| + |
MAP4K1 | up-regulates activity 
phosphorylation
|
CARD11 |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276259 |
Ser556 |
TKMQPPRsRSSIMSI |
in vitro |
|
| pmid |
sentence |
| 19706536 |
HPK1 interacts with CARMA1 in a TCR stimulation-dependent manner and phosphorylates the linker region of CARMA1. Interestingly, the putative HPK1 phosphorylation sites in CARMA1 are different from known PKC consensus sites. Mutations of residues S549, S551, and S552 in CARMA1 abrogated phosphorylation of a CARMA1-linker construct by HPK1 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276257 |
Ser558 |
MQPPRSRsSIMSITA |
in vitro |
|
| pmid |
sentence |
| 19706536 |
HPK1 interacts with CARMA1 in a TCR stimulation-dependent manner and phosphorylates the linker region of CARMA1. Interestingly, the putative HPK1 phosphorylation sites in CARMA1 are different from known PKC consensus sites. Mutations of residues S549, S551, and S552 in CARMA1 abrogated phosphorylation of a CARMA1-linker construct by HPK1 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276258 |
Ser559 |
QPPRSRSsIMSITAE |
in vitro |
|
| pmid |
sentence |
| 19706536 |
HPK1 interacts with CARMA1 in a TCR stimulation-dependent manner and phosphorylates the linker region of CARMA1. Interestingly, the putative HPK1 phosphorylation sites in CARMA1 are different from known PKC consensus sites. Mutations of residues S549, S551, and S552 in CARMA1 abrogated phosphorylation of a CARMA1-linker construct by HPK1 in vitro. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
AKT1 | up-regulates activity
phosphorylation
|
CARD11 |
0.538 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276254 |
Ser558 |
MQPPRSRsSIMSITA |
in vitro |
|
| pmid |
sentence |
| 24548923 |
Here we show that Akt-mediated NF-κB activation is mediated at least in part through direct phosphorylation of the adaptor protein Carma1, which we previously demonstrated could interact with Akt in a TCR ligation-dependent manner. The putative Akt phosphorylation sites in Carma1 are distinct from known PKC consensus sites. Mutation of S551, S637 and S645 in Carma1 to non-phosphorylatable residues decreased phosphorylation of GST-Carma1-linker construct by Akt in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276621 |
Ser644 |
NLMFRKFsLERPFRP |
in vitro |
|
| pmid |
sentence |
| 24548923 |
Akt phosphorylates S637 and S645 in the linker region of Carma1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276255 |
Ser644 |
NLMFRKFsLERPFRP |
in vitro |
|
| pmid |
sentence |
| 24548923 |
Here we show that Akt-mediated NF-κB activation is mediated at least in part through direct phosphorylation of the adaptor protein Carma1, which we previously demonstrated could interact with Akt in a TCR ligation-dependent manner. The putative Akt phosphorylation sites in Carma1 are distinct from known PKC consensus sites. Mutation of S551, S637 and S645 in Carma1 to non-phosphorylatable residues decreased phosphorylation of GST-Carma1-linker construct by Akt in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276256 |
Ser652 |
LERPFRPsVTSVGHV |
in vitro |
|
| pmid |
sentence |
| 24548923 |
Here we show that Akt-mediated NF-κB activation is mediated at least in part through direct phosphorylation of the adaptor protein Carma1, which we previously demonstrated could interact with Akt in a TCR ligation-dependent manner. The putative Akt phosphorylation sites in Carma1 are distinct from known PKC consensus sites. Mutation of S551, S637 and S645 in Carma1 to non-phosphorylatable residues decreased phosphorylation of GST-Carma1-linker construct by Akt in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276620 |
Ser652 |
LERPFRPsVTSVGHV |
in vitro |
|
| pmid |
sentence |
| 24548923 |
Akt phosphorylates S637 and S645 in the linker region of Carma1 |
|
| Publications: |
5 |
Organism: |
In Vitro |
| + |
PPP2CB | down-regulates activity 
dephosphorylation
|
CARD11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248607 |
Ser644 |
NLMFRKFsLERPFRP |
Homo sapiens |
|
| pmid |
sentence |
| 21157432 |
NF-kappaB activation is triggered by PKCtheta-dependent phosphorylation of Carma1 after TCR/CD28 co-stimulation. PKCtheta-phosphorylated Carma1 was suggested to function as a molecular scaffold that recruits preassembled Bcl10-Malt1 complexes to the membrane|we demonstrate that PP2A removes PKCtheta-dependent phosphorylation of Ser645 in Carma1, and show that maintenance of this phosphorylation is correlated with increased T-cell activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | up-regulates activity
phosphorylation
|
CARD11 |
0.767 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249193 |
Ser644 |
NLMFRKFsLERPFRP |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 21157432 |
NF-kappaB activation is triggered by PKCteta-dependent phosphorylation of Carma1 after TCR/CD28 co-stimulation. PKCteta-phosphorylated Carma1 was suggested to function as a molecular scaffold that recruits preassembled Bcl10-Malt1 complexes to the membrane|we demonstrate that PP2A removes PKCteta-dependent phosphorylation of Ser645 in Carma1, and show that maintenance of this phosphorylation is correlated with increased T-cell activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2CA | down-regulates activity
dephosphorylation
|
CARD11 |
0.314 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248650 |
Ser644 |
NLMFRKFsLERPFRP |
Homo sapiens |
|
| pmid |
sentence |
| 21157432 |
NF-kappaB activation is triggered by PKCtheta-dependent phosphorylation of Carma1 after TCR/CD28 co-stimulation. PKCtheta-phosphorylated Carma1 was suggested to function as a molecular scaffold that recruits preassembled Bcl10-Malt1 complexes to the membrane|we demonstrate that PP2A removes PKCtheta-dependent phosphorylation of Ser645 in Carma1, and show that maintenance of this phosphorylation is correlated with increased T-cell activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | down-regulates activity
phosphorylation
|
CARD11 |
0.767 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276298 |
Ser893 |
SPRLSRAsFLFGQLL |
in vitro |
|
| pmid |
sentence |
| 35230873 |
PKCθ-catalyzed CARD11 Ser893 phosphorylation impairs CBM complex formation |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PDPK1 | up-regulates
phosphorylation
|
CARD11 |
0.53 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134866 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 15802604 |
We demonstrate that 3-phosphoinositide-dependent kinase 1 (pdk1) has an essential role in this pathway by regulating the activation of pkc and through signal-dependent recruiting of both pkc and card11 to lipid rafts. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CARD11 | up-regulates
binding
|
MALT1 |
0.798 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167393 |
|
|
Homo sapiens |
Lymphoma Cell |
| pmid |
sentence |
| 20685844 |
The carboxy-terminal part of the bcl10 card and a short stretch of 13 amino acids following the card are required for constitutive binding to malt1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CARD11 | form complex 
binding
|
CBM |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276296 |
|
|
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
CARD11
- 
- 