| + |
CDK2 | down-regulates activity 
phosphorylation
|
PTPN12 |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277366 |
Ser19 |
QRVQAMKsPDHNGED |
Homo sapiens |
MDA-MB-231 Cell |
| pmid |
sentence |
| 28842430 |
In the present study, we found that S19 site phosphorylation of PTPN12 by CDK2 discharged its antitumor activity by down-regulation of its inhibitory role in cell migration, but not affecting its other regulatory functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCA | down-regulates
phosphorylation
|
PTPN12 |
0.328 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-27300 |
Ser39 |
FMRLRRLsTKYRTEK |
Homo sapiens |
|
| pmid |
sentence |
| 7520867 |
Ptp-pest is phosphorylated in vitro by both cyclic amp-dependent protein kinase (pka) and protein kinase c (pkc) at two major sites, which we have identified as ser39 and ser435 / phosphorylation of ser39 in vitro decreases the activity of ptp-pest by reducing its affinity for substrate. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-27304 |
Ser435 |
KKLERNLsFEIKKVP |
Homo sapiens |
|
| pmid |
sentence |
| 7520867 |
Ptp-pest is phosphorylated in vitro by both cyclic amp-dependent protein kinase (pka) and protein kinase c (pkc) at two major sites, which we have identified as ser39 and ser435. our results suggest that both pkc and pka are capable of phosphorylating, and therefore inhibiting, ptp-pest in vivo |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates activity
dephosphorylation
|
JAK2 |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248657 |
Tyr1007 |
VLPQDKEyYKVKEPG |
Homo sapiens |
HC-11 Cell |
| pmid |
sentence |
| 11731619 |
PTP-PEST-Containing Lysates from EGF-Treated HC11 Cells Dephosphorylate JAK2 More Efficiently than Lysates from Control Cells|phospho-JAK2-specific rabbit polyclonal antiserum (44-426, BioSource Technologies, Inc., Camarillo, CA) which recognizes Tyr1007/1008 in the activation site |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248658 |
Tyr1008 |
LPQDKEYyKVKEPGE |
Homo sapiens |
HC-11 Cell |
| pmid |
sentence |
| 11731619 |
PTP-PEST-Containing Lysates from EGF-Treated HC11 Cells Dephosphorylate JAK2 More Efficiently than Lysates from Control Cells|phospho-JAK2-specific rabbit polyclonal antiserum (44-426, BioSource Technologies, Inc., Camarillo, CA) which recognizes Tyr1007/1008 in the activation site |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates
dephosphorylation
|
INSR |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-39147 |
Tyr1185 |
FGMTRDIyETDYYRK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 8454633 |
Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75894 |
Tyr1185 |
FGMTRDIyETDYYRK |
in vitro |
|
| pmid |
sentence |
| 10734133 |
Interestingly, all PTPs that were tested could completely dephosphorylate the receptor, given sufficient time, including a negative control (PTP-PEST) that failed to bind IRK as a trapping mutant. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75898 |
Tyr1189 |
RDIYETDyYRKGGKG |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-39151 |
Tyr1189 |
RDIYETDyYRKGGKG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 8454633 |
Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75902 |
Tyr1190 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262291 |
Tyr1190 |
DIYETDYyRKGGKGL |
in vitro |
|
| pmid |
sentence |
| 10734133 |
Interestingly, all PTPs that were tested could completely dephosphorylate the receptor, given sufficient time, including a negative control (PTP-PEST) that failed to bind IRK as a trapping mutant. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-75906 |
Tyr999 |
YASSNPEyLSASDVF |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-39159 |
Tyr999 |
YASSNPEyLSASDVF |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 8454633 |
Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-39155 |
|
|
in vitro |
|
| pmid |
sentence |
| 8454633 |
Intrinsic activity was demonstrated in vitro against a variety of phosphotyrosine-containing substrates including BIRK, the autophosphorylated cytoplasmic kinase domain of the insulin receptor beta subunit. |
|
| Publications: |
9 |
Organism: |
Homo Sapiens, In Vitro |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
PTPN12 | down-regulates activity
dephosphorylation
|
ERBB2 |
0.604 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277038 |
Tyr1196 |
GAVENPEyLTPQGGA |
Homo sapiens |
|
| pmid |
sentence |
| 29330094 |
In MDA-MB-231 cells, a human triple negative breast cancer cell line, phosphorylation of PTPN12 on Ser 19 was increased in response to cyclin dependent kinase 2 (CDK2), and this impaired PTPN12 's ability to dephosphorylate HER2 on Y1196.|PTPN12 negatively regulates Her2, by dephosphorylation on Tyr 1196 on Her2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates
dephosphorylation
|
GIT2 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142711 |
Tyr286 |
EELAMDVyDEVDRRE |
Homo sapiens |
|
| pmid |
sentence |
| 16317044 |
Conversely, a gfp-pkl phosphorylation mutant, y286/392/592f (gfp-pkl triple yf) (brown et al., 2005), was not phosphorylated during adhesion and the addition of ptp-pest had no effect, suggesting one or more of these tyrosine residues are dephosphorylated by ptppest. Taken together, these data strongly suggest pkl as a direct substrate for ptp-pest. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142715 |
Tyr392 |
QDNDQPDyDSVASDE |
Homo sapiens |
|
| pmid |
sentence |
| 16317044 |
Conversely, a gfp-pkl phosphorylation mutant, y286/392/592f (gfp-pkl triple yf) (brown et al., 2005), was not phosphorylated during adhesion and the addition of ptp-pest had no effect, suggesting one or more of these tyrosine residues are dephosphorylated by ptppest. Taken together, these data strongly suggest pkl as a direct substrate for ptp-pest. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142719 |
Tyr592 |
NSTPESDyDNTPNDM |
Homo sapiens |
|
| pmid |
sentence |
| 16317044 |
Conversely, a gfp-pkl phosphorylation mutant, y286/392/592f (gfp-pkl triple yf) (brown et al., 2005), was not phosphorylated during adhesion and the addition of ptp-pest had no effect, suggesting one or more of these tyrosine residues are dephosphorylated by ptppest. Taken together, these data strongly suggest pkl as a direct substrate for ptp-pest. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates activity
dephosphorylation
|
WAS |
0.455 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248660 |
Tyr291 |
AETSKLIyDFIEDQG |
Mus musculus |
|
| pmid |
sentence |
| 14707117 |
Mutation of tyrosine residue Y291, identified here as the major site of TCR-induced WASp tyrosine phosphorylation, abrogated induction of WASp tyrosine phosphorylation and its effector activities|WASp was tyrosine dephosphorylated by protein tyrosine phosphatase (PTP)-PEST |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PTPN12 | down-regulates activity
dephosphorylation
|
PSTPIP1 |
0.628 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248656 |
Tyr345 |
PERNEGVyTAIAVQE |
Mus musculus |
|
| pmid |
sentence |
| 11711533 |
We also demonstrate that PTP-PEST dephosphorylates PSTPIP at tyrosine 344. Importantly, we identified tyrosine 344 as the main phosphorylation site of PSTPIP by performing tryptic phosphopeptide maps. |The biological functions of the complexes formed between PSTPIP and SH2 domain-containing tyrosine kinases may be to transmit the signals from activated EGF and PDGF receptor.|Furthermore, we show that PSTPIP is phosphorylated downstream of the activated PDGF and EGF receptors. This phosphorylation of PSTPIP is most likely mediated by c-Abl |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PTPN12 | down-regulates
dephosphorylation
|
SHC1 |
0.662 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-44361 |
Tyr349 |
EEPPDHQyYNDFPGK |
Homo sapiens |
|
| pmid |
sentence |
| 8939605 |
The shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (y239/240) that mediate protein-protein interactions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-44862 |
Tyr350 |
EPPDHQYyNDFPGKE |
Homo sapiens |
|
| pmid |
sentence |
| 8939605 |
The shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (y239/240) that mediate protein-protein interactions. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates activity
dephosphorylation
|
ABL1 |
0.449 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235568 |
Tyr393 |
RLMTGDTyTAHAGAK |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 11163214 |
Several experiments suggest that the pest-type ptps negatively regulate c-abl activity: c-abl was hyperphosphorylated in ptp-pest-deficient cells dephosphorylation of c-abl by pest-type ptp represents a novel mechanism by which c-abl activity is regulated. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246222 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 11163214 |
Several experiments suggest that the PEST-type PTPs negatively regulate c-Abl activity: c-Abl was hyperphosphorylated in PTP-PEST-deficient cells; disruption of the c-Abl-PSTPIP1-PEST-type PTP ternary complex by overexpression of PSTPIP1 mutants increased c-Abl phosphotyrosine content |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops, Mus Musculus |
| + |
PTPN12 | down-regulates activity
dephosphorylation
|
PTK2 |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248661 |
Tyr397 |
SVSETDDyAEIIDEE |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 19595712 |
We demonstrate here that activated Ras induces tyrosine dephosphorylation and inhibition of FAK mediated by the Ras downstream Fgd1-Cdc42-PAK1-MEK-ERK signaling cascade.| PIN1 binding and prolyl isomerization of FAK cause PTP-PEST to interact with and dephosphorylate FAK Y397. Inhibition of FAK mediated by this signal relay promotes Ras-induced cell migration, invasion, and metastasis. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PTPN12 | down-regulates activity
dephosphorylation
|
PTK2B |
0.56 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248662 |
Tyr402 |
CSIESDIyAEIPDET |
Rattus norvegicus |
|
| pmid |
sentence |
| 11337490 |
Inhibition of the catalytic activity of cell adhesion kinase beta by protein-tyrosine phosphatase-PEST-mediated dephosphorylation|CAKbeta was found to be a substrate for PTP-PEST. Both the major autophosphorylation site of CAKbeta (Tyr(402)) and activation loop tyrosine residues, Tyr(579) and Tyr(580), were targeted for dephosphorylation by PTP-PEST. Dephosphorylation of CAKbeta by PTP-PEST dramatically inhibited CAKbeta kinase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107502 |
Tyr579 |
RYIEDEDyYKASVTR |
Homo sapiens |
|
| pmid |
sentence |
| 11337490 |
Inhibition of the catalytic activity of cell adhesion kinase beta by protein-tyrosine phosphatase-pest-mediated dephosphorylation. / dephosphorylation of tyr402 and tyr579/580 by ptp-pest |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248664 |
Tyr580 |
YIEDEDYyKASVTRL |
Rattus norvegicus |
|
| pmid |
sentence |
| 11337490 |
Inhibition of the catalytic activity of cell adhesion kinase beta by protein-tyrosine phosphatase-PEST-mediated dephosphorylation|CAKbeta was found to be a substrate for PTP-PEST. Both the major autophosphorylation site of CAKbeta (Tyr(402)) and activation loop tyrosine residues, Tyr(579) and Tyr(580), were targeted for dephosphorylation by PTP-PEST. Dephosphorylation of CAKbeta by PTP-PEST dramatically inhibited CAKbeta kinase activity. |
|
| Publications: |
3 |
Organism: |
Rattus Norvegicus, Homo Sapiens |
| + |
PTPN12 | down-regulates activity
dephosphorylation
|
SRC |
0.543 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248659 |
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 |
| + |
PTPN12 | up-regulates activity 
dephosphorylation
|
SRC |
0.543 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277086 |
Tyr530 |
FTSTEPQyQPGENL |
Homo sapiens |
|
| pmid |
sentence |
| 19350555 |
PTP-PEST increases dephosphorylation of Src at Y527 and activates it.|The data presented here supports our hypothesis that PTP-PEST activates Src via dephosphorylating it at Y527 (Tyr530 in human c-Src equivalent to Tyr527 in chicken Src). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | up-regulates activity
dephosphorylation
|
ARHGDIA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277175 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25666508 |
Integrin-bound PTP-PEST dephosphorylates RhoGDI1.|Translocation of Src phosphorylated RhoGDI1 to the cell 's leading edge promotes local activation of Rac1 and Cdc42, whereas dephosphorylation of RhoGDI1 by integrin bound PTP-PEST promotes RhoGDI1 release from the membrane and sequestration of inactive Rac1 and Cdc42 in the cytoplasm.|Translocation of Src-phosphorylated RhoGDI1 to the cell's leading edge promotes local activation of Rac1 and Cdc42, whereas dephosphorylation of RhoGDI1 by integrin-bound PTP-PEST promotes RhoGDI1 release from the membrane and sequestration of inactive Rac1/Cdc42 in the cytoplasm. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates
dephosphorylation
|
WAS |
0.455 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121136 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 14707117 |
Furthermore, we demonstrate that pstpip serves as a scaffold protein between ptp-pest and wasp and allows ptp-pest to dephosphorylate wasp. This finding suggests a possible mechanism for ptp-pest to directly modulate actin remodeling through the pstpip-wasp interaction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111688 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11711533 |
Furthermore, we demonstrate that pstpip serves as a scaffold protein between ptp-pest and wasp and allows ptp-pest to dephosphorylate wasp. This finding suggests a possible mechanism for ptp-pest to directly modulate actin remodeling through the pstpip-wasp interaction. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates
dephosphorylation
|
BCAR1 |
0.562 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109032 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 11432829 |
Ptp-pest is an efficient negative regulator of lymphocyte activation. This function correlated with the ability of ptp-pest to induce dephosphorylation of shc, pyk2, fak and cas, and inactivate the ras pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates
dephosphorylation
|
JAK2 |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112383 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11731619 |
In intact hc11 cells, ptp-pest was constitutively associated with jak2, and in response to egf treatment there was an increased level of ptp-pest in jak2 complexes. An in vitro phosphatase assay, using prl-activated jak2 as the substrate and lysates from hc11 cells as the source of ptp-pest, revealed that jak2 could serve as a ptp-pest substrate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates
dephosphorylation
|
PTK2 |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109035 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11432829 |
This function correlated with the ability of ptp-pest to induce dephosphorylation of shc, pyk2, fak and cas, and inactivate the ras pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PTPN12
- 
- 