| + |
IKBKB | up-regulates activity 
phosphorylation
|
BCL10 |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276291 |
Ser134 |
DGATNNLsRSNSDES |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16818229 |
Here we show that the putative downstream kinase IKKbeta is required for initial CBM complex formation. Further, upon engagement of IKKbeta/Malt1/Bcl10 with Carma1, IKKbeta phosphorylates Bcl10 in the C terminus and thereby interferes with Bcl10/Malt1 association and Bcl10-mediated IKKgamma ubiquitination. Since only mutation of all serines 134, 136, 138, 141, and 144 completely prevented signal-induced Bcl10 phosphorylation, the Bcl10 5×S/A mutant was used to elucidate the effects of C-terminal Bcl10 phosphorylation on downstream signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276290 |
Ser136 |
ATNNLSRsNSDESNF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16818229 |
Here we show that the putative downstream kinase IKKbeta is required for initial CBM complex formation. Further, upon engagement of IKKbeta/Malt1/Bcl10 with Carma1, IKKbeta phosphorylates Bcl10 in the C terminus and thereby interferes with Bcl10/Malt1 association and Bcl10-mediated IKKgamma ubiquitination. Since only mutation of all serines 134, 136, 138, 141, and 144 completely prevented signal-induced Bcl10 phosphorylation, the Bcl10 5×S/A mutant was used to elucidate the effects of C-terminal Bcl10 phosphorylation on downstream signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276292 |
Ser138 |
NNLSRSNsDESNFSE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16818229 |
Here we show that the putative downstream kinase IKKbeta is required for initial CBM complex formation. Further, upon engagement of IKKbeta/Malt1/Bcl10 with Carma1, IKKbeta phosphorylates Bcl10 in the C terminus and thereby interferes with Bcl10/Malt1 association and Bcl10-mediated IKKgamma ubiquitination. Since only mutation of all serines 134, 136, 138, 141, and 144 completely prevented signal-induced Bcl10 phosphorylation, the Bcl10 5×S/A mutant was used to elucidate the effects of C-terminal Bcl10 phosphorylation on downstream signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276293 |
Ser141 |
SRSNSDEsNFSEKLR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16818229 |
Here we show that the putative downstream kinase IKKbeta is required for initial CBM complex formation. Further, upon engagement of IKKbeta/Malt1/Bcl10 with Carma1, IKKbeta phosphorylates Bcl10 in the C terminus and thereby interferes with Bcl10/Malt1 association and Bcl10-mediated IKKgamma ubiquitination. Since only mutation of all serines 134, 136, 138, 141, and 144 completely prevented signal-induced Bcl10 phosphorylation, the Bcl10 5×S/A mutant was used to elucidate the effects of C-terminal Bcl10 phosphorylation on downstream signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276289 |
Ser144 |
NSDESNFsEKLRAST |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16818229 |
Here we show that the putative downstream kinase IKKbeta is required for initial CBM complex formation. Further, upon engagement of IKKbeta/Malt1/Bcl10 with Carma1, IKKbeta phosphorylates Bcl10 in the C terminus and thereby interferes with Bcl10/Malt1 association and Bcl10-mediated IKKgamma ubiquitination. Since only mutation of all serines 134, 136, 138, 141, and 144 completely prevented signal-induced Bcl10 phosphorylation, the Bcl10 5×S/A mutant was used to elucidate the effects of C-terminal Bcl10 phosphorylation on downstream signaling. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
BCL10 | up-regulates quantity by expression 
transcriptional regulation
|
NFKB1 |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274145 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14695475 |
The adaptor protein Bcl10 promotes activation of NF-κB transcription factors through paracaspase- and UBC13-dependent ubiquitination of NEMO. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITCH | down-regulates quantity by destabilization 
ubiquitination
|
BCL10 |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271413 |
|
|
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 15082780 |
The HECT domain ubiquitin ligases NEDD4 and Itch promote ubiquitination and degradation of Bcl10, thus downmodulating NF-kappa B activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271414 |
|
|
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 15082780 |
The HECT domain ubiquitin ligases NEDD4 and Itch promote ubiquitination and degradation of Bcl10, thus downmodulating NF-kappa B activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CARD9 | up-regulates quantity by stabilization
binding
|
BCL10 |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257602 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11053425 |
To identify upstream signaling partners of BCL10, we performed a mammalian two-hybrid analysis and identified CARD9 as a novel CARD-containing protein that interacts selectively with the CARD activation domain of BCL10. When expressed in cells, CARD9 binds to BCL10 and activates NF-kappaB. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IKBKG | up-regulates activity
ubiquitination
|
BCL10 |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274149 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14695475 |
Here we show that Bcl10 targets NEMO for lysine-63-linked ubiquitination. Notably, a mutant form of NEMO that cannot be ubiquitinated inhibited Bcl10-induced NF-κB activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL10 | up-regulates
binding
|
IKBKG |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18287044 |
Here, we show that bcl10 undergoes k63-linked polyubiquitination in response to t cell activation and subsequently binds nemo, the regulatory subunit of ikk. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCL10 | form complex 
binding
|
CBM |
0.827 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276294 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15122200 |
CARMA1, the adaptor protein BCL-10 (B-cell lymphoma 10) and the caspase-like protein MALT1 (mucosa-associated lymphoid tissue lymphoma translocation protein 1) form a signalling complex that has a key role in antigen-receptor-mediated activation of the nuclear factor-κB (NF-κB) and JUN N-terminal kinase (JNK) pathways. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CARD11 | up-regulates
binding
|
BCL10 |
0.841 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93869 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12356734 |
Card11 cooperates with bcl10 in a card domain-dependent manner.;These results implicate card11 in factor- specific activation of nf-kappab |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BCL10
- 
- 