| + |
BTRC | down-regulates quantity by destabilization 
ubiquitination
|
GLI3 |
0.657 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145116 |
Lys773 |
RRNPAGTkWMEHVKL |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 17283082 |
Third, we and others have recently shown that only phosphorylated Ci/Gli3 are able to directly bind Slimb/BetaTrCP, that Gli3 is polyubiquitinated in the cell, and that mutations of 4 lysine residues, the putative ubiquitination sites in the Gli3 C-terminal region, inhibit Gli3 processing These observations further support the notion that Ci/Gli3 processing is carried out by the proteasome because the deletion of the cleavage site is expected to often disrupt the protease-mediated site-specific cleavage. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249576 |
Lys779 |
TKWMEHVkLERLKQV |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 17283082 |
Third, we and others have recently shown that only phosphorylated Ci/Gli3 are able to directly bind Slimb/BetaTrCP, that Gli3 is polyubiquitinated in the cell, and that mutations of 4 lysine residues, the putative ubiquitination sites in the Gli3 C-terminal region, inhibit Gli3 processing These observations further support the notion that Ci/Gli3 processing is carried out by the proteasome because the deletion of the cleavage site is expected to often disrupt the protease-mediated site-specific cleavage. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249577 |
Lys784 |
HVKLERLkQVNGMFP |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 17283082 |
Third, we and others have recently shown that only phosphorylated Ci/Gli3 are able to directly bind Slimb/BetaTrCP, that Gli3 is polyubiquitinated in the cell, and that mutations of 4 lysine residues, the putative ubiquitination sites in the Gli3 C-terminal region, inhibit Gli3 processing These observations further support the notion that Ci/Gli3 processing is carried out by the proteasome because the deletion of the cleavage site is expected to often disrupt the protease-mediated site-specific cleavage. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249578 |
Lys800 |
LNPILPPkAPAVSPL |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 17283082 |
Third, we and others have recently shown that only phosphorylated Ci/Gli3 are able to directly bind Slimb/BetaTrCP, that Gli3 is polyubiquitinated in the cell, and that mutations of 4 lysine residues, the putative ubiquitination sites in the Gli3 C-terminal region, inhibit Gli3 processing These observations further support the notion that Ci/Gli3 processing is carried out by the proteasome because the deletion of the cleavage site is expected to often disrupt the protease-mediated site-specific cleavage. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143171 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16371461 |
Phosphorylated gli3 can bind beta-trcp directly both in vitro and in vivo, resulting in polyubiquitination of gli3 and processing through proteasome activity |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| Pathways: | Sonic Hedgehog |
| + |
ATM | up-regulates quantity by stabilization 
phosphorylation
|
BTRC |
0.304 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277549 |
Ser158 |
EFVEHLIsQMCHYQH |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 33676897 |
ATM phosphorylates and stabilizes β-TrCP1 upon DNA damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA1 | down-regulates quantity by destabilization
phosphorylation
|
BTRC |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277475 |
Ser82 |
SLRQTYNsCARLCLN |
Homo sapiens |
SK-BR-3 Cell |
| pmid |
sentence |
| 31406304 |
Glucose deprivation activates AMPK kinase to phosphorylate β-TrCP1 and promotes the subsequent ubiquitination and degradation of β-TrCP1 by β-TrCP2, but does not promote β-TrCP2 degradation by β-TrCP1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | down-regulates quantity by destabilization
ubiquitination
|
GLI1 |
0.649 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235631 |
|
|
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 16421275 |
Here we show that Gli is rapidly destroyed by the proteasome and that mouse basal cell carcinoma induction correlates with Gli protein accumulation. We identify two independent destruction signals in Gli1, D(N) and D(C), and show that removal of these signals stabilizes Gli1 protein and rapidly accelerates tumor formation in transgenic animals.Levels of _TrCP appeared to be limiting for Gli1 degradation, as increasing the levels of _TrCP protein significantly decreased steady-state levels of Gli1 protein |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Sonic Hedgehog |
| + |
BTRC | up-regulates
ubiquitination
|
CDC25A |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128436 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15340381 |
Scfb-trcp has recently been shown to degrade phosphorylated cdc25a in the s and g2 phases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | down-regulates
binding
|
WEE1 |
0.403 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128439 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15340381 |
Scfb-trcp continues to have a role in this phase, however, through its induced degradation of the cdk1 inhibitor, wee1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | down-regulates
ubiquitination
|
YAP1 |
0.527 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201138 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23431053 |
This cascade of phosphorylation allows the binding of scfbetatrcp that promotes the ubiquitination and degradation of yap. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | down-regulates
ubiquitination
|
PER1 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-137755 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15917223 |
We have found that per1 interacts with both _-trcp1 and _-trcp2 in a manner that depends on casein kinase 1 activity, and depletion of both _-trcp1 and _-trcp2 by rnai leads to dramatic stabilization of per1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXW11 | down-regulates quantity by destabilization
binding
|
BTRC |
0.572 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277476 |
|
|
Homo sapiens |
SK-BR-3 Cell |
| pmid |
sentence |
| 31406304 |
Glucose deprivation activates AMPK kinase to phosphorylate β-TrCP1 and promotes the subsequent ubiquitination and degradation of β-TrCP1 by β-TrCP2, but does not promote β-TrCP2 degradation by β-TrCP1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | down-regulates quantity by destabilization
ubiquitination
|
GLI2 |
0.636 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146109 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 16611981 |
The phosphorylated gli2 protein interacts with beta-trcp, and is ubiquitinated and degraded by the proteasome |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Sonic Hedgehog |
| + |
mTORC1 | up-regulates activity
phosphorylation
|
BTRC |
0.291 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267829 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 33861966 |
mTORC1 regulates the stability of CREB2. Our data suggest that mTORC1 promotes the binding of the E3 ligase, βTrCP, to CREB2 (Figure 4D), promoting CREB2 degradation by the proteasome (Figure 4E). Here, we show that mTORC1 promotes glutamine anaplerosis by activating glutamate dehydrogenase (GDH). This regulation requires transcriptional repression of SIRT4, the mitochondrial-localized sirtuin that inhibits GDH. Mechanistically, mTORC1 represses SIRT4 by promoting the proteasome-mediated destabilization of cAMP-responsive element binding 2 (CREB2). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BTRC | down-regulates
ubiquitination
|
EZH2 |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-204481 |
|
|
Homo sapiens |
Lymphoma Cell |
| pmid |
sentence |
| 24469040 |
_-trcp ubiquitinates ezh2 and jak2-mediated phosphorylation on y641 directs _-trcp-mediated ezh2 degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | down-regulates
ubiquitination
|
RAP1GAP |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203548 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25329897 |
Here, we demonstrated that rap1gap is ubiquitinated and degraded through proteasome pathway in mitosis. Proteolysis of rap1gap requires the plk1 kinase and _-trcp ubiquitin ligase complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | down-regulates
ubiquitination
|
SMAD4 |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123057 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14988407 |
Here we show that beta-trcp1, a f-box protein in the scf e3 ligase complex, interacts with smad4 and induces the degradation of smad4 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | up-regulates activity
binding
|
Cullin 1-RBX1-Skp1 |
0.791 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272555 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 10514424 |
Interaction with beta-TrCP is also necessary for ubiquitination of IkappaBbeta upon stimulation of cells, and deletion of the F-box in beta-TrCP abolishes its ability to ubiquitinate IkappaBbeta. Therefore, these results indicate that beta-TrCP plays a critical role in the activation of NF-kappaB by assembling the ubiquitin ligase complex for both phosphorylated IkappaBalpha and IkappaBbeta.β-TrCP recognizes IκBα phosphorylated at Ser-32 and Ser-36 through its WD40 domain, whereas the F-box motif recruits additional proteins including Skp1 and Cullin to form the Skp1-cullin-F-box (SCF) ubiquitin ligase complex |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
BTRC | down-regulates quantity by destabilization
polyubiquitination
|
NFKB1 |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272570 |
|
|
in vitro |
|
| pmid |
sentence |
| 10835356 |
Here we demonstrate that following IkappaB kinase (IkappaK)-mediated phosphorylation, the C-terminal domain of p105 (residues 918-934) serves as a recognition motif for the SCF(beta)(-TrCP) ubiquitin ligase.In vitro, SCF(beta)(-TrCP) specifically conjugates and promotes processing of phosphorylated p105. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BTRC | down-regulates
ubiquitination
|
PDCD4 |
0.435 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160985 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18296647 |
Both akt and p70(s6k) phosphorylate pdcd4, allowing for binding of the e3-ubiquitin ligase beta-trcp and consequently ubiquitylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skin |
| + |
BTRC | form complex 
binding
|
SCF-betaTRCP |
0.818 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-64496 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10023660 |
The human f box protein beta-trcp associates with the cul1/skp1 complex and regulates the stability of beta-catenin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | down-regulates
ubiquitination
|
CTNNB1 |
0.867 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-67374 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10228155 |
Here we show that fwd1 (the mouse homologue of slimb/betatrcp), an f-box/wd40-repeat protein, specifically formed a multi-molecular complex with beta-catenin, axin, gsk-3beta and apc. Mutations at the signal-induced phosphorylation site of beta-catenin inhibited its association with fwd1. Fwd1 facilitated ubiquitination and promoted degradation of beta-catenin, resulting in reduced cytoplasmic beta-catenin levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | down-regulates quantity by destabilization
binding
|
NFKBIB |
0.564 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272554 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 10514424 |
Interaction with beta-TrCP is also necessary for ubiquitination of IkappaBbeta upon stimulation of cells, and deletion of the F-box in beta-TrCP abolishes its ability to ubiquitinate IkappaBbeta. Therefore, these results indicate that beta-TrCP plays a critical role in the activation of NF-kappaB by assembling the ubiquitin ligase complex for both phosphorylated IkappaBalpha and IkappaBbeta.β-TrCP recognizes IκBα phosphorylated at Ser-32 and Ser-36 through its WD40 domain, whereas the F-box motif recruits additional proteins including Skp1 and Cullin to form the Skp1-cullin-F-box (SCF) ubiquitin ligase complex |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
BTRC |
0.791 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277477 |
|
|
Homo sapiens |
SK-BR-3 Cell |
| pmid |
sentence |
| 31406304 |
Glucose deprivation activates AMPK kinase to phosphorylate β-TrCP1 and promotes the subsequent ubiquitination and degradation of β-TrCP1 by β-TrCP2, but does not promote β-TrCP2 degradation by β-TrCP1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | down-regulates
ubiquitination
|
SMAD3 |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-108237 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11359933 |
An e3 ubiquitin ligase complex roc1-scffbw1a consisting of roc1, skp1, cullin1, and fbw1a (also termed trcp1) induces ubiquitination of smad3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTRC | down-regulates quantity by destabilization
ubiquitination
|
ATF2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267830 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 33861966 |
Our data suggest that mTORC1 promotes the binding of the E3 ligase, βTrCP, to CREB2 (Figure 4D), promoting CREB2 degradation by the proteasome (Figure 4E). Here, we show that mTORC1 promotes glutamine anaplerosis by activating glutamate dehydrogenase (GDH). This regulation requires transcriptional repression of SIRT4, the mitochondrial-localized sirtuin that inhibits GDH. Mechanistically, mTORC1 represses SIRT4 by promoting the proteasome-mediated destabilization of cAMP-responsive element binding 2 (CREB2). |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
BTRC
- 
- 