+ |
Ub:E2 | up-regulates activity
ubiquitination
|
SYVN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271126 |
|
|
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 |
+ |
SYVN1 | down-regulates quantity by destabilization
polyubiquitination
|
HMGCR |
0.579 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272594 |
|
|
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
14593114 |
In the presence of the ubiquitin-conjugating enzyme UBC7, the RING-H2 finger has in vitro ubiquitination activity for Lys(48)-specific polyubiquitin linkage, suggesting that human HRD1 is an E3 ubiquitin ligase involved in protein degradation.Human HRD1 appears to be involved in the basal degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase but not in the degradation that is regulated by sterols. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
SYVN1 | down-regulates quantity by destabilization
ubiquitination
|
NFE2L2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267360 |
|
|
Homo sapiens |
|
pmid |
sentence |
29731393 |
NRF2 is negatively regulated by three E3 ubiquitin ligase complexes: the KEAP1-CUL3-RBX1 complex, the β-TrCP-SKP1-CUL1-RBX1 complex, and HRD1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
UBE2G2 | up-regulates activity
ubiquitination
|
SYVN1 |
0.681 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272593 |
|
|
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
14593114 |
We show that human HRD1 is a non-glycosylated, stable ER protein with a cytosolic RING-H2 finger domain. In the presence of the ubiquitin-conjugating enzyme UBC7, the RING-H2 finger has in vitro ubiquitination activity for Lys(48)-specific polyubiquitin linkage, suggesting that human HRD1 is an E3 ubiquitin ligase involved in protein degradation. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
SYVN1 | up-regulates activity
binding
|
HERPUD1 |
0.592 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261349 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
28827405 |
FAM8A1 enhances binding of Herp to Hrd1, an interaction that is required for ERAD. Our findings support a model of Hrd1 complex formation, where the Hrd1 cytoplasmic domain and FAM8A1 have a central role in the assembly and activity of this ERAD machinery. A conserved Hrd1 cytoplasmic domain interacts with FAM8A1 and Herp |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SYVN1 | down-regulates quantity by destabilization
polyubiquitination
|
SERPINI1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272757 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21507957 |
In this study, we demonstrate that two ER-associated E3 ligases, Hrd1 and gp78, are involved in the ubiquitination and degradation of mutant neuroserpin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SYVN1 | down-regulates quantity by destabilization
polyubiquitination
|
GPR37 |
0.409 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272631 |
|
|
Homo sapiens |
|
pmid |
sentence |
18241051 |
We demonstrated that endogenous HRD1 interacts with Pael-R, and that HRD1 promotes the degradation of Pael-R and protects cell death caused by the accumulation of Pael-R. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SYVN1 | down-regulates quantity by destabilization
polyubiquitination
|
CLU |
0.325 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272629 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
17451556 |
We also report that the ER-associated ubiquitin ligase Hrd1/synoviolin can interact with, and ubiquitinate clusterin. The fact that cleaved endogenous clusterin appears, under certain conditions, to be subject to polyubiquitination (Figure 2C) and proteasomal degradation (1, 2) strongly suggests that it passed through the secretory pathway before reaching the cytosol. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
FAM8A1 | up-regulates activity
binding
|
SYVN1 |
0.593 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261348 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
28827405 |
FAM8A1 enhances binding of Herp to Hrd1, an interaction that is required for ERAD. Our findings support a model of Hrd1 complex formation, where the Hrd1 cytoplasmic domain and FAM8A1 have a central role in the assembly and activity of this ERAD machinery. A conserved Hrd1 cytoplasmic domain interacts with FAM8A1 and Herp |
|
Publications: |
1 |
Organism: |
Homo Sapiens |