Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-250775	Ser242	MDKRKDPsSVDIKKV	in vitro
pmid	sentence
10480872	The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B. \| although CLK1 and CLK2 directly phosphorylate PTP-1B on both Ser50 and Ser242/Ser243, the preferred CLK phosphorylation site is Ser50, as it is preferentially phosphorylated at an approximate ratio of 9:1 over the Ser242/Ser243 site.

Identifier	Residue	Sequence	Organism
SIGNOR-250776	Ser243	DKRKDPSsVDIKKVL	in vitro
pmid	sentence
10480872	The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B. \| although CLK1 and CLK2 directly phosphorylate PTP-1B on both Ser50 and Ser242/Ser243, the preferred CLK phosphorylation site is Ser50, as it is preferentially phosphorylated at an approximate ratio of 9:1 over the Ser242/Ser243 site.

Identifier	Residue	Sequence	Organism
SIGNOR-70603	Ser50	RNRYRDVsPFDHSRI	Homo sapiens
pmid	sentence
10480872	The clk family kinases, clk1 and clk2, phosphorylate and activate the tyrosine phosphatase, ptp-1b.\|Phosphorylation of PTP-1B at Ser(50) by CLK1 or CLK2 is responsible for its enzymatic activation.

Publications:

3

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250773	Ser242	MDKRKDPsSVDIKKV	in vitro
pmid	sentence
10480872	The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B. \| although CLK1 and CLK2 directly phosphorylate PTP-1B on both Ser50 and Ser242/Ser243, the preferred CLK phosphorylation site is Ser50, as it is preferentially phosphorylated at an approximate ratio of 9:1 over the Ser242/Ser243 site.

Identifier	Residue	Sequence	Organism
SIGNOR-250774	Ser243	DKRKDPSsVDIKKVL	in vitro
pmid	sentence
10480872	The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B. \| although CLK1 and CLK2 directly phosphorylate PTP-1B on both Ser50 and Ser242/Ser243, the preferred CLK phosphorylation site is Ser50, as it is preferentially phosphorylated at an approximate ratio of 9:1 over the Ser242/Ser243 site.

Identifier	Residue	Sequence	Organism
SIGNOR-70563	Ser50	RNRYRDVsPFDHSRI	Homo sapiens
pmid	sentence
10480872	The clk family kinases, clk1 and clk2, phosphorylate and activate the tyrosine phosphatase, ptp-1b.\|Phosphorylation of PTP-1B at Ser(50) by CLK1 or CLK2 is responsible for its enzymatic activation.

Publications:

3

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272990	Ser286	KFIMGDSsVQDQWKE	Homo sapiens	HeLa Cell
pmid	sentence
23348582	Cdk1-cyclin B1 directly phosphorylates PTP1B at serine 386 in a kinase assay. Recombinant Plk1 phosphorylates PTP1B on serine 286 and 393 in vitro, however, it requires a priming phosphorylation by Cdk1 at serine 386 highlighting a novel co-operation between Cdk1 and Plk1 in the regulation of PTP1B.\|Finally, phosphorylation on serine 286 enhanced PTP1B phosphatase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-39233	Ser386	LRGAQAAsPAKGEPS	Homo sapiens	HeLa Cell
pmid	sentence
8491187	Ptp1b is phosphorylated on ser386 by p34cdc2 in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272971	Ser386	LRGAQAAsPAKGEPS	Homo sapiens	HeLa Cell
pmid	sentence
23348582	Cdk1-cyclin B1 directly phosphorylates PTP1B at serine 386 in a kinase assay. Recombinant Plk1 phosphorylates PTP1B on serine 286 and 393 in vitro, however, it requires a priming phosphorylation by Cdk1 at serine 386 highlighting a novel co-operation between Cdk1 and Plk1 in the regulation of PTP1B.\|Finally, phosphorylation on serine 286 enhanced PTP1B phosphatase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272970	Ser386	LRGAQAAsPAKGEPS	Homo sapiens	HeLa Cell
pmid	sentence
23348582	Cdk1-cyclin B1 directly phosphorylates PTP1B at serine 386 in a kinase assay. Recombinant Plk1 phosphorylates PTP1B on serine 286 and 393 in vitro, however, it requires a priming phosphorylation by Cdk1 at serine 386 highlighting a novel co-operation between Cdk1 and Plk1 in the regulation of PTP1B.\|Finally, phosphorylation on serine 286 enhanced PTP1B phosphatase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235411	Ser50	RNRYRDVsPFDHSRI	Mus musculus	NIH-3T3 Cell
pmid	sentence
11579209	Phosphorylation of ptp1b at ser(50) by akt impairs its ability to dephosphorylate the insulin receptor.

Publications:

1

Organism:

Mus Musculus

Pathways:

Insulin Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-235491	Ser50	RNRYRDVsPFDHSRI	Mus musculus
pmid	sentence
11579209	We conclude that ptp1b is a novel substrate for akt and that phosphorylation of ptp1b by akt at ser(50) may negatively modulate its phosphatase activity creating a positive feedback mechanism forinsulin signaling

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252542	Ser50	RNRYRDVsPFDHSRI	Mus musculus	NIH-3T3 Cell
pmid	sentence
11579209	Phosphorylation of ptp1b at ser(50) by akt impairs its ability to dephosphorylate the insulin receptor.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248404	Tyr1007	VLPQDKEyYKVKEPG	Homo sapiens	HEK-293 Cell
pmid	sentence
11970898	Immunoblots with phospho-specific antibodies confirmed that PTP1B suppresses phosphorylation of the Jak2 activation site tyrosines (Y1007/Y1008) and Stat3 in a dose-dependent manner

Identifier	Residue	Sequence	Organism
SIGNOR-248405	Tyr1008	LPQDKEYyKVKEPGE	Homo sapiens
pmid	sentence
11970898	Immunoblots with phospho-specific antibodies confirmed that PTP1B suppresses phosphorylation of the Jak2 activation site tyrosines (Y1007/Y1008) and Stat3 in a dose-dependent manner

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-134955	Tyr1007	VLPQDKEyYKVKEPG	Homo sapiens
pmid	sentence
15821101	Ptp1b has been shown to regulate the activation of cytokine receptors through the dephosphorylation of specific members of the jak family, namely jak2 and tyk2

Identifier	Residue	Sequence	Organism
SIGNOR-133852	Tyr1008	LPQDKEYyKVKEPGE	Homo sapiens
pmid	sentence
15780598	JAK2 and STAT3 are dephosphorylated by PTP1B in vitro

Identifier	Residue	Organism
SIGNOR-135207		Homo sapiens
pmid	sentence
15821101	Ptp1b has been shown to regulate the activation of cytokine receptors through the dephosphorylation of specific members of the jak family, namely jak2 and tyk2

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248416	Tyr1009	LDTSSVLyTAVQPNE	in vitro
pmid	sentence
7545675	Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.\|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a\|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides

Identifier	Residue	Sequence	Organism
SIGNOR-248417	Tyr1021	PNEGDNDyIIPLPDP	in vitro
pmid	sentence
7545675	Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.\|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a\|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides

Identifier	Residue	Sequence	Organism
SIGNOR-248413	Tyr740	TGESDGGyMDMSKDE	in vitro
pmid	sentence
7545675	Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.\|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a\|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides

Identifier	Residue	Sequence	Organism
SIGNOR-248414	Tyr751	SKDESVDyVPMLDMK	in vitro
pmid	sentence
7545675	Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.\|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a\|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides

Identifier	Residue	Sequence	Organism
SIGNOR-248415	Tyr771	ADIESSNyMAPYDNY	in vitro
pmid	sentence
7545675	Upon activation, the βPDGFR is phosphorylated at multiple tyrosine residues and thereby becomes a docking site for SH2-domain-containing signal transduction proteins.\|While all phosphotyrosine sites on the βPDGFR are equally good targets for rPTP1B, maps of the βPDGFR dephosphorylated by rSyp showed that rSyp had a distinct preference for certain sites (Fig. 4 D-F). The low dose of rSyp primarily dephosphorylated spots 1, 6, 7, 9, and to a lesser extent 8a\|Spot 1 corresponds to tyrosine 751; spot 3 corresponds to tyrosine 1009; spot 6 corresponds to tyrosine 740; spot 8b corresponds to tyrosine 1021; spot 9 corresponds to tyrosine 771, and spots 2, 7, and 8a are as yet unidentified phosphopeptides

Publications:

5

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-179064	Tyr1009	LDTSSVLyTAVQPNE	Homo sapiens
pmid	sentence
18567737	Ptp1b blocked pdgf-induced tyr716 and tyr751 phosphorylation of the pdgfr.

Identifier	Residue	Sequence	Organism
SIGNOR-179068	Tyr1021	PNEGDNDyIIPLPDP	Homo sapiens
pmid	sentence
18567737	Interestingly, resveratrol increased the activity of protein tyrosine phosphatase ptp1b, which dephosphorylates pdgf-stimulated phosphorylation at tyrosine-751 and tyrosine-716 on pdgfr with concomitant reduction in akt and erk1/2 kinase activity. these results for the first time provide evidence that the stilbene resveratrol targets ptp1b to inhibit pdgfr mitogenic signaling.

Identifier	Residue	Sequence	Organism
SIGNOR-179072	Tyr716	RPPSAELySNALPVG	Homo sapiens
pmid	sentence
18567737	Ptp1b blocked pdgf-induced tyr716 and tyr751 phosphorylation of the pdgfr.

Identifier	Residue	Sequence	Organism
SIGNOR-179076	Tyr751	SKDESVDyVPMLDMK	Homo sapiens
pmid	sentence
18567737	Ptp1b blocked pdgf-induced tyr716 and tyr751 phosphorylation of the pdgfr.

Identifier	Residue	Sequence	Organism
SIGNOR-179080	Tyr771	ADIESSNyMAPYDNY	Homo sapiens
pmid	sentence
18567737	Ptp1b blocked pdgf-induced tyr716 and tyr751 phosphorylation of the pdgfr.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248407	Tyr1016	DVVDADEyLIPQQGF	in vitro
pmid	sentence
8621392	We have shown previously that amino acid residues flanking the phosphotyrosine are important for efficient PTP1 catalysis (Table 1 and Refs. 9, 10, and 17). For example, the kcat/Km value for the undecapeptide, EGFR988-989 (epidermal growth factor autophosphorylation site Tyr992, residues 988-998) (Asp-Ala-Asp-Glu-pTyr-Leu-Ile-Pro-Gln-Gln-Gly) is 3220-fold higher than that of phosphotyrosine (Table 1). We further demonstrated that a minimum of six amino acid residues are required for the most efficient PTP1 binding and catalysis.

Identifier	Residue	Organism
SIGNOR-276981		Homo sapiens
pmid	sentence
18253097	The protein tyrosine phosphatase, PTP1B, is known to negatively regulate EGF-induced signaling in several cell types by dephosphorylating the epidermal growth factor receptor (EGFR).\|Together, these findings provide evidence that PTP1B plays a role in the negative regulation of EGFR signaling in rat corneal endothelial cells, at least at the level of Tyr992 phosphorylation.

Publications:

2

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277011	Tyr1175	AQQDGKDyIVLPISE	Homo sapiens
pmid	sentence
23639442	This led to increased PTPN1 (PTP1b)-mediated dephosphorylation of VEGFR2 at Y 1175 , the site involved in activating ERK signaling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248408	Tyr1185	FGMTRDIyETDYYRK	Homo sapiens	HEK-293 Cell
pmid	sentence
16582879	Binding of insulin to the IR results in autophosphorylation of each beta‐subunit on at least six different tyrosines. This autophosphorylation occurs first on three tyrosines located in the activation loop of the kinase domain (Y1158, 1162 and 1163), resulting in the stabilization of the kinase in an active conformation.\|Termination of the signal involves inactivation of the IR by dephosphorylation of the three tyrosines of the kinase domain (Tonks, 2003). PTP1B is a protein tyrosine phosphatase located in the endoplasmic reticulum that has an important role in the dephosphorylation of these tyrosines after internalization of the IR

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235495	Tyr1185	FGMTRDIyETDYYRK	Mus musculus	NIH-3T3 Cell
pmid	sentence
11579209	Ptp1b is a protein tyrosine phosphatase that negatively regulates insulin sensitivity by dephosphorylating the insulin receptor.

Identifier	Residue	Sequence	Organism
SIGNOR-276947	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
22124607	Moreover, we reported that TCPTP knockdown in PTP1B deficient MEFS further enhanced IR activation, consistent with the two PTPs acting in a coordinated manner to attenuate insulin signalling .\|Therefore, the inhibition of PTPs such as PTP1B that attenuate IR activation and signalling might be particularly effective in alleviating insulin resistance.\|The prototypic family member PTP1B (encoded by PTPN1) dephosphorylates the IR beta subunit Y1162 and Y1163 activation loop autophosphorylation site to attenuate insulin signalling in vivo .

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248409	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens	HEK-293 Cell
pmid	sentence
16582879	Binding of insulin to the IR results in autophosphorylation of each beta‐subunit on at least six different tyrosines. This autophosphorylation occurs first on three tyrosines located in the activation loop of the kinase domain (Y1158, 1162 and 1163), resulting in the stabilization of the kinase in an active conformation.\|Termination of the signal involves inactivation of the IR by dephosphorylation of the three tyrosines of the kinase domain (Tonks, 2003). PTP1B is a protein tyrosine phosphatase located in the endoplasmic reticulum that has an important role in the dephosphorylation of these tyrosines after internalization of the IR

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235499	Tyr1189	RDIYETDyYRKGGKG	Mus musculus	NIH-3T3 Cell
pmid	sentence
11579209	Ptp1b is a protein tyrosine phosphatase that negatively regulates insulin sensitivity by dephosphorylating the insulin receptor.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235503	Tyr1190	DIYETDYyRKGGKGL	Mus musculus	NIH-3T3 Cell
pmid	sentence
11579209	Ptp1b is a protein tyrosine phosphatase that negatively regulates insulin sensitivity by dephosphorylating the insulin receptor.

Identifier	Residue	Sequence	Organism
SIGNOR-248410	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
16582879	Binding of insulin to the IR results in autophosphorylation of each beta‐subunit on at least six different tyrosines. This autophosphorylation occurs first on three tyrosines located in the activation loop of the kinase domain (Y1158, 1162 and 1163), resulting in the stabilization of the kinase in an active conformation.\|Termination of the signal involves inactivation of the IR by dephosphorylation of the three tyrosines of the kinase domain (Tonks, 2003). PTP1B is a protein tyrosine phosphatase located in the endoplasmic reticulum that has an important role in the dephosphorylation of these tyrosines after internalization of the IR

Identifier	Residue	Sequence	Organism
SIGNOR-276946	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
22124607	Moreover, we reported that TCPTP knockdown in PTP1B deficient MEFS further enhanced IR activation, consistent with the two PTPs acting in a coordinated manner to attenuate insulin signalling .\|Therefore, the inhibition of PTPs such as PTP1B that attenuate IR activation and signalling might be particularly effective in alleviating insulin resistance.\|The prototypic family member PTP1B (encoded by PTPN1) dephosphorylates the IR beta subunit Y1162 and Y1163 activation loop autophosphorylation site to attenuate insulin signalling in vivo .

Publications:

8

Organism:

Homo Sapiens, Mus Musculus

Pathways:

Insulin Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-270539	Tyr12	DSQQTNDyMQPEEDW	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
16291744	Here we report that protein-tyrosine phosphatase 1B (PTP 1B) is an alpha-actinin phosphatase. PTP 1B-dependent dephosphorylation of alpha-actinin was seen in COS-7 cells\|No dephosphorylation was observed in cells coexpressing the alpha-actinin phosphorylation mutant Y12F and PTP 1B. \|A reversible interaction between alpha-actinin and Src enables the dephosphorylation of alpha-actinin by PTP 1B, releasing Src

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-141634	Tyr12	DSQQTNDyMQPEEDW	Homo sapiens
pmid	sentence
16291744	Here we report that protein-tyrosine phosphatase 1b (ptp 1b) is an ?-Actinin phosphatase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-145141	Tyr1234	RDMYDKEyYSVHNKT	Homo sapiens
pmid	sentence
16537444	Using substrate trapping mutants of ptp1b or tcptp, we have demonstrated that both phosphatases interact with met and that these interactions require phosphorylation of twin tyrosines (tyr-1234/1235) in the activation loop of the met kinase domain. We demonstrate that phosphorylation of tyr-1234/1235 in the activation loop of the met receptor is elevated in the absence of either ptp1b or tcptp and further elevated upon loss of both phosphatases. This enhanced phosphorylation of met corresponds to enhanced biological activity and cellular invasion.

Identifier	Residue	Sequence	Organism
SIGNOR-181323	Tyr1234	RDMYDKEyYSVHNKT	Homo sapiens
pmid	sentence
18819921	Using substrate trapping mutants of ptp1b or tcptp, we have demonstrated that both phosphatases interact with met and that these interactions require phosphorylation of twin tyrosines (tyr-1234/1235) in the activation loop of the met kinase domain. We demonstrate that phosphorylation of tyr-1234/1235 in the activation loop of the met receptor is elevated in the absence of either ptp1b or tcptp and further elevated upon loss of both phosphatases. This enhanced phosphorylation of met corresponds to enhanced biological activity and cellular invasion.

Identifier	Residue	Sequence	Organism
SIGNOR-181327	Tyr1235	DMYDKEYySVHNKTG	Homo sapiens
pmid	sentence
18819921	Using substrate trapping mutants of ptp1b or tcptp, we have demonstrated that both phosphatases interact with met and that these interactions require phosphorylation of twin tyrosines (tyr-1234/1235) in the activation loop of the met kinase domain. We demonstrate that phosphorylation of tyr-1234/1235 in the activation loop of the met receptor is elevated in the absence of either ptp1b or tcptp and further elevated upon loss of both phosphatases. This enhanced phosphorylation of met corresponds to enhanced biological activity and cellular invasion.

Identifier	Residue	Sequence	Organism
SIGNOR-145145	Tyr1235	DMYDKEYySVHNKTG	Homo sapiens
pmid	sentence
16537444	Using substrate trapping mutants of ptp1b or tcptp, we have demonstrated that both phosphatases interact with met and that these interactions require phosphorylation of twin tyrosines (tyr-1234/1235) in the activation loop of the met kinase domain. We demonstrate that phosphorylation of tyr-1234/1235 in the activation loop of the met receptor is elevated in the absence of either ptp1b or tcptp and further elevated upon loss of both phosphatases. This enhanced phosphorylation of met corresponds to enhanced biological activity and cellular invasion.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248411	Tyr1234	RDMYDKEyYSVHNKT	Homo sapiens
pmid	sentence
18819921	Using substrate trapping mutants of PTP1B or TCPTP, we have demonstrated that both phosphatases interact with Met and that these interactions require phosphorylation of twin tyrosines (Tyr-1234/1235) in the activation loop of the Met kinase domain.\|Using small interfering RNA against PTP1B and TCPTP, we demonstrate that phosphorylation of Tyr-1234/1235 in the activation loop of the Met receptor is elevated in the absence of either PTP1B or TCPTP and further elevated upon loss of both phosphatases.

Identifier	Residue	Sequence	Organism
SIGNOR-248412	Tyr1235	DMYDKEYySVHNKTG	Homo sapiens
pmid	sentence
18819921	Using substrate trapping mutants of PTP1B or TCPTP, we have demonstrated that both phosphatases interact with Met and that these interactions require phosphorylation of twin tyrosines (Tyr-1234/1235) in the activation loop of the Met kinase domain.\|Using small interfering RNA against PTP1B and TCPTP, we demonstrate that phosphorylation of Tyr-1234/1235 in the activation loop of the Met receptor is elevated in the absence of either PTP1B or TCPTP and further elevated upon loss of both phosphatases.

Identifier	Residue	Organism
SIGNOR-277001		Homo sapiens
pmid	sentence
29920310	It has been reported that the protein tyrosine phosphatase PTP1B could inactivate MET by direct dephosphorylation of Tyr 1234 and 1235 in its activation loop, and that this dephosphorylation takes place in peri-nuclear region of the cell [ xref ].

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248430	Tyr14	VDSEGHLyTVPIREQ	in vitro
pmid	sentence
16388599	The scaffolding protein caveolin-1 is also a participant in these pathways and is specifically phosphorylated on tyrosine 14, when these pathways are activated. Here, we provide evidence that PTP1B can efficiently catalyze the removal of the phosphoryl group from phosphocaveolin-1.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248424	Tyr152	ISEDIKSyYTVRQLE	in vitro
pmid	sentence
11506178	Tyrosine residues 66, 152 and/or 153 of PTP1B are phosphorylated by the activated insulin receptor and are also necessary for formation of the PTP1B:insulin receptor complex\| Furthermore, tyrosine phosphorylation of PTP1B by the insulin receptor tyrosine kinase increases the catalytic activity of PTP1B\|These results suggest that PTP1B can dephosphorylate itself under in vitro conditions.

Identifier	Residue	Sequence	Organism
SIGNOR-248425	Tyr153	SEDIKSYyTVRQLEL	in vitro
pmid	sentence
11506178	Tyrosine residues 66, 152 and/or 153 of PTP1B are phosphorylated by the activated insulin receptor and are also necessary for formation of the PTP1B:insulin receptor complex\| Furthermore, tyrosine phosphorylation of PTP1B by the insulin receptor tyrosine kinase increases the catalytic activity of PTP1B\|These results suggest that PTP1B can dephosphorylate itself under in vitro conditions.

Identifier	Residue	Sequence	Organism
SIGNOR-248423	Tyr66	LHQEDNDyINASLIK	in vitro
pmid	sentence
11506178	Tyrosine residues 66, 152 and/or 153 of PTP1B are phosphorylated by the activated insulin receptor and are also necessary for formation of the PTP1B:insulin receptor complex\| Furthermore, tyrosine phosphorylation of PTP1B by the insulin receptor tyrosine kinase increases the catalytic activity of PTP1B\|These results suggest that PTP1B can dephosphorylate itself under in vitro conditions.

Publications:

3

Organism:

In Vitro

Pathways:

Insulin Signaling, Rett syndrome

Identifier	Residue	Sequence	Organism
SIGNOR-249368	Tyr152	ISEDIKSyYTVRQLE	in vitro
pmid	sentence
11506178	Tyrosine residues 66, 152 and/or 153 of PTP1B are phosphorylated by the activated insulin receptor and are also necessary for formation of the PTP1B:insulin receptor complex\| Furthermore, tyrosine phosphorylation of PTP1B by the insulin receptor tyrosine kinase increases the catalytic activity of PTP1B

Identifier	Residue	Sequence	Organism
SIGNOR-249369	Tyr153	SEDIKSYyTVRQLEL	in vitro
pmid	sentence
11506178	Tyrosine residues 66, 152 and/or 153 of PTP1B are phosphorylated by the activated insulin receptor and are also necessary for formation of the PTP1B:insulin receptor complex\| Furthermore, tyrosine phosphorylation of PTP1B by the insulin receptor tyrosine kinase increases the catalytic activity of PTP1B

Identifier	Residue	Sequence	Organism
SIGNOR-249370	Tyr66	LHQEDNDyINASLIK	in vitro
pmid	sentence
11506178	Tyrosine residues 66, 152 and/or 153 of PTP1B are phosphorylated by the activated insulin receptor and are also necessary for formation of the PTP1B:insulin receptor complex\| Furthermore, tyrosine phosphorylation of PTP1B by the insulin receptor tyrosine kinase increases the catalytic activity of PTP1B

Publications:

3

Organism:

In Vitro

Pathways:

Insulin Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-276974	Tyr160	LDLCKGGyVPQFSGL	Homo sapiens
pmid	sentence
27752061	PTP1B dephosphorylates PITX-1 at Y160, 175 and Y179.\|Through directly dephosphorylating PITX-1 at Y160, Y175 and Y179, PTP1B promoted proteasomal degradation of PITX-1, thus leaded in downregulating p120RasGAP and CRC cell survival.

Identifier	Residue	Sequence	Organism
SIGNOR-276973	Tyr179	EDVYAAGySYNNWAA	Homo sapiens
pmid	sentence
27752061	PTP1B dephosphorylates PITX-1 at Y160, 175 and Y179.\|Through directly dephosphorylating PITX-1 at Y160, Y175 and Y179, PTP1B promoted proteasomal degradation of PITX-1, thus leaded in downregulating p120RasGAP and CRC cell survival.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-142981	Tyr177	EDQAVTEyVATRWYR	Homo sapiens
pmid	sentence
16336213	Erk8 (extracellular-signal-regulated protein kinase 8) expressed in escherichia coli or insect cells was catalytically active and phosphorylated at both residues of the thr-glu-tyr motif. Dephosphorylation of the threonine residue by pp2a (protein serine/threonine phosphatase 2a) decreased erk8 activity by over 95% in vitro, whereas complete dephosphorylation of the tyrosine residue by ptp1b (protein tyrosine phosphatase 1b) decreased activity by only 15-20%

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-154199	Tyr2110	FGLARDIyKNDYYRK	Homo sapiens
pmid	sentence
17416557	In an approach to gain insight into the sequence-dependent dephosphorylation of multiple phosphotyrosyl-containing peptides by the phosphatases shp-1 and ptp1b, we applied a chromatographic technique for the analysis of the dephosphorylation products.

Identifier	Residue	Sequence	Organism
SIGNOR-154203	Tyr2114	RDIYKNDyYRKRGEG	Homo sapiens
pmid	sentence
17416557	In an approach to gain insight into the sequence-dependent dephosphorylation of multiple phosphotyrosyl-containing peptides by the phosphatases shp-1 and ptp1b, we applied a chromatographic technique for the analysis of the dephosphorylation products.

Identifier	Residue	Sequence	Organism
SIGNOR-154207	Tyr2115	DIYKNDYyRKRGEGL	Homo sapiens
pmid	sentence
17416557	In an approach to gain insight into the sequence-dependent dephosphorylation of multiple phosphotyrosyl-containing peptides by the phosphatases shp-1 and ptp1b, we applied a chromatographic technique for the analysis of the dephosphorylation products.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265495	Tyr267	IAEVKAQyEDIANRS	Homo sapiens	HT-29 Cell
pmid	sentence
24003221	Keratin 8 phospho-Tyr-267 is dephosphorylated by PTP1B and promotes insolubility and filament organization, as does the paralogous GFAP tyrosine.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248406	Tyr291	KSEPEPVyIDEDKMD	Homo sapiens
pmid	sentence
20504764	Together, the results presented here demonstrate that PTP1B can influence RTK signaling in a previously unrecognized manner. We show that PTP1B directly targets STAM2, part of the ESCRT-0 endosomal sorting complex, and we provide the first evidence that tyrosine phosphorylation affects STAM localization and function. This regulatory mechanism could impact signaling downstream of numerous cell surface receptors that are ubiquitinated and recognized by this conserved sorting machinery.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248418	Tyr332	ILAIHDSyKPEFHSD	Cricetulus griseus
pmid	sentence
12907755	PTPH1 only bound Tyr534, whereas PTP1B and TC-PTP bound multiple phosphopeptides. Earlier work suggests that Tyr332, Tyr487, Tyr534, Tyr566, and Tyr627 are all phosphorylated after GH stimulation (21). Apart from Tyr627, all of these also appear good PTP substrates

Identifier	Residue	Sequence	Organism
SIGNOR-248419	Tyr487	SLSNIDFyAQVSDIT	Cricetulus griseus
pmid	sentence
12907755	PTPH1 only bound Tyr534, whereas PTP1B and TC-PTP bound multiple phosphopeptides. Earlier work suggests that Tyr332, Tyr487, Tyr534, Tyr566, and Tyr627 are all phosphorylated after GH stimulation (21). Apart from Tyr627, all of these also appear good PTP substrates

Identifier	Residue	Sequence	Organism
SIGNOR-248420	Tyr534	NFLMDNAyFCEADAK	Cricetulus griseus
pmid	sentence
12907755	PTPH1 only bound Tyr534, whereas PTP1B and TC-PTP bound multiple phosphopeptides. Earlier work suggests that Tyr332, Tyr487, Tyr534, Tyr566, and Tyr627 are all phosphorylated after GH stimulation (21). Apart from Tyr627, all of these also appear good PTP substrates

Identifier	Residue	Sequence	Organism
SIGNOR-248421	Tyr566	SLNQEDIyITTESLT	Cricetulus griseus
pmid	sentence
12907755	PTPH1 only bound Tyr534, whereas PTP1B and TC-PTP bound multiple phosphopeptides. Earlier work suggests that Tyr332, Tyr487, Tyr534, Tyr566, and Tyr627 are all phosphorylated after GH stimulation (21). Apart from Tyr627, all of these also appear good PTP substrates

Publications:

4

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism
SIGNOR-277082	Tyr342	RLIKEDVyLSHDHNI	Homo sapiens
pmid	sentence
29142193	Using a variety of PTEN mutant constructs, we show that protein phosphatase activity of PTEN targets PTK6, with efficiency similar to PTP1B, a phosphatase that directly dephosphorylates PTK6 Y342.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277120	Tyr393	ASFNTDPyVREFGIM	Homo sapiens
pmid	sentence
25175024	Taken together, our results indicate that Tyr 393 of AGO2 is hyperphosphorylated in response to PTP1B inactivation and may contribute to H-RAS V12 -induced development of senescence.\|We identified phospho-Tyr 393 of argonaute 2 (AGO2) as a direct substrate of PTP1B.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248431	Tyr397	SVSETDDyAEIIDEE	Chlorocebus aethiops	COS Cell
pmid	sentence
16291744	The focal adhesion kinase (FAK) is a key regulator of cell migration. Phosphorylation at Tyr-397 activates FAK \|The dephosphorylation at Tyr-397 in FAK triggered by wild-type alpha-actinin and PTP 1B caused a significant increase in cell migration.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-245299	Tyr419	RLIEDNEyTARQGAK	Homo sapiens	HEK-293 Cell
pmid	sentence
11007774	Incubation of the inactivated c-Src with PTP1B results in a dose-dependent reactivation of c-Src tyrosine kinase activity. Incubation of c-Src with 2 or 10 g of PTP1B results in partial or full restoration of c-Src kinase activity, respectively. The activation is accompanied by dephosphorylation of c-Src, both of Tyr-419 and of Tyr-530

Identifier	Residue	Sequence	Organism
SIGNOR-248422	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
17974954	Overexpression of PTP1B increased Src specific activity in colon cancer cells by reducing phosphorylation at Y530 of Src.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-45004	Tyr42	DSMKDEEyEQMVKEL	Homo sapiens
pmid	sentence
8940099	Ptp1b is able to dephosphorylate phosphorylated-tyr-42 on ikappabalpha

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277027	Tyr421	RLPSSPVyEDAASFK	Homo sapiens
pmid	sentence
27824079	We conclude that Mena INV promotes invadopodium maturation by inhibiting normal dephosphorylation of cortactin at tyrosine 421 by the phosphatase PTP1B.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248432	Tyr446	GTEPEPVySMEAADY	Chlorocebus aethiops	COS Cell
pmid	sentence
18387954	Here, we have identified cortactin, a central regulator of actin cytoskeletal dynamics, as a substrate of PTP1B. A trapping mutant of PTP1B binds cortactin at the phosphorylation site Tyr446, \|Cortactin exerts its effects on the actin cytoskeleton by interacting directly with the Arp2/3 complex , F-actin \|Src phosphorylates murine cortactin predominantly at three key sites in vitro, Tyr421, Tyr466, and Tyr482 (corresponding to Tyr421, Tyr470, and Try486 in human cortactin), resulting in decreased actin cross-linking activity

Publications:

2

Organism:

Homo Sapiens, Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-103607	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
12857726	The tyrosine kinase pp60c-src has also been identified as a good substrate of ptp1b leading to an activation of this kinase (27).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-52950	Tyr66	LHQEDNDyINASLIK	Homo sapiens
pmid	sentence
9355745	After binding to egfr, ptp1b becomes tyrosine-phosphorylated at tyr-66 phosphorylation of ptp1b by egfr enhances its catalytic activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248428	Tyr694	LAKAVDGyVKPQIKQ	Chlorocebus aethiops
pmid	sentence
10993888	A Cytosolic Protein-tyrosine Phosphatase PTP1B Specifically Dephosphorylates and Deactivates Prolactin-activated STAT5a and STAT5b

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-82042	Tyr699	TAKAVDGyVKPQIKQ	Homo sapiens
pmid	sentence
10993888	A cytosolic protein-tyrosine phosphatase ptp1b specifically dephosphorylates and deactivates prolactin-activated stat5a and stat5b.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Breast

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248429	Tyr699	TAKAVDGyVKPQIKQ	Chlorocebus aethiops	COS Cell
pmid	sentence
10993888	A Cytosolic Protein-tyrosine Phosphatase PTP1B Specifically Dephosphorylates and Deactivates Prolactin-activated STAT5a and STAT5b

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-135211	Tyr705	DPGSAAPyLKTKFIC	Homo sapiens
pmid	sentence
15821101	Mechanism of protein tyrosine phosphatase 1b-mediated inhibition of leptin signalling. Ptp1b plays a critical role in the down-regulation of activated-stat3 by dephosphorylating tyr705, that is the phosphorylation site of activation of stat3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248427	Tyr705	DPGSAAPyLKTKFIC	Homo sapiens
pmid	sentence
15821101	PTP1B was able to dephosphorylate activated JAK2 and STAT3 in vitro, whereas either no or a minimal effect was observed with cluster of differentiation 45 (CD45), PTPalpha and leukocyte antigen-related (LAR). By utilisation of a selective PTP1B inhibitor, the leptin-induced STAT3 activation was enhanced in cells. In conclusion, these results suggested that the negative regulatory role of PTP1B on leptin signalling is mediated through a direct and selective dephosphorylation of the two signalling molecules, JAK2 and STAT3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264554	Tyr706	RDVYSTDyYRVGGHT	Homo sapiens	SH-SY5Y Cell
pmid	sentence
26214522	Collectively, these data establish a direct enzyme-substrate interaction between PTP1B and phosphorylated Y705/706 (p-Y705/706) TRKB, the critical autophosphorylation sites that mediate BDNF-induced signaling.\| Therefore, the data are consistent with a role of PTP1B as an inhibitor of BDNF/TRKB signaling

Identifier	Residue	Sequence	Organism
SIGNOR-264553	Tyr707	DVYSTDYyRVGGHTM	Homo sapiens
pmid	sentence
26214522	Collectively, these data establish a direct enzyme-substrate interaction between PTP1B and phosphorylated Y705/706 (p-Y705/706) TRKB, the critical autophosphorylation sites that mediate BDNF-induced signaling.\| Therefore, the data are consistent with a role of PTP1B as an inhibitor of BDNF/TRKB signaling

Publications:

2

Organism:

Homo Sapiens

Pathways:

Rett syndrome

Identifier	Residue	Sequence	Organism
SIGNOR-248426	Tyr779	EDDPEAAyTTRGGKI	Homo sapiens
pmid	sentence
21135139	Nevertheless, the finding that phosphorylation of the activation loop tyrosine (EphA3-Y779), a recently identified PTP1B substrate (Mertins et al., 2008), is essential for ligand-induced endocytosis (Janes et al., 2009)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-56818		Homo sapiens
pmid	sentence
9566916	These results illustrate selectivity in the effects of ptps in a cellular context and suggest that ptp1b may function as a specific, negative regulator of p210 bcr-abl signalling in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277051		Homo sapiens
pmid	sentence
22169477	Finally, we demonstrated that wild-type PTP1B directly dephosphorylated myc-tagged PERK that had been isolated from tunicamycin-treated HEK293T cells by immunoprecipitation ( xref ).\|The ability of PTP1B to dephosphorylate Tyr619 and inactivate PERK is fine tuned by the production of H 2 S by CSE in response to ER stress.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-141637		Homo sapiens
pmid	sentence
16291744	We show that coexpression of wild-type alpha-actinin and ptp 1b causes dephosphorylation at tyr-397 in fak.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279724		Homo sapiens
pmid	sentence
21554241	GSK-3beta phosphorylates PTP1B at serine residues, and activation of GSK-3beta reduces the mRNA level of PTP1B.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Insulin Signaling

Identifier	Residue	Organism
SIGNOR-248403		Homo sapiens
pmid	sentence
12857726	Using a pharmacological inhibitor, we provide evidence that PTP1B activation and LAT dephosphorylation processes were required for irreversible platelet aggregation.\|In collagen-stimulated platelets, the signaling complexes recruited by tyrosine-phosphorylated LAT are essential for PLCgamma2 activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252639		Homo sapiens
pmid	sentence
15632081	Whereas insulin-induced phosphatidylinositol 3-kinase/akt signaling was prolonged in both tcptp-/- and ptp1b-/- immortalized mouse embryo fibroblasts (mefs), mitogen-activated protein kinase erk1/2 signaling was elevated only in ptp1b- mefs

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-264546		Homo sapiens	Fibroblast
pmid	sentence
26214522	In this study, we have demonstrated that the PTPN1 gene, which encodes PTP1B, was a direct target of MECP2 and that PTP1B protein levels were dramatically increased in Mecp2-mutant mice and in fibroblasts derived from patients with RTT.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Rett syndrome

Identifier	Residue	Organism	Cell Line
SIGNOR-151711		Homo sapiens	HEK-293 Cell
pmid	sentence
17197020	We conclude that phosphorylation/dephosphorylation of tyrosines in position 161 and 162 is essential for regulation of ca2+ influx through trpv6 ca2+ channels in hek293 cells. Co-transfection with src led to tyrosine phosphorylation of trpv6 which could be dephosphorylated by ptp1b. y161/162 are essential for tyrosine phosphorylation-dependent modulation of trpv6-mediated ca2+ entry.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-132959		Homo sapiens
pmid	sentence
15632081	Whereas insulin-induced phosphatidylinositol 3-kinase/akt signaling was prolonged in both tcptp-/- and ptp1b-/- immortalized mouse embryo fibroblasts (mefs), mitogen-activated protein kinase erk1/2 signaling was elevated only in ptp1b- mefs

Publications:

1

Organism:

Homo Sapiens

Pathways:

Insulin Signaling

Identifier	Residue	Organism
SIGNOR-95313		Homo sapiens
pmid	sentence
12414790	Therefore, we conclude that an increase in soluble ptp1b activity contributes to the anti-migratory, but not anti-mitogenic, actions of hspry2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279257		Homo sapiens
pmid	sentence
22031842	PKC\u03b1 then phosphorylates and activates endothelial cell protein tyrosine phosphatase 1B (PTP1B) , .

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-56815		Homo sapiens
pmid	sentence
9566916	These results illustrate selectivity in the effects of ptps in a cellular context and suggest that ptp1b may function as a specific, negative regulator of p210 bcr-abl signalling in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-276965		Homo sapiens
pmid	sentence
23521888	Since Gab1 is negatively regulated by PTP1B, a part of the retinal neuroprotective effect we have observed previously in PTP1B deficient mice could be contributed by Gab1 as well.\|The results indicate that PTP1B completely dephosphorylated Gab1 and the mutant protein failed to dephosphorylate Gab1 (Figure\u00a0 xref C).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277122		Homo sapiens
pmid	sentence
22156494	Phosphorylated STAT6 may also serve as a cytoplasmic substrate for PTP1B since overexpression of PTP1B leads to STAT6 dephosphorylation and the suppression of STAT6 transcriptional activity, whereas PTP1B deficiency increases IL-4-induced STAT6 signaling in B-cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-278703		Homo sapiens
pmid	sentence
34434118	Proteasome inhibitor treatment diminished the decrease of PTP1B (Figure 5F) caused by TRIM18 overexpression.\|TRIM18 Interacts With PTP1B and Promotes PTP1B Ubiquitination.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190254		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-250941		in vitro
pmid	sentence
9600099	In this study, we demonstrate that HPTP1B are multiple phosphorylated on threonine and tyrosine as well as serine near its N-terminus by CKII and p60c-src in vitro.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-74852		in vitro
pmid	sentence
10660596	Tyrosine dephosphorylation and deactivation of insulin receptor substrate-1 by protein-tyrosine phosphatase 1B. Possible facilitation by the formation of a ternary complex with the Grb2 adaptor protein.

Publications:

1

Organism:

In Vitro

Pathways:

Insulin Signaling

Identifier	Residue	Organism
SIGNOR-107754		Homo sapiens
pmid	sentence
11350745	Dephosphorylation of tyrosine residues by ptp1b, a protein tyrosine phosphatase, reduced the enhanced pkcdelta activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-56822		Homo sapiens
pmid	sentence
9566916	We have observed association and dephosphorylation of p210 bcr-abl, but not v-abl, by ptp1b in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277121		Homo sapiens
pmid	sentence
12377785	PTP1B modulates the association of beta-catenin with N-cadherin through binding to an adjacent and partially overlapping target site.\|The nonreceptor tyrosine phosphatase PTP1B associates with the cytoplasmic domain of N-cadherin and may regulate cadherin function through dephosphorylation of beta-catenin.\|Thus, interaction of PTP1B with N-cadherin is essential for its association with beta-catenin, stable expression at the cell surface, and consequently, cadherin function.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-134564		Homo sapiens
pmid	sentence
15780598	Upon ligand binding, IL-2R , IL-6R or LeptinR , IFN-_R , IFN-_R and PRLR or growth hormone (GH) receptor associated JAKs become activated. These JAKs mediate phosphorylation of specific tyrosine residues and recruit STATs. Activated STATs are released from the receptor and translocate to the nucleus. PTP1B dephosphorylates JAK2, TYK2 and STAT5 . The 45-kDa form of TC-PTP was shown to dephosphorylate JAK1 and JAK3 as well as STAT1, STAT3 and STAT5.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-115709		Homo sapiens
pmid	sentence
11884589	Ptp-1b can regulate igf-ir kinase activity and function and that loss of ptp-1b can enhance igf-i-mediated cell survival, growth, and motility in transformed cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-103599		Homo sapiens
pmid	sentence
12857726	Our results demonstrate that ptp1b plays an important role in the integrin-mediated dephosphorylation of lat in human platelets and is involved in the control of irreversible aggregation upon fcgammariia stimulation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-276994		Homo sapiens
pmid	sentence
14527337	In vivo interaction between EPO-R and PTP1B suggested that PTP1B dephosphorylates the EPO-R intracellularly.\|Protein tyrosine phosphatase 1B participates in the down-regulation of erythropoietin receptor signalling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277167		Homo sapiens
pmid	sentence
24590766	Here, we show that PTP1B regulates CD40 and BAFF-R signaling and dephosphorylates the mitogen-activated protein kinase p38.\|Specifically, PTP1B counteracts p38 mitogen-activated protein kinase activation by directly dephosphorylating Tyr182 of this kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-251028		in vitro
pmid	sentence
9600099	In this study, we demonstrate that HPTP1B are multiple phosphorylated on threonine and tyrosine as well as serine near its N-terminus by CKII and p60c-src in vitro.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-261800
pmid	sentence
16115959	N this study, we demonstrate an essential role for protein-tyrosine phosphatase (PTP)-1B in this process. In resting platelets, c-Src forms a complex with alphaIIbbeta3 and Csk, which phosphorylates c-Src tyrosine 529 to maintain c-Src autoinhibition. Fibrinogen binding to alphaIIbbeta3 triggers PTP-1B recruitment to the alphaIIbbeta3-c-Src-Csk complex in a manner that is dependent on c-Src and specific tyrosine (tyrosine 152 and 153) and proline (proline 309 and 310) residues in PTP-1B. Studies of PTP-1B-deficient mouse platelets indicate that PTP-1B is required for fibrinogen-dependent Csk dissociation from alphaIIbbeta3, dephosphorylation of c-Src tyrosine 529, and c-Src activation.

Publications:

1

Identifier	Residue	Organism
SIGNOR-277081		Homo sapiens
pmid	sentence
28919207	PTP1B inactivation prevents TrkA exit from soma and causes receptor degradation, suggesting a " gate-keeper " mechanism that ensures targeting of inactive receptors to axons to engage with ligand.\|We identify a gate keeping mechanism in which TrkA receptors, destined for transcytosis, are dephosphorylated in neuronal soma by the ER-resident tyrosine phosphatase, PTP1B.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-264552		Mus musculus	Forebrain
pmid	sentence
26214522	We demonstrated that the PTPN1 gene, which encodes PTP1B, was a target of MECP2 and that disruption of MECP2 function was associated with increased levels of PTP1B in RTT models.

Publications:

1

Organism:

Mus Musculus

Pathways:

Rett syndrome

Identifier	Residue	Organism	Cell Line
SIGNOR-248433		Homo sapiens	HEK-293 Cell
pmid	sentence
17197020	In HEK293 cells, transfected with the Ca2+ channel protein TRPV6, Ca2+ influx is increased and TRPV6 is tyrosine phosphorylated following addition of the tyrosine phosphatase inhibitor\|PTP1B interacts with the N-terminal domain of TRPV6 within a region of amino acids 1-191 as shown by co-immunoprecipitation, bimolecular fluorescence complementation and the yeast 2-hybrid system. Point mutation of both tyrosines 161 and 162 in the TRPV6 protein abolishes the DMHV-effect on Ca2+ influx and tyrosine phosphorylation by Src. Single mutations of Y161 or Y162 shows that each of both tyrosines alone is sufficient for the DMHV-effect. We conclude that phosphorylation/dephosphorylation of tyrosines in position 161 and 162 is essential for regulation of Ca2+ influx through TRPV6 Ca2+ channels in HEK293 cells.

Publications:

1

Organism:

Homo Sapiens

Name	PTPN1 View Modifications
Full Name	Tyrosine-protein phosphatase non-receptor type 1
Synonyms	Protein-tyrosine phosphatase 1B, PTP-1B \| PTP1B
Primary ID	P18031
Links	- -
Type	protein
Relations	116
Pathways	Insulin Signaling, Rett syndrome
Inhibitors	(E)-3-tosylacrylonitrile
Function	Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET.

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