| + |
PTPRF | down-regulates 
dephosphorylation
|
AKT1 |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-137246 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
|
| pmid |
sentence |
| 15896785 |
Knock-down of lar by the l3 sirna probe markedly inhibited the insulin-stimulated increase in the phosphorylation of protein kinase b (pkb, also called akt) on serine 473 by >90% |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRF | down-regulates
dephosphorylation
|
RET |
0.438 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85170 |
Tyr1062 |
TWIENKLyGMSDPNW |
Homo sapiens |
|
| pmid |
sentence |
| 11121408 |
Lar expression significantly reduced tyrosine-1062 phosphorylation in ret-men2a but not in ret-men2b |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRF | down-regulates
dephosphorylation
|
INSR |
0.559 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-16235 |
Tyr1185 |
FGMTRDIyETDYYRK |
Homo sapiens |
|
| pmid |
sentence |
| 1303753 |
Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76005 |
Tyr1185 |
FGMTRDIyETDYYRK |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76009 |
Tyr1189 |
RDIYETDyYRKGGKG |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-16239 |
Tyr1189 |
RDIYETDyYRKGGKG |
Homo sapiens |
|
| pmid |
sentence |
| 1303753 |
Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-16243 |
Tyr1190 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
| pmid |
sentence |
| 1303753 |
Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76013 |
Tyr1190 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76017 |
Tyr999 |
YASSNPEyLSASDVF |
Homo sapiens |
|
| pmid |
sentence |
| 10734133 |
Many cellular receptors signal via tyrosine phosphorylation. The tyrosine kinases required for this activity are often recruited upon ligand bindingAlternatively, receptors themselves have kinase activity, like insulin receptors. In either case, the receptors are returned to their original state through the activity of protein-tyrosine phosphatases (PTPs)The major candidate PTPs previously implicated in IRK dephosphorylation are PTP-1b and LAR. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-16247 |
Tyr999 |
YASSNPEyLSASDVF |
Homo sapiens |
|
| pmid |
sentence |
| 1303753 |
Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product. |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| + |
PTPRF | down-regulates
dephosphorylation
|
FYN |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96768 |
Tyr420 |
RLIEDNEyTARQGAK |
Homo sapiens |
|
| pmid |
sentence |
| 12496362 |
Regulation of lck and fyn tyrosine kinase activities by transmembrane protein tyrosine phosphatase leukocyte common antigen-related molecule. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRF | up-regulates 
dephosphorylation
|
DAPK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157702 |
Tyr490 |
HCAAWHGyYSVAKAL |
Homo sapiens |
|
| pmid |
sentence |
| 17803936 |
Here, we show that the leukocyte common antigen-related (lar) tyrosine phosphatase dephosphorylates dapk at py491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of dapk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157706 |
Tyr491 |
CAAWHGYySVAKALC |
Homo sapiens |
|
| pmid |
sentence |
| 17803936 |
Lar tyrosine phosphatase dephosphorylates dapk at py491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of dapk |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRF | up-regulates activity
dephosphorylation
|
DAPK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276076 |
Tyr490 |
HCAAWHGyYSVAKAL |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 17803936 |
Here, we show that the leukocyte common antigen-related (LAR) tyrosine phosphatase dephosphorylates DAPK at pY491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of DAPK. Conversely, Src phosphorylates DAPK at Y491/492, which induces DAPK intra-/intermolecular interaction and inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276075 |
Tyr491 |
CAAWHGYySVAKALC |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 17803936 |
Here, we show that the leukocyte common antigen-related (LAR) tyrosine phosphatase dephosphorylates DAPK at pY491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of DAPK. Conversely, Src phosphorylates DAPK at Y491/492, which induces DAPK intra-/intermolecular interaction and inactivation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRF | up-regulates
dephosphorylation
|
FYN |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96764 |
Tyr531 |
FTATEPQyQPGENL |
Homo sapiens |
|
| pmid |
sentence |
| 12496362 |
Regulation of lck and fyn tyrosine kinase activities by transmembrane protein tyrosine phosphatase leukocyte common antigen-related molecule. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LRFN5 | up-regulates activity
binding
|
PTPRF |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264087 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 27225731 |
SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development. we identified LAR-RPTPs as novel ligands of SALM5 that mediates SALM5-dependent presynaptic differentiation in a splicing-dependent manner. Our data indicate that SALM5 interacts with all three known LAR-RPTPs—LAR, PTPδ, and PTPσ (Fig. 1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRF | down-regulates
dephosphorylation
|
PLCG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85166 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11121408 |
Here we show that lar reduces the constitutive tyrosine autophosphorylation and kinase activity of ret-men2a but not ret-men2b, accompanying a significant decrease of phosphorylation of phospholipase cgamma, akt, and erk1/2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MARCHF9 | down-regulates quantity by destabilization
ubiquitination
|
PTPRF |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271536 |
|
|
Homo sapiens |
B-lymphocyte Cell Line |
| pmid |
sentence |
| 19457934 |
MARCH9, a member of the RING-CH family of transmembrane E3 ubiquitin ligases, down-regulates CD4, major histocompatibility complex-I (MHC), and ICAM-1 in lymphoid cells. To identify novel MARCH9 substrates, we used high throughput flow cytometry and quantitative mass spectrometry by stable isotope labeling by amino acids in cell culture (SILAC) to determine the differential expression of plasma membrane proteins in a MARCH9-expressing B cell line. This combined approach identified 13 potential new MARCH9 targets. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRF | up-regulates activity
binding
|
LRRC4B |
0.599 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264049 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19467332 |
The NGL (netrin-G ligand; LRRC4) family of synaptic cell adhesion molecules belongs to the superfamily of leucine-rich repeat (LRR) proteins. The three known members of the NGL family, NGL-1, NGL-2, and NGL-3, are mainly localized to the postsynaptic side of excitatory synapses, and interact with the presynaptic ligands, netrin-G1, netrin-G2, and LAR, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FYN | up-regulates activity
phosphorylation
|
PTPRF |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251180 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12496362 |
LAR PTPase domain 2 was tyrosine phosphorylated by Fyn tyrosine kinase. we confirmed that LAR dephosphorylated the phosphorylated tyrosine residues of Lck and Fyn, and tyrosine residue(s) in LAR PTPase D2 was phosphorylated by Fyn to supply Fyn SH2 binding site. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PPFIA1 | up-regulates activity
relocalization
|
PTPRF |
0.793 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264141 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 7796809 |
We have identified a novel cytoplasmic 160 kDa phosphoserine protein termed LAR-interacting protein 1 (LIP.1), which binds to the LAR membrane-distal D2 protein tyrosine phosphatase domain and appears to localize LAR to focal adhesions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRF | up-regulates
dephosphorylation
|
LCK |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96771 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12496362 |
We confirmed that lar dephosphorylated the phosphorylated tyrosine residues of lck..Activation Of lck and fyn involves tyrosine dephosphorylation of the cooh-terminal regulatory domain of kinases, followed by autophosphorylation of the kinase domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRF | up-regulates 
|
Synaptic_plasticity |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264090 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 27225731 |
LAR (for leukocyte common antigen-related) is a family of receptor protein tyrosine phosphatases (LAR-RPTPs) with three known members: LAR/PTPRF, PTPδ/PTPRD, and PTPσ/PTPRS. In mammals, LAR-RPTPs have been shown to regulate dendrite and excitatory synapse development and maintenance |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PTPRF
- 
- 