| + |
PLK1 | up-regulates quantity by stabilization 
phosphorylation
|
TNKS |
0.439 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276242 |
Ser978 |
VVSASLIsPASTPSC |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21818122 |
Here, we report that Plk1 forms a complex with TNKS1 in vitro and in vivo, and phosphorylates TNKS1. Phosphorylation of TNKS1 by Plk1 appears to increase TNKS1 stability and telomeric poly(ADP-ribose) polymerase (PARP) activity. By contrast, targeted inhibition of Plk1 or mutation of phosphorylation sites decreased the stability and PARP activity of TNKS1, leading to distort mitotic spindle-pole assembly and telomeric ends. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276244 |
Thr1128 |
VEEEMQStIREHRDG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21818122 |
Here, we report that Plk1 forms a complex with TNKS1 in vitro and in vivo, and phosphorylates TNKS1. Phosphorylation of TNKS1 by Plk1 appears to increase TNKS1 stability and telomeric poly(ADP-ribose) polymerase (PARP) activity. By contrast, targeted inhibition of Plk1 or mutation of phosphorylation sites decreased the stability and PARP activity of TNKS1, leading to distort mitotic spindle-pole assembly and telomeric ends. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276245 |
Thr839 |
DTQGRNStPLHLAAG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21818122 |
Here, we report that Plk1 forms a complex with TNKS1 in vitro and in vivo, and phosphorylates TNKS1. Phosphorylation of TNKS1 by Plk1 appears to increase TNKS1 stability and telomeric poly(ADP-ribose) polymerase (PARP) activity. By contrast, targeted inhibition of Plk1 or mutation of phosphorylation sites decreased the stability and PARP activity of TNKS1, leading to distort mitotic spindle-pole assembly and telomeric ends. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276243 |
Thr930 |
LAHGADPtMKNQEGQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21818122 |
Here, we report that Plk1 forms a complex with TNKS1 in vitro and in vivo, and phosphorylates TNKS1. Phosphorylation of TNKS1 by Plk1 appears to increase TNKS1 stability and telomeric poly(ADP-ribose) polymerase (PARP) activity. By contrast, targeted inhibition of Plk1 or mutation of phosphorylation sites decreased the stability and PARP activity of TNKS1, leading to distort mitotic spindle-pole assembly and telomeric ends. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276241 |
Thr982 |
SLISPAStPSCLSAA |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21818122 |
Here, we report that Plk1 forms a complex with TNKS1 in vitro and in vivo, and phosphorylates TNKS1. Phosphorylation of TNKS1 by Plk1 appears to increase TNKS1 stability and telomeric poly(ADP-ribose) polymerase (PARP) activity. By contrast, targeted inhibition of Plk1 or mutation of phosphorylation sites decreased the stability and PARP activity of TNKS1, leading to distort mitotic spindle-pole assembly and telomeric ends. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
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 |
| + |
XAV939 | down-regulates
chemical inhibition
|
TNKS |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188054 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19759537 |
Xav939 inhibits the poly-adp-ribosylating enzymes tankyrase 1 and tankyrase 2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207830 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
TNKS | up-regulates quantity by stabilization
binding
|
TARDBP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262115 |
|
|
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 |
| + |
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 |
| + |
XAV939 | down-regulates activity
chemical inhibition
|
TNKS |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259994 |
|
|
in vitro |
|
| pmid |
sentence |
| 19759537 |
In biochemical activity assays, XAV939 strongly inhibited TNKS1 and TNKS2, with half-maximal inhibitory concentration values of 0.011 and 0.004 μM, respectively, but displayed much weaker effects on PARP1 and PARP2 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
TNKS | down-regulates activity
ADP-ribosylation
|
TERF1 |
0.796 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263377 |
|
|
in vitro |
|
| pmid |
sentence |
| 11739745 |
Tankyrase 1 ADP-ribosylates TRF1, inhibiting its binding to telomeric DNA. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
TNKS | down-regulates quantity by destabilization
ADP-ribosylation
|
BLZF1 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263385 |
|
|
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 | down-regulates quantity by destabilization
ADP-ribosylation
|
CASC3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263383 |
|
|
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 |
| + |
TNKS | down-regulates quantity by destabilization
ubiquitination, ADP-ribosylation
|
AXIN2 |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187975 |
|
|
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-263381 |
|
|
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: |
2 |
Organism: |
Homo Sapiens |
| + |
TNKS | down-regulates quantity by destabilization
ubiquitination, ADP-ribosylation
|
AXIN1 |
0.766 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187972 |
|
|
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-263379 |
|
|
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 |
| + |
TNKS | down-regulates quantity by destabilization
|
GSK3B/Axin/APC |
0.523 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261249 |
|
|
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 |
| + |
TNKS | down-regulates quantity by destabilization
ADP-ribosylation
|
PSMF1 |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263387 |
|
|
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 |
3.0
TNKS
- 
- 