| + |
CHUK | up-regulates activity 
phosphorylation
|
BCL3 |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277362 |
Ser122 |
CPMEHPLsADIAMAT |
in vitro |
|
| pmid |
sentence |
| 28689659 |
Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277363 |
Ser454 |
PSPAPGGs |
in vitro |
|
| pmid |
sentence |
| 28689659 |
Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MAPK1 | up-regulates activity
phosphorylation
|
BCL3 |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277360 |
Ser122 |
CPMEHPLsADIAMAT |
in vitro |
|
| pmid |
sentence |
| 28689659 |
Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277361 |
Ser454 |
PSPAPGGs |
in vitro |
|
| pmid |
sentence |
| 28689659 |
Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
IKBKB | up-regulates activity
phosphorylation
|
BCL3 |
0.361 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277364 |
Ser122 |
CPMEHPLsADIAMAT |
in vitro |
|
| pmid |
sentence |
| 28689659 |
Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277365 |
Ser454 |
PSPAPGGs |
in vitro |
|
| pmid |
sentence |
| 28689659 |
Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
GSK3A | down-regulates quantity by destabilization 
phosphorylation
|
BCL3 |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276011 |
Ser402 |
LSASPSSsPSQSPPR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15469820 |
In this report, we show that BCL-3 is a substrate for the protein kinase GSK3 and that GSK3-mediated BCL-3 phosphorylation, which is inhibited by Akt activation, targets its degradation through the proteasome pathway. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276012 |
Ser406 |
PSSSPSQsPPRDPPG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 15469820 |
In this report, we show that BCL-3 is a substrate for the protein kinase GSK3 and that GSK3-mediated BCL-3 phosphorylation, which is inhibited by Akt activation, targets its degradation through the proteasome pathway. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates quantity by stabilization
phosphorylation
|
BCL3 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277359 |
Ser41 |
KRPLRAPsPEPAAPR |
in vitro |
|
| pmid |
sentence |
| 28689659 |
Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AKT1 | up-regulates quantity by stabilization
phosphorylation
|
BCL3 |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277358 |
Ser41 |
KRPLRAPsPEPAAPR |
in vitro |
|
| pmid |
sentence |
| 28689659 |
Here we show that Akt, Erk2, and IKK1/2 phosphorylate Bcl3. Phosphorylation of Ser33 by Akt induces switching of K48 ubiquitination to K63 ubiquitination and thus promotes nuclear localization and stabilization of Bcl3. Phosphorylation by Erk2 and IKK1/2 of Ser114 and Ser446 converts Bcl3 into a transcriptional coregulator by facilitating its recruitment to DNA. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
DMTF1 | up-regulates quantity by expression 
transcriptional regulation
|
BCL3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261583 |
|
|
Mus musculus |
C-10 Cell |
| pmid |
sentence |
| 19816943 |
Notably, amphiregulin (Areg), thrombospondin-1 (Tsp-1), JunB, Egr1, adrenomedullin (Adm), Bcl-3 and methyl-CpG binding domain protein 1 (Mbd1) were downregulated in the lungs from Dmp1-null mice while Gas1 and Ect2 genes were upregulated. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BCL3 | up-regulates quantity by expression
transcriptional regulation
|
MDM2 |
0.284 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143403 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16384933 |
One mechanism by which this inhibition occurs is through bcl-3-mediated induction of the p53 inhibitor hdm2. Both stable and transient overexpression of bcl-3 leads to increased hdm2 expression, and small interfering rna (sirna)-mediated knockdown of bcl-3 blocks expression of hdm2. ( articolo-abstract) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL3 | up-regulates
binding
|
HDAC3 |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129804 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15469820 |
We show that bcl-3 is a substrate for the protein kinase gsk3 and that gsk3-mediated bcl-3 phosphorylation, which is inhibited by akt activation, targets its degradation through the proteasome pathway. This phosphorylation modulates its association with hdac1, 3 and 6. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL3 | up-regulates
binding
|
HDAC1 |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129801 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15469820 |
We show that bcl-3 is a substrate for the protein kinase gsk3 and that gsk3-mediated bcl-3 phosphorylation, which is inhibited by akt activation, targets its degradation through the proteasome pathway. This phosphorylation modulates its association with hdac1, -3, and -6 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL3 | down-regulates quantity by repression 
transcriptional regulation
|
CTCF |
0.297 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253757 |
|
|
Homo sapiens |
Corneal Epithelial Cell |
| pmid |
sentence |
| 21912613 |
In the present study, we report that regulation of CTCF by extracellular stress signals is dependent upon activations of an oxidative stress-regulated protein Bcl-3. We found that activated Bcl-3 was able to bind to the κB sites identified in the CTCF promoter region. Bcl-3 was activated by UV irradiation to interact with NF-κB p50 by forming a Bcl-3/p50 heterodimer complex. The Bcl-3/p50 complex suppressed CTCF promoter activity to down-regulate CTCF transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL3 | up-regulates activity
binding
|
NFKB1 |
0.603 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254789 |
|
|
Homo sapiens |
Corneal Epithelial Cell |
| pmid |
sentence |
| 21912613 |
In the present study, we report that regulation of CTCF by extracellular stress signals is dependent upon activations of an oxidative stress-regulated protein Bcl-3. We found that activated Bcl-3 was able to bind to the κB sites identified in the CTCF promoter region. Bcl-3 was activated by UV irradiation to interact with NF-κB p50 by forming a Bcl-3/p50 heterodimer complex. The Bcl-3/p50 complex suppressed CTCF promoter activity to down-regulate CTCF transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL3 | up-regulates
|
NFKB2 |
0.589 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146771 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16713561 |
The cyclin d1 elevation is caused not by increased p65/p50 action but rather by increased nuclear activity of bcl-3-associated nf-kappab p50 and p52 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TBL1XR1 | down-regulates
ubiquitination
|
BCL3 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166111 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20547759 |
We also defined the e3 ligase tblr1 as a protein involved in bcl-3 degradation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CRTC3 | up-regulates
binding
|
BCL3 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156950 |
|
|
Homo sapiens |
Leukemia Cell, B-lymphocyte, Tongue Cancer Cell Line |
| pmid |
sentence |
| 17644518 |
The ankyrin repeat domain of bcl3 interacted with torc3 / we determined that bcl3 inhibited transcription from the htlv-1 ltr in a manner dependent on torc3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CYLD | down-regulates
deubiquitination
|
BCL3 |
0.501 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146774 |
|
|
Homo sapiens |
Skin Cancer Cell |
| pmid |
sentence |
| 16713561 |
Cyld binds and deubiquitinates bcl-3in cyld+/+ keratinocytes, tpa or uv light triggers the translocation of cyld from the cytoplasm to the perinuclear region, where cyld binds and deubiquitinates bcl-3, thereby preventing nuclear accumulation of bcl-3 and p50/bcl-3- or p52/bcl-3-dependent proliferation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL3 | up-regulates
binding
|
NFKB2 |
0.589 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146768 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16713561 |
The cyclin d1 elevation is caused not by increased p65/p50 action but rather by increased nuclear activity of bcl-3-associated nf-kappab p50 and p52. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
BCL3
- 
- 