| + |
PRKACA | down-regulates activity 
phosphorylation
|
PTPN11 |
0.436 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276892 |
Ser189 |
GGGERFDsLTDLVEH |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25802336 |
We identified two key amino acids in Shp2 that are phosphorylated by PKA. Thr-73 contributes a helix cap to helix αB within the N-terminal SH2 domain of Shp2, whereas Ser-189 occupies an equivalent position within the C-terminal SH2 domain. Utilizing double mutant PKA phosphodeficient (T73A/S189A) and phosphomimetic (T73D/S189D) constructs, in vitro binding assays, and phosphatase activity assays, we demonstrate that phosphorylation of these residues disrupts Shp2 interaction with tyrosine-phosphorylated ligands and inhibits its protein-tyrosine phosphatase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276891 |
Thr73 |
YGGEKFAtLAELVQY |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25802336 |
We identified two key amino acids in Shp2 that are phosphorylated by PKA. Thr-73 contributes a helix cap to helix αB within the N-terminal SH2 domain of Shp2, whereas Ser-189 occupies an equivalent position within the C-terminal SH2 domain. Utilizing double mutant PKA phosphodeficient (T73A/S189A) and phosphomimetic (T73D/S189D) constructs, in vitro binding assays, and phosphatase activity assays, we demonstrate that phosphorylation of these residues disrupts Shp2 interaction with tyrosine-phosphorylated ligands and inhibits its protein-tyrosine phosphatase activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PKA | down-regulates activity
phosphorylation
|
PTPN11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276894 |
Ser189 |
GGGERFDsLTDLVEH |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25802336 |
We identified two key amino acids in Shp2 that are phosphorylated by PKA. Thr-73 contributes a helix cap to helix αB within the N-terminal SH2 domain of Shp2, whereas Ser-189 occupies an equivalent position within the C-terminal SH2 domain. Utilizing double mutant PKA phosphodeficient (T73A/S189A) and phosphomimetic (T73D/S189D) constructs, in vitro binding assays, and phosphatase activity assays, we demonstrate that phosphorylation of these residues disrupts Shp2 interaction with tyrosine-phosphorylated ligands and inhibits its protein-tyrosine phosphatase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276893 |
Thr73 |
YGGEKFAtLAELVQY |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25802336 |
We identified two key amino acids in Shp2 that are phosphorylated by PKA. Thr-73 contributes a helix cap to helix αB within the N-terminal SH2 domain of Shp2, whereas Ser-189 occupies an equivalent position within the C-terminal SH2 domain. Utilizing double mutant PKA phosphodeficient (T73A/S189A) and phosphomimetic (T73D/S189D) constructs, in vitro binding assays, and phosphatase activity assays, we demonstrate that phosphorylation of these residues disrupts Shp2 interaction with tyrosine-phosphorylated ligands and inhibits its protein-tyrosine phosphatase activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | FLT3-ITD signaling |
| + |
PRKCH |
phosphorylation
|
PTPN11 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249137 |
Ser576 |
CAEMREDsARVYENV |
Homo sapiens |
|
| pmid |
sentence |
| 11781100 |
In summary, SHP2 is phosphorylated on serine residues 576 and 591 by PKC isoforms alpha, beta 1, beta 2, and eta |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249140 |
Ser595 |
GLMQQQKsFR |
Homo sapiens |
|
| pmid |
sentence |
| 11781100 |
In summary, SHP2 is phosphorylated on serine residues 576 and 591 by PKC isoforms alpha, beta 1, beta 2, and eta. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCB |
phosphorylation
|
PTPN11 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249136 |
Ser576 |
CAEMREDsARVYENV |
Homo sapiens |
|
| pmid |
sentence |
| 11781100 |
In summary, SHP2 is phosphorylated on serine residues 576 and 591 by PKC isoforms alpha, beta 1, beta 2, and eta. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249139 |
Ser595 |
GLMQQQKsFR |
Homo sapiens |
|
| pmid |
sentence |
| 11781100 |
In summary, SHP2 is phosphorylated on serine residues 576 and 591 by PKC isoforms alpha, beta 1, beta 2, and eta. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCA |
phosphorylation
|
PTPN11 |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249138 |
Ser595 |
GLMQQQKsFR |
Homo sapiens |
|
| pmid |
sentence |
| 11781100 |
In summary, SHP2 is phosphorylated on serine residues 576 and 591 by PKC isoforms alpha, beta 1, beta 2, and eta. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
STAT1 |
0.737 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248673 |
Ser727 |
TDNLLPMsPEEFDEV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12270932 |
SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei|In SHP-2-/- mouse fibroblast cells, Stat1 phosphorylation at both the tyrosine residue Tyr(701) and the serine residue Ser(727) |Overexpression of SHP-2 in 293T cells inhibited IFNgamma-dependent Stat1 phosphorylation and suppressed Stat1-dependent induction of luciferase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248672 |
Tyr701 |
DGPKGTGyIKTELIS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12270932 |
SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei|In SHP-2-/- mouse fibroblast cells, Stat1 phosphorylation at both the tyrosine residue Tyr(701) and the serine residue Ser(727) |Overexpression of SHP-2 in 293T cells inhibited IFNgamma-dependent Stat1 phosphorylation and suppressed Stat1-dependent induction of luciferase activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling |
| + |
PTPN11 | up-regulates quantity by stabilization 
dephosphorylation
|
JAK2 |
0.789 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248665 |
Tyr1007 |
VLPQDKEyYKVKEPG |
Homo sapiens |
|
| pmid |
sentence |
| 14522994 |
We report that SHP-2 dephosphorylates tyrosine (Tyr-1007) of Jak2 kinase, a critical recruitment site for the ubiquitin ligase-associated inhibitory protein suppressor of cytokine signaling-1 (SOCS-1), thereby contributing to Jak2 stability. Inactivation of SHP-2 function by blocking receptor/SHP-2 association or by using a catalytically inactive mutant of SHP-2 led to a marked increase in Jak2 ubiquitination/degradation, Jak2 phosphorylation on Tyr-1007, and Jak2/SOCS-1 association |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, EGFR Signaling, Leptin Signaling |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
EGFR |
0.867 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248666 |
Tyr1016 |
DVVDADEyLIPQQGF |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 14560030 |
Inhibition is achieved through the dephosphorylation of RasGAP binding sites at the level of the plasma membrane. We have identified Tyr992 of the epidermal growth factor receptor (EGFR) to be one such site, since its mutation to Phe renders the EGFR refractory to the effect of dominant-negative SHP2. To our knowledge, this is the first report to outline the site and molecular mechanism of action of SHP2 in EGFR signaling, |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236424 |
Tyr1016 |
DVVDADEyLIPQQGF |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 12582165 |
Given that substrate trapping occurred in intact cells and that the interaction was very specific, it is highly likely that egfr and gab1 represent physiological shp2 substrates.To further confirm that phosphotyrosyl proteins trapped by SHP2 are target substrates, we carried out an immunocomplex in vitrophosphatase assay.The WT protein partially dephosphorylated both the EGFR and Gab1, whereas the DM protein did not |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Acute Myeloid Leukemia, EGFR Signaling, Noonan syndrome |
| + |
PTPN11 | down-regulates
dephosphorylation
|
ERBB2 |
0.834 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262957 |
Tyr1023 |
DLVDAEEyLVPQQGF |
in vitro |
|
| pmid |
sentence |
| 32024694 |
...which in turn suggests the importance SHP2 dephosphorylation of pTyr992 in EGFR and pTyr1023 in HER2 to mediate signaling.|More specifically, we show that acidic residues N-terminal to the substrate pTyr in EGFR and HER2 mediate specific binding by the SHP2 active site, leading to blockade of RasGAP binding and optimal signaling by the two receptors. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTPN11 | down-regulates
dephosphorylation
|
IRS1 |
0.895 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-27024 |
Tyr1179 |
GLENGLNyIDLDLVK |
Homo sapiens |
|
| pmid |
sentence |
| 7515062 |
The specific activity of four candidate protein-tyrosine phosphatases (protein-tyrosine phosphatase 1b (ptp1b), sh2 domain-containing ptpase-2 (shp-2), leukocyte common antigen-related (lar), and leukocyte antigen-related phosphatase) (lrp) toward irs-1 dephosphorylation was studied using recombinant proteins in vitro. Ptp1b exhibited the highest specific activity these results provide new insight into novel molecular interactions involving ptp1b and grb2 that may influence the steady-state capacity of irs-1 to function as a phosphotyrosine scaffold and possibly affect the balance of postreceptor insulin signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74856 |
Tyr1179 |
GLENGLNyIDLDLVK |
Homo sapiens |
|
| pmid |
sentence |
| 10660596 |
The specific activity of four candidate protein-tyrosine phosphatases (protein-tyrosine phosphatase 1b (ptp1b), sh2 domain-containing ptpase-2 (shp-2), leukocyte common antigen-related (lar), and leukocyte antigen-related phosphatase) (lrp) toward irs-1 dephosphorylation was studied using recombinant proteins in vitro. Ptp1b exhibited the highest specific activity these results provide new insight into novel molecular interactions involving ptp1b and grb2 that may influence the steady-state capacity of irs-1 to function as a phosphotyrosine scaffold and possibly affect the balance of postreceptor insulin signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-27028 |
Tyr896 |
EPKSPGEyVNIEFGS |
Homo sapiens |
|
| pmid |
sentence |
| 7515062 |
The specific activity of four candidate protein-tyrosine phosphatases (protein-tyrosine phosphatase 1b (ptp1b), sh2 domain-containing ptpase-2 (shp-2), leukocyte common antigen-related (lar), and leukocyte antigen-related phosphatase) (lrp) toward irs-1 dephosphorylation was studied using recombinant proteins in vitro. Ptp1b exhibited the highest specific activity these results provide new insight into novel molecular interactions involving ptp1b and grb2 that may influence the steady-state capacity of irs-1 to function as a phosphotyrosine scaffold and possibly affect the balance of postreceptor insulin signaling. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74860 |
Tyr896 |
EPKSPGEyVNIEFGS |
Homo sapiens |
|
| pmid |
sentence |
| 10660596 |
The specific activity of four candidate protein-tyrosine phosphatases (protein-tyrosine phosphatase 1b (ptp1b), sh2 domain-containing ptpase-2 (shp-2), leukocyte common antigen-related (lar), and leukocyte antigen-related phosphatase) (lrp) toward irs-1 dephosphorylation was studied using recombinant proteins in vitro. Ptp1b exhibited the highest specific activity these results provide new insight into novel molecular interactions involving ptp1b and grb2 that may influence the steady-state capacity of irs-1 to function as a phosphotyrosine scaffold and possibly affect the balance of postreceptor insulin signaling. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | Leptin Signaling |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
GRIN2B |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276950 |
Tyr1474 |
GSSNGHVyEKLSSIE |
Homo sapiens |
|
| pmid |
sentence |
| 32140036 |
In addition, surface expression of GluN2B was not reduced in mutant mice and it remains to be investigated how the direct dephosphorylation of GluN2B Y1252 by Shp2 reduces GluN2B function.|The increased GluN2B Y1472 phosphorylation was reversed by a Src family kinase inhibitor, suggesting that Shp2 may negatively regulate GluN2B Y1472 phosphorylation through suppressing Src activity . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates
dephosphorylation
|
CTNNA1 |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147075 |
Tyr148 |
LADMADVyKLLVQLK |
Homo sapiens |
|
| pmid |
sentence |
| 16767162 |
Tyr148 of beta-catenin is an shp2 target dephosphorylation site. Together, these results suggest that beta-catenin plays a suppressor role in cell transformation and that shp2, by dephosphorylating beta-catenin, promotes mitogenic, cell survival and transformation signals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | up-regulates activity
dephosphorylation, binding
|
GRB2 |
0.729 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276995 |
Tyr209 |
TGMFPRNyVTPVNRN |
Homo sapiens |
|
| pmid |
sentence |
| 23420874 |
Using an in vitro experiment in which purified full-length wild-type Shp2 (WT Shp2) was incubated with phosphorylated C-SH3 domain of Grb2 we demonstrated that Shp2 can dephosphorylate Grb2 on residue Y209 (XREF_FIG). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263498 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11085989 |
SHP-2 is thus a positive regulator of ERK by leptin receptors, and both the adaptor function and the phosphatase activity of SHP-2 are critical for this regulation. Based on these data, we conclude that tyrosinephosphorylation of SHP-2 is a mediator of ERK activation viaTyr-985. This is likely to occur via Grb-2 binding to SHP-2 atthe C terminus followed by activation of the Ras-Raf pathwayas suggested for other signaling systems (55, 56) and morerecently for the leptin receptor (33). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, EGFR Signaling, Noonan syndrome |
| + |
PTPN11 | down-regulates
dephosphorylation
|
MPZL1 |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75220 |
Tyr263 |
NKSESVVyADIRKN |
Homo sapiens |
|
| pmid |
sentence |
| 10681522 |
In vitro, tyrosine-phosphorylated pzr was efficiently dephosphorylated by the full-length form of shp-2 but not by its sh2 domain-truncated form. The coexisting binding and dephosphorylation of pzr by shp-2 may function to terminate signal transduction initiated by pzr and shp-2 and to set a threshold for the signal transduction to be initiated. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity
phosphorylation
|
PTPN11 |
0.789 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236266 |
Tyr304 |
PNEPVSDyINANIIM |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 8995399 |
Tyrosine residues 304 and 327 in shp-2 are phosphorylated by jaks, and phosphorylated shp-2 can associate with the downstream adapter protein grb2 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236270 |
Tyr327 |
NSKPKKSyIATQGCL |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 8995399 |
Tyrosine residues 304 and 327 in shp-2 are phosphorylated by jaks, and phosphorylated shp-2 can associate with the downstream adapter protein grb2 |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, EGFR Signaling, Leptin Signaling |
| + |
JAK1 | up-regulates activity
phosphorylation
|
PTPN11 |
0.762 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236282 |
Tyr304 |
PNEPVSDyINANIIM |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 8995399 |
Tyrosine residues 304 and 327 in shp-2 are phosphorylated by jaks, and phosphorylated shp-2 can associate with the downstream adapter protein grb2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236274 |
Tyr327 |
NSKPKKSyIATQGCL |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 8995399 |
Tyrosine residues 304 and 327 in shp-2 are phosphorylated by jaks, and phosphorylated shp-2 can associate with the downstream adapter protein grb2 |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
PTPN11 | up-regulates activity
dephosphorylation
|
NRAS |
0.666 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255754 |
Tyr32 |
QNHFVDEyDPTIEDS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26617336 |
Here we identify SHP2 as the ubiquitously expressed tyrosine phosphatase that preferentially binds to and dephosphorylates Ras to increase its association with Raf and activate downstream proliferative Ras/ERK/MAPK signalling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, KIT in AML, AML_TRIPLETS, NPM1_new, Noonan syndrome |
| + |
PTPN11 | up-regulates activity
dephosphorylation
|
KRAS |
0.652 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255982 |
Tyr32 |
QNHFVDEyDPTIEDS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26617336 |
Here we identify SHP2 as the ubiquitously expressed tyrosine phosphatase that preferentially binds to and dephosphorylates Ras to increase its association with Raf and activate downstream proliferative Ras/ERK/MAPK signalling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD signaling, Noonan syndrome |
| + |
PTPN11 | up-regulates activity
dephosphorylation
|
HRAS |
0.674 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252094 |
Tyr32 |
QNHFVDEyDPTIEDS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 26617336 |
Here we identify SHP2 as the ubiquitously expressed tyrosine phosphatase that preferentially binds to and dephosphorylates Ras to increase its association with Raf and activate downstream proliferative Ras/ERK/MAPK signalling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, Noonan syndrome |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
SRC |
0.644 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248670 |
Tyr419 |
RLIEDNEyTARQGAK |
Mus musculus |
|
| pmid |
sentence |
| 18482983 |
we identify SHP-2 and PTP-PEST as negative regulators of c-Src kinase | Inactivation of catalytically active c-Src kinase by the phosphatases SHP-2 or PTP-PEST by dephosphorylation of the tyrosine residue Tyr-416 within the c-Src kinase domain prevents the phosphorylation of villin |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | EGFR Signaling |
| + |
PTPN11 | up-regulates activity
dephosphorylation
|
SRC |
0.644 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248671 |
Tyr530 |
FTSTEPQyQPGENL |
Homo sapiens |
|
| pmid |
sentence |
| 17974954 |
Several protein tyrosine phosphatases are capable of activating Src by dephosphorylating Y530 (reviewed in ref. 9). These include PTP-α, PTP-λ, SHP-1, SHP-2, and PTP1B |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling |
| + |
PDGFRB | up-regulates activity
phosphorylation
|
PTPN11 |
0.743 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250260 |
Tyr542 |
SKRKGHEyTNIKYSL |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 8041791 |
Upon PDGF stimulation, SHPTP2 binds to the PDGFR and becomes tyrosine-phosphorylated. We have identified tyrosine-542 (pY542TNI) as the major in vivo site of SHPTP2 tyrosine phosphorylation. phosphorylation of SHPTP2 couples Grb2 to PDGFR in vivo, providing a mechanism for Ras activation by PDGFR and for positive signaling via SHPTP2 and Csw. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PTPN11 | up-regulates activity
dephosphorylation
|
JAK2 |
0.789 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277037 |
Tyr570 |
VRREVGDyGQLHETE |
Homo sapiens |
|
| pmid |
sentence |
| 30108215 |
Consistently, JAK2/STAT3 signaling was enhanced by overexpression of SHP2 with decreased levels of pJAK2 and increased levels of pJAK2 and pSTAT3 , while it was found suppressed by overexpression of SHP2 (Fig.\u00a06b).|We demonstrate that SHP2 can dephosphorylate JAK2 at Y570 to promote TGF\u03b2-dependent activation of JAK2 and its downstream mediator STAT3 (Supplementary Fig.\u00a04a). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, EGFR Signaling, Leptin Signaling |
| + |
PTPN11 | down-regulates
dephosphorylation
|
PTK2 |
0.725 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148926 |
Tyr577 |
YMEDSTYyKASKGKL |
Homo sapiens |
|
| pmid |
sentence |
| 16920701 |
Dca concomitantly and significantly increased association of tyrosine phosphatase shp2 with fak. Incubation of immunoprecipitated fak, in vitro, with glutathione-s-transferase-shp2 fusion protein resulted in tyrosine dephosphorylation of fak in a concentration-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates activity
phosphorylation
|
PTPN11 |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278217 |
Tyr580 |
REDSARVyENVGLMQ |
Homo sapiens |
|
| pmid |
sentence |
| 18827006 |
Direct phosphorylation of SHP-2 by Abl kinases (Y580) promotes sustained activation of SHP-2 signaling and proliferation, and c-Abl/Abl-Related Gene-dependent activation of tyrosine kinase X further potentiates SHP-2 signaling by phosphorylating SHP-2 on Y63.|Endogenous Abl kinases phosphorylate SHP-2 on Y580 and induce sustained ERK phosphorylation in response to PDGF. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
GAB1 |
0.952 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236258 |
Tyr589 |
SHDSEENyVPMNPNL |
Homo sapiens |
|
| pmid |
sentence |
| 10068651 |
Tyrosine phosphorylation of gab2 was induced by stimulation through gp130, il-2r, il-3r, tpor, scfr, and tcr. Gab1 and gab2 were shown to be substrates for shp-2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248674 |
Tyr627 |
KGDKQVEyLDLDLDS |
Homo sapiens |
|
| pmid |
sentence |
| 11323411 |
These results suggest that Tyr(P)-627 and Tyr(P)-659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) that binds and activates SHP2.|Thus, physical association of activated SHP2 with Gab1 is necessary and sufficient to mediate the ERK mitogen-activated protein kinase activation. Phosphopeptides derived from Gab1 were dephosphorylated by active SHP2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248675 |
Tyr659 |
VADERVDyVVVDQQK |
Homo sapiens |
|
| pmid |
sentence |
| 11323411 |
These results suggest that Tyr(P)-627 and Tyr(P)-659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) that binds and activates SHP2.|Thus, physical association of activated SHP2 with Gab1 is necessary and sufficient to mediate the ERK mitogen-activated protein kinase activation. Phosphopeptides derived from Gab1 were dephosphorylated by active SHP2 in vitro. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, Noonan syndrome |
| + |
PTPN11 | down-regulates
dephosphorylation
|
GAB2 |
0.737 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124958 |
Tyr614 |
KSTGSVDyLALDFQP |
Homo sapiens |
|
| pmid |
sentence |
| 15170389 |
Expression of the gab2 tyr-614-->phe (y614f) mutant, defective in shp-2 association, prevents erk (extracellular-signal-regulated kinase) activation and expression of a luciferase reporter plasmid driven by the c-fos sre (serum response element), indicating that interaction of shp-2 with gab2 is required for erk activation in response to il-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates
dephosphorylation
|
GAB1 |
0.952 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236262 |
Tyr627 |
KGDKQVEyLDLDLDS |
Homo sapiens |
|
| pmid |
sentence |
| 10068651 |
Tyrosine phosphorylation of gab2 was induced by stimulation through gp130, il-2r, il-3r, tpor, scfr, and tcr. Gab1 and gab2 were shown to be substrates for shp-2 in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236254 |
Tyr659 |
VADERVDyVVVDQQK |
Homo sapiens |
|
| pmid |
sentence |
| 10068651 |
Tyrosine phosphorylation of gab2 was induced by stimulation through gp130, il-2r, il-3r, tpor, scfr, and tcr. Gab1 and gab2 were shown to be substrates for shp-2 in vitro. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | EGFR Signaling, Noonan syndrome |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
STAT3 |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272404 |
Tyr705 |
DPGSAAPyLKTKFIC |
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 16611743 |
In addition, SHP-2 dephosphorylates tyrosine-phosphorylated Stat1/3/5A (Ohtani et al., 2000; Wu et al., 2002; Chen et al., 2003), and downregulates Stat3-mediated biological actions (Ohtani et al., 2000).|Inhibition of collagen-induced Stat3 tyrosine-705 (Stat3-p-Tyr) |
|
| Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
| Pathways: | Acute Myeloid Leukemia, KIT in AML, EGFR Signaling, FLT3-ITD signaling, Leptin Signaling |
| + |
PTPN11 | up-regulates
dephosphorylation
|
MAP3K5 |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184604 |
Tyr718 |
IPERDSRySQPLHEE |
Homo sapiens |
|
| pmid |
sentence |
| 19287004 |
Previously we have shown that tyrosine 718 of ask1 when phosphorylated is critical for socs1 binding and socs1-mediated degradation of ask1we identified jak2 and shp2 as a tyr-718-specific kinase and phosphatase, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
PDGFRB |
0.743 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248667 |
Tyr740 |
TGESDGGyMDMSKDE |
in vitro |
|
| pmid |
sentence |
| 7545675 |
Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248668 |
Tyr751 |
SKDESVDyVPMLDMK |
in vitro |
|
| pmid |
sentence |
| 7545675 |
Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248669 |
Tyr771 |
ADIESSNyMAPYDNY |
in vitro |
|
| pmid |
sentence |
| 7545675 |
Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
PTK2B |
0.718 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277084 |
Tyr906 |
CQLPPEGyVVVVKNV |
Homo sapiens |
|
| pmid |
sentence |
| 10880513 |
We demonstrate that RAFTK is a direct substrate of SHP2 both in vitro and in vivo, and that Tyr(906) in the C-terminal domain of RAFTK mediates its interaction with SHP2. |We demonstrate that RAFTK is a direct substrate of SHP2 both in vitro and in vivo, and that Tyr(906) in the C-terminal domain of RAFTK mediates its interaction with SHP2. Moreover, overexpression of dominant negative SHP2 blocked the protective effect of IL-6 against Dex-induced apoptosis. These findings demonstrate that SHP2 mediates the anti-apoptotic effect of IL-6 and suggest SHP2 as a novel therapeutic target in MM..... 1) RAFTK is a substrate of SHP2 in vitro and 2) dephosphorylation of RAFTK by SHP2 inhibits its kinase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DDR1 | up-regulates activity
relocalization
|
PTPN11 |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272403 |
|
|
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 16611743 |
Overexpression of DDR1a/b increased the interaction of DDR1 with SHP-2 and up-regulated the tyrosine phosphatase activity of SHP-2. |
|
| Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
| + |
PTPN11 | up-regulates activity
dephosphorylation
|
GRB7 |
0.441 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277169 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20142421 |
Dephosphorylation of Grb7 was blocked by the SHP inhibitor NSC-87877 (Zhan et al., 2009), supporting the specificity of SHP-2 in dephosphorylating Grb7.|Nuclear SHP-2 mediates the formation of an EGF induced complex of Grb7, HuR, and CRM1.|Using the \u03ba\u2013opioid receptor (OR [KOR]) as a model, we demonstrate that EGF activates nuclear SHP-2 (Src homology region 2\u2013containing tyrosine phosphatase), which dephosphorylates Grb7 in the nucleus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
8-Hydroxy-7-(6-sulfo-naphthalen-2-ylazo)-quinoline-5-sulfonic acid | down-regulates activity
chemical inhibition
|
PTPN11 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261977 |
|
|
in vitro |
|
| pmid |
sentence |
| 19233143 |
In this study, we screened protein tyrosine phosphatases (PTPs) by in vitro phosphatase assays to identify PTPs that are inhibited by 8-hydroxy-7-(6-sulfonaphthalen-2-yl)diazenyl-quinoline-5-sulfonic acid (NSC-87877), a potent inhibitor of SHP-1 and SHP-2 PTPs. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
FCRL3 | up-regulates activity
binding
|
PTPN11 |
0.389 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274014 |
|
|
in vitro |
|
| pmid |
sentence |
| 12051764 |
Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
NTRK2 |
0.699 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277123 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28947394 |
Conversely, PTPN11 knockdown lead to increased Y 515 phosphorylation of TrkB compared to the scramble control in the neuronal cells.|This study established that TrkB activation as demonstrated by receptor phosphorylation at Tyr 515 in the SH-SY5Y cells is negatively regulated by PTPN11 actions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
NEDD9 |
0.497 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277083 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19275884 |
In this study we demonstrated that SHP-2 inhibits tyrosine phosphorylation of Cas-L, and negatively regulates the cell migration induced by Cas-L.|These results show that both SH2 domains of SHP-2 are necessary for the interaction with Cas-L.\nIn this study we demonstrated that SHP-2 inhibits tyrosine phosphorylation of Cas-L, and negatively regulates the cell migration induced by Cas-L. Furthermore, our data raise the possibility that Cas-L is a direct substrate for SHP-2, although SHP-2 may inhibit Cas-L phosphorylation indirectly by regulating kinase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | up-regulates activity
dephosphorylation
|
CDC73 |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277036 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21726809 |
We found in this work that SHP2 dephosphorylates parafibromin and Cdc73, a component of the nuclear RNA polymerase II associated factor (PAF) complex, which can function as a tumor suppressor or oncoprotein in a context dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HOOK1 | down-regulates activity
binding
|
PTPN11 |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260642 |
|
|
Homo sapiens |
A-549 Cell |
| pmid |
sentence |
| 25331952 |
The protein-tyrosine phosphatase domain and N-terminal SH2 domain of SHP2 directly interacted with Hook1. Down-regulation of Hook1 increased SHP2 activity. These results suggested that Hook1 was an endogenous negative regulator of SHP2 phosphatase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LEPR | up-regulates activity
binding
|
PTPN11 |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263506 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11085989 |
Because the long leptin receptor lacking tyrosine 985 exhibits a significantly reduced ability to activate ERK phosphorylation, this residue is at least in part mediating stimulation of the ERK pathway by ObRb. This residue binds SHP-2 and is required for tyrosine phosphorylation of SHP-2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Leptin Signaling |
| + |
KIT | up-regulates activity
phosphorylation
|
PTPN11 |
0.677 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256140 |
|
|
Mus musculus |
32D Cell |
| pmid |
sentence |
| 22806893 |
SHP2 can be phosphorylated at 2 C-terminal tyrosyl residues by receptor tyrosine kinases, including KIT as well as cytosolic tyrosine kinases, including Src and Abl. The level of tyrosyl phosphorylation of SHP2 has been associated with its recruitment to the receptor.Thus, pharmacologic inhibition of SHP2 phosphatase function might permit SHP2 to return to its inactive conformation resulting in reduced tyrosine phosphorylation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, KIT in AML |
| + |
FLT3 | up-regulates activity
binding
|
PTPN11 |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245057 |
|
|
Mus musculus |
32D Cell |
| pmid |
sentence |
| 16684964 |
Y599 was additionally found to interact with the protein tyrosine phosphatase SHP2 in a phosphorylation-dependent manner. As Y599F-Flt3-32D was unable to associate with and to phosphorylate SHP2 and since silencing of SHP2 in WT-Flt3-expressing cells mimicked the Y599F-Flt3 phenotype, we hypothesize that recruitment of SHP2 to pY599 contributes to FL-mediated Erk activation and proliferation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, AML_TRIPLETS, FLT3-ITD signaling, NPM1_new |
| + |
PTPN11 | down-regulates
dephosphorylation
|
SPRY1 |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144547 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16481357 |
These results identify sprouty proteins as in vivo targets of corkscrew/shp-2 tyrosine phosphatases and show how corkscrew/shp-2 proteins can promote rtk signaling by inactivating a feedback inhibitor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Noonan syndrome |
| + |
PTPN11 | up-regulates
dephosphorylation
|
CSF2RB |
0.497 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-48557 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9162089 |
Shp2 is thought to act as a positive mediator of growth factor signals.. Hp2 could act as an adaptor between the activated c and grb2, thus leading to activation of the ras/mitogen-activated protein kinase pathway, known to be activated by il-3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
8-oxo-7-[(6-sulfo-2-naphthalenyl)hydrazinylidene]-5-quinolinesulfonic acid | down-regulates activity
chemical inhibition
|
PTPN11 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261912 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16717135 |
These results identified NSC-87877 as the first PTP inhibitor capable of inhibiting Shp2 PTP in cell cultures without a detectable off-target effect. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FRS2 | up-regulates
phosphorylation
|
PTPN11 |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-58196 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9632781 |
In addition to the direct interactions with grb2, tyrosine-phosphorylated frs2 forms a complex with the sh2 domain-containing protein tyrosine phosphatase shp2. This interaction results in tyrosine phosphorylation of shp2 and complex formation between shp2 and grb2. the catalytic activity of shp2 is essential for a sustained map kinase response and for potentiation of fgf-induced neurite outgrowth in pc12 cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
ITK |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277174 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33624224 |
Using genetic and pharmacological approaches, we discovered that SHP2 dephosphorylates ITK specifically downstream of PD-1 and that this event was associated with PD-1 inhibitory cellular functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | up-regulates activity 
|
ERK1/2 |
0.863 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263500 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11085989 |
We show here that leptin can activate ERK signaling in thehypothalamus and that this stimulation is likely to occur viatwo pathways, both involving SHP-2.We have shown above that SHP-2 is a positive mediator of ERK activation by ObRb and that this requires both the phosphatase activity and tyrosine phosphorylation of SHP-2. Furthermore,Tyr-985 is required for maximal ERK phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263499 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11085989 |
We show here that leptin can activate ERK signaling in thehypothalamus and that this stimulation is likely to occur viatwo pathways, both involving SHP-2.We have shown above that SHP-2 is a positive mediator of ERK activation by ObRb and that this requires both the phosphatase activity and tyrosine phosphorylation of SHP-2. Furthermore,Tyr-985 is required for maximal ERK phosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, AML_TRIPLETS, EGFR Signaling, FLT3-ITD signaling, Leptin Signaling, NPM1_new, Noonan syndrome |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
SYK |
0.533 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277085 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23182168 |
Another SHP isoform, SHP-2, has been linked to negative regulation of Syk.|Syk and LAT are differentially dephosphorylated by SHP-2 and SHP-1, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
SLC25A4 |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277124 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29255148 |
Specifically, SHP2-mediated dephosphorylation of ANT1 at Tyr 191 is essential for mitochondrial homeostasis and mitigation of NLRP3 inflammasome activation.|The interaction between SHP2 and ANT1 (Fig.\u00a0 xref ), and the opposite effects of SHP2 and ANT1 shRNAs in the activation of NLRP3 inflammasome (Figs.\u00a0 xref and xref ) raised the possibility that the SHP2 may inhibit ANT1 to suppress NLRP3 inflammasome activation.|To further determine which tyrosine phosphorylation site of ANT1 is dephosphorylated by SHP2, we created the dephosphorylated mutant of ANT1, in which tyrosine was replaced with phenylalanine (Y to F mutation). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | up-regulates quantity by stabilization
dephosphorylation
|
MAP3K5 |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276144 |
|
|
Homo sapiens |
Aorta Cell Line |
| pmid |
sentence |
| 19287004 |
In this study, we identified JAK2 and SHP2 as a Tyr-718-specific kinase and phosphatase, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
FGFR2 |
0.613 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277030 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23420874 |
In forming this heterotetrameric complex Grb2 inhibits both the dephosphorylation of FGFR2 by Shp2 and the phosphorylation of Shp2 by FGFR2 (XREF_FIG, respectively).|Knockdown of Grb2 elevates Shp2 phosphorylation (XREF_FIG), strongly suggesting that the inability of Shp2 to interact directly with the receptor in the presence of Grb2 prevents FGFR2 kinase activity toward Shp2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
IRF8 |
0.358 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277173 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27769062 |
We found that Bcr-abl-induced, Shp2 dependent dephosphorylation of Icsbp impaired repression of GAS2 by this transcription factor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
PDCD1 |
0.651 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277052 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32437509 |
Related to the latter notion, we recently showed that SHP2 dephosphorylates PD-1 to disassemble the PD-1:SHP2 complex ( xref ). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | up-regulates activity
dephosphorylation
|
CDKN1B |
0.284 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277168 |
|
|
in vitro |
|
| pmid |
sentence |
| 19066472 |
Moreover, SHP-2 was strongly activated on G-CSF stimulation and specifically dephosphorylated p27(Kip1) in vitro.|Most importantly, we could illustrate that SHP-2 modulates p27 (Kip1) stability and contributes to p27 (Kip1)-mediated cell cycle progression. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Acute Myeloid Leukemia |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
α-Catenin |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265824 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16767162 |
Tyr148 of beta-catenin is an shp2 target dephosphorylation site. Together, these results suggest that beta-catenin plays a suppressor role in cell transformation and that shp2, by dephosphorylating beta-catenin, promotes mitogenic, cell survival and transformation signals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | up-regulates
dephosphorylation
|
HOXA10 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182475 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19022774 |
We also identified hoxa10 as a substrate for shp2 in undifferentiated myeloid cells, an effect that diminished during myelopoiesis. However, a constitutively active form of shp2 dephosphorylated hoxa10 throughout ex vivo myelopoiesis and sustained repression of hoxa10 target genes involved in phagocyte effector functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PTPN11
- 
- 