. 2 / 2
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reach
"Recent studies have shown that excessive ROS generated in H. pylori infection induces direct degradation of STAMBPL1 by cullin 1-RING ubiquitin ligase and the 26S proteasome, while STAMBPL1 can lead to cell apoptosis by reducing the anti-apoptotic protein survivin (Chaithongyot and Naumann, 2022)."
STAMBPL1 is modified
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Neoplasm Invasiveness affects STAMBPL1
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Neoplasm Invasiveness decreases the amount of STAMBPL1.
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Neoplasm Invasiveness decreases the amount of STAMBPL1. 1 / 1
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Neoplasm Invasiveness activates STAMBPL1.
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Neoplasm Invasiveness activates STAMBPL1. 1 / 1
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ShSTAMBPL1 affects STAMBPL1
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ShSTAMBPL1#2 affects STAMBPL1
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ShSTAMBPL1#1 affects STAMBPL1
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Rpn11 affects Ubiquitin
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Polyubiquitin affects STAMBPL1
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Patch affects Ubiquitin
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Ectopic following affects STAMBPL1
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eidos
"A 137 number of novel host factors have been confirmed to facilitate SARS-CoV-2 pseudovirus entry ,138 151HEK293T cells , besides ACE2 and CTSL , the ectopic expression of any of the following genes could 152 effectively enable SARS-CoV-2 infection , CLEC4G , CPLX1 , LDLRAD3 , TMEM30A , and STAMBPL1 153 ( Fig. 3B ) ."
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DiUb affects STAMBPL1
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Cepharanthine affects STAMBPL1
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Cepharanthine inhibits STAMBPL1. 1 / 1
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Ubiquitin affects rpn11
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Ubiquitin affects patch
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UbV affects STAMBPL1
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reach
"A strong hydrogen bond network is then formed between the Arg72 guanidinium and the backbone carbonyl group of Glu326 in ins-1 and between the amide group of Gln49 of UbV with the backbone carbonyl and amide of Val328 and Glu326, thus stabilizing the interaction between the STAMBPL1 and UbV (Fig. 2G)."
UbV SP.1 affects STAMBPL1
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UBD affects Phe403
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reach
"X-ray crystal structures of the DUB domains of both AMSH-LP and Sst2 bound to diubiquitin shows Phe403 collapsed onto the Lys63 side chain of the proximal ubiquitin; however, the flap residues appear to retain their mobility even in presence of bound substrate or product (indicated by relatively weak electron density enveloping these residues and higher B-factors than internal residues)."
TBMS-1- affects STAMBPL1
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STAMBPL1 affects survivin c-FLIP protein
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STAMBPL1 affects sensitization
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STAMBPL1 activates sensitization. 1 / 1
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STAMBPL1 affects rpn11
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STAMBPL1 affects polyubiquitin
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STAMBPL1 affects pathway
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STAMBPL1 affects patch
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STAMBPL1 affects messenger RNA
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STAMBPL1 increases the amount of messenger RNA. 1 / 1
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STAMBPL1 affects ferroptosis
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STAMBPL1 inhibits ferroptosis. 1 / 1
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STAMBPL1 activates epithelial to mesenchymal transition. 1 / 1
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STAMBPL1 affects diUb
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STAMBPL1 affects cepharanthine-mediated survivin
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STAMBPL1 affects breast cancer cell resistance cisplatin
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STAMBPL1 affects Wnt/β-catenin
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STAMBPL1 affects WNT/PI3K/NF-kb
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STAMBPL1 affects UbV
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reach
"A strong hydrogen bond network is then formed between the Arg72 guanidinium and the backbone carbonyl group of Glu326 in ins-1 and between the amide group of Gln49 of UbV with the backbone carbonyl and amide of Val328 and Glu326, thus stabilizing the interaction between the STAMBPL1 and UbV (Fig. 2G)."
STAMBPL1 affects Sestrin2-GATOR2
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reach
"Interestingly, Wang et al. reported that gastric cancer and colorectal cancer downregulate an E3 ubiquitin ligase RING finger protein 167 (RNF167) and upregulate a deubiquitinase STAMBPL1 that can prevent the ubiquitination of Sestrin2, decrease Sestrin2-GATOR2 interaction and increase mTORC1 signaling [119]."
reach
"We further constructed stable STAMBPL1 over-expressed cells (including HCCLM3 and Hep3B), and the efficiency of overexpression STAMBPL1 were examined by qRT-PCR and WB, the results showed that overexpression STAMBPL1 can upregulate the STAMBPL1 expression in HCCLM3 cells and Hep3B cells (Fig. 4A–D)."
sparser
"While our study highlights and connect three key signalling pathways: mutant p53, EMT and DUBs, showing that STAMBPL1 is transcriptionally elevated in mutant p53-expressing cells, STAMBPL1 seems not to be under a direct regulation by p53 R175H . However, out of the known TFs that help recruit mutant p53 to the chromatin to upregulate genes, xref we found that E2F2, E2F6, MAFF and SP1 can bind to the core promoter region of STAMBPL1 by their motif search using Eukaryotic promoter database."
STAMBPL1 affects S7B
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STAMBPL1 affects Phe403
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reach
"X-ray crystal structures of the DUB domains of both AMSH-LP and Sst2 bound to diubiquitin shows Phe403 collapsed onto the Lys63 side chain of the proximal ubiquitin; however, the flap residues appear to retain their mobility even in presence of bound substrate or product (indicated by relatively weak electron density enveloping these residues and higher B-factors than internal residues)."
STAMBPL1 affects NSCLC
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sparser
"While our study highlights and connect three key signalling pathways: mutant p53, EMT and DUBs, showing that STAMBPL1 is transcriptionally elevated in mutant p53-expressing cells, STAMBPL1 seems not to be under a direct regulation by p53 R175H . However, out of the known TFs that help recruit mutant p53 to the chromatin to upregulate genes, xref we found that E2F2, E2F6, MAFF and SP1 can bind to the core promoter region of STAMBPL1 by their motif search using Eukaryotic promoter database."
STAMBPL1 affects Lys63-Ub 2
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STAMBPL1 affects Liu et al., 2022
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STAMBPL1 affects LUAD
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sparser
"The Flag-STAMBPL1 plasmid were well constructed and transferred to HCCLM3 and Hep3B cell, including (Control, Flag-STAMBPL1-2ug, Flag-STAMBPL1-3ug, Flag-STAMBPL1-4ug), The findings indicated that elevated STAMBPL1 levels led to a decrease in the ubiquitination levels of TRAF2 in both HCCLM3 and Hep3B cells (Fig. xref A, B)."
sparser
"While our study highlights and connect three key signalling pathways: mutant p53, EMT and DUBs, showing that STAMBPL1 is transcriptionally elevated in mutant p53-expressing cells, STAMBPL1 seems not to be under a direct regulation by p53 R175H . However, out of the known TFs that help recruit mutant p53 to the chromatin to upregulate genes, xref we found that E2F2, E2F6, MAFF and SP1 can bind to the core promoter region of STAMBPL1 by their motif search using Eukaryotic promoter database."
STAMBPL1 affects Deubiquitinase
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STAMBPL1 deubiquitinates Deubiquitinase on K63. 1 / 1
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STAMBPL1 affects DUB domain
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STAMBPL1 affects DNA-templated transcription
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STAMBPL1 inhibits DNA-templated transcription. 1 / 1
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sparser
"Furthermore, by transcriptomic analysis we were able to identify 10 fusions compatible with inter-chromosomal translocations not previously showed by conventional methods ( PAX5::POM121C, IK::FBXW2, ZNF444::HLA-B, NFX1::DICER1, DCAF8::ZNF836, DMD::STAMBPL1, SLFNL1::SMPD2, RP11-148O21.2::ATG4B, TMEM263::CD47,INPP5A::SETD7 ) and 6 intra-chromosomal events involving distant genes ( NUP214::ABL1, MAEA::CTBP1, ZC3H12D::RP11-445F6.2, MAML2::FAT3, MNT::CLUH, TSKS::ARRDC2 ) ( xref )."
STAMBPL1 affects Cholangiocarcinoma
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STAMBPL1 activates Cholangiocarcinoma. 1 / 1
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STAMBPL1 activates Carcinoma, Non-Small-Cell Lung. 1 / 1
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STAMBPL1 affects Carcinogenesis
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STAMBPL1 activates Carcinogenesis. 1 / 1
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reach
"Recent studies have shown that excessive ROS generated in H. pylori infection induces direct degradation of STAMBPL1 by cullin 1-RING ubiquitin ligase and the 26S proteasome, while STAMBPL1 can lead to cell apoptosis by reducing the anti-apoptotic protein survivin (Chaithongyot and Naumann, 2022)."
STAMBPL1 affects Adenocarcinoma of Lung
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STAMBPL1 activates Adenocarcinoma of Lung. 1 / 1
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sparser
"While our study highlights and connect three key signalling pathways: mutant p53, EMT and DUBs, showing that STAMBPL1 is transcriptionally elevated in mutant p53-expressing cells, STAMBPL1 seems not to be under a direct regulation by p53 R175H . However, out of the known TFs that help recruit mutant p53 to the chromatin to upregulate genes, xref we found that E2F2, E2F6, MAFF and SP1 can bind to the core promoter region of STAMBPL1 by their motif search using Eukaryotic promoter database."
SNP rs2862833 affects STAMBPL1
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Phe403 affects UBD
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reach
"X-ray crystal structures of the DUB domains of both AMSH-LP and Sst2 bound to diubiquitin shows Phe403 collapsed onto the Lys63 side chain of the proximal ubiquitin; however, the flap residues appear to retain their mobility even in presence of bound substrate or product (indicated by relatively weak electron density enveloping these residues and higher B-factors than internal residues)."
Neoplasm Metastasis affects STAMBPL1
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Neoplasm Metastasis decreases the amount of STAMBPL1. 1 / 1
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sparser
"While our study highlights and connect three key signalling pathways: mutant p53, EMT and DUBs, showing that STAMBPL1 is transcriptionally elevated in mutant p53-expressing cells, STAMBPL1 seems not to be under a direct regulation by p53 R175H . However, out of the known TFs that help recruit mutant p53 to the chromatin to upregulate genes, xref we found that E2F2, E2F6, MAFF and SP1 can bind to the core promoter region of STAMBPL1 by their motif search using Eukaryotic promoter database."
Lys63-Ub 2 affects STAMBPL1
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K63-Ub 2 affects DUB domain
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reach
"Consistent with the effect of GSK-3 inhibition to stimulate the transcription of Snail, in this study, we show that GSK-3α/β inhibition can induce a significant STAMBPL1 expression in all cell lines tested, signifying that this stimulation is able to trigger similar STAMBPL1 molecular response in several cell and cancer types and suggest that GSK-3α/β inhibition may converge upon common signalling element in multiple carcinomas to activate STAMBPL1."
sparser
"The Flag-STAMBPL1 plasmid were well constructed and transferred to HCCLM3 and Hep3B cell, including (Control, Flag-STAMBPL1-2ug, Flag-STAMBPL1-3ug, Flag-STAMBPL1-4ug), The findings indicated that elevated STAMBPL1 levels led to a decrease in the ubiquitination levels of TRAF2 in both HCCLM3 and Hep3B cells (Fig. xref A, B)."
sparser
"While our study highlights and connect three key signalling pathways: mutant p53, EMT and DUBs, showing that STAMBPL1 is transcriptionally elevated in mutant p53-expressing cells, STAMBPL1 seems not to be under a direct regulation by p53 R175H . However, out of the known TFs that help recruit mutant p53 to the chromatin to upregulate genes, xref we found that E2F2, E2F6, MAFF and SP1 can bind to the core promoter region of STAMBPL1 by their motif search using Eukaryotic promoter database."
DUB domain affects STAMBPL1
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sparser
"Furthermore, by transcriptomic analysis we were able to identify 10 fusions compatible with inter-chromosomal translocations not previously showed by conventional methods ( PAX5::POM121C, IK::FBXW2, ZNF444::HLA-B, NFX1::DICER1, DCAF8::ZNF836, DMD::STAMBPL1, SLFNL1::SMPD2, RP11-148O21.2::ATG4B, TMEM263::CD47,INPP5A::SETD7 ) and 6 intra-chromosomal events involving distant genes ( NUP214::ABL1, MAEA::CTBP1, ZC3H12D::RP11-445F6.2, MAML2::FAT3, MNT::CLUH, TSKS::ARRDC2 ) ( xref )."