+ |
CASP1 | down-regulates activity
cleavage
|
RNF31 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272192 |
Asp348 |
GTGGLEPdLARGRWA |
Homo sapiens |
HaCaT II-4 Cell |
pmid |
sentence |
32122970 |
We show that LUBAC interacted with caspase-1 via HOIP and modified its CARD domain with linear polyubiquitin and that depletion of HOIP or Sharpin resulted in heightened caspase-1 activation and cell death in response to inflammasome activation, unlike what is observed in macrophages. Reciprocally, caspase-1, as well as caspase-8, regulated LUBAC activity by proteolytically processing HOIP at Asp-348 and Asp-387 during the execution of cell death. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272193 |
Asp387 |
QPPSLVVdSRDAGIC |
Homo sapiens |
HaCaT II-4 Cell |
pmid |
sentence |
32122970 |
We show that LUBAC interacted with caspase-1 via HOIP and modified its CARD domain with linear polyubiquitin and that depletion of HOIP or Sharpin resulted in heightened caspase-1 activation and cell death in response to inflammasome activation, unlike what is observed in macrophages. Reciprocally, caspase-1, as well as caspase-8, regulated LUBAC activity by proteolytically processing HOIP at Asp-348 and Asp-387 during the execution of cell death. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CASP8 | down-regulates activity
cleavage
|
RNF31 |
0.321 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272194 |
Asp348 |
GTGGLEPdLARGRWA |
Homo sapiens |
HaCaT II-4 Cell |
pmid |
sentence |
32122970 |
We show that LUBAC interacted with caspase-1 via HOIP and modified its CARD domain with linear polyubiquitin and that depletion of HOIP or Sharpin resulted in heightened caspase-1 activation and cell death in response to inflammasome activation, unlike what is observed in macrophages. Reciprocally, caspase-1, as well as caspase-8, regulated LUBAC activity by proteolytically processing HOIP at Asp-348 and Asp-387 during the execution of cell death. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272195 |
Asp387 |
QPPSLVVdSRDAGIC |
Homo sapiens |
HaCaT II-4 Cell |
pmid |
sentence |
32122970 |
We show that LUBAC interacted with caspase-1 via HOIP and modified its CARD domain with linear polyubiquitin and that depletion of HOIP or Sharpin resulted in heightened caspase-1 activation and cell death in response to inflammasome activation, unlike what is observed in macrophages. Reciprocally, caspase-1, as well as caspase-8, regulated LUBAC activity by proteolytically processing HOIP at Asp-348 and Asp-387 during the execution of cell death. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
RNF31 | up-regulates quantity by stabilization
monoubiquitination
|
NR0B1 |
0.449 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271786 |
|
|
Homo sapiens |
NCI-H295R Cell |
pmid |
sentence |
19237537 |
RNF31 promotes monoubiquitination of DAX-1 in an RBR domain-dependent manner. In conclusion, our results suggest that the major DAX-1 modification observed in different experimental settings is likely to be monoubiquitination at one or more lysine residues (multiubiquitination) possibly located within the LBD of DAX-1. RNF31 stabilizes endogenous DAX-1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF31 | form complex
binding
|
LUBAC |
0.945 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271616 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
17006537 |
Here, we report that a protein complex consisting of two RING finger proteins, HOIL-1L and HOIP, exhibits ubiquitin polymerization activity by recognizing ubiquitin moieties of proteins. The polyubiquitin chain generated by the complex is not formed by Lys linkages, but by linkages between the C- and N-termini of ubiquitin, indicating that the ligase complex possesses a unique feature to assemble a novel head-to-tail linear polyubiquitin chain. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF31 | up-regulates activity
polyubiquitination
|
CASP1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272191 |
|
|
Homo sapiens |
HaCaT II-4 Cell |
pmid |
sentence |
32122970 |
HOIP forms a constitutive interaction with caspase-1 and mediates the linear ubiquitination of the CARD pro-domain. Upon engagement of apoptosis, caspase-1 and caspase-8 cleave HOIP at Asp-348 and Asp-387, limiting the ability of LUBAC to ubiquitinate substrates. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF31 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270985 |
|
|
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 |
+ |
RNF31 | up-regulates activity
polyubiquitination
|
IKBKG |
0.844 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272052 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24469399 |
Involvement of Gln271 and Asp275 of NEMO in LUBAC-mediated linear polyubiquitination.vHOIP NZF1 also recognizes NEMO, and this recognition is involved in linear polyubiquitination of NEMO. Linear chains conjugated to NEMO are recognized by NEMO in trans on another IKK complex, thereby inducing multimerization of the IKK complex and trans autophosphorylation of IKK2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |