| + |
ACP1 | down-regulates activity 
dephosphorylation
|
AKT3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248457 |
Ser472 |
RPHFPQFsYSASGRE |
Mus musculus |
|
| pmid |
sentence |
| 17353188 |
Reduction in the levels of both LMW-PTP isoforms in vitro and in vivo increased tyrosine phosphorylation of IR and AktSer473 and increased IRS-1- and IRS-2-associated PI3-K activities in both liver and fat.|Activated PI3-K stimulates Akt (or protein kinase B) that in turn phosphorylates and inactivates glycogen synthase kinase-3 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ACP1 | down-regulates activity
dephosphorylation
|
AKT1 |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248455 |
Ser473 |
RPHFPQFsYSASGTA |
Mus musculus |
|
| pmid |
sentence |
| 17353188 |
Reduction in the levels of both LMW-PTP isoforms in vitro and in vivo increased tyrosine phosphorylation of IR and AktSer473 and increased IRS-1- and IRS-2-associated PI3-K activities in both liver and fat.|Activated PI3-K stimulates Akt (or protein kinase B) that in turn phosphorylates and inactivates glycogen synthase kinase-3 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ACP1 | down-regulates activity
dephosphorylation
|
AKT2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248456 |
Ser474 |
RTHFPQFsYSASIRE |
Mus musculus |
|
| pmid |
sentence |
| 17353188 |
Reduction in the levels of both LMW-PTP isoforms in vitro and in vivo increased tyrosine phosphorylation of IR and AktSer473 and increased IRS-1- and IRS-2-associated PI3-K activities in both liver and fat.|Activated PI3-K stimulates Akt (or protein kinase B) that in turn phosphorylates and inactivates glycogen synthase kinase-3 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FYN | up-regulates activity 
phosphorylation
|
ACP1 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251149 |
Tyr132 |
QLIIEDPyYGNDSDF |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9038134 |
We identify Tyr-131 as the major phosphorylation site and Tyr-132 as a minor site and the Src family PTKs Lck and Fyn as enzymes capable of phosphorylating these sites in vivo and in vitro. Both Tyr-131 and Tyr-132 are located next to the catalytic pocket of LMPTP, and especially, Tyr-131 seems to be important for the activity of LMPTP. Phosphorylation of Tyr-131 or Tyr-132, particularly the former, caused an increase in the activity of LMPTP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251150 |
Tyr133 |
LIIEDPYyGNDSDFE |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9038134 |
We identify Tyr-131 as the major phosphorylation site and Tyr-132 as a minor site and the Src family PTKs Lck and Fyn as enzymes capable of phosphorylating these sites in vivo and in vitro. Both Tyr-131 and Tyr-132 are located next to the catalytic pocket of LMPTP, and especially, Tyr-131 seems to be important for the activity of LMPTP. Phosphorylation of Tyr-131 or Tyr-132, particularly the former, caused an increase in the activity of LMPTP. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
LCK | up-regulates activity
phosphorylation
|
ACP1 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251366 |
Tyr132 |
QLIIEDPyYGNDSDF |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9038134 |
In co-transfected COS cells, Lck and Fyn caused phosphorylation of LMPTP. Most of the phosphate was located at Tyr-131, and some was also located at Tyr-132. Site-directed mutagenesis showed that Tyr-131 is important for the catalytic activity of LMPTP, and that thiophosphorylation of Tyr-131, and to a lesser degree Tyr-132, is responsible for the activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251367 |
Tyr133 |
LIIEDPYyGNDSDFE |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 9038134 |
In co-transfected COS cells, Lck and Fyn caused phosphorylation of LMPTP. Most of the phosphate was located at Tyr-131, and some was also located at Tyr-132. Site-directed mutagenesis showed that Tyr-131 is important for the catalytic activity of LMPTP, and that thiophosphorylation of Tyr-131, and to a lesser degree Tyr-132, is responsible for the activation. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
ACP1 | up-regulates activity
dephosphorylation
|
SRC |
0.433 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248454 |
Tyr530 |
FTSTEPQyQPGENL |
Mus musculus |
|
| pmid |
sentence |
| 19088431 |
LMWPTP dephosphorylated pY(527)-Src and pY(416)-Src in vitro, with greater specificity for pY(527)Src. Activation of LMWPTP produced strong activation of Src mediated by fast dephosphorylation of pY(527)-Src, followed by slower deactivation of this kinase via dephosphorylation of pY(416)Src. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ACP1 | down-regulates activity
dephosphorylation
|
EPHA2 |
0.674 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246031 |
Tyr575 |
RQSPEDVyFSKSEQL |
in vitro |
|
| pmid |
sentence |
| 21538645 |
The SAM domain tyrosine Y960 which has been implicated in downstream PI3K signaling is dephosphorylated exclusively by HCPTP-B. The activation loop tyrosine (Y772) which directly controls kinase activity is dephosphorylated about six times faster by HCPTP-A. In contrast, the juxtamembrane tyrosines (Y575, Y588 and Y594) which are implicated in both control of kinase activity and downstream signaling are dephosphorylated by both variants with similar rates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246035 |
Tyr588 |
QLKPLKTyVDPHTYE |
in vitro |
|
| pmid |
sentence |
| 21538645 |
The SAM domain tyrosine Y960 which has been implicated in downstream PI3K signaling is dephosphorylated exclusively by HCPTP-B. The activation loop tyrosine (Y772) which directly controls kinase activity is dephosphorylated about six times faster by HCPTP-A. In contrast, the juxtamembrane tyrosines (Y575, Y588 and Y594) which are implicated in both control of kinase activity and downstream signaling are dephosphorylated by both variants with similar rates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246039 |
Tyr594 |
TYVDPHTyEDPNQAV |
in vitro |
|
| pmid |
sentence |
| 21538645 |
The SAM domain tyrosine Y960 which has been implicated in downstream PI3K signaling is dephosphorylated exclusively by HCPTP-B. The activation loop tyrosine (Y772) which directly controls kinase activity is dephosphorylated about six times faster by HCPTP-A. In contrast, the juxtamembrane tyrosines (Y575, Y588 and Y594) which are implicated in both control of kinase activity and downstream signaling are dephosphorylated by both variants with similar rates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246027 |
Tyr772 |
EDDPEATyTTSGGKI |
in vitro |
|
| pmid |
sentence |
| 21538645 |
The SAM domain tyrosine Y960 which has been implicated in downstream PI3K signaling is dephosphorylated exclusively by HCPTP-B. The activation loop tyrosine (Y772) which directly controls kinase activity is dephosphorylated about six times faster by HCPTP-A. In contrast, the juxtamembrane tyrosines (Y575, Y588 and Y594) which are implicated in both control of kinase activity and downstream signaling are dephosphorylated by both variants with similar rates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246023 |
Tyr960 |
GHQKRIAySLLGLKD |
in vitro |
|
| pmid |
sentence |
| 21538645 |
The SAM domain tyrosine Y960 which has been implicated in downstream PI3K signaling is dephosphorylated exclusively by HCPTP-B. The activation loop tyrosine (Y772) which directly controls kinase activity is dephosphorylated about six times faster by HCPTP-A. In contrast, the juxtamembrane tyrosines (Y575, Y588 and Y594) which are implicated in both control of kinase activity and downstream signaling are dephosphorylated by both variants with similar rates |
|
| Publications: |
5 |
Organism: |
In Vitro |
| + |
ACP1 | down-regulates activity
dephosphorylation
|
PDGFRB |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248452 |
Tyr857 |
DIMRDSNyISKGSTF |
Homo sapiens |
|
| pmid |
sentence |
| 12149261 |
Insight into the role of low molecular weight phosphotyrosine phosphatase (LMW-PTP) on platelet-derived growth factor receptor (PDGF-r) signaling. LMW-PTP controls PDGF-r kinase activity through TYR-857 dephosphorylation|On the basis of these results, we propose a key role for LMW-PTP in PDGF-r down-regulation through the dephosphorylation of the activation loop Tyr-857, thus determining a general negative regulation of all downstream signals, with the exception of those elicited by internalized receptors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACP1 | down-regulates activity
dephosphorylation
|
AKT |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248458 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 17353188 |
Reduction in the levels of both LMW-PTP isoforms in vitro and in vivo increased tyrosine phosphorylation of IR and AktSer473 and increased IRS-1- and IRS-2-associated PI3-K activities in both liver and fat.|Activated PI3-K stimulates Akt (or protein kinase B) that in turn phosphorylates and inactivates glycogen synthase kinase-3 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ACP1 | up-regulates activity
dephosphorylation
|
PKM |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277134 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30251652 |
Indeed, it is evident that LMW-PTP, hydrolyzing phosphotyrosine residues, contributes to maintain PKM2 in its active form.|We speculate that this effect is in large part due to LMW-PTP inhibition, which leads a fast PKM2 phosphorylation and inactivation.|we demonstrate that in melanoma cells the overexpression of LMW-PTP is functional to maintain PKM2 in its dephosphorylate status – the tetrameric, “full active” form - which is retained in the cytoplasm |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACP1 | down-regulates activity
dephosphorylation
|
PTK2 |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277064 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12815062 |
Lymphocyte function-associated antigen-1-mediated T cell adhesion is impaired by low molecular weight phosphotyrosine phosphatase-dependent inhibition of FAK activity. 4000254={CellProcess=4107155 CellType=10000184}}|Moreover, in these conditions LMW-PTP causes FAK dephosphorylation, thus preventing the activation of FAK downstream pathways. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
ACP1
- 
- 