| + |
CDK1 |
phosphorylation
|
PTPN2 |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123467 |
Ser304 |
LSPAFDHsPNKIMTE |
Homo sapiens |
|
| pmid |
sentence |
| 15030318 |
Our studies identify ser-304 as a major phosphorylation site in human tcptp, and the tc45 variant as a novel mitotic cdk substrate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK2 |
phosphorylation
|
PTPN2 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123471 |
Ser304 |
LSPAFDHsPNKIMTE |
Homo sapiens |
|
| pmid |
sentence |
| 15030318 |
Our studies identify ser-304 as a major phosphorylation site in human tcptp, and the tc45 variant as a novel mitotic cdk substrate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity 
dephosphorylation
|
PDGFRB |
0.545 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248390 |
Tyr1021 |
PNEGDNDyIIPLPDP |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 14966296 |
The PDGF beta receptor is negatively regulated by protein tyrosine phosphatases (PTPs).|In summary, our findings identify TC-PTP as a previously unrecognized negative regulator of PDGF beta receptor signaling and support the general notion that PTPs display site selectivity in their action on tyrosine kinase receptors.The fact that two of the investigated PDGF β receptor sites, Y1021 and Y771, displayed a larger increase in phosphorylation than Y579 and Y751 in TC-PTP ko MEFs indicated that these two sites are preferred substrates for TC-PTP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248389 |
Tyr771 |
ADIESSNyMAPYDNY |
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 14966296 |
The PDGF beta receptor is negatively regulated by protein tyrosine phosphatases (PTPs).|In summary, our findings identify TC-PTP as a previously unrecognized negative regulator of PDGF beta receptor signaling and support the general notion that PTPs display site selectivity in their action on tyrosine kinase receptors.The fact that two of the investigated PDGF β receptor sites, Y1021 and Y771, displayed a larger increase in phosphorylation than Y579 and Y751 in TC-PTP ko MEFs indicated that these two sites are preferred substrates for TC-PTP. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
JAK1 |
0.758 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248395 |
Tyr1034 |
AIETDKEyYTVKDDR |
Mus musculus |
|
| pmid |
sentence |
| 11909529 |
The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3|We have identified JAK1 and JAK3 as physiological substrates of TCPTP.| Using a site-specific antibody directed against the activation loop phosphotyrosines in JAK1 (pY1022/pY1023), we found that these sites were in fact dephosphorylated by TCPTP |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248396 |
Tyr1035 |
IETDKEYyTVKDDRD |
Mus musculus |
|
| pmid |
sentence |
| 11909529 |
The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3|We have identified JAK1 and JAK3 as physiological substrates of TCPTP.| Using a site-specific antibody directed against the activation loop phosphotyrosines in JAK1 (pY1022/pY1023), we found that these sites were in fact dephosphorylated by TCPTP |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134620 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15780598 |
Upon ligand binding, IL-2R , IL-6R or LeptinR , IFN-_R , IFN-_R and PRLR or growth hormone (GH) receptor associated JAKs become activated. These JAKs mediate phosphorylation of specific tyrosine residues and recruit STATs. Activated STATs are released from the receptor and translocate to the nucleus. PTP1B dephosphorylates JAK2, TYK2 and STAT5 . The 45-kDa form of TC-PTP was shown to dephosphorylate JAK1 and JAK3 as well as STAT1, STAT3 and STAT5. |
|
| Publications: |
3 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
KDR |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248399 |
Tyr1054 |
FGLARDIyKDPDYVR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18840653 |
We show that a TCPTP substrate-trapping mutant interacts with VEGFR2. Moreover, TCPTP dephosphorylates VEGFR2 in a phosphosite-specific manner, inhibits its kinase activity and prevents its internalization from the cell surface. |The autophosphorylation sites Tyr1054/1059 and Tyr1214 were dephosphorylated by TCPTP (Fig. 4B). Tyr996, the functional significance of which is currently uncertain (Olsson et al., 2006), was a TCPTP target as well. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248400 |
Tyr1059 |
DIYKDPDyVRKGDAR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18840653 |
We show that a TCPTP substrate-trapping mutant interacts with VEGFR2. Moreover, TCPTP dephosphorylates VEGFR2 in a phosphosite-specific manner, inhibits its kinase activity and prevents its internalization from the cell surface. |The autophosphorylation sites Tyr1054/1059 and Tyr1214 were dephosphorylated by TCPTP (Fig. 4B). Tyr996, the functional significance of which is currently uncertain (Olsson et al., 2006), was a TCPTP target as well. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276962 |
Tyr1059 |
DIYKDPDyVRKGDAR |
Homo sapiens |
|
| pmid |
sentence |
| 29955047 |
Collectively, our findings indicate that TC-PTP negatively regulates Flk-1 and JNK signaling via direct dephosphorylation of Flk-1 on its Y1173 residue, which contributes to increased epidermal apoptosis in response to UVB exposure.|Use of a TC-PTP substrate trapping mutant for immunoprecipitation analysis showed that TC-PTP dephosphorylates four different tyrosine residues of Flk-1 -- Y1052, Y1057, Y1212, and Y994 -- in human umbilical vein endothelial cells; however, it did not dephosphorylate the Y1173 residue of Flk-1 38. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276961 |
Tyr1175 |
AQQDGKDyIVLPISE |
Homo sapiens |
|
| pmid |
sentence |
| 29955047 |
Collectively, our findings indicate that TC-PTP negatively regulates Flk-1 and JNK signaling via direct dephosphorylation of Flk-1 on its Y1173 residue, which contributes to increased epidermal apoptosis in response to UVB exposure.|TC-PTP dephosphorylates activated Flk-1 at Y1173 after UVB irradiation, which is followed by the suppression of JNK phosphorylation.|TC-PTP promotes UVB induced apoptosis in keratinocytes by dephosphorylating Flk-1 tyrosine residue 1173. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248401 |
Tyr1214 |
VCDPKFHyDNTAGIS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18840653 |
We show that a TCPTP substrate-trapping mutant interacts with VEGFR2. Moreover, TCPTP dephosphorylates VEGFR2 in a phosphosite-specific manner, inhibits its kinase activity and prevents its internalization from the cell surface. |The autophosphorylation sites Tyr1054/1059 and Tyr1214 were dephosphorylated by TCPTP (Fig. 4B). Tyr996, the functional significance of which is currently uncertain (Olsson et al., 2006), was a TCPTP target as well. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
dephosphorylation
|
INSR |
0.604 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75910 |
Tyr1185 |
FGMTRDIyETDYYRK |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75914 |
Tyr1189 |
RDIYETDyYRKGGKG |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75918 |
Tyr1190 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-18018 |
Tyr1190 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
| pmid |
sentence |
| 1373652 |
The question of whether protein tyrosine phosphatases (ptpases) dephosphorylate a multiply phosphorylated peptide in a random or ordered manner was investigated using the synthetic triphosphotyrosyl peptide trdiy(p)etdy(p)y(p)rk, corresponding to the major sites of autophosphorylation of the insulin receptor, as a substrate for four purified ptpases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75922 |
Tyr999 |
YASSNPEyLSASDVF |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
INSR |
0.604 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248385 |
Tyr1189 |
RDIYETDyYRKGGKG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12612081 |
In this study, we investigated the downregulation of insulin receptor (IR) signaling by TCPTP. In response to insulin stimulation, the TC48-D182A and TC45-D182A substrate-trapping mutants formed stable complexes with the endogenous tyrosine-phosphorylated IR beta-subunit in 293 cells.|IR β-subunit phosphorylated on tyrosine and specifically on tyrosines 1162 and 1163 could be coimmunoprecipitated with the TC48-D182A and TC45-D182A mutants but not the wild-type TC48 or TC45 in response to insulin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248386 |
Tyr1190 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
| pmid |
sentence |
| 12612081 |
In this study, we investigated the downregulation of insulin receptor (IR) signaling by TCPTP. In response to insulin stimulation, the TC48-D182A and TC45-D182A substrate-trapping mutants formed stable complexes with the endogenous tyrosine-phosphorylated IR beta-subunit in 293 cells.|IR β-subunit phosphorylated on tyrosine and specifically on tyrosines 1162 and 1163 could be coimmunoprecipitated with the TC48-D182A and TC45-D182A mutants but not the wild-type TC48 or TC45 in response to insulin |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity 
dephosphorylation
|
INSR |
0.604 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276956 |
Tyr1189 |
RDIYETDyYRKGGKG |
Homo sapiens |
|
| pmid |
sentence |
| 30230471 |
In keeping with the overall improvement in insulin sensitivity we found that insulin-induced IR Y1162/Y1163 tyrosine phosphorylation and activation and downstream PI3K/AKT signaling in the liver (as monitored by AKT Ser-473 phosphorylation) were dramatically enhanced by POMC TCPTP deficiency (Figure 4h).|This would suggest that TCPTP deletion, or decreased TCPTP in POMC neurons in response to feeding, represses HGP by enhancing IR signaling and permitting POMC neurons to be activated by insulin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276957 |
Tyr1190 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
| pmid |
sentence |
| 30230471 |
In keeping with the overall improvement in insulin sensitivity we found that insulin-induced IR Y1162/Y1163 tyrosine phosphorylation and activation and downstream PI3K/AKT signaling in the liver (as monitored by AKT Ser-473 phosphorylation) were dramatically enhanced by POMC TCPTP deficiency (Figure 4h).|This would suggest that TCPTP deletion, or decreased TCPTP in POMC neurons in response to feeding, represses HGP by enhancing IR signaling and permitting POMC neurons to be activated by insulin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
dephosphorylation
|
KDR |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181546 |
Tyr1214 |
VCDPKFHyDNTAGIS |
Homo sapiens |
|
| pmid |
sentence |
| 18840653 |
Vegfr2 contains several critical tyrosine residues that are autophosphorylated following activation. Our phosphorylation assays showed that tcptp was able to target specific tyrosines in vegfr2. The autophosphorylation sites tyr1054/1059 and tyr1214 were dephosphorylated by tcptp. Tyr996 was a tcptp target as well. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181550 |
Tyr996 |
EEAPEDLyKDFLTLE |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 18840653 |
Vegfr2 contains several critical tyrosine residues that are autophosphorylated following activation. Our phosphorylation assays showed that tcptp was able to target specific tyrosines in vegfr2. The autophosphorylation sites tyr1054/1059 and tyr1214 were dephosphorylated by tcptp. Tyr996 was a tcptp target as well. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
MET |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248387 |
Tyr1234 |
RDMYDKEyYSVHNKT |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
Using substrate trapping mutants of PTP1B or TCPTP, we have demonstrated that both phosphatases interact with Met and that these interactions require phosphorylation of twin tyrosines (Tyr-1234/1235) in the activation loop of the Met kinase domain.|Using small interfering RNA against PTP1B and TCPTP, we demonstrate that phosphorylation of Tyr-1234/1235 in the activation loop of the Met receptor is elevated in the absence of either PTP1B or TCPTP and further elevated upon loss of both phosphatases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248388 |
Tyr1235 |
DMYDKEYySVHNKTG |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
Using substrate trapping mutants of PTP1B or TCPTP, we have demonstrated that both phosphatases interact with Met and that these interactions require phosphorylation of twin tyrosines (Tyr-1234/1235) in the activation loop of the Met kinase domain.|Using small interfering RNA against PTP1B and TCPTP, we demonstrate that phosphorylation of Tyr-1234/1235 in the activation loop of the Met receptor is elevated in the absence of either PTP1B or TCPTP and further elevated upon loss of both phosphatases. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
dephosphorylation
|
MET |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181331 |
Tyr1234 |
RDMYDKEyYSVHNKT |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
We have identified ptp1b and tcptp as negative regulators of the hepatocyte growth factor receptor, the met receptor-tyrosine kinase. In vivo, loss of ptp1b or tcptp enhances hepatocyte growth factor-mediated phosphorylation of met. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181335 |
Tyr1235 |
DMYDKEYySVHNKTG |
Homo sapiens |
|
| pmid |
sentence |
| 18819921 |
We have identified ptp1b and tcptp as negative regulators of the hepatocyte growth factor receptor, the met receptor-tyrosine kinase. In vivo, loss of ptp1b or tcptp enhances hepatocyte growth factor-mediated phosphorylation of met. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | up-regulates 
dephosphorylation
|
GJA1 |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205097 |
Tyr247 |
VKGKSDPyHATSGAL |
Homo sapiens |
|
| pmid |
sentence |
| 24849651 |
Tc-ptp dephosphorylates cx43 residues y247 and y265, dephosphorylation maintained cx43 gap junctions at the plaque and partially reversed the channel closure caused by v-src-mediated phosphorylation of cx43. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205101 |
Tyr265 |
KDCGSQKyAYFNGCS |
Homo sapiens |
|
| pmid |
sentence |
| 24849651 |
Tc-ptp dephosphorylates cx43 residues y247 and y265, dephosphorylation maintained cx43 gap junctions at the plaque and partially reversed the channel closure caused by v-src-mediated phosphorylation of cx43. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
PTPN2 | down-regulates
dephosphorylation
|
WASL |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141652 |
Tyr256 |
RETSKVIyDFIEKTG |
Homo sapiens |
|
| pmid |
sentence |
| 16293614 |
Similarly, the t cell phosphatase has a 30-fold lower kcat/km toward autoinhibited p-n-wasp than toward the isolated p-gbd, and again this effect is largely reversed by that cdc42 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
GHR |
0.298 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248391 |
Tyr332 |
ILAIHDSyKPEFHSD |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 12907755 |
PTPH1 only bound Tyr534, whereas PTP1B and TC-PTP bound multiple phosphopeptides. Earlier work suggests that Tyr332, Tyr487, Tyr534, Tyr566, and Tyr627 are all phosphorylated after GH stimulation (21). Apart from Tyr627, all of these also appear good PTP substrates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248392 |
Tyr487 |
SLSNIDFyAQVSDIT |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 12907755 |
PTPH1 only bound Tyr534, whereas PTP1B and TC-PTP bound multiple phosphopeptides. Earlier work suggests that Tyr332, Tyr487, Tyr534, Tyr566, and Tyr627 are all phosphorylated after GH stimulation (21). Apart from Tyr627, all of these also appear good PTP substrates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248393 |
Tyr534 |
NFLMDNAyFCEADAK |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 12907755 |
PTPH1 only bound Tyr534, whereas PTP1B and TC-PTP bound multiple phosphopeptides. Earlier work suggests that Tyr332, Tyr487, Tyr534, Tyr566, and Tyr627 are all phosphorylated after GH stimulation (21). Apart from Tyr627, all of these also appear good PTP substrates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248394 |
Tyr566 |
SLNQEDIyITTESLT |
Cricetulus griseus |
CHO Cell |
| pmid |
sentence |
| 12907755 |
PTPH1 only bound Tyr534, whereas PTP1B and TC-PTP bound multiple phosphopeptides. Earlier work suggests that Tyr332, Tyr487, Tyr534, Tyr566, and Tyr627 are all phosphorylated after GH stimulation (21). Apart from Tyr627, all of these also appear good PTP substrates |
|
| Publications: |
4 |
Organism: |
Cricetulus Griseus |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
SHC1 |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248397 |
Tyr349 |
EEPPDHQyYNDFPGK |
Homo sapiens |
|
| pmid |
sentence |
| 9488479 |
However, TC45 inhibited the EGF-induced association of p52Shc with Grb2, which was attributed to the ability of the PTP to recognize specifically p52Shc phosphorylated on Y239. These results indicate that TC45 recognizes not only selected substrates in a cellular context but also specific sites within substrates and thus may regulate discrete signaling events. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
dephosphorylation
|
FYN |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177113 |
Tyr420 |
RLIEDNEyTARQGAK |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 22080863 |
Previously, we reported that sfks can serve as bona fide substrates for tcptp and that tcptp dephosphorylates the y418 activation loop autophosphorylation site (corresponding to y394 in lck and y417 in fyn) to inactivate sfks |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
STAT1 |
0.724 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248402 |
Tyr701 |
DGPKGTGyIKTELIS |
Homo sapiens |
|
| pmid |
sentence |
| 12138178 |
Upon interferon (IFN) stimulation, Stat1 becomes tyrosine phosphorylated and translocates into the nucleus, where it binds to DNA to activate transcription. The activity of Stat1 is dependent on tyrosine phosphorylation, and its inactivation in the nucleus is accomplished by a previously unknown protein tyrosine phosphatase (PTP). We have now purified a Stat1 PTP activity from HeLa cell nuclear extract and identified it as TC45, the nuclear isoform of the T-cell PTP (TC-PTP). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133279 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15780598 |
Upon ligand binding, IL-2R , IL-6R or LeptinR , IFN-_R , IFN-_R and PRLR or growth hormone (GH) receptor associated JAKs become activated. These JAKs mediate phosphorylation of specific tyrosine residues and recruit STATs. Activated STATs are released from the receptor and translocate to the nucleus. PTP1B dephosphorylates JAK2, TYK2 and STAT5 . The 45-kDa form of TC-PTP was shown to dephosphorylate JAK1 and JAK3 as well as STAT1, STAT3 and STAT5. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
dephosphorylation
|
STAT1 |
0.724 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90814 |
Tyr701 |
DGPKGTGyIKTELIS |
Homo sapiens |
|
| pmid |
sentence |
| 12138178 |
Stat1 becomes tyrosine phosphorylated and translocates into the nucleus, where it binds to dna to activate transcription. The activity of stat1 is dependent on tyrosine phosphorylation, and its inactivation in the nucleus is accomplished by a previously unknown protein tyrosine phosphatase (ptp). We have now purified a stat1 ptp activity from hela cell nuclear extract and identified it as tc45, the nuclear isoform of the t-cell ptp (tc-ptp). Tc45 can dephosphorylate stat1 both in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
dephosphorylation
|
STAT3 |
0.725 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90818 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
|
| pmid |
sentence |
| 12138178 |
The nuclear isoform of protein-tyrosine phosphatase tc-ptp regulates interleukin-6-mediated signaling pathway through stat3 dephosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
STAT3 |
0.725 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93998 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
|
| pmid |
sentence |
| 15780598 |
Upon ligand binding, IL-2R , IL-6R or LeptinR , IFN-_R , IFN-_R and PRLR or growth hormone (GH) receptor associated JAKs become activated. These JAKs mediate phosphorylation of specific tyrosine residues and recruit STATs. Activated STATs are released from the receptor and translocate to the nucleus. PTP1B dephosphorylates JAK2, TYK2 and STAT5 . The 45-kDa form of TC-PTP was shown to dephosphorylate JAK1 and JAK3 as well as STAT1, STAT3 and STAT5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 |
dephosphorylation
|
KDR |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248398 |
Tyr996 |
EEAPEDLyKDFLTLE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18840653 |
We show that a TCPTP substrate-trapping mutant interacts with VEGFR2. Moreover, TCPTP dephosphorylates VEGFR2 in a phosphosite-specific manner, inhibits its kinase activity and prevents its internalization from the cell surface. |The autophosphorylation sites Tyr1054/1059 and Tyr1214 were dephosphorylated by TCPTP (Fig. 4B). Tyr996, the functional significance of which is currently uncertain (Olsson et al., 2006), was a TCPTP target as well. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
STAT5B |
0.722 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277126 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12359225 |
In the previous study, we demonstrated that the nuclear isoform of T-cell protein-tyrosine phosphatase (TC-PTP) dephosphorylated and deactivated signal transducer and activator of transcription 5a (STAT5a) and STAT5b, thereby negatively regulating prolactin (PRL)-mediated signaling pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
JAK3 |
0.684 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133078 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15780598 |
Upon ligand binding, IL-2R , IL-6R or LeptinR , IFN-_R , IFN-_R and PRLR or growth hormone (GH) receptor associated JAKs become activated. These JAKs mediate phosphorylation of specific tyrosine residues and recruit STATs. Activated STATs are released from the receptor and translocate to the nucleus. PTP1B dephosphorylates JAK2, TYK2 and STAT5 . The 45-kDa form of TC-PTP was shown to dephosphorylate JAK1 and JAK3 as well as STAT1, STAT3 and STAT5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
SRC |
0.709 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276996 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33603165 |
Since PTPN2 dephosphorylates and inactivates Src [ xref ], the increase of pY439 might have resulted from reduced dephosphorylation or elevated Src activity or both. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | up-regulates activity 
dephosphorylation
|
BCL2L11 |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277055 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21984578 |
Moreover, it indicates that PTPN2 modulates the apoptotic activity of Bim via regulation of the protein kinase JNK1.|PTPN2 inhibition increased Bim phosphorylation at residue 65 in untreated INS-1E cells, and this effect was prolonged until 4 h of treatment with IFNalpha or 8 h after treatment with IFNgamma (XREF_FIG). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
STAT5A |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133547 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15780598 |
Upon ligand binding, IL-2R , IL-6R or LeptinR , IFN-_R , IFN-_R and PRLR or growth hormone (GH) receptor associated JAKs become activated. These JAKs mediate phosphorylation of specific tyrosine residues and recruit STATs. Activated STATs are released from the receptor and translocate to the nucleus. PTP1B dephosphorylates JAK2, TYK2 and STAT5 . The 45-kDa form of TC-PTP was shown to dephosphorylate JAK1 and JAK3 as well as STAT1, STAT3 and STAT5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
STAT6 |
0.666 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235192 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17210636 |
These results identify TCPTP as a physiological regulator of STAT6 phosphorylation and suggest that specific increases in TCPTP expression in ABC-like DLBCLs may contribute to the different biological characteristics of these tumors |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
|
AKT1 |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252640 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12612081 |
We found that insulin-induced ir tyrosine phosphorylation and pkb/akt sig- naling were enhanced in tcptp- cells and suppressed upon tcptp reconstitution, providing persuasive evidence that tcptp can regulate ir activation and signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
dephosphorylation
|
EGFR |
0.62 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109804 |
|
|
Homo sapiens |
Glioblastoma Cell |
| pmid |
sentence |
| 11514572 |
Tc45 dephosphorylated delta egfr in u87mg glioblastoma cells and inhibited mitogen-activated protein kinase erk2 and phosphatidylinositol 3-kinase signaling. In contrast, the substrate-trapping tc45-d182a mutant, which is capable of forming stable complexes with tc45 substrates, suppressed the activation of erk2 but not phosphatidylinositol 3-kinase. The activation results in reduced egfr phosphorylation after egf stimulation. Introduction of the alpha(1) cytoplasmic domain peptide into cells induces phosphatase activation and inhibits egf-induced cell proliferation and anchorage-independent growth of malignant cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132316 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15592458 |
Here, we report that the 45-kda variant of the protein tyrosine phosphatase tcptp (tc45) can recognize delta egfr as a cellular substrate |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
dephosphorylation
|
SRC |
0.709 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177116 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22080863 |
We found that tcptp dephosphorylates and inactivates src family kinases to regulate t cell responses._ |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates activity
dephosphorylation
|
KRAS |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277039 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33122197 |
Mechanistically, PTPN2 negatively regulates tyrosine phosphorylation of KRAS, which, in turn, affects the activation KRAS and its downstream signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
|
AKT |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98811 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12612081 |
We found that insulin-induced ir tyrosine phosphorylation and pkb/akt sig- naling were enhanced in tcptp- cells and suppressed upon tcptp reconstitution, providing persuasive evidence that tcptp can regulate ir activation and signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
dephosphorylation
|
FKBP4 |
0.408 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97794 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12552015 |
We have documented that a cellular protein that binds the immunosuppressant drug fk506, termed the fk506-binding protein (fkbp52), interacts with the single-stranded d sequence within the aav inverted terminal repeats, inhibits viral second-strand dna synthesis, and consequently limits high-efficiency transgene expression. Deliberate overexpression of the murine wild-type (wt) tc-ptp gene, but not that of a cysteine-to-serine (c-s) mutant, caused tyrosine dephosphorylation of fkbp52, leading to efficient viral second-strand dna synthesis and resulting in a significant increase in aav-mediated transduction efficiency in hela cells in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PTPN2
- 
- 