+ |
PPP1CB | down-regulates activity
dephosphorylation
|
AXIN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248569 |
Ser217 |
YTRTGSEsPKVCSDQ |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248570 |
Ser469 |
AHEENPEsILDEHVQ |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248567 |
Ser75 |
LGYEPEGsASPTPPY |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248568 |
Ser77 |
YEPEGSAsPTPPYLK |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
PPP1CC | down-regulates activity
dephosphorylation
|
AXIN1 |
0.272 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248496 |
Ser217 |
YTRTGSEsPKVCSDQ |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248497 |
Ser469 |
AHEENPEsILDEHVQ |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248494 |
Ser75 |
LGYEPEGsASPTPPY |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248495 |
Ser77 |
YEPEGSAsPTPPYLK |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
PP1 | down-regulates activity
dephosphorylation
|
AXIN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264660 |
Ser217 |
YTRTGSEsPKVCSDQ |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PPP1CA | down-regulates activity
dephosphorylation
|
AXIN1 |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248553 |
Ser217 |
YTRTGSEsPKVCSDQ |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248554 |
Ser469 |
AHEENPEsILDEHVQ |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248551 |
Ser75 |
LGYEPEGsASPTPPY |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248552 |
Ser77 |
YEPEGSAsPTPPYLK |
Homo sapiens |
|
pmid |
sentence |
17318175 |
The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin| Axin phosphorylation markedly enhances the binding of glycogen synthase kinase 3, leading to a more active beta-catenin destruction complex. Wnt-regulated changes in axin phosphorylation, mediated by PP1, may therefore determine beta-catenin transcriptional activity| Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
CSNK1D | up-regulates
phosphorylation, binding
|
AXIN1 |
0.537 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-87437 |
Ser46 |
PASYSFCsGKGVGIK |
Homo sapiens |
|
pmid |
sentence |
12000790 |
We conclude that a major role of axin in the wnt is to provide the kinase activity that initiates the betBeta-catenin phosphorylation cascade at s45 . This process is mediated by cki, the alfa, delta, or ? Isoform, all detected in association with axin by lc/mscomplex of axin and casein kinase i (cki) induces betBeta-catenin phosphorylation at a single site: serine 45 (s45) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-87433 |
|
|
Homo sapiens |
|
pmid |
sentence |
12000790 |
We conclude that a major role of axin in the wnt is to provide the kinase activity that initiates the beta-catenin phosphorylation cascade at s45. This process is mediated by cki, the alfa, delta, or epsilon isoform, all detected in association with axin by lc/ms. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CSNK1A1 | up-regulates activity
phosphorylation
|
AXIN1 |
0.776 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249192 |
Ser469 |
AHEENPEsILDEHVQ |
in vitro |
|
pmid |
sentence |
17318175 |
Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated (Supplementary Figure 3). Three of them (S80, S82, and S473) were also phosphorylated in vitro by CKI and are conserved between axin1 and axin2/conductin.|This suggests that cumulative phosphorylation of axin is required for it to fully downregulate Wnt/beta_catenin signaling. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249189 |
Ser75 |
LGYEPEGsASPTPPY |
in vitro |
|
pmid |
sentence |
17318175 |
Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated (Supplementary Figure 3). Three of them (S80, S82, and S473) were also phosphorylated in vitro by CKI and are conserved between axin1 and axin2/conductin.|This suggests that cumulative phosphorylation of axin is required for it to fully downregulate Wnt/beta_catenin signaling. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249191 |
Ser77 |
YEPEGSAsPTPPYLK |
in vitro |
|
pmid |
sentence |
17318175 |
Four sites, S80, S82, S222, and S473, were identified to be PP1 regulated (Supplementary Figure 3). Three of them (S80, S82, and S473) were also phosphorylated in vitro by CKI and are conserved between axin1 and axin2/conductin.|This suggests that cumulative phosphorylation of axin is required for it to fully downregulate Wnt/beta_catenin signaling. |
|
Publications: |
3 |
Organism: |
In Vitro |
+ |
GSK3B | up-regulates activity
phosphorylation
|
AXIN1 |
0.917 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251221 |
Ser486 |
LRTPGRQsPGPGHRS |
Homo sapiens |
|
pmid |
sentence |
10581160 |
Axin residues T609 and S614 are physiological GSK3beta targets. Axin phosphorylation in the regulation of b-catenin stability. When active (left), GSK3b phosphorylates Axin as well as APC and b-catenin. The phosphorylated form of Axin binds strongly to b-catenin and promotes the phosphorylation of b-catenin by GSK3b, leading to strong interaction with b-TrCP |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251222 |
Thr481 |
HVQRVLRtPGRQSPG |
Homo sapiens |
|
pmid |
sentence |
10581160 |
Axin residues T609 and S614 are physiological GSK3beta targets. Axin phosphorylation in the regulation of b-catenin stability. When active (left), GSK3b phosphorylates Axin as well as APC and b-catenin. The phosphorylated form of Axin binds strongly to b-catenin and promotes the phosphorylation of b-catenin by GSK3b, leading to strong interaction with b-TrCP |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PPM1A | down-regulates
dephosphorylation
|
AXIN1 |
0.446 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-74231 |
|
|
Homo sapiens |
|
pmid |
sentence |
10644691 |
Pp2c utilizes axin as a substrate both in vitro and in vivo and decreases its half-life. These results indicate that pp2c is a positive regulator of wnt signal transduction and mediates its effects through the dephosphorylation of axin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LRP6 | down-regulates activity
relocalization
|
AXIN1 |
0.829 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-104493 |
|
|
Homo sapiens |
|
pmid |
sentence |
12897152 |
The phosphorylation of lrp6 generates a docking site for axin and recruits it to the plasma membrane, where axin is inactivated and/or targeted for degradation by an unknown mechanism. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-179469 |
|
|
Homo sapiens |
|
pmid |
sentence |
18632848 |
The phosphorylation of lrp6 generates a docking site for axin and recruits it to the plasma membrane, where axin is inactivated and/or targeted for degradation by an unknown mechanism. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-148668 |
|
|
Homo sapiens |
|
pmid |
sentence |
16890161 |
The phosphorylation of lrp6 generates a docking site for axin and recruits it to the plasma membrane, where axin is inactivated and/or targeted for degradation by an unknown mechanism. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
DVL2 | up-regulates activity
binding
|
AXIN1 |
0.655 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155221 |
|
|
Homo sapiens |
|
pmid |
sentence |
17529994 |
Dishevelled (dvl) transduces the wnt signal by interacting with the cytoplasmic axin complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AXIN1 | up-regulates activity
binding
|
APC |
0.943 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-60043 |
|
|
Homo sapiens |
SW-480 Cell |
pmid |
sentence |
9734785 |
Axin, an inhibitor of the wnt pathway, interacts with beta-catenin, gsk-3beta and apc and reduces the beta-catenin level. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AXIN1 | form complex
binding
|
GSK3B/Axin/APC |
0.93 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-227292 |
|
|
Homo sapiens |
Colonic Cancer Cell |
pmid |
sentence |
9734785 |
Axin, an inhibitor of the wnt pathway, interacts with beta-catenin, gsk-3beta and apc and reduces the beta-catenin level. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GSK3B | up-regulates
binding, phosphorylation
|
AXIN1 |
0.917 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-67438 |
|
|
Homo sapiens |
|
pmid |
sentence |
10318824 |
From the binding experiments, we defined the domains of Axin that bind glycogen synthase kinase-3beta (GSK-3beta) and beta-catenin. We also examined the ability of each Axin mutant to inhibit lymphoid enhancer factor-1 (Lef-1) reporter activity in a cell line expressing high levels of beta-catenin. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-201683 |
|
|
Homo sapiens |
|
pmid |
sentence |
23579495 |
Phosphorylation by GSK3 kept Axin activated (open) for _-catenin interaction and poised for engagement of LRP6. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-60046 |
|
|
Homo sapiens |
|
pmid |
sentence |
9734785 |
Interaction with beta-catenin and GSK-3beta was required for the Axin-mediated beta-catenin reduction. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
APC2 | up-regulates
binding
|
AXIN1 |
0.765 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-57673 |
|
|
Homo sapiens |
|
pmid |
sentence |
9601641 |
Human axin (haxin) binds directly to beta-catenin, gsk3 beta, and apc in vitro, and the endogenous proteins are found in a complex in cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GNAS | up-regulates
binding
|
AXIN1 |
0.389 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-141789 |
|
|
Homo sapiens |
|
pmid |
sentence |
16293724 |
We show that pge2 stimulates colon cancer cell growth through its heterotrimeric guanine nucleotide-binding protein (g protein) coupled receptor, ep2, by a signaling route that involves the activation of phosphoinositide 3-kinase and the protein kinase akt by free g protein bg subunits and the direct association of the g protein as subunit with the regulator of g protein signaling (rgs) domain of axin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AXIN1 | up-regulates
binding
|
CSNK1D |
0.537 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-87401 |
|
|
Homo sapiens |
|
pmid |
sentence |
12000790 |
Complex of axin and casein kinase i (cki) induces beta-catenin phosphorylation at a single site: serine 45 (s45). |
|
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 |
+ |
AXIN1 | up-regulates
|
SMAD3 |
0.652 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145848 |
|
|
Homo sapiens |
|
pmid |
sentence |
16601693 |
Axin promotes smad3 phosphorylation;phosphorylated smad3 dissociates from the axin complex and then combines with smad4 to activate transcription in the nucleus. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMER1 | up-regulates activity
relocalization
|
AXIN1 |
0.78 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-171886 |
|
|
Homo sapiens |
|
pmid |
sentence |
21304492 |
Amer1 binds ck1gamma, recruits axin and gsk3beta to the plasma membrane and promotes complex formation between axin and lrp6. |
|
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 |
+ |
DVL1 | down-regulates activity
binding
|
AXIN1 |
0.813 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-219356 |
|
|
Chlorocebus aethiops |
|
pmid |
sentence |
10196136 |
We have recently found that Dvl-1 directly binds to Axin and that the binding of Dvl-1 to Axin does not affect the interaction of GSK-3beta with Axin. It is possible that the binding of Dvl to Axin induces the structural change of the Axin complex; therefore GSK-3beta does not effectively phosphorylate Axin. This is the first demostration showing that Dvl inhibits the function of GSK-3beta directly. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
LRP5 | down-regulates quantity
relocalization
|
AXIN1 |
0.825 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236997 |
|
|
Mus musculus |
|
pmid |
sentence |
11336703 |
Axin is a protein that interacts with the intracellular domain of LRP-5. LRP-5 active form bind Axin and induce LEF-1 activation by destabilizing Axin and stabilizing beta-catenin. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
PPM1A | down-regulates quantity by destabilization
dephosphorylation
|
AXIN1 |
0.446 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248488 |
|
|
Homo sapiens |
|
pmid |
sentence |
10644691 |
In addition, PP2C expression relieves Axin-mediated repression of LEF-1-dependent transcription. PP2C utilizes Axin as a substrate both in vitro and in vivo and decreases its half-life. These results indicate that PP2C is a positive regulator of Wnt signal transduction and mediates its effects through the dephosphorylation of Axin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK1E | up-regulates
phosphorylation
|
AXIN1 |
0.737 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-87444 |
|
|
Homo sapiens |
|
pmid |
sentence |
12000790 |
We conclude that a major role of axin in the wnt is to provide the kinase activity that initiates the betBeta-catenin phosphorylation cascade at s45. This process is mediated by cki, the alfa, delta, or ? Isoform, all detected in association with axin by lc/ms. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MACF1 | down-regulates quantity by destabilization
|
AXIN1 |
0.414 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-147448 |
|
|
Homo sapiens |
|
pmid |
sentence |
16815997 |
In the absence of wnt, macf1 associated with a complex that contained axin, betBeta-catenin, gsk3beta, and apc. Upon wnt stimulation, macf1 appeared to be involved in the translocation and subsequent binding of the axin complex to lrp6 at the cell membrane. Macf1 is involved in the translocation of the complex containing axin, Beta-catenin, and gsk3_ but not apc from the cytosol to the cell membrane, where axin and macf1 bind to lrp-5/6. Subsequently, gsk3_ is inactivated by phosphorylation, axin is degraded, and Beta-catenin is released and enters the nucleus, where it can activate the wnt-responsive genes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
XAV939 | up-regulates
|
AXIN1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-188045 |
|
|
Homo sapiens |
|
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 |
|
Publications: |
1 |
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 |
+ |
TNKS2 | down-regulates quantity by destabilization
ADP-ribosylation, ubiquitination
|
AXIN1 |
0.693 |
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. |
|
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. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
AXIN1 | down-regulates
binding
|
SMAD7 |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145851 |
|
|
Homo sapiens |
|
pmid |
sentence |
16601693 |
Here, we show that axin activates tgf-beta signaling by forming a multimeric complex consisting of smad7 and ubiquitin e3 ligase arkadia. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AXIN1 | down-regulates
ubiquitination
|
BMPR1A |
0.337 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-195552 |
|
|
Homo sapiens |
|
pmid |
sentence |
22298955 |
Other proteins, such as the serine/threonine kinase fused (fu), can function in concert with the e3 ligase smurf to regulate ubiquitination and proteolysis of the bmp receptor |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AXIN1 | up-regulates
binding
|
RNF111 |
0.626 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145845 |
|
|
Homo sapiens |
|
pmid |
sentence |
16601693 |
Here, we show that axin activates tgf-beta signaling by forming a multimeric complex consisting of smad7 and ubiquitin e3 ligase arkadia. Axin is a scaffold protein in tgf-beta signaling that promotes degradation of smad7 by arkadia. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-119660 |
|
|
Homo sapiens |
|
pmid |
sentence |
14657019 |
Here, we show that axin activates tgf-beta signaling by forming a multimeric complex consisting of smad7 and ubiquitin e3 ligase arkadia. Axin is a scaffold protein in tgf-beta signaling that promotes degradation of smad7 by arkadia. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
WNT5A | down-regulates
|
AXIN1 |
0.488 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-169663 |
|
|
Homo sapiens |
|
pmid |
sentence |
21078818 |
We demonstrate here that prototype canonical wnt3a and noncanonical wnt5a ligands specifically trigger completely unrelated endogenous coreceptors-lrp5/6 and ror1/2, respectively-through a common mechanism that involves their wnt-dependent coupling to the frizzled (fzd) coreceptor and recruitment of shared components, including dishevelled (dvl), axin, and glycogen synthase kinase 3 (gsk3). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AXIN1 | up-regulates
binding
|
MAP3K4 |
0.43 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-104003 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
12878610 |
Mekk4, also binds to axin in vivo and mediates axin-induced jnk activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AXIN1 | up-regulates
binding
|
MAP3K1 |
0.529 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-77591 |
|
|
Homo sapiens |
|
pmid |
sentence |
10829020 |
We found that in contrast to axin, dvl2 activation of jnk does not require mekk1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AXIN1 | up-regulates activity
binding
|
AXIN1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155218 |
|
|
Homo sapiens |
|
pmid |
sentence |
17529994 |
The axin dix domain has a novel structural fold largely composed of beta-strands that engage in head-to-tail self-interaction to form filaments in the crystal |
|
Publications: |
1 |
Organism: |
Homo Sapiens |