+ |
TNKS2 | down-regulates activity
ADP-ribosylation
|
TERF1 |
0.567 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263376 |
|
|
in vitro |
|
pmid |
sentence |
11739745 |
Tankyrase 2 poly(ADP-ribosyl)ated itself and TRF1. Overexpression of tankyrase 2 in the nucleus released endogenous TRF1 from telomeres. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
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 |
+ |
TNKS2 | down-regulates quantity by destabilization
ADP-ribosylation
|
CASC3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263382 |
|
|
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 |
+ |
TNKS2 | down-regulates quantity by destabilization
ubiquitination, ADP-ribosylation
|
AXIN1 |
0.693 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-188033 |
|
|
Homo sapiens |
|
pmid |
sentence |
19759537 |
Both tankyrase isoforms interact with a highly conserved domain of axin and stimulate its degradation through the ubiquitin-proteasome pathway. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263378 |
|
|
Homo sapiens |
|
pmid |
sentence |
19759537 |
Together, these findings are consistent with the hypothesis that TNKS promotes the ubiquitination and degradation of axin, which may be mediated, at least in part, through the direct PARsylation of axin. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
TNKS2 | up-regulates quantity by stabilization
binding
|
TARDBP |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262116 |
|
|
Rattus norvegicus |
|
pmid |
sentence |
32409565 |
Upon investigating the functional effect, we find that interaction with Tnks-1/2 inhibits the ubiquitination and proteasomal turnover of TDP-43, leading to its stabilization. We further show that proteasomal turnover of TDP-43 occurs preferentially in the nucleus; our data indicate that Tnks-1/2 stabilizes TDP-43 by promoting cytoplasmic accumulation, which sequesters the protein from nuclear proteasome degradation. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
Tissue: |
Brain |
+ |
XAV939 | down-regulates
chemical inhibition
|
TNKS2 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-207833 |
|
|
Homo sapiens |
|
pmid |
sentence |
Other |
|
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-188057 |
|
|
Homo sapiens |
|
pmid |
sentence |
19759537 |
Xav939 inhibits the poly-adp-ribosylating enzymes tankyrase 1 and tankyrase 2. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
TNKS2 | down-regulates quantity by destabilization
|
GSK3B/Axin/APC |
0.451 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261248 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19759537 |
Using a quantitative chemical proteomic approach, we discovered that XAV939 stabilizes axin by inhibiting the poly-ADP-ribosylating enzymes tankyrase 1 and tankyrase 2. Both tankyrase isoforms interact with a highly conserved domain of axin and stimulate its degradation through the ubiquitin-proteasome pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TNKS2 | down-regulates
ubiquitination
|
AXIN2 |
0.684 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-188036 |
|
|
Homo sapiens |
|
pmid |
sentence |
19759537 |
Both tankyrase isoforms interact with a highly conserved domain of axin and stimulate its degradation through the ubiquitin-proteasome pathway. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TNKS2 | down-regulates quantity by destabilization
ADP-ribosylation
|
AXIN2 |
0.684 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263380 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19759537 |
Together, these findings are consistent with the hypothesis that TNKS promotes the ubiquitination and degradation of axin, which may be mediated, at least in part, through the direct PARsylation of axin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TNKS2 | down-regulates quantity by destabilization
ADP-ribosylation
|
PSMF1 |
0.474 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263386 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
23622245 |
We identify the ADP-ribosyltransferase tankyrase (TNKS) and the 19S assembly chaperones dp27 and dS5b as direct binding partners of the proteasome regulator PI31. TNKS-mediated ADP-ribosylation of PI31 drastically reduces its affinity for 20S proteasome alpha subunits to relieve 20S repression by PI31. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TNKS2 | down-regulates quantity by destabilization
ADP-ribosylation
|
BLZF1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263384 |
|
|
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
|
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 |
+ |
XAV939 | down-regulates activity
chemical inhibition
|
TNKS2 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259995 |
|
|
in vitro |
|
pmid |
sentence |
20565110 |
We report two crystal structures of the PARP domain of human tankyrase-2 (TNKS2). Tankyrases are involved in fundamental cellular processes such as telomere homeostasis and Wnt signaling. |
|
Publications: |
1 |
Organism: |
In Vitro |