+ |
PTPRD | down-regulates
dephosphorylation
|
STAT3 |
0.533 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-185933 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
Lung Cancer Cell, Glioblastoma Cell |
pmid |
sentence |
19478061 |
Transfection of wild-type ptprd resulted in the specific dephosphorylation of stat3 at tyrosine 705, a residue that must be phosphorylated for stat3 to be active |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain |
+ |
PTPRD | down-regulates activity
dephosphorylation
|
STAT3 |
0.533 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248442 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19478061 |
Transfection of wild-type PTPRD resulted in the specific dephosphorylation of STAT3 at tyrosine 705, a residue that must be phosphorylated for STAT3 to be active |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LRFN5 | up-regulates activity
binding
|
PTPRD |
0.281 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264086 |
|
|
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 |
+ |
PTPRD | up-regulates
|
Synaptic_plasticity |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264089 |
|
|
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 |