| + |
PTPN18 | down-regulates quantity by destabilization 
dephosphorylation
|
ERBB2 |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262595 |
Tyr1112 |
DPSPLQRySEDPTVP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25081058 |
PTPN18 knockdown selectively enhances the EGF-induced tyrosine phosphorylation of the HER2 Y1112, Y1196 and Y1248 sites. |Whereas the catalytic domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation of HER2 on pY(1112), the PEST domain of PTPN18 promotes K48-linked HER2 ubiquitination and its rapid destruction via the proteasome pathway and an HER2 negative feedback loop. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262596 |
Tyr1196 |
GAVENPEyLTPQGGA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25081058 |
PTPN18 knockdown selectively enhances the EGF-induced tyrosine phosphorylation of the HER2 Y1112, Y1196 and Y1248 sites. |Whereas the catalytic domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation of HER2 on pY(1112), the PEST domain of PTPN18 promotes K48-linked HER2 ubiquitination and its rapid destruction via the proteasome pathway and an HER2 negative feedback loop. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262597 |
Tyr1248 |
PTAENPEyLGLDVPV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25081058 |
PTPN18 knockdown selectively enhances the EGF-induced tyrosine phosphorylation of the HER2 Y1112, Y1196 and Y1248 sites. |Whereas the catalytic domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation of HER2 on pY(1112), the PEST domain of PTPN18 promotes K48-linked HER2 ubiquitination and its rapid destruction via the proteasome pathway and an HER2 negative feedback loop. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277031 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25081058 |
In the present study, we demonstrated that PTPN18 specifically dephosphorylates HER2 pY 1112, pY 1196 and pY 1248 sites among ten HER2 and EGFR C-terminal tyrosine phosphorylation sites (XREF_FIG).|Taken together, these data suggest that PTPN18 promotes the proteasome dependent degradation of HER2 through K48 linked polyubiquitination. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PSTPIP1 | up-regulates activity 
binding
|
PTPN18 |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262594 |
|
|
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 9422760 |
These data confirm the importance of these residues to the binding interaction, and they suggest that much of the COOH-terminal region of PTP HSCF may be required for highest affinity binding to PST PIP.|Because this protein-protein interaction appears to be required for the dephosphorylation of PST PIP phosphotyrosines (20), it may be a potentially important new mechanism for the regulation of the cytoskeleton. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
3.0
PTPN18
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