+ |
RNF146 | down-regulates quantity
ubiquitination
|
TNKS |
0.713 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260004 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21799911 |
We show that RNF146, tankyrase, and Axin form a protein complex, and that RNF146 mediates ubiquitylation of all three proteins to target them for proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TNKS2 | up-regulates activity
|
RNF146 |
0.599 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263337 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21478859 |
Here, we identify RNF146, a RING-domain E3 ubiquitin ligase, as a positive regulator of Wnt signalling. RNF146 promotes Wnt signalling by mediating tankyrase-dependent degradation of axin. Mechanistically, RNF146 directly interacts with poly(ADP-ribose) through its WWE domain, and promotes degradation of PARsylated proteins. Using proteomics approaches, we have identified BLZF1 and CASC3 as further substrates targeted by tankyrase and RNF146 for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TNKS | up-regulates activity
|
RNF146 |
0.713 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263338 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21478859 |
Here, we identify RNF146, a RING-domain E3 ubiquitin ligase, as a positive regulator of Wnt signalling. RNF146 promotes Wnt signalling by mediating tankyrase-dependent degradation of axin. Mechanistically, RNF146 directly interacts with poly(ADP-ribose) through its WWE domain, and promotes degradation of PARsylated proteins. Using proteomics approaches, we have identified BLZF1 and CASC3 as further substrates targeted by tankyrase and RNF146 for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF146 | down-regulates quantity by destabilization
ubiquitination
|
AXIN2 |
0.658 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263336 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21478859 |
Here, we identify RNF146, a RING-domain E3 ubiquitin ligase, as a positive regulator of Wnt signalling. RNF146 promotes Wnt signalling by mediating tankyrase-dependent degradation of axin. Mechanistically, RNF146 directly interacts with poly(ADP-ribose) through its WWE domain, and promotes degradation of PARsylated proteins. Using proteomics approaches, we have identified BLZF1 and CASC3 as further substrates targeted by tankyrase and RNF146 for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF146 | down-regulates quantity by destabilization
ubiquitination
|
AXIN1 |
0.633 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263335 |
|
|
Homo sapiens |
|
pmid |
sentence |
21478859 |
Here, we identify RNF146, a RING-domain E3 ubiquitin ligase, as a positive regulator of Wnt signalling. RNF146 promotes Wnt signalling by mediating tankyrase-dependent degradation of axin. Mechanistically, RNF146 directly interacts with poly(ADP-ribose) through its WWE domain, and promotes degradation of PARsylated proteins. Using proteomics approaches, we have identified BLZF1 and CASC3 as further substrates targeted by tankyrase and RNF146 for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF146 | down-regulates quantity
ubiquitination
|
AXIN2 |
0.658 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259997 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21799911 |
By RNAi screening, we identified the RNF146 RING-type ubiquitin E3 ligase as a positive regulator of Wnt signaling that operates with tankyrase to maintain low steady-state levels of Axin proteins. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF146 | down-regulates quantity
ubiquitination
|
AXIN1 |
0.633 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259996 |
|
|
Homo sapiens |
|
pmid |
sentence |
21799911 |
By RNAi screening, we identified the RNF146 RING-type ubiquitin E3 ligase as a positive regulator of Wnt signaling that operates with tankyrase to maintain low steady-state levels of Axin proteins. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF146 | down-regulates quantity by destabilization
ubiquitination
|
BLZF1 |
0.419 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263340 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21478859 |
Here, we identify RNF146, a RING-domain E3 ubiquitin ligase, as a positive regulator of Wnt signalling. RNF146 promotes Wnt signalling by mediating tankyrase-dependent degradation of axin. Mechanistically, RNF146 directly interacts with poly(ADP-ribose) through its WWE domain, and promotes degradation of PARsylated proteins. Using proteomics approaches, we have identified BLZF1 and CASC3 as further substrates targeted by tankyrase and RNF146 for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF146 | down-regulates quantity
ubiquitination
|
GSK3B/Axin/APC |
0.515 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259998 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21799911 |
By RNAi screening, we identified the RNF146 RING-type ubiquitin E3 ligase as a positive regulator of Wnt signaling that operates with tankyrase to maintain low steady-state levels of Axin proteins. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Wnt in cancer |
+ |
RNF146 | down-regulates quantity
ubiquitination
|
RNF146 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260006 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21799911 |
We show that RNF146, tankyrase, and Axin form a protein complex, and that RNF146 mediates ubiquitylation of all three proteins to target them for proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Wnt in cancer |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF146 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271078 |
|
|
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 |
+ |
RNF146 | down-regulates quantity
ubiquitination
|
TNKS2 |
0.599 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260005 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
21799911 |
We show that RNF146, tankyrase, and Axin form a protein complex, and that RNF146 mediates ubiquitylation of all three proteins to target them for proteasomal degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF146 | down-regulates quantity by destabilization
ubiquitination
|
CASC3 |
0.266 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263339 |
|
|
Homo sapiens |
|
pmid |
sentence |
21478859 |
Here, we identify RNF146, a RING-domain E3 ubiquitin ligase, as a positive regulator of Wnt signalling. RNF146 promotes Wnt signalling by mediating tankyrase-dependent degradation of axin. Mechanistically, RNF146 directly interacts with poly(ADP-ribose) through its WWE domain, and promotes degradation of PARsylated proteins. Using proteomics approaches, we have identified BLZF1 and CASC3 as further substrates targeted by tankyrase and RNF146 for degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |