| + |
PTPN2 | down-regulates activity
dephosphorylation
|
KDR |
0.586 |
| 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-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-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-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 |
| + |
PTPRJ | down-regulates activity
dephosphorylation
|
KDR |
0.712 |
| 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 |
0.712 |
| 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 |
| + |
KDR | up-regulates
phosphorylation
|
KDR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157081 |
Tyr1054 |
FGLARDIyKDPDYVR |
Homo sapiens |
Macrophage, Monocyte |
| pmid |
sentence |
| 17658244 |
Binding of vegf to the receptor induces dimerisation and autophosphorylation of specific intracellular tyrosine residues. Activation of intracellular cascades results in proliferation, migration, survival and increased permeability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157085 |
Tyr1059 |
DIYKDPDyVRKGDAR |
Homo sapiens |
Macrophage, Monocyte |
| pmid |
sentence |
| 17658244 |
Binding of vegf to the receptor induces dimerisation and autophosphorylation of specific intracellular tyrosine residues. Activation of intracellular cascades results in proliferation, migration, survival and increased permeability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157089 |
Tyr1175 |
AQQDGKDyIVLPISE |
Homo sapiens |
Macrophage, Monocyte |
| pmid |
sentence |
| 17658244 |
Binding of vegf to the receptor induces dimerisation and autophosphorylation of specific intracellular tyrosine residues. Activation of intracellular cascades results in proliferation, migration, survival and increased permeability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157093 |
Tyr1214 |
VCDPKFHyDNTAGIS |
Homo sapiens |
Macrophage, Monocyte |
| pmid |
sentence |
| 17658244 |
Binding of vegf to the receptor induces dimerisation and autophosphorylation of specific intracellular tyrosine residues. Activation of intracellular cascades results in proliferation, migration, survival and increased permeability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157097 |
Tyr951 |
RFRQGKDyVGAIPVD |
Homo sapiens |
Macrophage, Monocyte |
| pmid |
sentence |
| 17658244 |
Binding of vegf to the receptor induces dimerisation and autophosphorylation of specific intracellular tyrosine residues. Activation of intracellular cascades results in proliferation, migration, survival and increased permeability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66040 |
Tyr996 |
EEAPEDLyKDFLTLE |
Homo sapiens |
|
| pmid |
sentence |
| 10102632 |
Autophosphorylation of kdr in the kinase domain is required for maximal vegf-stimulated kinase activity and receptor internalizationthe intensity of vegf-induced autophosphorylation is significantly reduced when using receptor mutated at y996, confirming that this is a major site of autophosphorylation. Second, tyrosines 951 and 996 are the only two tyrosines in the receptor's kinase insert domain, and there is strong evidence from studies using the pdgfr and cfms that autophosphorylation of tyrosines in this domain leads to important signaling events. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| Pathways: | VEGF Signaling |
| + |
PTPRG | down-regulates activity
dephosphorylation
|
KDR |
0.251 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254707 |
Tyr1054 |
FGLARDIyKDPDYVR |
in vitro |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254708 |
Tyr1059 |
DIYKDPDyVRKGDAR |
in vitro |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
KDR |
0.682 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248474 |
Tyr1059 |
DIYKDPDyVRKGDAR |
Homo sapiens |
|
| pmid |
sentence |
| 18377662 |
Src homology 2 (SH2) domain containing protein tyrosine phosphatase-1 (SHP-1) dephosphorylates VEGF Receptor-2 and attenuates endothelial DNA synthesis, but not migration|Knockdown of SHP-1 by siRNA or inhibition of c-Src by an inhibitor, results in augmented DNA synthesis perhaps due to increased phosphorylation of at least three tyrosine residues of KDR 996, 1059 and 1175 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248475 |
Tyr1175 |
AQQDGKDyIVLPISE |
Homo sapiens |
|
| pmid |
sentence |
| 18377662 |
Src homology 2 (SH2) domain containing protein tyrosine phosphatase-1 (SHP-1) dephosphorylates VEGF Receptor-2 and attenuates endothelial DNA synthesis, but not migration|Knockdown of SHP-1 by siRNA or inhibition of c-Src by an inhibitor, results in augmented DNA synthesis perhaps due to increased phosphorylation of at least three tyrosine residues of KDR 996, 1059 and 1175 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates activity
phosphorylation
|
KDR |
0.629 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279120 |
Tyr1175 |
AQQDGKDyIVLPISE |
Homo sapiens |
|
| pmid |
sentence |
| 19050761 |
In contrast, our analysis showed that over-expression of c-Src significantly enhances the ability of VEGFR-2 to stimulate proliferation of PAE cells and over-expression of dominant negative Src (Src kinase-dead) inhibits the VEGFR-2 driven proliferation of PAE cells (XREF_FIG).|Taken together, the data demonstrate that Src kinases upon activation by VEGFR-2 phosphorylate Y1173 of VEGFR-2 (XREF_FIG). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRB | down-regulates activity
dephosphorylation
|
KDR |
0.447 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248441 |
Tyr1175 |
AQQDGKDyIVLPISE |
Homo sapiens |
|
| pmid |
sentence |
| 19136612 |
VE-PTP/VEGFR2 complex formation resumes with time, leading to dephosphorylation and deactivation of VEGFR2 (right). B) In VE-PTP-deficient cells, such as after siRNA treatment, VEGFR2 activation (middle) is exaggerated, leading to increased phosphorylation at the Y951 and Y1175 phosphorylation sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN1 | down-regulates activity
dephosphorylation
|
KDR |
0.413 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277011 |
Tyr1175 |
AQQDGKDyIVLPISE |
Homo sapiens |
|
| pmid |
sentence |
| 23639442 |
This led to increased PTPN1 (PTP1b)-mediated dephosphorylation of VEGFR2 at Y 1175 , the site involved in activating ERK signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN2 | down-regulates
dephosphorylation
|
KDR |
0.586 |
| 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 |
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