+ |
PTPN5 | up-regulates activity
dephosphorylation
|
BAK1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248542 |
Tyr108 |
QPTAENAyEYFTKIA |
Homo sapiens |
|
pmid |
sentence |
20959805 |
In this study, we report that on apoptotic stimulation Bak undergoes dephosphorylation at tyrosine residue 108 (Y108), a critical event that is necessary but not sufficient for Bak activation, but is required both for early exposure of the occluded N-terminal domain and multimerisation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN5 | down-regulates activity
dephosphorylation
|
GRIN2B |
0.571 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265744 |
Tyr1474 |
GSSNGHVyEKLSSIE |
Mus musculus |
Cerebral Cortical Neuron |
pmid |
sentence |
20427654 |
These previous results, together with the present findings, indicate that STEP61 dephosphorylates the NR2B subunit at its regulatory tyr1472 site, and dephosphorylation of this site leads to internalization of the NMDAR complex from neuronal surface membranes. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
PTPN5 | down-regulates
dephosphorylation
|
FYN |
0.547 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-86791 |
Tyr420 |
RLIEDNEyTARQGAK |
Homo sapiens |
Neuron |
pmid |
sentence |
11983687 |
Wild-type step(61) dephosphorylates fyn at tyr(420) but not at tyr(531). These results suggest that step regulates the activity of fyn by specifically dephosphorylating the regulatory tyr(420) and may be one mechanism by which fyn activity is decreased within psds. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Kidney |
+ |
PTPN5 | up-regulates
binding
|
MAPK14 |
0.475 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-194829 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
23932588 |
First [] step prevents upstream activating kinases from promiscuously binding and activating p38a. Second, by blocking access to the mapk insert pocket, through the stepcat interaction, step can prevent the binding of allosteric signaling molecules that induce autoactivation of p38a. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |