+ |
PRKCD | down-regulates
phosphorylation
|
PTPN22 |
0.318 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159591 |
Ser35 |
FLKLKRQsTKYKADK |
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
18056643 |
We show that lyp is phosphorylated exclusively at ser-35 by pkc both in vitro and in vivo. our data establish a mechanism by which pkc could attenuate the cellular function of lyp, thereby augmenting t cell activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN22 | down-regulates
dephosphorylation
|
CBL |
0.395 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-65405 |
Ser798 |
SDISNASsSFGWLSL |
Homo sapiens |
T-lymphocyte |
pmid |
sentence |
10068674 |
The tyrosine phosphatase lyp1 was found to be constitutively associated with the proto-oncogene c-cbl in thymocytes and t cells. Overexpression of lyp1 reduces cbl tyrosine phosphorylation. It is known that cbl is heavily tyrosine phosphorylated after tcr stimulation and can associate with the syk and zap tyrosine kinases, negatively regulating their activities. Tyrosine phosphatases keep cbl in a basally dephosphorylated state. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN22 | down-regulates activity
dephosphorylation
|
LCK |
0.741 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248836 |
Tyr394 |
RLIEDNEyTAREGAK |
Homo sapiens |
|
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 |
+ |
PTPN22 | down-regulates
dephosphorylation
|
LCK |
0.741 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-144341 |
Tyr394 |
RLIEDNEyTAREGAK |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16461343 |
Native ptpn22 dephosphorylated lck at its activating tyrosine residues tyr-394. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN22 | down-regulates activity
dephosphorylation
|
ZAP70 |
0.693 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248838 |
Tyr493 |
LGADDSYyTARSAGK |
Homo sapiens |
|
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 |
+ |
PTPN22 | down-regulates
dephosphorylation
|
ZAP70 |
0.693 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-144345 |
Tyr493 |
LGADDSYyTARSAGK |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16461343 |
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). |
|
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 |
+ |
PTPN22 | up-regulates activity
dephosphorylation
|
NLRP3 |
0.364 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277056 |
|
|
Homo sapiens |
|
pmid |
sentence |
28786745 |
Further, this explains how loss of PTPN22 and subsequent enhanced NLRP3 phosphorylation mediate a decrease in NLRP3 inflammasome activation.|Upon NLRP3 activation, PTPN22 dephosphorylates NLRP3 and thereby protects it from degradation, allowing robust inflammasome activity (summarized in Fig.S6). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
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 |