+ |
CD247 | form complex
binding
|
CD3 |
0.694 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-255290 |
|
|
Homo sapiens |
|
pmid |
sentence |
12507424 |
The T cell receptor-CD3 complex (TCR-CD3) serves a critical role in the differentiation, survival, and function of T cells, and receptor triggering elicits a complex set of biological responses that serve to protect the organism from infectious agents. The receptor is composed of six different chains that form the TCR heterodimer responsible for ligand recognition, as well as the CD3γε, CD3δε, and ζζ signaling modules. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | T cell activation |
+ |
LCK | up-regulates
phosphorylation
|
CD247 |
0.755 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-41361 |
|
|
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
8626561 |
During tcr signaling, lck interacts with numerous molecules, including tcr-zeta. The binding of lck to the tyrosine-phosphorylated zeta chain of the tcr would serve to strengthen the interaction of the associated cd4 and the tcr complex, leading to increased avidity for the antigen-major histocompatibility protein complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | T cell activation |
+ |
PTPN22 | down-regulates
dephosphorylation
|
CD247 |
0.458 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-144337 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16461343 |
T cell signaling is negatively regulated by the activity of protein-tyrosine phosphatases. Native ptpn22 dephosphorylated tcrzeta in vitro and in cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN22 | down-regulates activity
dephosphorylation
|
CD247 |
0.458 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248837 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16461343 |
In vitro experiments with purified recombinant proteins demonstrated that PTPN22-D195A/C227S interacted directly with activated Lck, Zap70, and TCRzeta, confirming the initial substrate trap results. Native PTPN22 dephosphorylated Lck and Zap70 at their activating tyrosine residues Tyr-394 and Tyr-493, respectively, but not at the regulatory tyrosines Tyr-505 (Lck) or Tyr-319 (Zap70). Native PTPN22 also dephosphorylated TCRzeta in vitro and in cells, and its substrate trap variant co-immunoprecipitated with TCRzeta when both were coexpressed in 293T cells, establishing TCRzeta as a direct substrate of PTPN22. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |