| + |
FYN | up-regulates quantity by stabilization 
phosphorylation
|
CTLA4 |
0.762 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251161 |
Tyr201 |
SPLTTGVyVKMPPTE |
Homo sapiens |
|
| pmid |
sentence |
| 9973379 |
CTLA-4 can associate with the Src kinases Fyn and Lck and that transfection of Fyn or Lck, but not the unrelated kinase ZAP70, can induce tyrosine phosphorylation of CTLA-4 on residues Y201 and Y218.  Phosphorylation of CTLA-4 Y201 in Jurkat cells correlated with cell surface accumulation of CTLA-4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates quantity by stabilization
phosphorylation
|
CTLA4 |
0.456 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251346 |
Tyr201 |
SPLTTGVyVKMPPTE |
Homo sapiens |
|
| pmid |
sentence |
| 10842319 |
Janus Kinase 2 (Jak2) was directly associated with a box 1-like motif in the cytoplasmic tail of CTLA-4 molecule. Jak2 phosphorylated Y-165 residue in the cytoplasmic region of CTLA-4. It has been reported that phosphorylation and dephosphorylation of tyrosine residue Y-165 in the cytoplasmic region of CTLA-4 play an important role in its negative signaling and cell surface expression. Some signaling molecules such as Src homology 2 protein tyrosine phosphatase 2 (SHP-2) and the p85 subunit of phosphatidylinositol 3 kinase (PI3 kinase) associate with phosphorylated tyrosine residue Y-165, through Src homology 2 (SH2) domains. On the other hand, the adapter complex proteins, AP-2 and AP-50 interact with the same tyrosine residue when unphosphorylated, resulting in clathrin-mediated endocytosis of CTLA-4 molecules. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TXK | up-regulates quantity by stabilization
phosphorylation
|
CTLA4 |
0.513 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-61624 |
Tyr201 |
SPLTTGVyVKMPPTE |
Homo sapiens |
|
| pmid |
sentence |
| 9813138 |
We demonstrate that rlk (resting lymphocyte kinase) is capable of phosphorylating ctla-4 at the yvkm motif. Consistent with this finding, rlk is capable of providing conditions for the binding of the sh2 domains of pi 3-kinase to the receptor. Ctla-4 is therefore the first known substrate for rlk suggesting the possibility that this kinase may participate in ctla-4 function |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LCK | up-regulates quantity by stabilization
phosphorylation
|
CTLA4 |
0.74 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251370 |
Tyr201 |
SPLTTGVyVKMPPTE |
Homo sapiens |
|
| pmid |
sentence |
| 9973379 |
Lck and Fyn, but not ZAP70, induce tyrosine phosphorylation of CTLA-4 in the cell line HEK293. Phosphorylation of CTLA-4 occurs on both Y201 and Y218. Phosphorylation of Y201 correlated with accumulation of CTLA-4 on the cell surface. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LCK |
phosphorylation
|
CTLA4 |
0.74 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251371 |
Tyr218 |
CEKQFQPyFIPIN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 9973379 |
Lck and Fyn, but not ZAP70, induce tyrosine phosphorylation of CTLA-4 in the cell line HEK293. Phosphorylation of CTLA-4 occurs on both Y201 and Y218.the role of Y218 in CTLA-4 biology is not known at the present |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FYN |
phosphorylation
|
CTLA4 |
0.762 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251160 |
Tyr218 |
CEKQFQPyFIPIN |
Homo sapiens |
|
| pmid |
sentence |
| 9973379 |
CTLA-4 can associate with the Src kinases Fyn and Lck and that transfection of Fyn or Lck, but not the unrelated kinase ZAP70, can induce tyrosine phosphorylation of CTLA-4 on residues Y201 and Y218. Phosphorylation of CTLA-4 Y201 in Jurkat cells correlated with cell surface accumulation of CTLA-4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTLA4 | down-regulates activity 
|
AKT |
0.589 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275409 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16227604 |
Akt phosphorylation in cells stimulated by CD3/CD28/CTLA-4 or CD3/CD28/PD-1 aAPCs did not have detectable phosphorylated Akt at any time point, indicating that CTLA-4 and PD-1 signaling blocked rather than delayed Akt activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTLA4 | up-regulates 
|
T cell exhaustion |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275415 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 26086965 |
Both PD-1 and CTLA-4 inhibited the activity of Akt, a crucial molecular in regulating glucose metabolism of T cells by elevating glucose transporter 1 expression and glycolysis, suggesting that glucose metabolism may contribute to T-cell exhaustion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ipilimumab | down-regulates activity 
binding
|
CTLA4 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259894 |
|
|
Homo sapiens |
Metastatic Renal Cell Carcinoma Cell |
| pmid |
sentence |
| 18049334 |
The inhibitory receptor CTLA4 has a key role in peripheral tolerance of T cells for both normal and tumor-associated antigens. CTLA4 blockade with ipilimumab induces cancer regression in some patients with metastatic clear cell renal cancer, even if they have not responded to other immunotherapies. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CTLA4
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