| + |
PRKG2 | up-regulates activity 
phosphorylation
|
PTPN6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276288 |
Ser553 |
KNAHAKAsRTSSKHK |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21177494 |
PKGII directly phosphorylated and stimulated SHP-1 activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276286 |
Ser556 |
HAKASRTsSKHKEDV |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21177494 |
PKGII directly phosphorylated and stimulated SHP-1 activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276287 |
Ser557 |
AKASRTSsKHKEDVY |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 21177494 |
PKGII directly phosphorylated and stimulated SHP-1 activity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKCA | down-regulates 
phosphorylation
|
PTPN6 |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126876 |
Ser591 |
DKEKSKGsLKRK |
Homo sapiens |
|
| pmid |
sentence |
| 15269224 |
Protein kinase calpha therefore critically and negatively regulates shp-1 function, forming part of a mechanism to retain shp-1 in a basal active state through interaction with its sh2 domains, and phosphorylating its c-terminal ser591 upon cellular activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCQ | down-regulates activity
phosphorylation
|
PTPN6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277590 |
Ser591 |
DKEKSKGsLKRK |
Homo sapiens |
Natural Killer Cell |
| pmid |
sentence |
| 35258455 |
SHP-1 phosphorylation is mediated through PKC-θ. Here, we show that phosphorylation of SHP-1 in NK cells on the S591 residue by PKC-θ promotes the inhibited SHP-1 'folded' state. Silencing PKC-θ maintains SHP-1 in the active conformation, reduces NK cell activation and cytotoxicity, and promotes tumor progression in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
PKM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276997 |
Tyr105 |
FASDPILyRPVAVAL |
Homo sapiens |
|
| pmid |
sentence |
| 26959741 |
SHP-1 dephosphorylates PKM2 at Y105 to inhibit nuclear function of PKM2 and determines the efficacy of targeted drugs.|SHP-1 directly dephosphorylated PKM2 at Y105 and further decreased the proliferative activity of PKM2; similar effects were found in sorafenib-treated hepatocellular carcinoma cells.|SHP-1 dephosphorylates p-PKM2Y105 and further affects the nucleus-related cell proliferation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
KDR |
0.654 |
| 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 |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
TRAF3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277527 |
Tyr116 |
EILALQIyCRNESRG |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 32779804 |
We identified a direct interaction between SHP‐1 and TRAF3; the association between these two proteins resulted in diminished recruitment of CK1ε to TRAF3 and inhibited its K63‐linked ubiquitination; SHP‐1 inhibited K63‐linked ubiquitination of TRAF3 by promoting dephosphorylation at Tyr116 and Tyr446. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277526 |
Tyr446 |
SLYSQPFyTGYFGYK |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 32779804 |
We identified a direct interaction between SHP‐1 and TRAF3; the association between these two proteins resulted in diminished recruitment of CK1ε to TRAF3 and inhibited its K63‐linked ubiquitination; SHP‐1 inhibited K63‐linked ubiquitination of TRAF3 by promoting dephosphorylation at Tyr116 and Tyr446. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
dephosphorylation
|
INSR |
0.366 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75926 |
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-75930 |
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-75934 |
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-75938 |
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: |
4 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
dephosphorylation
|
EGFR |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59965 |
Tyr1197 |
STAENAEyLRVAPQS |
Homo sapiens |
|
| pmid |
sentence |
| 9733788 |
The sh2-domain ptpase shp-1 binds to and dephosphorylates autophosphorylated egfr and may participate in modulation of egfr signaling in epithelial cells. Reduced shp-1 binding to the egfr y1173f mutant resulted in a reduced receptor dephosphorylation by coexpressed shp-1 and less interference with egf-dependent mitogen-activated protein kinase stimulation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD in AML |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
NFAT5 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248467 |
Tyr143 |
PKRHTVLyISPPPED |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20351292 |
We confirmed that SHP-1 is inhibitory by overexpressing it, which reduces TonEBP/OREBP transcriptional activity at 500 mosmol/kg. SHP-1 dephosphorylates TonEBP/OREBP at a known regulatory site, Y143, both in vivo and in vitro. It inhibits TonEBP/OREBP by both reducing TonEBP/OREBP nuclear localization, which is Y143 dependent, and by lowering high NaCl-induced TonEBP/OREBP transactivating activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
dephosphorylation
|
ACTG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-99565 |
Tyr218 |
DIKEKLCyVALDFEQ |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 12646642 |
Our data suggest that shp-1 plays a pivotal role in reorganization of cytoskeletal architecture inducing actin dephosphorylation. These results clearly demonstrate the direct interaction of shp-1 with actin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
dephosphorylation
|
ROS1 |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105919 |
Tyr2274 |
KNREGLNyMVLATEC |
Homo sapiens |
|
| pmid |
sentence |
| 11266449 |
Phosphorylated ros strongly and directly associates with shp-1.Overexpression Of shp-1 results in ros dephosphorylation and effectively downregulates ros-dependent proliferation and transformation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105922 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11266449 |
Overexpression of shp-1 results in ros dephosphorylation and effectively downregulates ros-dependent proliferation and transformation. We propose that shp-1 is an important downstream regulator of ros signaling. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | up-regulates activity
dephosphorylation
|
CASP8 |
0.361 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248477 |
Tyr380 |
TDSEEQPyLEMDLSS |
Homo sapiens |
|
| pmid |
sentence |
| 18086677 |
Caspase-8 is tyrosine-phosphorylated in freshly isolated neutrophils but spontaneously dephosphorylates in culture, in association with the progression of constitutive apoptosis. Phosphorylation of caspase-8 on Tyr-310 facilitates its interaction with the Src-homology domain 2 containing tyrosine phosphatase-1 (SHP-1) and enables SHP-1 to dephosphorylate caspase-8, permitting apoptosis to proceed. The non-receptor tyrosine kinase, Lyn, can phosphorylate caspase-8 on Tyr-397 and Tyr-465, rendering it resistant to activational cleavage and inhibiting apoptosis. Exposure to lipopolysaccharide reduces SHP-1 activity and binding to caspase-8, caspase-8 activity, and rates of spontaneous apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248478 |
Tyr448 |
TILTEVNyEVSNKDD |
Homo sapiens |
|
| pmid |
sentence |
| 18086677 |
Caspase-8 is tyrosine-phosphorylated in freshly isolated neutrophils but spontaneously dephosphorylates in culture, in association with the progression of constitutive apoptosis. Phosphorylation of caspase-8 on Tyr-310 facilitates its interaction with the Src-homology domain 2 containing tyrosine phosphatase-1 (SHP-1) and enables SHP-1 to dephosphorylate caspase-8, permitting apoptosis to proceed. The non-receptor tyrosine kinase, Lyn, can phosphorylate caspase-8 on Tyr-397 and Tyr-465, rendering it resistant to activational cleavage and inhibiting apoptosis. Exposure to lipopolysaccharide reduces SHP-1 activity and binding to caspase-8, caspase-8 activity, and rates of spontaneous apoptosis. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
LCK |
0.596 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106604 |
Tyr394 |
RLIEDNEyTAREGAK |
Homo sapiens |
|
| pmid |
sentence |
| 11294838 |
We demonstrate that shp-1 dephosphorylates the lymphoid-specific src family kinase lck at tyr-394. Because phosphorylation of tyr-394 activates lck, the fact that shp-1 specifically dephosphorylates this site suggests that shp-1 is a negative regulator of lck. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
LYN |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248471 |
Tyr397 |
RVIEDNEyTAREGAK |
Rattus norvegicus |
|
| pmid |
sentence |
| 15537644 |
SHP-1 efficiently inhibits Lyn autophosphorylation and suppresses FcϵRI stimulation|We found that PTPα and SHP-1 both dephosphorylate Lyn exclusively at Tyr-397 |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PTPN6 | down-regulates
dephosphorylation
|
PTK2B |
0.366 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71414 |
Tyr402 |
CSIESDIyAEIPDET |
Homo sapiens |
|
| pmid |
sentence |
| 10521452 |
Raftk binds constitutively to the protein tyrosine phosphatase shptp1.SHPTP1 Plays a negative role in pyk2/raftk signaling by dephosphorylating raftk on tyr-402, thereby inhibiting the interaction of the sh2 domain of c-src with raftk |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
CTTN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277003 |
Tyr421 |
RLPSSPVyEDAASFK |
Homo sapiens |
|
| pmid |
sentence |
| 34088320 |
Shp1 interacts with cortactin and reduces cortactin phosphorylation at tyrosine 421; 3.|induction of Shp1-cortactin complex formation impairs cortactin scaffolding-activity and negatively affects invadopodia behaviour; 4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
SH3BP2 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277172 |
Tyr448 |
GDDSDEDyEKVPLPN |
Homo sapiens |
|
| pmid |
sentence |
| 16649996 |
Shp-1 dephosphorylates 3bp2 and potentially downregulates 3bp2-mediated t cell antigen receptor signaling|adaptor protein 3BP2 serves as a binding protein and a physiological substrate of SHP-1. 3BP2 is phosphorylated on tyrosyl residue 448 in response to TCR activation, and the phosphorylation is required for T c |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | up-regulates activity
dephosphorylation
|
SRC |
0.542 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248473 |
Tyr530 |
FTSTEPQyQPGENL |
Homo sapiens |
|
| pmid |
sentence |
| 9261115 |
To determine whether the COOH-terminal or other phosphotyrosine residues within Src are subject to dephosphorylation by SHP-1, the effects of this phosphatase on Src tyrosine phosphorylation were initially examined using CNBr cleavage analysis. As illustrated in Fig.1 A, CNBr treatment of 32P-labeled human Src has been shown previously to yield phosphorylated cleavage fragments of about 31, 9.7, and 4.7 kDa, which, respectively, contain the Src NH2-terminal region encompassing the major sites for serine phosphorylation on Src, Ser-12 and Ser-17 (31-kDa fragment), the inhibitory tyrosine phosphorylation site, Tyr-530 (4.7-kDa fragment), and a key site for autophosphorylation on activated Src, Tyr-419 [} These observations, together with the finding of reduced Src activity in HEY cells expressing a dominant negative form of SHP-1, provide compelling evidence that SHP-1 functions include the positive regulation of Src activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248472 |
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: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates
phosphorylation
|
PTPN6 |
0.542 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120488 |
Tyr536 |
QKGQESEyGNITYPP |
Homo sapiens |
|
| pmid |
sentence |
| 14699166 |
Recombinant shp-1 had elevated activity subsequent to phosphorylation by src in vitro, and shp-1 variants with mutated phosphorylation sites in the c terminus, shp-1 y538f, and shp-1 y538f,y566f were less active toward src-generated phosphoproteins in intact cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120492 |
Tyr564 |
SKHKEDVyENLHTKN |
Homo sapiens |
|
| pmid |
sentence |
| 14699166 |
Recombinant shp-1 had elevated activity subsequent to phosphorylation by src in vitro, and shp-1 variants with mutated phosphorylation sites in the c terminus, shp-1 y538f, and shp-1 y538f,y566f were less active toward src-generated phosphoproteins in intact cells. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates activity
phosphorylation
|
PTPN6 |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246236 |
Tyr536 |
QKGQESEyGNITYPP |
in vitro |
|
| pmid |
sentence |
| 12468540 |
Incorporation of Pmp at the 536 site led to 4-fold stimulation of the SHP-1 tyrosine phosphatase activity whereas incorporation at the 564 site led to no effect |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246227 |
Tyr536 |
QKGQESEyGNITYPP |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 8692915 |
Treatment with ionizing radiation is associated with c-Abl-dependent tyrosine phosphorylation of SHPTP1. The results demonstrate that the SH3 domain of c-Abl interacts with a WPDHGVPSEP motif (residues 417-426) in the catalytic domain of SHPTP1 and that c-Abl phosphorylates C terminal Y536 and Y564 sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260820 |
Tyr536 |
QKGQESEyGNITYPP |
Homo sapiens |
|
| pmid |
sentence |
| 8692915 |
The results demonstrate that the SH3 domain of ABL1 interacts with a WPDHGVPSEP motif (residues 417-426) in the catalytic domain of SHPTP1 and that ABL1 phosphorylates C terminal Y536 and Y564 sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251433 |
Tyr564 |
SKHKEDVyENLHTKN |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 8692915 |
The SH3 domain of c-Abl interacts with a WPDHGVPSEP motif (residues 417-426) in the catalytic domain of SHPTP1 and that c-Abl phosphorylates C terminal Y536 and Y564 sites. The functional significance of the c-Abl-SHPTP1 interaction is supported by the demonstration that, like c-Abl, SHPTP1 regulates the induction of Jun kinase activity following DNA damage. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260821 |
Tyr564 |
SKHKEDVyENLHTKN |
Homo sapiens |
|
| pmid |
sentence |
| 8692915 |
The results demonstrate that the SH3 domain of ABL1 interacts with a WPDHGVPSEP motif (residues 417-426) in the catalytic domain of SHPTP1 and that ABL1 phosphorylates C terminal Y536 and Y564 sites. |
|
| Publications: |
5 |
Organism: |
In Vitro, Homo Sapiens |
| + |
INSR | up-regulates
phosphorylation
|
PTPN6 |
0.366 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-26870 |
Tyr536 |
QKGQESEyGNITYPP |
Homo sapiens |
|
| pmid |
sentence |
| 7512963 |
Insulin stimulates the phosphorylation of tyr538 and the catalytic activity of ptp1c, a protein tyrosine phosphatase with src homology-2 domains. these results suggest that ptp1c is a target protein for the insulin receptor tyrosine kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LCK | up-regulates activity
phosphorylation
|
PTPN6 |
0.596 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251387 |
Tyr536 |
QKGQESEyGNITYPP |
Mus musculus |
T-lymphocyte |
| pmid |
sentence |
| 8114715 |
Two sites (Y-536 and Y-564) which are directly phosphorylated by Lck in vitro are also phosphorylated in vivo in LSTRA cells. . |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ABL1 |
phosphorylation
|
PTPN6 |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246240 |
Tyr564 |
SKHKEDVyENLHTKN |
in vitro |
|
| pmid |
sentence |
| 12468540 |
Incorporation of Pmp at the 536 site led to 4-fold stimulation of the SHP-1 tyrosine phosphatase activity whereas incorporation at the 564 site led to no effect |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246231 |
Tyr564 |
SKHKEDVyENLHTKN |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 8692915 |
Treatment with ionizing radiation is associated with c-Abl-dependent tyrosine phosphorylation of SHPTP1. The results demonstrate that the SH3 domain of c-Abl interacts with a WPDHGVPSEP motif (residues 417-426) in the catalytic domain of SHPTP1 and that c-Abl phosphorylates C terminal Y536 and Y564 sites. |
|
| Publications: |
2 |
Organism: |
In Vitro, Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
PTPN6 |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251409 |
Tyr564 |
SKHKEDVyENLHTKN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10574931 |
Lyn phosphorylates SHPTP1 at the C-terminal Tyr-564 site. Lyn-mediated phosphorylation of SHPTP1 stimulates SHPTP1 tyrosine phosphatase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LCK | up-regulates
phosphorylation
|
PTPN6 |
0.596 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36121 |
Tyr564 |
SKHKEDVyENLHTKN |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 8114715 |
The two sites (y-536 and y-564) which are directly phosphorylated by lck in vitro are also phosphorylated in vivo in lstra cells. One of these sites (y-564) is phosphorylated in t cells in response to lck activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
dephosphorylation
|
CSF2RB |
0.5 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-48561 |
Tyr628 |
PPPGSLEyLCLPAGG |
Homo sapiens |
|
| pmid |
sentence |
| 9162089 |
However, inhibition of shp2 binding to betac, did not prevent tyrosine phosphorylation of shp2. Interestingly, this same phosphopeptide served as a substrate for the tyrosine phosphatase activity of both shp1 and shp2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-114597 |
Tyr628 |
PPPGSLEyLCLPAGG |
Homo sapiens |
|
| pmid |
sentence |
| 11812650 |
However, inhibition of shp2 binding to betac, did not prevent tyrosine phosphorylation of shp2. Interestingly, this same phosphopeptide served as a substrate for the tyrosine phosphatase activity of both shp1 and shp2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates quantity by destabilization
dephosphorylation
|
CTNNB1 |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277014 |
Tyr654 |
RNEGVATyAAAVLFR |
Homo sapiens |
|
| pmid |
sentence |
| 20840866 |
Because SHP-1 can dephosphorylate residues Y86 and Y654 on the \u03b2-catenin protein, these residues were therefore mutated into phenylalanine and the transcriptional activity of the subsequent \u03b2-catenin mutants analyzed: \u03b2-catenin/Y86F, \u03b2-catenin/Y654F and \u03b2-catenin/Y86F/Y654F. As shown in Fig.\u00a03 B, the mutants \u03b2-catenin/Y86F, \u03b2-catenin/Y654F and \u03b2-catenin/Y86F/Y654F had a significantly reduced transcriptional activity in comparison to wild-type \u03b2-catenin.|SHP-1 inhibits \u03b2-catenin function by inducing its degradation and interfering with its association with TATA-binding protein. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277013 |
Tyr86 |
VADIDGQyAMTRAQR |
Homo sapiens |
|
| pmid |
sentence |
| 20840866 |
In the present investigation, we demonstrate that SHP-1 dephosphorylates \u03b2-catenin on tyrosines 86 and 654 and promotes its proteasomal degradation.|SHP-1 inhibits \u03b2-catenin function by inducing its degradation and interfering with its association with TATA-binding protein. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
NTRK1 |
0.489 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248468 |
Tyr680 |
RDIYSTDyYRVGGRT |
Rattus norvegicus |
|
| pmid |
sentence |
| 14662744 |
Here, we identify SHP-1 as a phosphotyrosine phosphatase that negatively regulates TrkA. SHP-1 formed complexes with TrkA at Y490, and dephosphorylated it at Y674/675. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248469 |
Tyr681 |
DIYSTDYyRVGGRTM |
Rattus norvegicus |
|
| pmid |
sentence |
| 14662744 |
Here, we identify SHP-1 as a phosphotyrosine phosphatase that negatively regulates TrkA. SHP-1 formed complexes with TrkA at Y490, and dephosphorylated it at Y674/675. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
PTPN6 |
dephosphorylation
|
KDR |
0.654 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248476 |
Tyr996 |
EEAPEDLyKDFLTLE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18840653 |
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: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
dephosphorylation
|
ZAP70 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-70237 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 10458769 |
We propose that shp1 can dephosphorylate sites in zap-70 and syk that are involved in coupling these kinases to downstream signaling cascades, including erk2 and elements of the il-2 gene. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FLT3 | down-regulates quantity 
transcriptional regulation
|
PTPN6 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259950 |
|
|
Homo sapiens |
TF-1 Cell |
| pmid |
sentence |
| 15574429 |
Furthermore, a small but reproducible growth/survival advantage was observed in both TF-1 and TF-1/ITD cells when SHP-1 expression was knocked down by RNAi. Taken together, these data provide the first evidence that suppression of SHP-1 by FLT3/ITD signaling may be another mechanism contributing to the transformation by FLT3/ITD mutations |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML |
| + |
PTPN6 | up-regulates
dephosphorylation
|
JAK3 |
0.675 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-82764 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11021818 |
The expression of shp-1 protein was associated with dephosphorylation of the jak3 kinase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FCRL3 | up-regulates activity
binding
|
PTPN6 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274013 |
|
|
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 |
| + |
PKNOX1 | up-regulates quantity by expression 
transcriptional regulation
|
PTPN6 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254924 |
|
|
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 20864515 |
Prep1 overexpression in HepG2 liver cells upregulated SYP and SHP1 and inhibited insulin-induced IR and IRS1/2 phosphorylation and was accompanied by reduced glycogen content. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | up-regulates
binding
|
SOCS1 |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-118572 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14551136 |
All together, our results indicate that shp-1 inhibits prlr and epor signaling by recruitment and targeting of socs-1 to jak2, highlighting a new mechanism of shp-1 regulation of cytokine-receptor signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
dephosphorylation
|
CD72 |
0.607 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60155 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 9740800 |
Our work clearly identifies cd72 as both an shp-1 binding protein (figure 1,figure 2) and a direct substrate for shp-1 in vivo (figure 3). As tyrosine phosphorylation of cd72 strongly correlates with the ability of the bcr to deliver growth-inhibitory/apoptosis-inducing signals (figure 4), our results suggest that shp-1-catalyzed dephosphorylation of cd72 may antagonize these signals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
JAK2 |
0.718 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248466 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 8943354 |
Direct association with and dephosphorylation of Jak2 kinase by the SH2-domain-containing protein tyrosine phosphatase SHP-1 |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML |
| + |
PTPN6 | down-regulates
|
TYK2 |
0.589 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119200 |
|
|
Homo sapiens |
Breast Cancer Cell, Leukemia Cell, Lymphoma Cell, JURKAT Cell, RAMOS Cell |
| pmid |
sentence |
| 14624462 |
We find, for the first time, that shp-1 down-regulates the level of tyk2 kinase in h9 cells and of jak1 kinase in htb26 cells, by accelerating their degradation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
dephosphorylation
|
SH3BP2 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146508 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16649996 |
Shp-1 dephosphorylates 3bp2 and potentially downregulates 3bp2-mediated t cell antigen receptor signaling |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FLT3 | down-regulates quantity by repression
transcriptional regulation
|
PTPN6 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261532 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15574429 |
Expression of FLT3/ITD induces down-regulation of SHP-1 expression and activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, FLT3 in AML, FLT3-ITD in AML |
| + |
8-Hydroxy-7-(6-sulfo-naphthalen-2-ylazo)-quinoline-5-sulfonic acid | down-regulates activity
chemical inhibition
|
PTPN6 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261978 |
|
|
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 |
| + |
PTPN6 | down-regulates
dephosphorylation
|
IL2RB |
0.51 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-55989 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 9520455 |
We have found that il-2 induces association of shp-1 with the il-2 receptor complex, and that once shp-1 is recruited to the activated receptor it is able to decrease tyrosine phosphorylation of il-2rbeta and the associated tyrosine kinases jak1 and jak3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
|
STAT6 |
0.603 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-62578 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 9852037 |
Expression of an shp-1 transgene in nih 3t3 cells markedly reduces both il-4-dependent stat6 activation and stat6-mediated transcription of il-4-responsive genes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
8-oxo-7-[(6-sulfo-2-naphthalenyl)hydrazinylidene]-5-quinolinesulfonic acid | down-regulates activity
chemical inhibition
|
PTPN6 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261913 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20337577 |
NSC-87877 (1, Fig. (7)) was identified as a Shp2 PTP inhibitor with an IC50 of 0.33 μM [83]. NSC-87877 inhibits Shp1 with the same potency. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
dephosphorylation
|
KCNH2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94007 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12361947 |
Our results show that erg-1 is a shp-1 substrate constituting the first report that an ion current is regulated by shp-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
binding
|
KIT |
0.557 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-56104 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9528781 |
Shp-1 binds and negatively modulates the c-kit receptor by interaction with tyrosine 569 in the c-kit juxtamembrane domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
TRPV1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277129 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 25790452 |
Shp-1 dephosphorylates TRPV1 in dorsal root ganglion neurons and alleviates CFA-induced inflammatory pain in rats.|These results suggested that Shp-1 dephosphorylated and inhibited TRPV1 in DRG neurons, contributing to maintain thermal nociceptive thresholds in normal rats, and as a compensatory mechanism, Shp-1 increased in DRGs of rats with CFA-induced inflammatory pain, which was involved in protecting against excessive thermal hyperalgesia. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
VAV1 |
0.561 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277171 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30567306 |
SHP-1 dephosphorylates and inactivates the guanine exchange factor Vav1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
MAP3K7 |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277128 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31130074 |
Mechanistically, the association of EHEC Tir with SHP-1 facilitated the recruitment of SHP-1 to TAK1 and inhibited TAK1 phosphorylation, which then negatively regulated K63-linked polyubiquitination of TAK1 and downstream signal transduction.|SHP-1 inhibits TAK1 activity to down-regulate signal transduction and subsequent cytokine production.Innate immune responses are achieved by the activation of several pathogen-recognition receptors (PRPs), including TLRs, retinoic acid inducible gene I (RIG-I)-like receptors (RLRs) and nucleotide-binding oligomerization domain (NOD)-like receptors (NLRs). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
dephosphorylation
|
SYK |
0.726 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-70234 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 10458769 |
We propose that shp1 can dephosphorylate sites in zap-70 and syk that are involved in coupling these kinases to downstream signaling cascades, including erk2 and elements of the il-2 gene. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN6 | down-regulates
dephosphorylation
|
STAT3 |
0.47 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178699 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18508557 |
Stat3 may also be a substrate of shp1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
PTPN6 | down-regulates
dephosphorylation
|
JAK1 |
0.63 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119197 |
|
|
Homo sapiens |
Breast Cancer Cell, Leukemia Cell, Lymphoma Cell, JURKAT Cell, RAMOS Cell |
| pmid |
sentence |
| 14624462 |
We find, for the first time, that shp-1 down-regulates the level of tyk2 kinase in h9 cells and of jak1 kinase in htb26 cells, by accelerating their degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PTPN6
- 
- 