| + |
CSNK2A1 | up-regulates activity 
phosphorylation
|
PTPRJ |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277876 |
Thr1318 |
YQNTTAMtIYENLAP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 24583284 |
CK2-dependent phosphorylation of DEP-1 T1318 promotes Y1320 phosphorylation and Src activation upon VEGF stimulation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates activity 
dephosphorylation
|
PDGFRB |
0.565 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248704 |
Tyr1021 |
PNEGDNDyIIPLPDP |
Homo sapiens |
|
| pmid |
sentence |
| 12062403 |
Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1|DEP-1 dephosphorylation of original and chimeric phospho-peptides spanning the preferred pY1021 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
KDR |
0.687 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248709 |
Tyr1054 |
FGLARDIyKDPDYVR |
Homo sapiens |
|
| pmid |
sentence |
| 18936167 |
These results therefore suggest that the autoactivation residues Y1054 and Y1059 are targeted by DEP-1 and that this results in the inhibition of kinase activity and the consequent general dephosphorylation of VEGFR2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248710 |
Tyr1059 |
DIYKDPDyVRKGDAR |
Homo sapiens |
|
| pmid |
sentence |
| 18936167 |
These results therefore suggest that the autoactivation residues Y1054 and Y1059 are targeted by DEP-1 and that this results in the inhibition of kinase activity and the consequent general dephosphorylation of VEGFR2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates
dephosphorylation
|
KDR |
0.687 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181672 |
Tyr1054 |
FGLARDIyKDPDYVR |
Homo sapiens |
|
| pmid |
sentence |
| 18936167 |
The autoactivation residues y1054 and y1059 are targeted by dep-1 and this results in the inhibition of kinase activity and the consequent general dephosphorylation of vegfr2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181676 |
Tyr1059 |
DIYKDPDyVRKGDAR |
Homo sapiens |
|
| pmid |
sentence |
| 18936167 |
The autoactivation residues y1054 and y1059 are targeted by dep-1 and this results in the inhibition of kinase activity and the consequent general dephosphorylation of vegfr2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates
dephosphorylation
|
RET |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147161 |
Tyr1062 |
TWIENKLyGMSDPNW |
Homo sapiens |
|
| pmid |
sentence |
| 16778204 |
Ptprj expression induces dephosphorylation of the ret(c634r) and, probably via an indirect mechanism, ret/ptc1 oncoproteins on two key ret autophosphorylation sites (tyr1062 and tyr905). in line with this finding, adoptive ptprj expression reduced the oncogenic activity of ret |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147165 |
Tyr905 |
DVYEEDSyVKRSQGR |
Homo sapiens |
|
| pmid |
sentence |
| 16778204 |
Ptprj expression induces dephosphorylation of the ret(c634r) and, probably via an indirect mechanism, ret/ptc1 oncoproteins on two key ret autophosphorylation sites (tyr1062 and tyr905). in line with this finding, adoptive ptprj expression reduced the oncogenic activity of ret |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
RET |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248700 |
Tyr1062 |
TWIENKLyGMSDPNW |
Homo sapiens |
|
| pmid |
sentence |
| 16778204 |
The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins.|PTPRJ expression induces dephosphorylation of the RET(C634R) and, probably via an indirect mechanism, RET/PTC1 oncoproteins on two key RET autophosphorylation sites (Tyr1062 and Tyr905). This results in a significant decrease of RET-induced Shc and extracellular signal-regulated kinase 1/2 phosphorylation levels |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248701 |
Tyr905 |
DVYEEDSyVKRSQGR |
Homo sapiens |
|
| pmid |
sentence |
| 16778204 |
The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins.|PTPRJ expression induces dephosphorylation of the RET(C634R) and, probably via an indirect mechanism, RET/PTC1 oncoproteins on two key RET autophosphorylation sites (Tyr1062 and Tyr905). This results in a significant decrease of RET-induced Shc and extracellular signal-regulated kinase 1/2 phosphorylation levels |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | up-regulates quantity by stabilization
dephosphorylation
|
EGFR |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248697 |
Tyr1069 |
EDSFLQRySSDPTGA |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19836242 |
We report the identification of PTPRK and PTPRJ (density-enhanced phosphatase-1 [DEP-1]) as EGFR-targeting phosphatases. DEP-1 is a tumor suppressor that dephosphorylates and thereby stabilizes EGFR by hampering its ability to associate with the CBL-GRB2 ubiquitin ligase complex|By employing commercially available antibodies, which are supposed to recognize specific tyrosine phosphorylation sites of EGFR, we found that depletion of endogenous DEP-1 nonselectively increased receptor phosphorylation, affecting all three sites we analyzed (tyrosines 1045, 1068, and 1173 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248698 |
Tyr1092 |
TFLPVPEyINQSVPK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19836242 |
We report the identification of PTPRK and PTPRJ (density-enhanced phosphatase-1 [DEP-1]) as EGFR-targeting phosphatases. DEP-1 is a tumor suppressor that dephosphorylates and thereby stabilizes EGFR by hampering its ability to associate with the CBL-GRB2 ubiquitin ligase complex|By employing commercially available antibodies, which are supposed to recognize specific tyrosine phosphorylation sites of EGFR, we found that depletion of endogenous DEP-1 nonselectively increased receptor phosphorylation, affecting all three sites we analyzed (tyrosines 1045, 1068, and 1173 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248699 |
Tyr1197 |
STAENAEyLRVAPQS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19836242 |
We report the identification of PTPRK and PTPRJ (density-enhanced phosphatase-1 [DEP-1]) as EGFR-targeting phosphatases. DEP-1 is a tumor suppressor that dephosphorylates and thereby stabilizes EGFR by hampering its ability to associate with the CBL-GRB2 ubiquitin ligase complex|By employing commercially available antibodies, which are supposed to recognize specific tyrosine phosphorylation sites of EGFR, we found that depletion of endogenous DEP-1 nonselectively increased receptor phosphorylation, affecting all three sites we analyzed (tyrosines 1045, 1068, and 1173 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD in AML |
| + |
PTPRJ | down-regulates
dephosphorylation
|
INSR |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76088 |
Tyr1185 |
FGMTRDIyETDYYRK |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
These results, combined with secondary dephosphorylation tests, confirm and extend earlier findings that ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21295 |
Tyr1185 |
FGMTRDIyETDYYRK |
Homo sapiens |
|
| pmid |
sentence |
| 1715686 |
Dephosphorylation of autophosphorylated insulin and epidermal-growth-factor receptors by two major subtypes of protein-tyrosine-phosphatase from human placenta. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76092 |
Tyr1189 |
RDIYETDyYRKGGKG |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
These results, combined with secondary dephosphorylation tests, confirm and extend earlier findings that ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21299 |
Tyr1189 |
RDIYETDyYRKGGKG |
Homo sapiens |
|
| pmid |
sentence |
| 1715686 |
Dephosphorylation of autophosphorylated insulin and epidermal-growth-factor receptors by two major subtypes of protein-tyrosine-phosphatase from human placenta. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21303 |
Tyr1190 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
| pmid |
sentence |
| 1715686 |
Dephosphorylation of autophosphorylated insulin and epidermal-growth-factor receptors by two major subtypes of protein-tyrosine-phosphatase from human placenta. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76096 |
Tyr1190 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76100 |
Tyr999 |
YASSNPEyLSASDVF |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
These results, combined with secondary dephosphorylation tests, confirm and extend earlier findings that ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21307 |
Tyr999 |
YASSNPEyLSASDVF |
Homo sapiens |
|
| pmid |
sentence |
| 1715686 |
Dephosphorylation of autophosphorylated insulin and epidermal-growth-factor receptors by two major subtypes of protein-tyrosine-phosphatase from human placenta. |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| + |
FYN | up-regulates activity
phosphorylation
|
PTPRJ |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276372 |
Tyr1311 |
DSKVDLIyQNTTAMT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22898603 |
We demonstrate here that DEP-1 is phosphorylated in a Src- and Fyn-dependent manner on Y1311 and Y1320, which bind the Src SH2 domain. This allows DEP-1-catalyzed dephosphorylation of Src inhibitory Y529 and favors the VEGF-induced phosphorylation of Src substrates VE-cadherin and Cortactin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276374 |
Tyr1320 |
NTTAMTIyENLAPVT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22898603 |
We demonstrate here that DEP-1 is phosphorylated in a Src- and Fyn-dependent manner on Y1311 and Y1320, which bind the Src SH2 domain. This allows DEP-1-catalyzed dephosphorylation of Src inhibitory Y529 and favors the VEGF-induced phosphorylation of Src substrates VE-cadherin and Cortactin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates activity
phosphorylation
|
PTPRJ |
0.621 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276373 |
Tyr1311 |
DSKVDLIyQNTTAMT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22898603 |
We demonstrate here that DEP-1 is phosphorylated in a Src- and Fyn-dependent manner on Y1311 and Y1320, which bind the Src SH2 domain. This allows DEP-1-catalyzed dephosphorylation of Src inhibitory Y529 and favors the VEGF-induced phosphorylation of Src substrates VE-cadherin and Cortactin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276375 |
Tyr1320 |
NTTAMTIyENLAPVT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22898603 |
We demonstrate here that DEP-1 is phosphorylated in a Src- and Fyn-dependent manner on Y1311 and Y1320, which bind the Src SH2 domain. This allows DEP-1-catalyzed dephosphorylation of Src inhibitory Y529 and favors the VEGF-induced phosphorylation of Src substrates VE-cadherin and Cortactin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | up-regulates activity
phosphorylation, dephosphorylation
|
SRC |
0.621 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277877 |
Tyr1320 |
Y>1319 |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 24583284 |
CK2-dependent phosphorylation of DEP-1 T1318 promotes Y1320 phosphorylation and Src activation upon VEGF stimulation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248705 |
Tyr530 |
FTSTEPQyQPGENL |
Rattus norvegicus |
|
| pmid |
sentence |
| 15735685 |
The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276977 |
Tyr530 |
FTSTEPQyQPGENL |
Rattus norvegicus |
|
| pmid |
sentence |
| 26556953 |
Expression of Dep1 in transformed rat thyroid PCMPSV cells increased Src activity via Y527 dephosphorylation (corresponding to Y530 in human Src) without affecting the level of phosphorylated Y416 (Y419 in human Src).|Reciprocally, Dep1 can be phosphorylated by Src and Fyn on Y1311 and Y1320, leading to the dephosphorylation of Y530 Src by Dep1 . |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, Rattus Norvegicus |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
MET |
0.592 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248702 |
Tyr1349 |
STFIGEHyVHVNATY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12475979 |
When co-expressed in 293 cells, the full-length substrate-trapping mutant form of DEP-1 formed a stable complex with the chimeric receptor colony stimulating factor 1 (CSF)-Met and wild type DEP-1 dephosphorylated CSF-Met. Furthermore, we observed that DEP-1 preferentially dephosphorylated a Gab1 binding site (Tyr(1349)) and a COOH-terminal tyrosine implicated in morphogenesis (Tyr(1365)), |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248703 |
Tyr1365 |
NVKCVAPyPSLLSSE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12475979 |
When co-expressed in 293 cells, the full-length substrate-trapping mutant form of DEP-1 formed a stable complex with the chimeric receptor colony stimulating factor 1 (CSF)-Met and wild type DEP-1 dephosphorylated CSF-Met. Furthermore, we observed that DEP-1 preferentially dephosphorylated a Gab1 binding site (Tyr(1349)) and a COOH-terminal tyrosine implicated in morphogenesis (Tyr(1365)), |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates
dephosphorylation
|
MET |
0.592 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96347 |
Tyr1365 |
NVKCVAPyPSLLSSE |
Homo sapiens |
Breast Cancer Cell, Lung Cancer Cell |
| pmid |
sentence |
| 12475979 |
Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase dep-1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
MAPK1 |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248708 |
Tyr187 |
HTGFLTEyVATRWYR |
in vitro |
|
| pmid |
sentence |
| 19494114 |
Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases.|Pulldown and in vitro dephosphorylation assays confirmed our prediction and demonstrated an overall specificity of DEP-1 in targeting the phosphorylated tyrosine 204 of ERK1/2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101276 |
Tyr205 |
IMLNSKGyTKSIDIW |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19494114 |
In this study we show that one of these potential targets, the erk1/2, is indeed a direct dep-1 substrate in vivo. |
|
| Publications: |
2 |
Organism: |
In Vitro, Homo Sapiens |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
MAPK3 |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248707 |
Tyr204 |
HTGFLTEyVATRWYR |
in vitro |
|
| pmid |
sentence |
| 19494114 |
Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases|Pulldown and in vitro dephosphorylation assays confirmed our prediction and demonstrated an overall specificity of DEP-1 in targeting the phosphorylated tyrosine 204 of ERK1/2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTPRJ | down-regulates
dephosphorylation
|
MAPK1 |
0.416 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161536 |
Tyr205 |
IMLNSKGyTKSIDIW |
Homo sapiens |
|
| pmid |
sentence |
| 19494114 |
In this study we show that one of these potential targets, the erk1/2, is indeed a direct dep-1 substrate in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101279 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12771128 |
A dominant-negative mutant of high cell density-enhanced ptp 1 (dep-1)//cd148 as well as reduction of its expression by rna interference partially restore vegfr-2 phosphorylation and map kinase activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
SRC |
0.621 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276978 |
Tyr419 |
RLIEDNEyTARQGAK |
Homo sapiens |
|
| pmid |
sentence |
| 22898603 |
In addition, our work further reveals that above a threshold expression level, DEP-1 can also dephosphorylate Src Y418 and attenuate downstream signaling and biologic responses, consistent with the quiescent behavior of confluent endothelial cells that express the highest levels of endogenous DEP-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
JAK2 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277093 |
Tyr813 |
NSLFTPDyELLTEND |
Homo sapiens |
|
| pmid |
sentence |
| 28912580 |
These results support PTPRJ preferentially dephosphorylating Y813 and Y868 in JAK2.|We revealed that PTPRJ negatively regulates leptin signaling by dephosphorylating specific tyrosine residues (Y813 and Y868) in JAK2, the simultaneous phosphorylation of which plays a pivotal role in JAK2 activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277094 |
Tyr868 |
GSVEMCRyDPLQDNT |
Homo sapiens |
|
| pmid |
sentence |
| 28912580 |
These results support PTPRJ preferentially dephosphorylating Y813 and Y868 in JAK2.|We revealed that PTPRJ negatively regulates leptin signaling by dephosphorylating specific tyrosine residues (Y813 and Y868) in JAK2, the simultaneous phosphorylation of which plays a pivotal role in JAK2 activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
FLT3 |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277092 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21262971 |
Moreover, activated FLT3 could be dephosphorylated by recombinant DEP-1 in vitro.|The data indicate that DEP-1 is negatively regulating FLT3 signaling activity and that its loss may contribute to but is not sufficient for leukemogenic cell transformation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD in AML |
| + |
PTPRJ | down-regulates
dephosphorylation
|
ERK1/2 |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269919 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12771128 |
A dominant-negative mutant of high cell densityenhanced ptp 1 (dep-1)//cd148 as well as reduction of its expression by rna interference partially restore vegfr-2 phosphorylation and map kinase activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD in AML |
| + |
FLT3 | down-regulates activity 
|
PTPRJ |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261553 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 22438257 |
Taken together, the described findings supported the notion that FLT3 ITD causes reduced DEP-1 activity compared with cells expressing WT FLT3 rather than alterations in mRNA or protein levels. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD in AML |
| + |
PTPRJ | down-regulates
dephosphorylation
|
MAPK3 |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101282 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12771128 |
A dominant-negative mutant of high cell densityenhanced ptp 1 (dep-1)//cd148 as well as reduction of its expression by rna interference partially restore vegfr-2 phosphorylation and map kinase activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates
dephosphorylation
|
PLCG1 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105790 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11259588 |
Cd148 can dephosphorylate lat and plc?1 In vitro. / plc?1 Undergoes inducible tyrosine phosphorylation following tcr stimulation (46), and this phosphorylation is required to stimulate its catalytic activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates
dephosphorylation
|
Gbeta |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269897 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12771128 |
A dominant-negative mutant of high cell densityenhanced ptp 1 (dep-1)//cd148 as well as reduction of its expression by rna interference partially restore vegfr-2 phosphorylation and map kinase activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates
dephosphorylation
|
PI3K |
0.264 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252727 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18348712 |
As reduction of pi3k activity by cd148 or shp-1 [32] is not large (2540%), it is likely that these ptps may function as modulators of the pi3k pathway rather than suppressors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD in AML |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
CEACAM3 |
0.361 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277091 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 35850306 |
We also determined that recombinant PTPRJ directly dephosphorylates the cytoplasmic tyrosine residues of purified full-length CEACAM3 and recognizes synthetic CEACAM3-derived phospho-peptides as substrates.|We show depletion of PTPRJ results in a gain-of-function phenotype, while overexpression of a constitutively active PTPRJ phosphatase strongly reduces bacterial uptake via CEACAM3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
LAT |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248696 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11259588 |
Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates
dephosphorylation
|
PIK3R1 |
0.264 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178049 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18348712 |
As reduction of pi3k activity by cd148 or shp-1 [32] is not large (2540%), it is likely that these ptps may function as modulators of the pi3k pathway rather than suppressors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates
dephosphorylation
|
FLT1 |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101272 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12771128 |
Vegf acts by binding to two high affinity receptor tyrosine kinases: vegf receptor (vegfr)* 1 also called flt-1, and vegfr-2, also called flk-1/kdr a dominant-negative mutant of high cell densityenhanced ptp 1 (dep-1)//cd148 as well as reduction of its expression by rna interference partially restore vegfr-2 phosphorylation and map kinase activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | up-regulates activity
dephosphorylation
|
CTNNB1 |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276992 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25386896 |
Our data demonstrate that CD148 promotes E-cadherin cell adhesion by regulating Rac1 activity, concomitant with modulation of p120, \u03b2-catenin, and Src tyrosine phosphorylation, and that this effect requires E-cadherin and p120 association.|Taken together, it is likely that CD148 dephosphorylation of \u03b2-catenin enhances the cadherin cell adhesion independent of Rho family GTPases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD in AML |
| + |
MARCHF9 | down-regulates quantity by destabilization
ubiquitination
|
PTPRJ |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271535 |
|
|
Homo sapiens |
B-lymphocyte Cell Line |
| pmid |
sentence |
| 19457934 |
MARCH9, a member of the RING-CH family of transmembrane E3 ubiquitin ligases, down-regulates CD4, major histocompatibility complex-I (MHC), and ICAM-1 in lymphoid cells. To identify novel MARCH9 substrates, we used high throughput flow cytometry and quantitative mass spectrometry by stable isotope labeling by amino acids in cell culture (SILAC) to determine the differential expression of plasma membrane proteins in a MARCH9-expressing B cell line. This combined approach identified 13 potential new MARCH9 targets. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates
dephosphorylation
|
LAT |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105787 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 11259588 |
We propose that cd148 negatively regulates tcr signaling by interfering with the phosphorylation and function of plcgamma1 and lat |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ |
dephosphorylation
|
PLCG1 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248706 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11259588 |
Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRJ | down-regulates activity
|
CBL |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248839 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19836242 |
Because c-CBL’s activation is achieved via tyrosine phosphorylation, we tested the effect of DEP-1 on modification of a major site of phosphorylation, namely tyro- sine 731. Upon DEP-1 overexpression, c-CBL displayed reduced phosphorylation on this site compared to control cells (Figure 7B). This result offers a mechanism by which DEP-1 affects EGFR trafficking: by dephosphorylating EGFR, and possibly also SRC family kinases involved in phosphoryla- tion of c-CBL [31, 32], DEP-1 reduces activation of c-CBL and its recruitment to the activated EGFR, hence inhibiting subsequent receptor internalization and degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
3.0
PTPRJ
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