Relation Results

Summary

Name PTPN13
Full Name Tyrosine-protein phosphatase non-receptor type 13
Synonyms Fas-associated protein-tyrosine phosphatase 1, FAP-1, PTP-BAS, Protein-tyrosine phosphatase 1E, PTP-E1, hPTPE1, Protein-tyrosine phosphatase PTPL1 | PNP1, PTP1E, PTPL1
Primary ID Q12923
Links - -
Type protein
Relations 14
Function Tyrosine phosphatase which regulates negatively FAS-induced apoptosis and NGFR-mediated pro-apoptotic signaling (PubMed:15611135). May regulate phosph ...
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Type: Score: Layout: SPV 
0.2610.3920.4440.4350.7070.5380.4690.4230.3340.571PTPN13INSRABL1NFKBIATRIP6EFNB1SRCIRS1STK25ERBB2PDCD10

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ PTPN13down-regulates img/direct_inhibition.png dephosphorylation INSR 0.261
Identifier Residue Sequence Organism Cell Line
SIGNOR-132551 Tyr1185 FGMTRDIyETDYYRK Homo sapiens
pmid sentence
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
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
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
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
+ PTPN13down-regulates activity img/direct_inhibition.png dephosphorylation ABL1 0.392
Identifier Residue Sequence Organism Cell Line
SIGNOR-277012 Tyr226 KRNKPTVyGVSPNYD Homo sapiens
pmid sentence
We also found that PTPN13 dephosphorylates and inhibits c-Abl.|While the above results indicated that calpain-2 could cleave PTPN13 and that PTPN13 could dephosphorylate c-Abl at tyrosine 245, they did not determine whether calpain-2-mediated cleavage of PTPN13 resulted in its inactivation and increased tyrosine phosphorylation of c-Abl at tyrosine 245.
Publications: 1 Organism: Homo Sapiens
+ PTPN13up-regulates quantity by stabilization img/direct-activation.png dephosphorylation NFKBIA 0.444
Identifier Residue Sequence Organism Cell Line
SIGNOR-248712 Tyr42 DSMKDEEyEQMVKEL Homo sapiens HEK-293 Cell
pmid sentence
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
+ PTPN13down-regulates activity img/direct_inhibition.png dephosphorylation TRIP6 0.435
Identifier Residue Sequence Organism Cell Line
SIGNOR-248713 Tyr55 PLPSEQCyQAPGGPE Mus musculus MEF Cell
pmid sentence
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
+ PTPN13up-regulates activity img/direct-activation.png dephosphorylation EFNB1 0.707
Identifier Residue Sequence Organism Cell Line
SIGNOR-277002 Homo sapiens
pmid sentence
Loss of PTPN13 function increases EFNB1 phosphorylation, enhances EFNB1 's interaction with ERBB1 and correlates with potentiated ERK1/2 activation.|Moreover, acquisition of PTPN13 loss-of-function mutations or its decreased expression (due to HPV infection or epigenetic silencing) may further enhance ERBB1 and EFNB1 mediated signals.
Publications: 1 Organism: Homo Sapiens
+ PTPN13down-regulates activity img/direct_inhibition.png dephosphorylation SRC 0.538
Identifier Residue Sequence Organism Cell Line
SIGNOR-277125 Homo sapiens
pmid sentence
Mechanistically, RIL suppresses Src activation through interacting with Src and PTPL1, allowing PTPL1 dependent dephosphorylation of Src at the activation loop.|Our results reveal a novel Src inactivation cycle in which reversion-induced LIM preferentially recognizes active Src and facilitates PTPL1-mediated inactivation of Src.
Publications: 1 Organism: Homo Sapiens
+ PTPN13down-regulates activity img/direct_inhibition.png dephosphorylation IRS1 0.469
Identifier Residue Sequence Organism Cell Line
SIGNOR-277053 Homo sapiens
pmid sentence
Finally, we report that PTPL1 expression is sufficient to block the IRS-1/phosphatidylinositol 3-kinase/Akt signaling pathway, to inhibit the insulin-like growth factor-I effect on cell survival, and to induce apoptosis.|We first show by complementary approaches that PTPL1 specifically dephosphorylates insulin receptor substrate-1 (IRS-1) in vitro and in cellulo.
Publications: 1 Organism: Homo Sapiens
+ PTPN13down-regulates activity img/direct_inhibition.png dephosphorylation STK25 0.423
Identifier Residue Sequence Organism Cell Line
SIGNOR-248711 Homo sapiens
pmid sentence
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
+ PTPN13down-regulates activity img/direct_inhibition.png dephosphorylation ERBB2 0.334
Identifier Residue Sequence Organism Cell Line
SIGNOR-277087 Homo sapiens
pmid sentence
Since a previous report showed PTPN13 may dephosphorylate ErbB2 directly, we also examined levels of phospho-ErbB2 (tyr 1248), and we also observed a small effect in the presence of wild-type PTPN13 (XREF_FIG).|The fact that both ErbB2 and H-RasV12 were potentiated by PTPN13 loss and PTPN13 inhibited MAP kinase signaling downstream of multiple oncogenes (ErbB2, EGFR, H-RasV12), suggest that the phosphatase target that inhibits MAP kinase signaling may not only be limited to ErbB2 tyrosine 1248.
Publications: 1 Organism: Homo Sapiens
+ PTPN13down-regulates img/direct_inhibition.png dephosphorylation PDCD10 0.571
Identifier Residue Sequence Organism Cell Line
SIGNOR-157076 Homo sapiens
pmid sentence
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
+ PTPN13down-regulates activity img/direct_inhibition.png dephosphorylation PDCD10 0.571
Identifier Residue Sequence Organism Cell Line
SIGNOR-248714 Homo sapiens
pmid sentence
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
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