+ |
ITK | up-regulates
phosphorylation
|
CD28 |
0.677 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198747 |
Tyr191 |
SRLLHSDyMNMTPRR |
Homo sapiens |
|
pmid |
sentence |
22936936 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tail, in contrast to lck, which phosphorylates only tyrosine 173. Together with evidence that in vivo, tyrosines other than tyrosine 173 become phosphorylated following cd28 stimulation, this finding suggests that, like lck, one function of emt during cd28 signaling is phosphorylation of the receptor |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45512 |
Tyr191 |
SRLLHSDyMNMTPRR |
Homo sapiens |
T-lymphocyte, Leukemia Cell |
pmid |
sentence |
8992971 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tail, in contrast to lck, which phosphorylates only tyrosine 173. Together with evidence that in vivo, tyrosines other than tyrosine 173 become phosphorylated following cd28 stimulation, this finding suggests that, like lck, one function of emt during cd28 signaling is phosphorylation of the receptor |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198751 |
Tyr209 |
TRKHYQPyAPPRDFA |
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
22936936 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tailother studies demonstrated that tyr191 within the p190yap motif is one of two major phosphorylation sites in cd28-stimulated jurkat t cells, and the only tyrosine residue within the cd28 cytoplasmic tail that is essential for delivery of costimulatory signals |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45516 |
Tyr209 |
TRKHYQPyAPPRDFA |
Homo sapiens |
T-lymphocyte, Leukemia Cell |
pmid |
sentence |
8992971 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tailother studies demonstrated that tyr191 within the p190yap motif is one of two major phosphorylation sites in cd28-stimulated jurkat t cells, and the only tyrosine residue within the cd28 cytoplasmic tail that is essential for delivery of costimulatory signals |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45520 |
Tyr218 |
PPRDFAAyRS |
Homo sapiens |
T-lymphocyte, Leukemia Cell |
pmid |
sentence |
8992971 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tail |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
ITK | up-regulates activity
phosphorylation
|
CD28 |
0.677 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251336 |
Tyr191 |
SRLLHSDyMNMTPRR |
|
|
pmid |
sentence |
8992971 |
EMT can phosphorylate all four tyrosines of the CD28 tail. in vivo, tyrosines other than tyrosine 173 become phosphorylated following CD28 stimulation, this finding suggests that, like LCK, one function of EMT during CD28 signaling is phosphorylation of the receptor. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251334 |
Tyr206 |
PGPTRKHyQPYAPPR |
|
|
pmid |
sentence |
8992971 |
EMT can phosphorylate all four tyrosines of the CD28 tail. in vivo, tyrosines other than tyrosine 173 become phosphorylated following CD28 stimulation, this finding suggests that, like LCK, one function of EMT during CD28 signaling is phosphorylation of the receptor. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251337 |
Tyr218 |
PPRDFAAyRS |
|
|
pmid |
sentence |
8992971 |
EMT can phosphorylate all four tyrosines of the CD28 tail. in vivo, tyrosines other than tyrosine 173 become phosphorylated following CD28 stimulation, this finding suggests that, like LCK, one function of EMT during CD28 signaling is phosphorylation of the receptor. |
|
Publications: |
3 |
+ |
LCK | up-regulates
phosphorylation
|
CD28 |
0.745 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45524 |
Tyr191 |
SRLLHSDyMNMTPRR |
Homo sapiens |
T-lymphocyte, Leukemia Cell |
pmid |
sentence |
8992971 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tail, in contrast to lck, which phosphorylates only tyrosine 173. Together with evidence that in vivo, tyrosines other than tyrosine 173 become phosphorylated following cd28 stimulation, this finding suggests that, like lck, one function of emt during cd28 signaling is phosphorylation of the receptor |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198755 |
Tyr191 |
SRLLHSDyMNMTPRR |
Homo sapiens |
|
pmid |
sentence |
22936936 |
We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tail, in contrast to lck, which phosphorylates only tyrosine 173. Together with evidence that in vivo, tyrosines other than tyrosine 173 become phosphorylated following cd28 stimulation, this finding suggests that, like lck, one function of emt during cd28 signaling is phosphorylation of the receptor |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | T cell activation |
+ |
CD28 | up-regulates
binding
|
GRB2 |
0.69 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-202706 |
|
|
Homo sapiens |
|
pmid |
sentence |
24098653 |
Binding of the py site in cd28 (py-m-n-m) by pi3k and grb2 through their sh2 domains is a key step that triggers the cd28 signal transduction for t cell activation and differentiation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-32509 |
|
|
Homo sapiens |
|
pmid |
sentence |
7737275 |
In this study, we demonstrate that the co-stimulatory antigen cd28 binds to grb-2 by means of a cytoplasmic pymnm motif, which is the same motif bound by pi 3-kinase. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | T cell activation |
+ |
CD28 | up-regulates
binding
|
PIK3CG |
0.376 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159322 |
|
|
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
18006698 |
Cd28 can bind directly to pi3k by a well-characterized ymnm binding motif in its cytoplasmic domain. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |