| + |
LUBAC | down-regulates quantity by destabilization 
ubiquitination
|
GLYR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272836 |
Lys338 |
VSDPKAAkDLVLGPS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272838 |
Lys495 |
NILQGNFkPDFYLKY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272839 |
Lys505 |
FYLKYIQkDLRLAIA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272840 |
Lys535 |
NEVYKRAkALDQSDN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25278611 |
Here, we analyzed changes in the ubiquitin landscape induced by prostate cancer-associated mutations of SPOP, an E3 ubiquitin ligase substrate-binding protein. SPOP mutants impaired ubiquitylation of a subset of proteins in a dominant-negative fashion. Of these, DEK and TRIM24 emerged as effector substrates consistently up-regulated by SPOP mutants. Up-regulation of DEK, TRIM24 and NCOA3 is a feature of prostate cancer SPOP mutations. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
LUBAC | up-regulates activity 
polyubiquitination
|
TRAF1 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272435 |
|
|
Homo sapiens |
BL-2 Cell |
| pmid |
sentence |
| 25996949 |
LUBAC attaches M1-pUb chains to LMP1/TRAF1 complexes, which recruits the IKK complex.we found that LMP1 TES1 domain signaling induced an association between TRAF1 and the linear ubiquitin chain assembly complex (LUBAC), and stimulated linear (M1)-linked polyubiquitin chain attachment to TRAF1 complexes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LUBAC | down-regulates quantity by destabilization
polyubiquitination
|
TRIM25 |
0.48 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271859 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21292167 |
HOIL-1L/HOIP LUBAC induces TRIM25 ubiquitination and degradation.Upon detection of viral RNA, retinoic acid-inducible gene I (RIG-I) undergoes TRIM25-mediated K63-linked ubiquitination, leading to type I interferon (IFN) production. In this study, we demonstrate that the linear ubiquitin assembly complex (LUBAC), comprised of two RING-IBR-RING (RBR)-containing E3 ligases, HOIL-1L and HOIP, independently targets TRIM25 and RIG-I to effectively suppress virus-induced IFN production. RBR E3 ligase domains of HOIL-1L and HOIP bind and induce proteasomal degradation of TRIM25, whereas the NZF domain of HOIL-1L competes with TRIM25 for RIG-I binding. Consequently, both actions by the HOIL-1L/HOIP LUBAC potently inhibit RIG-I ubiquitination and antiviral activity, but in a mechanistically separate manner. |
|
| 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 |
| + |
LUBAC | down-regulates quantity by destabilization
polyubiquitination
|
PRKCB |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271617 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 17069764 |
In this report, we demonstrated that LUBAC, a ubiquitin ligase complex, is an E3 of activated cPKCs. LUBAC preferentially bound PMA-activated PKCa and PKCbII and their constitutively active mutants (Fig. 2). degradation of PMA-activated PKCa was delayed in HOIL-1L/-MEF (Fig. 3F). These results indicate that LUBAC is the ubiquitin ligase that induces ubiquitination and degradation of activated cPKCs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RBCK1 | form complex
binding
|
LUBAC |
0.945 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271615 |
|
|
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 |
| + |
LUBAC | down-regulates quantity by destabilization
polyubiquitination
|
PRKCA |
0.401 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271618 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 17069764 |
In this report, we demonstrated that LUBAC, a ubiquitin ligase complex, is an E3 of activated cPKCs. LUBAC preferentially bound PMA-activated PKCa and PKCbII and their constitutively active mutants (Fig. 2). degradation of PMA-activated PKCa was delayed in HOIL-1L/-MEF (Fig. 3F). These results indicate that LUBAC is the ubiquitin ligase that induces ubiquitination and degradation of activated cPKCs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LUBAC | down-regulates activity
binding
|
DDX58 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271860 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21292167 |
HOIL-1L/HOIP LUBAC induces TRIM25 ubiquitination and degradation Upon detection of viral RNA, retinoic acid-inducible gene I (RIG-I) undergoes TRIM25-mediated K63-linked ubiquitination, leading to type I interferon (IFN) production. In this study, we demonstrate that the linear ubiquitin assembly complex (LUBAC), comprised of two RING-IBR-RING (RBR)-containing E3 ligases, HOIL-1L and HOIP, independently targets TRIM25 and RIG-I to effectively suppress virus-induced IFN production. RBR E3 ligase domains of HOIL-1L and HOIP bind and induce proteasomal degradation of TRIM25, whereas the NZF domain of HOIL-1L competes with TRIM25 for RIG-I binding. Consequently, both actions by the HOIL-1L/HOIP LUBAC potently inhibit RIG-I ubiquitination and antiviral activity, but in a mechanistically separate manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
LUBAC