+ |
PTPN13 | down-regulates
dephosphorylation
|
INSR |
0.263 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132551 |
Tyr1185 |
FGMTRDIyETDYYRK |
Homo sapiens |
|
pmid |
sentence |
15611135 |
We demonstrate that ptpl1, like ptp1b, interacts with and dephosphorylates a bis-phosphorylated insulin receptor peptide more efficiently than monophosphorylated peptides, indicating that ptpl1 may down-regulate the phosphatidylinositol 3-kinase pathway, by dephosphorylating insulin or growth factor receptors that contain tandem phosphotyrosines. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132555 |
Tyr1189 |
RDIYETDyYRKGGKG |
Homo sapiens |
|
pmid |
sentence |
15611135 |
We demonstrate that ptpl1, like ptp1b, interacts with and dephosphorylates a bis-phosphorylated insulin receptor peptide more efficiently than monophosphorylated peptides, indicating that ptpl1 may down-regulate the phosphatidylinositol 3-kinase pathway, by dephosphorylating insulin or growth factor receptors that contain tandem phosphotyrosines. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132559 |
Tyr1190 |
DIYETDYyRKGGKGL |
Homo sapiens |
|
pmid |
sentence |
15611135 |
We demonstrate that ptpl1, like ptp1b, interacts with and dephosphorylates a bis-phosphorylated insulin receptor peptide more efficiently than monophosphorylated peptides, indicating that ptpl1 may down-regulate the phosphatidylinositol 3-kinase pathway, by dephosphorylating insulin or growth factor receptors that contain tandem phosphotyrosines. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132563 |
Tyr999 |
YASSNPEyLSASDVF |
Homo sapiens |
|
pmid |
sentence |
15611135 |
We demonstrate that ptpl1, like ptp1b, interacts with and dephosphorylates a bis-phosphorylated insulin receptor peptide more efficiently than monophosphorylated peptides, indicating that ptpl1 may down-regulate the phosphatidylinositol 3-kinase pathway, by dephosphorylating insulin or growth factor receptors that contain tandem phosphotyrosines. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
PTPN13 | up-regulates quantity by stabilization
dephosphorylation
|
NFKBIA |
0.456 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248712 |
Tyr42 |
DSMKDEEyEQMVKEL |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11106428 |
Identification of IkappaBalpha as a substrate of Fas-associated phosphatase-1|A full-length FAP-1 protein preferentially dephosphorylates Tyr-42 of IkBa|Moreover, other studies have shown that tyrosine phosphorylation of IkBa on Tyr-42 (which occurs with Fas ligand binging) protected against inducible degradation both in vitro [30] and in vivo [38] |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN13 | down-regulates activity
dephosphorylation
|
TRIP6 |
0.446 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248713 |
Tyr55 |
PLPSEQCyQAPGGPE |
Mus musculus |
MEF Cell |
pmid |
sentence |
17591779 |
PTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidic acid-induced cell migration.|Here we further demonstrate that a switch from c-Src-mediated phosphorylation to PTPL1/Fas-associated phosphatase-1-dependent dephosphorylation serves as an inhibitory feedback control mechanism of TRIP6 function in LPA-induced cell migration. PTPL1 dephosphorylates phosphotyrosine 55 of TRIP6 in vitro and inhibits LPA-induced tyrosine phosphorylation of TRIP6 in cells. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
PTPN13 | down-regulates activity
dephosphorylation
|
STK25 |
0.434 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248711 |
|
|
Homo sapiens |
|
pmid |
sentence |
17657516 |
To investigate dephosphorylation of CCM3 by FAP-1, phosphorylated GST-CCM3 was incubated with cdFAP-1, and reactions were analyzed by autoradiography. Again, GST-STK25 phosphorylated GST-CCM3 and possessed autophosphorylation activity. cdFAP-1 of 0.005 U were sufficient to dephosphorylate GST-CCM3 as well as the kinase GST-STK25.|More recently, the Golgi matrix protein GM130 was shown to function as a scaffold protein for STK25 and to activate STK25 through stimulation of autophosphorylation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN13 | down-regulates
dephosphorylation
|
PDCD10 |
0.592 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-157076 |
|
|
Homo sapiens |
|
pmid |
sentence |
17657516 |
We also show that ccm3 directly binds to serine/threonine kinase 25 (stk25, ysk1, sok1) and the phosphatase domain of fas-associated phosphatase-1 (fap-1, ptpn13, ptp-bas, ptp-bl). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN13 | down-regulates activity
dephosphorylation
|
PDCD10 |
0.592 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248714 |
|
|
Homo sapiens |
|
pmid |
sentence |
17657516 |
In addition, our yeast two-hybrid analysis revealed that CCM3 also binds to the 270-kDa nonreceptor protein tyrosine phos- phatase FAP-1 in a region predicted to contain the C- terminal phosphatase domain [23]. We have shown that this catalytic domain is capable to dephosphorylate CCM3. By dephosphorylation, FAP-1 might therefore negatively reg- ulate CCM3 activity and downstream signaling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |