+ |
AMFR | down-regulates activity
polyubiquitination
|
UBL4A |
0.535 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272856 |
Lys48 |
QRLLFKGkALADGKR |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24424410 |
USP13 and gp78 control ubiquitination of Ubl4A.These data suggest that USP13 and gp78 play antagonizing roles in regulation of Ubl4A ubiquitination: While gp78 assembles ubiquitin chains on Ubl4A, USP13 antagonizes this activity to limit Ubl4A ubiquitination.Ubiquitination of Ubl4A preferentially occurs on Lys48. We identify the Bag6 cofactor Ubl4A as a shared substrate of gp78 and USP13. USP13 depletion is associated with hyper-ubiquitination of Ubl4A and altered interaction between the Bag6 complex and its co-chaperone SGTA. Because the interaction of Ubl4A with SGTA is mediated by positively-charged residues in Ubl4A including Lys48 (Chartron et al., 2012; Xu et al., 2012), which happens to be the major ubiquitination site, the simplest model to explain reduced Bag6-SGTA interaction in USP13 knockdown cells is that ubiquitin conjugates on Ubl4A sterically hinder SGTA binding. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5 | down-regulates quantity by destabilization
phosphorylation
|
AMFR |
0.25 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277356 |
Ser516 |
SIRPALNsPVERPSS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
28528366 |
We found that GP78 expression is decreased in MPTP-based cellular and animal PD models, and CDK5 directly phosphorylated GP78 at Ser516, which promoted the ubiquitination and degradation of GP78. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMFR | down-regulates quantity by destabilization
polyubiquitination
|
GPI |
0.546 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272177 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24810856 |
Gp78 is a ubiquitin ligase that plays a vital role in endoplasmic reticulum (ER)-associated degradation (ERAD). Here we report that autocrine motility factor (AMF), also known as phosphoglucose isomerase (PGI), is a novel substrate of gp78. We show that polyubiquitylation of AMF requires cooperative interaction between gp78 and the ubiquitin ligase TRIM25 (tripartite motif-containing protein 25). While TRIM25 mediates the initial round of ubiquitylation, gp78 catalyzes polyubiquitylation of AMF. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMFR | down-regulates quantity by destabilization
polyubiquitination
|
CD3D |
0.486 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272670 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11724934 |
Gp78 specifically recruits MmUBC7, a ubiquitin-conjugating enzyme (E2) implicated in ER-associated degradation (ERAD), through a region distinct from the RING finger. gp78 can target itself for proteasomal degradation in a RING finger- and MmUBC7-dependent manner. Importantly, gp78 can also mediate degradation of CD3-delta, a well-characterized ERAD substrate. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMFR | down-regulates quantity by destabilization
polyubiquitination
|
MFN1 |
0.315 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272886 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
23427266 |
Gp78 induces ubiquitylation and proteasomal degradation of Mfn1 and Mfn2. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
AMFR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271104 |
|
|
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 |
+ |
UFD1 | up-regulates activity
binding
|
AMFR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252425 |
|
|
|
|
pmid |
sentence |
17681147 |
Here we show that Ufd1 directly interacts with gp78 and functions as a cofactor. Ufd1 enhances the E3 activity of gp78, accelerates the ubiquitination and degradation of reductase, and eventually promotes receptor-mediated uptake of low-density lipoprotein. |
|
Publications: |
1 |
+ |
GPI | up-regulates
binding
|
AMFR |
0.546 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-97270 |
|
|
Homo sapiens |
|
pmid |
sentence |
12527360 |
Pgi is a housekeeping gene encoding phosphoglucose isomerase (pgi) a glycolytic enzyme that also functions as a cytokine (autocrine motility factor (amf)/neuroleukin/maturation factor) upon secretion from the cell and binding to its 78 kda seven-transmembrane domain receptor (gp78/amf-r) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMFR | down-regulates quantity by destabilization
polyubiquitination
|
SERPINI1 |
0.301 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272756 |
|
|
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 |
+ |
AMFR | down-regulates quantity by destabilization
polyubiquitination
|
MFN2 |
0.305 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272887 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
23427266 |
Gp78 induces ubiquitylation and proteasomal degradation of Mfn1 and Mfn2. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
TRIM25 | down-regulates quantity by destabilization
polyubiquitination
|
AMFR |
0.372 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272176 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24810856 |
We further demonstrate that TRIM25 ubiquitylates gp78 and that overexpression of TRIM25 accelerates the degradation of gp78. Our data suggest that TRIM25 not only cooperates with gp78 in polyubiquitylation of AMF but also gauges the steady-state level of gp78. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |