| + |
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 |
0.356 |
| 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 |
| + |
FYN | up-regulates activity
phosphorylation
|
PTPN6 |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279716 |
Ser591 |
DKEKSKGsLKRK |
Homo sapiens |
|
| pmid |
sentence |
| 28811476 |
By contrast, receptor multivalent aggregation induced a Fyn-dependent SHP-1 S591 phosphorylation (Fig.\u00a0 xref ).|Fyn simultaneously activates the PI3K-PKC\u03b1 pathway, leading to SHP-1 phosphorylation on serine 591. |
|
| 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 |
0.682 |
| 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 |
| + |
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 |
0.35 |
| 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 |
0.406 |
| 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 |
0.335 |
| 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 |
0.359 |
| 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 |
0.346 |
| 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 |
0.628 |
| 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 |
0.746 |
| 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 |
0.35 |
| 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 |
0.587 |
| 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 |
0.515 |
| 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 |
|
| 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. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates
phosphorylation
|
PTPN6 |
0.515 |
| 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 |
0.404 |
| 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-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-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. |
|
| 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. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens, In Vitro |
| + |
LCK | up-regulates activity
phosphorylation
|
PTPN6 |
0.628 |
| 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 |
| + |
INSR | up-regulates
phosphorylation
|
PTPN6 |
0.35 |
| 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
phosphorylation
|
PTPN6 |
0.628 |
| 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 |
| + |
ABL1 |
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PTPN6
- 
- 