+ |
RNF128 | down-regulates quantity by destabilization
polyubiquitination
|
CD83 |
0.359 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271850 |
Lys177 |
SIFPDFSkAGMERAF |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19542455 |
In this study, we show that GRAIL can down-modulate the expression of CD83 (previously described as a cell surface marker for mature dendritic cells) on CD4 T cells. GRAIL-mediated down-modulation of CD83 is dependent on an intact GRAIL extracellular protease-associated domain and an enzymatically active cytosolic RING domain, and proceeds via the ubiquitin-dependent 26S proteosome pathway. Ubiquitin modification of lysine residues K168 and K183, but not K192, in the cytoplasmic domain of CD83 was shown to be necessary for GRAIL-mediated degradation of CD83. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271849 |
Lys192 |
LPVTSPNkHLGLVTP |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19542455 |
In this study, we show that GRAIL can down-modulate the expression of CD83 (previously described as a cell surface marker for mature dendritic cells) on CD4 T cells. GRAIL-mediated down-modulation of CD83 is dependent on an intact GRAIL extracellular protease-associated domain and an enzymatically active cytosolic RING domain, and proceeds via the ubiquitin-dependent 26S proteosome pathway. Ubiquitin modification of lysine residues K168 and K183, but not K192, in the cytoplasmic domain of CD83 was shown to be necessary for GRAIL-mediated degradation of CD83. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
RNF128 | up-regulates quantity by stabilization
polyubiquitination
|
ARHGDIB |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271621 |
|
|
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
17114425 |
We found that RhoGDIα and RhoGDIβ are ubiquitin E3 substrates of GRAIL. GRAIL uses nonlysine 48-ubiquitin linkage in polyubiquitinating RhoGDI. GRAIL was subsequently demonstrated to bind and ubiquitinate RhoGDI, although GRAIL-mediated ubiquitination of RhoGDI did not result in proteosomal degradation. Our data suggest that ubiquitination of RhoGDI by GRAIL does not result in proteolytic degradation. In fact, GRAIL activity appeared to increase RhoGDI stability. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF128 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270953 |
|
|
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 |
+ |
RNF128 | up-regulates quantity by stabilization
polyubiquitination
|
ARHGDIA |
0.27 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271622 |
|
|
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
17114425 |
We found that RhoGDIα and RhoGDIβ are ubiquitin E3 substrates of GRAIL. GRAIL uses nonlysine 48-ubiquitin linkage in polyubiquitinating RhoGDI. GRAIL was subsequently demonstrated to bind and ubiquitinate RhoGDI, although GRAIL-mediated ubiquitination of RhoGDI did not result in proteosomal degradation. Our data suggest that ubiquitination of RhoGDI by GRAIL does not result in proteolytic degradation. In fact, GRAIL activity appeared to increase RhoGDI stability. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |