| + |
UBE3A | down-regulates quantity by destabilization 
polyubiquitination
|
PSMD4 |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272743 |
Lys122 |
SPVEDNEkDLVKLAK |
in vitro |
|
| pmid |
sentence |
| 19240029 |
S5a/Rpn10 is a ubiquitin (Ub)-binding protein that is a subunit of the 26S proteasome but also exists free in the cytosol. It binds poly-Ub chains through its two Ub-interacting motifs (UIMs). We discovered that, unlike typical substrates of Ub ligases (E3s), S5a can be ubiquitinated by all E3s tested including multimeric and monomeric Ring finger E3s (MuRF1, Siah2, Parkin, APC, and SCF(betaTRCP1)), the U-box E3, CHIP, and HECT domain E3s (E6AP and Nedd4) when assayed with UbcH5 or related Ub-conjugating enzymes.The short half-life of S5a presumably is because of the presence of the UIM domain and reflects the ubiquitination of free S5a by many E3s. Surprisingly, the same four Lys residues on S5a, Lys-74, Lys-122, Lys-262, and Lys-365 were ubiquitinated by MuRF1 and E6AP (Fig. 10). Two additional Lys residues (Lys-126 and -135) were ubiquitinated by E6AP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272746 |
Lys126 |
DNEKDLVkLAKRLKK |
in vitro |
|
| pmid |
sentence |
| 19240029 |
S5a/Rpn10 is a ubiquitin (Ub)-binding protein that is a subunit of the 26S proteasome but also exists free in the cytosol. It binds poly-Ub chains through its two Ub-interacting motifs (UIMs). We discovered that, unlike typical substrates of Ub ligases (E3s), S5a can be ubiquitinated by all E3s tested including multimeric and monomeric Ring finger E3s (MuRF1, Siah2, Parkin, APC, and SCF(betaTRCP1)), the U-box E3, CHIP, and HECT domain E3s (E6AP and Nedd4) when assayed with UbcH5 or related Ub-conjugating enzymes.The short half-life of S5a presumably is because of the presence of the UIM domain and reflects the ubiquitination of free S5a by many E3s. Surprisingly, the same four Lys residues on S5a, Lys-74, Lys-122, Lys-262, and Lys-365 were ubiquitinated by MuRF1 and E6AP (Fig. 10). Two additional Lys residues (Lys-126 and -135) were ubiquitinated by E6AP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272747 |
Lys135 |
AKRLKKEkVNVDIIN |
in vitro |
|
| pmid |
sentence |
| 19240029 |
S5a/Rpn10 is a ubiquitin (Ub)-binding protein that is a subunit of the 26S proteasome but also exists free in the cytosol. It binds poly-Ub chains through its two Ub-interacting motifs (UIMs). We discovered that, unlike typical substrates of Ub ligases (E3s), S5a can be ubiquitinated by all E3s tested including multimeric and monomeric Ring finger E3s (MuRF1, Siah2, Parkin, APC, and SCF(betaTRCP1)), the U-box E3, CHIP, and HECT domain E3s (E6AP and Nedd4) when assayed with UbcH5 or related Ub-conjugating enzymes.The short half-life of S5a presumably is because of the presence of the UIM domain and reflects the ubiquitination of free S5a by many E3s. Surprisingly, the same four Lys residues on S5a, Lys-74, Lys-122, Lys-262, and Lys-365 were ubiquitinated by MuRF1 and E6AP (Fig. 10). Two additional Lys residues (Lys-126 and -135) were ubiquitinated by E6AP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272744 |
Lys262 |
DSDDALLkMTISQQE |
in vitro |
|
| pmid |
sentence |
| 19240029 |
S5a/Rpn10 is a ubiquitin (Ub)-binding protein that is a subunit of the 26S proteasome but also exists free in the cytosol. It binds poly-Ub chains through its two Ub-interacting motifs (UIMs). We discovered that, unlike typical substrates of Ub ligases (E3s), S5a can be ubiquitinated by all E3s tested including multimeric and monomeric Ring finger E3s (MuRF1, Siah2, Parkin, APC, and SCF(betaTRCP1)), the U-box E3, CHIP, and HECT domain E3s (E6AP and Nedd4) when assayed with UbcH5 or related Ub-conjugating enzymes.The short half-life of S5a presumably is because of the presence of the UIM domain and reflects the ubiquitination of free S5a by many E3s. Surprisingly, the same four Lys residues on S5a, Lys-74, Lys-122, Lys-262, and Lys-365 were ubiquitinated by MuRF1 and E6AP (Fig. 10). Two additional Lys residues (Lys-126 and -135) were ubiquitinated by E6AP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272745 |
Lys365 |
SLASQATkDGKKDKK |
in vitro |
|
| pmid |
sentence |
| 19240029 |
S5a/Rpn10 is a ubiquitin (Ub)-binding protein that is a subunit of the 26S proteasome but also exists free in the cytosol. It binds poly-Ub chains through its two Ub-interacting motifs (UIMs). We discovered that, unlike typical substrates of Ub ligases (E3s), S5a can be ubiquitinated by all E3s tested including multimeric and monomeric Ring finger E3s (MuRF1, Siah2, Parkin, APC, and SCF(betaTRCP1)), the U-box E3, CHIP, and HECT domain E3s (E6AP and Nedd4) when assayed with UbcH5 or related Ub-conjugating enzymes.The short half-life of S5a presumably is because of the presence of the UIM domain and reflects the ubiquitination of free S5a by many E3s. Surprisingly, the same four Lys residues on S5a, Lys-74, Lys-122, Lys-262, and Lys-365 were ubiquitinated by MuRF1 and E6AP (Fig. 10). Two additional Lys residues (Lys-126 and -135) were ubiquitinated by E6AP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272742 |
Lys74 |
DTGRILSkLHTVQPK |
in vitro |
|
| pmid |
sentence |
| 19240029 |
S5a/Rpn10 is a ubiquitin (Ub)-binding protein that is a subunit of the 26S proteasome but also exists free in the cytosol. It binds poly-Ub chains through its two Ub-interacting motifs (UIMs). We discovered that, unlike typical substrates of Ub ligases (E3s), S5a can be ubiquitinated by all E3s tested including multimeric and monomeric Ring finger E3s (MuRF1, Siah2, Parkin, APC, and SCF(betaTRCP1)), the U-box E3, CHIP, and HECT domain E3s (E6AP and Nedd4) when assayed with UbcH5 or related Ub-conjugating enzymes.The short half-life of S5a presumably is because of the presence of the UIM domain and reflects the ubiquitination of free S5a by many E3s. Surprisingly, the same four Lys residues on S5a, Lys-74, Lys-122, Lys-262, and Lys-365 were ubiquitinated by MuRF1 and E6AP (Fig. 10). Two additional Lys residues (Lys-126 and -135) were ubiquitinated by E6AP. |
|
| Publications: |
6 |
Organism: |
In Vitro |
| + |
PRKACA | down-regulates activity
phosphorylation
|
UBE3A |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236899 |
Thr508 |
MYSERRItVLYSLVQ |
Mus musculus |
|
| pmid |
sentence |
| 26255772 |
These data suggest that PKA phosphorylation at T485 inhibits UBE3A ubiquitin ligase activity in cells. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
ABL1 | down-regulates activity
phosphorylation
|
UBE3A |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260930 |
Tyr659 |
GDSHPVLyQSLKDLL |
Homo sapiens |
|
| pmid |
sentence |
| 23581475 |
Our results suggest that c-Abl protects p53 from HPV-E6-E6AP complex-mediated degradation by phosphorylating E6AP and impairing its E3 ligase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates activity
ubiquitination
|
26S Proteasome |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270339 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28559284 |
Through quantitative proteomics and reporter assays, we found that the UBE3AT485A protein ubiquitinates multiple proteasome subunits, reduces proteasome subunit abundance and activity, stabilizes nuclear β-catenin, and stimulates canonical Wnt signaling more effectively than wild-type UBE3A |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270946 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28559284 |
Through quantitative proteomics and reporter assays, we found that the UBE3AT485A protein ubiquitinates multiple proteasome subunits, reduces proteasome subunit abundance and activity, stabilizes nuclear β-catenin, and stimulates canonical Wnt signaling more effectively than wild-type UBE3A |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
SOX9 |
0.264 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272134 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24155239 |
We show that E6-AP ubiquitinates SOX9 in vitro and in vivo and that SOX9 levels are enhanced after addition of the proteasome inhibitor bortezomib. Similar, siRNA knockdown of E6-AP and the E2 ligase Ubc9 increased cellular SOX9 amounts, supporting the notion that SOX9 may be ubiquitinated in hypertrophic chondrocytes by E6-AP and degraded by proteasomes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
ALDH1A2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265135 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 29076503 |
Hyperactivity of E3 ubiquitin (Ub) ligase UBE3A, stemming from 15q11-q13 copy number variations, accounts for 1%-3% of ASD cases worldwide, but the underlying mechanisms remain incompletely characterized. Here we report that the functionality of ALDH1A2, the rate-limiting enzyme of retinoic acid (RA) synthesis, is negatively regulated by UBE3A in a ubiquitylation-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
NELFCD |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271404 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17131388 |
In this paper, we identify here trihydrophobin 1 (TH1), an integral subunit of the human negative transcription elongation factor (NELF) complex, as a novel E6-AP interaction protein and a target of E6-AP-mediated degradation. Overexpression of E6-AP results in degradation of TH1 in a dose-dependent manner, whereas knock-down of endogenous E6-AP elevates the TH1 protein level. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
PSMC2 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265132 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28559284 |
Our experiments collectively suggest that UBE3A stimulates Wnt pathway activation by interacting with, ubiquitinating, and reducing the levels of multiple (PSMB1, PSMC2, PSMD2, and PSMD7) proteasome subunits. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
UBE3A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271398 |
|
|
Homo sapiens |
C-33A Cell |
| pmid |
sentence |
| 10864652 |
We show here that HPV16 E6 promotes the ubiquitination and degradation of E6AP itself. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
polyubiquitination
|
MCM7 |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272543 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9852095 |
The characterization of this interaction in turn led to the discovery that Mcm7 is a substrate for both E6-AP-dependent and -independent ubiquitination and is specifically targeted for degradation by the 26 S proteasome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
polyubiquitination
|
TP53 |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272552 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9497376 |
E6AP and E6 together provide the E3-ubiquitin protein ligase activity in the transfer of ubiquitin to p53. In vitro studies have shown that E6AP can form a high energy thiolester bond with ubiquitin and, in the presence of E6, transfer ubiquitin to p53. In this study we have addressed the role of E6AP in vivo in the degradation of p53. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
polyubiquitination
|
RAD23B |
0.413 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272551 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 10373495 |
Here we report the identification of HHR23A, one of the human homologues of the yeast DNA repair protein Rad23, as an E6-independent target of E6AP. E6AP-mediated ubiquitination and degradation of HHR23A and HHR23B. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
PSMD7 |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265134 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28559284 |
Our experiments collectively suggest that UBE3A stimulates Wnt pathway activation by interacting with, ubiquitinating, and reducing the levels of multiple (PSMB1, PSMC2, PSMD2, and PSMD7) proteasome subunits. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
polyubiquitination
|
SIPA1L1 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272608 |
|
|
in vitro |
|
| pmid |
sentence |
| 12036950 |
the purified E6AP enhanced the ubiquitination and degradation of E6TP1 in the presence of E6 in vitro. Additionally, the expression of a dominant-negative E6AP mutant (C833A) in cells inhibited the E6-induced degradation of E6TP1. These findings demonstrate that the E6-induced decrease in the levels of E6TP1 protein involves the E6AP-mediated ubiquitination followed by proteasome-dependent degradation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
PSMD2 |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265133 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28559284 |
Our experiments collectively suggest that UBE3A stimulates Wnt pathway activation by interacting with, ubiquitinating, and reducing the levels of multiple (PSMB1, PSMC2, PSMD2, and PSMD7) proteasome subunits. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
polyubiquitination
|
RAD23A |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272550 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 10373495 |
Here we report the identification of HHR23A, one of the human homologues of the yeast DNA repair protein Rad23, as an E6-independent target of E6AP. E6AP-mediated ubiquitination and degradation of HHR23A and HHR23B. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
UBE3A | down-regulates quantity by destabilization
polyubiquitination
|
SCRIB |
0.536 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272573 |
|
|
in vitro |
|
| pmid |
sentence |
| 11027293 |
Human scribble (Vartul) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the E6AP ubiquitin-protein ligase |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
TSC2 |
0.617 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271396 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18298802 |
An in vivo ubiquitination assay was done to reveal that E6AP promoted the ubiquitination of TSC2 independent of HPV16 E6. We further found that TSC2 bound E6AP in the presence as well as in the absence of HPV16 E6. The binding regions on E6AP and TSC2 have been identified as amino acid (aa) 260-316, aa 428-500 and aa 1-175, aa 1251-1807, respectively. Taken together, degradation of TSC2 is mediated by E6AP ubiquitin ligase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ub:E2 | up-regulates activity 
ubiquitination
|
UBE3A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271284 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
LAMTOR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256145 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 30020076 |
Ube3a regulates mTORC1 signaling by targeting p18, a subunit of the Ragulator. Ube3a ubiquinates p18, resulting in its proteasomal degradation, and Ube3a deficiency in the hippocampus of AS mice induces increased lysosomal localization of p18 and other members of the Ragulator-Rag complex, and increased mTORC1 activity |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
DLG4 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271397 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17121805 |
E6-induced degradation of DLG4 depends on E6AP in vivo. Our findings as a whole indicate that E6AP is involved in E6-mediated ubiquitination and degradation of DLG4 both in vivo and in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UBE3A | down-regulates quantity by destabilization
ubiquitination
|
PSMB1 |
0.363 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265131 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28559284 |
Our experiments collectively suggest that UBE3A stimulates Wnt pathway activation by interacting with, ubiquitinating, and reducing the levels of multiple (PSMB1, PSMC2, PSMD2, and PSMD7) proteasome subunits. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
UBE3A
- 
- 