| + |
LCK | up-regulates activity 
phosphorylation
|
DEF6 |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253367 |
Tyr133 |
NFLSEDKyPLIMVPD |
Homo sapiens |
|
| pmid |
sentence |
| 18976935 |
Here, we report that the T cell receptor (TCR)-induced translocation of SLAT to the immunological synapse required Lck-mediated phosphorylation of two tyrosine residues located in an immunoreceptor tyrosine-based activation motif-like sequence but was independent of the SLAT PH domain. This subcellular relocalization was coupled to, and necessary for, activation of the NFAT pathway|These results indicate that SLAT undergoes Lck-dependent phosphorylation on Tyr-144 and Tyr-133 upon TCR and CD28 stimulation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253368 |
Tyr144 |
MVPDEVEyLLKKVLS |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 18976935 |
Here, we report that the T cell receptor (TCR)-induced translocation of SLAT to the immunological synapse required Lck-mediated phosphorylation of two tyrosine residues located in an immunoreceptor tyrosine-based activation motif-like sequence but was independent of the SLAT PH domain. This subcellular relocalization was coupled to, and necessary for, activation of the NFAT pathway|These results indicate that SLAT undergoes Lck-dependent phosphorylation on Tyr-144 and Tyr-133 upon TCR and CD28 stimulation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251372 |
Tyr210 |
SMAIHEVyQELIQDV |
in vitro |
|
| pmid |
sentence |
| 12923183 |
In vitro kinase assays indeed demonstrated that Lck can phosphorylate wild-type IBP but not the Y210F mutant. IBP Binds PI(3,4,5)P3 upon Phosphorylation by Lck |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, In Vitro |
| + |
DEF6 | up-regulates activity
binding
|
RAP1A |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253365 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 26483383 |
Mechanistic studies revealed that SLAT interacts, through its PH domain, with a key component of inside-out signaling, namely the active form of the small GTPase Rap1 (which has two isoforms, Rap1A and Rap1B). This interaction has been further shown to facilitate the interdependent recruitment of Rap1 and SLAT to the T cell immunological synapse upon TCR engagement. Furthermore, a SLAT mutant lacking its PH domain drastically inhibited LFA-1 activation and CD4(+) T cell adhesion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DEF6 | up-regulates activity
guanine nucleotide exchange factor
|
CDC42 |
0.401 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253369 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18976935 |
Furthermore, membrane targeting of the SLAT Dbl-homology (catalytic) domain was sufficient to trigger TCR-mediated NFAT activation and Th1 and Th2 differentiation in a Cdc42-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DEF6 | up-regulates activity
binding
|
RAP1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253366 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 26483383 |
Mechanistic studies revealed that SLAT interacts, through its PH domain, with a key component of inside-out signaling, namely the active form of the small GTPase Rap1 (which has two isoforms, Rap1A and Rap1B). This interaction has been further shown to facilitate the interdependent recruitment of Rap1 and SLAT to the T cell immunological synapse upon TCR engagement. Furthermore, a SLAT mutant lacking its PH domain drastically inhibited LFA-1 activation and CD4(+) T cell adhesion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
DEF6
- 
- 