Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-248905	Ser1062	AVKTVNEsASLRERI	in vitro
pmid	sentence
7926007	Identification of serines-1035/1037 in the kinase domain of the insulin receptor as protein kinase C alpha mediated phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-248906	Ser1064	KTVNESAsLRERIEF	in vitro
pmid	sentence
7926007	Identification of serines-1035/1037 in the kinase domain of the insulin receptor as protein kinase C alpha mediated phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-248933	Thr1362	YEEHIPYtHMNGGKK	in vitro
pmid	sentence
8463287	Therefore, the present study directly identifies threonine 1336 in the HIR as a phosphorylation site for insulin and PMA.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-24782	Tyr100	FDKDGNGyISAAELR	Homo sapiens
pmid	sentence
3415247	The in vitro phosphorylation of calmodulin by the insulin receptor tyrosine kinase. Phosphorylated calmodulin does not exhibit the characteristic ca2+ shift normally observed with calmodulin in electrophoretic gels, an observation that is consistent with this modification affecting the biological activity of the molecule.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-266336	Tyr100	FDKDGNGyISAAELR	Homo sapiens
pmid	sentence
3415247	The in vitro phosphorylation of calmodulin by the insulin receptor tyrosine kinase. Phosphorylated calmodulin does not exhibit the characteristic ca2+ shift normally observed with calmodulin in electrophoretic gels, an observation that is consistent with this modification affecting the biological activity of the molecule.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-266320	Tyr100	FDKDGNGyISAAELR	Homo sapiens
pmid	sentence
3415247	The in vitro phosphorylation of calmodulin by the insulin receptor tyrosine kinase. Phosphorylated calmodulin does not exhibit the characteristic ca2+ shift normally observed with calmodulin in electrophoretic gels, an observation that is consistent with this modification affecting the biological activity of the molecule.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-233564	Tyr1011	DVFPCSVyVPDEWEV	in vitro
pmid	sentence
3166375	This approach revealed that insulin stimulates autophosphorylation of the insulin-receptor beta-subunit in vitro on at least seven tyrosine residues distributed among three distinct domainsAt least two further tyrosine residues appeared to be phosphorylated after those in domains 2 and 3. These residues probably residue within a domain lying in close proximity to the inner face of the plasma membrane containing tyrosines 953, 960 and 972

Identifier	Residue	Sequence	Organism
SIGNOR-106510	Tyr1185	FGMTRDIyETDYYRK	in vitro
pmid	sentence
2449432	We identified the major autophosphorylation sites in the insulin receptor and correlated their phosphorylation with the phosphotransferase activity of the receptor on synthetic peptides. We conclude that 1) autophosphorylation of the insulin receptor begins by phosphorylation of Tyr-1146 and either Tyr-1150 or Tyr-1151;

Identifier	Residue	Sequence	Organism
SIGNOR-106514	Tyr1189	RDIYETDyYRKGGKG	in vitro
pmid	sentence
2449432	We identified the major autophosphorylation sites in the insulin receptor and correlated their phosphorylation with the phosphotransferase activity of the receptor on synthetic peptides. We conclude that 1) autophosphorylation of the insulin receptor begins by phosphorylation of Tyr-1146 and either Tyr-1150 or Tyr-1151;

Identifier	Residue	Sequence	Organism
SIGNOR-106518	Tyr1190	DIYETDYyRKGGKGL	in vitro
pmid	sentence
2449432	We identified the major autophosphorylation sites in the insulin receptor and correlated their phosphorylation with the phosphotransferase activity of the receptor on synthetic peptides. We conclude that 1) autophosphorylation of the insulin receptor begins by phosphorylation of Tyr-1146 and either Tyr-1150 or Tyr-1151;

Identifier	Residue	Sequence	Organism
SIGNOR-22577	Tyr1355	SLGFKRSyEEHIPYT	in vitro
pmid	sentence
3166375	This approach revealed that insulin stimulates autophosphorylation of the insulin-receptor beta-subunit in vitro on at least seven tyrosine residues distributed among three distinct domainsAt least two further tyrosine residues appeared to be phosphorylated after those in domains 2 and 3. These residues probably residue within a domain lying in close proximity to the inner face of the plasma membrane containing tyrosines 953, 960 and 972

Identifier	Residue	Sequence	Organism
SIGNOR-233560	Tyr1361	SYEEHIPyTHMNGGK	in vitro
pmid	sentence
3166375	This approach revealed that insulin stimulates autophosphorylation of the insulin-receptor beta-subunit in vitro on at least seven tyrosine residues distributed among three distinct domainsAt least two further tyrosine residues appeared to be phosphorylated after those in domains 2 and 3. These residues probably residue within a domain lying in close proximity to the inner face of the plasma membrane containing tyrosines 953, 960 and 972

Identifier	Residue	Sequence	Organism
SIGNOR-106522	Tyr992	DGPLGPLyASSNPEY	in vitro
pmid	sentence
3166375	This approach revealed that insulin stimulates autophosphorylation of the insulin-receptor beta-subunit in vitro on at least seven tyrosine residues distributed among three distinct domainsAt least two further tyrosine residues appeared to be phosphorylated after those in domains 2 and 3. These residues probably residue within a domain lying in close proximity to the inner face of the plasma membrane containing tyrosines 953, 960 and 972

Identifier	Residue	Sequence	Organism
SIGNOR-106526	Tyr999	YASSNPEyLSASDVF	in vitro
pmid	sentence
3166375	This approach revealed that insulin stimulates autophosphorylation of the insulin-receptor beta-subunit in vitro on at least seven tyrosine residues distributed among three distinct domainsAt least two further tyrosine residues appeared to be phosphorylated after those in domains 2 and 3. These residues probably residue within a domain lying in close proximity to the inner face of the plasma membrane containing tyrosines 953, 960 and 972

Publications:

8

Organism:

In Vitro

Pathways:

Adipogenesis, AMPK Signaling, FAP: Insulin-mediated adipogenesis, Insulin Signaling, Luminal Breast Cancer, Leptin Signaling, mTOR in cancer, MTOR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-75989	Tyr1185	FGMTRDIyETDYYRK	Homo sapiens
pmid	sentence
10734133	Identification of tyrosine phosphatases that dephosphorylate the insulin receptor.

Identifier	Residue	Sequence	Organism
SIGNOR-75993	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
10734133	Identification of tyrosine phosphatases that dephosphorylate the insulin receptor.

Identifier	Residue	Sequence	Organism
SIGNOR-75997	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
10734133	Identification of tyrosine phosphatases that dephosphorylate the insulin receptor.

Identifier	Residue	Sequence	Organism
SIGNOR-76001	Tyr999	YASSNPEyLSASDVF	Homo sapiens
pmid	sentence
10734133	Identification of tyrosine phosphatases that dephosphorylate the insulin receptor.

Publications:

4

Organism:

Homo Sapiens

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	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-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
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-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
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 .

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.

Publications:

8

Organism:

Mus Musculus, Homo Sapiens

Pathways:

Insulin Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248444	Tyr1185	FGMTRDIyETDYYRK	Rattus norvegicus	Hepatocyte
pmid	sentence
15738637	In this study, we showed that receptor-type PTPepsilon (PTP epsilonM) dephosphorylated IR in rat primary hepatocytes and tyrosines 972, 1158, 1162 and 1163\| These results suggest that PTPepsilonM is a negative regulator of IR signaling and involved in insulin-induced glucose metabolism mainly through direct dephosphorylation and inactivation of IR in hepatocytes and liver.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248445	Tyr1189	RDIYETDyYRKGGKG	Rattus norvegicus	Hepatocyte
pmid	sentence
15738637	In this study, we showed that receptor-type PTPepsilon (PTP epsilonM) dephosphorylated IR in rat primary hepatocytes and tyrosines 972, 1158, 1162 and 1163\| These results suggest that PTPepsilonM is a negative regulator of IR signaling and involved in insulin-induced glucose metabolism mainly through direct dephosphorylation and inactivation of IR in hepatocytes and liver.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248446	Tyr1190	DIYETDYyRKGGKGL	Rattus norvegicus	Hepatocyte
pmid	sentence
15738637	In this study, we showed that receptor-type PTPepsilon (PTP epsilonM) dephosphorylated IR in rat primary hepatocytes and tyrosines 972, 1158, 1162 and 1163\| These results suggest that PTPepsilonM is a negative regulator of IR signaling and involved in insulin-induced glucose metabolism mainly through direct dephosphorylation and inactivation of IR in hepatocytes and liver.

Identifier	Residue	Sequence	Organism
SIGNOR-248443	Tyr999	YASSNPEyLSASDVF	Rattus norvegicus
pmid	sentence
15738637	In this study, we showed that receptor-type PTPepsilon (PTP epsilonM) dephosphorylated IR in rat primary hepatocytes and tyrosines 972, 1158, 1162 and 1163\| These results suggest that PTPepsilonM is a negative regulator of IR signaling and involved in insulin-induced glucose metabolism mainly through direct dephosphorylation and inactivation of IR in hepatocytes and liver.

Publications:

4

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-39147	Tyr1185	FGMTRDIyETDYYRK	Homo sapiens	HeLa Cell
pmid	sentence
8454633	Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190.

Identifier	Residue	Sequence	Organism
SIGNOR-75894	Tyr1185	FGMTRDIyETDYYRK	in vitro
pmid	sentence
10734133	Interestingly, all PTPs that were tested could completely dephosphorylate the receptor, given sufficient time, including a negative control (PTP-PEST) that failed to bind IRK as a trapping mutant.

Identifier	Residue	Sequence	Organism
SIGNOR-75898	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
10734133	Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-39151	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens	HeLa Cell
pmid	sentence
8454633	Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190.

Identifier	Residue	Sequence	Organism
SIGNOR-75902	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
10734133	Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190.

Identifier	Residue	Sequence	Organism
SIGNOR-262291	Tyr1190	DIYETDYyRKGGKGL	in vitro
pmid	sentence
10734133	Interestingly, all PTPs that were tested could completely dephosphorylate the receptor, given sufficient time, including a negative control (PTP-PEST) that failed to bind IRK as a trapping mutant.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-39159	Tyr999	YASSNPEyLSASDVF	Homo sapiens	HeLa Cell
pmid	sentence
8454633	Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190.

Identifier	Residue	Sequence	Organism
SIGNOR-75906	Tyr999	YASSNPEyLSASDVF	Homo sapiens
pmid	sentence
10734133	Autophosphorylated on tyrosine residues in response to insulin. Dephosphorylated by ptpreand ptpn1 at tyr-999, tyr-1185, tyr-1189 and tyr-1190.

Identifier	Residue	Organism
SIGNOR-39155		in vitro
pmid	sentence
8454633	Intrinsic activity was demonstrated in vitro against a variety of phosphotyrosine-containing substrates including BIRK, the autophosphorylated cytoplasmic kinase domain of the insulin receptor beta subunit.

Publications:

9

Organism:

Homo Sapiens, In Vitro

Tissue:

Muscle, Skeletal Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-75910	Tyr1185	FGMTRDIyETDYYRK	Homo sapiens
pmid	sentence
10734133	Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1.

Identifier	Residue	Sequence	Organism
SIGNOR-75914	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
10734133	Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1.

Identifier	Residue	Sequence	Organism
SIGNOR-18018	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
1373652	The question of whether protein tyrosine phosphatases (ptpases) dephosphorylate a multiply phosphorylated peptide in a random or ordered manner was investigated using the synthetic triphosphotyrosyl peptide trdiy(p)etdy(p)y(p)rk, corresponding to the major sites of autophosphorylation of the insulin receptor, as a substrate for four purified ptpases.

Identifier	Residue	Sequence	Organism
SIGNOR-75918	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
10734133	Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1.

Identifier	Residue	Sequence	Organism
SIGNOR-75922	Tyr999	YASSNPEyLSASDVF	Homo sapiens
pmid	sentence
10734133	Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-16235	Tyr1185	FGMTRDIyETDYYRK	Homo sapiens
pmid	sentence
1303753	Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product.

Identifier	Residue	Sequence	Organism
SIGNOR-76005	Tyr1185	FGMTRDIyETDYYRK	Homo sapiens
pmid	sentence
10734133	Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product.

Identifier	Residue	Sequence	Organism
SIGNOR-16239	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
1303753	Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product.

Identifier	Residue	Sequence	Organism
SIGNOR-76009	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
10734133	Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product.

Identifier	Residue	Sequence	Organism
SIGNOR-76013	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
10734133	Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product.

Identifier	Residue	Sequence	Organism
SIGNOR-16243	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
1303753	Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product.

Identifier	Residue	Sequence	Organism
SIGNOR-16247	Tyr999	YASSNPEyLSASDVF	Homo sapiens
pmid	sentence
1303753	Lar ptpase shows strong preference for dephosphorylation first at py5 (at tri-, di-, and monophosphotyrosyl levels). Initially this regioselectivity gives the y5(py9)(py10) diphospho regioisomer, followed by equal dephosphorylation at py9 or py10 to give the corresponding monophosphoryl species on the way to fully dephosphorylated product.

Identifier	Residue	Sequence	Organism
SIGNOR-76017	Tyr999	YASSNPEyLSASDVF	Homo sapiens
pmid	sentence
10734133	Many cellular receptors signal via tyrosine phosphorylation. The tyrosine kinases required for this activity are often recruited upon ligand bindingAlternatively, receptors themselves have kinase activity, like insulin receptors. In either case, the receptors are returned to their original state through the activity of protein-tyrosine phosphatases (PTPs)The major candidate PTPs previously implicated in IRK dephosphorylation are PTP-1b and LAR.

Publications:

8

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-75926	Tyr1185	FGMTRDIyETDYYRK	Homo sapiens
pmid	sentence
10734133	Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1.

Identifier	Residue	Sequence	Organism
SIGNOR-75930	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
10734133	Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1.

Identifier	Residue	Sequence	Organism
SIGNOR-75934	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
10734133	Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1.

Identifier	Residue	Sequence	Organism
SIGNOR-75938	Tyr999	YASSNPEyLSASDVF	Homo sapiens
pmid	sentence
10734133	Finally, we have tested the set of ptps for their ability to dephosphorylate a phosphopeptide corresponding to the irk autophosphorylation site. tc-ptp, sap-1, and ptp-1b all tested positive, but ptp-? Showed no activity, although the same gst-ptp preparation could efficiently convert pnpp (tablei). Interestingly, many other ptps showed activity, namely dep-1, glepp-1, lar, ptp-?, -?, -?, And shp-1.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
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
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
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
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

Identifier	Residue	Sequence	Organism
SIGNOR-146668	Tyr1185	FGMTRDIyETDYYRK	Homo sapiens
pmid	sentence
16679294	Ectopic expression of ptp-meg2 in cells inhibited insulin-induced phosphorylation of the insulin receptor, while rnai-mediated reduction of ptp-meg2 transcript levels enhanced insulin action

Identifier	Residue	Sequence	Organism
SIGNOR-146672	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
16679294	Ectopic expression of ptp-meg2 in cells inhibited insulin-induced phosphorylation of the insulin receptor, while rnai-mediated reduction of ptp-meg2 transcript levels enhanced insulin action

Identifier	Residue	Sequence	Organism
SIGNOR-146676	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
16679294	Ectopic expression of ptp-meg2 in cells inhibited insulin-induced phosphorylation of the insulin receptor, while rnai-mediated reduction of ptp-meg2 transcript levels enhanced insulin action

Identifier	Residue	Sequence	Organism
SIGNOR-146680	Tyr999	YASSNPEyLSASDVF	Homo sapiens
pmid	sentence
16679294	Ectopic expression of ptp-meg2 in cells inhibited insulin-induced phosphorylation of the insulin receptor, while rnai-mediated reduction of ptp-meg2 transcript levels enhanced insulin action

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-76072	Tyr1185	FGMTRDIyETDYYRK	Homo sapiens
pmid	sentence
10734133	These results, combined with secondary dephosphorylation tests, confirm and extend earlier findings that ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase

Identifier	Residue	Sequence	Organism
SIGNOR-76076	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
10734133	These results, combined with secondary dephosphorylation tests, confirm and extend earlier findings that ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase

Identifier	Residue	Sequence	Organism
SIGNOR-76080	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
10734133	These results, combined with secondary dephosphorylation tests, confirm and extend earlier findings that ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase

Identifier	Residue	Sequence	Organism
SIGNOR-76084	Tyr999	YASSNPEyLSASDVF	Homo sapiens
pmid	sentence
10734133	These results, combined with secondary dephosphorylation tests, confirm and extend earlier findings that ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-76088	Tyr1185	FGMTRDIyETDYYRK	Homo sapiens
pmid	sentence
10734133	These results, combined with secondary dephosphorylation tests, confirm and extend earlier findings that ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-21295	Tyr1185	FGMTRDIyETDYYRK	Homo sapiens
pmid	sentence
1715686	Dephosphorylation of autophosphorylated insulin and epidermal-growth-factor receptors by two major subtypes of protein-tyrosine-phosphatase from human placenta.

Identifier	Residue	Sequence	Organism
SIGNOR-76092	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
10734133	These results, combined with secondary dephosphorylation tests, confirm and extend earlier findings that ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-21299	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
1715686	Dephosphorylation of autophosphorylated insulin and epidermal-growth-factor receptors by two major subtypes of protein-tyrosine-phosphatase from human placenta.

Identifier	Residue	Sequence	Organism
SIGNOR-76096	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
10734133	Ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-21303	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
1715686	Dephosphorylation of autophosphorylated insulin and epidermal-growth-factor receptors by two major subtypes of protein-tyrosine-phosphatase from human placenta.

Identifier	Residue	Sequence	Organism
SIGNOR-21307	Tyr999	YASSNPEyLSASDVF	Homo sapiens
pmid	sentence
1715686	Dephosphorylation of autophosphorylated insulin and epidermal-growth-factor receptors by two major subtypes of protein-tyrosine-phosphatase from human placenta.

Identifier	Residue	Sequence	Organism
SIGNOR-76100	Tyr999	YASSNPEyLSASDVF	Homo sapiens
pmid	sentence
10734133	These results, combined with secondary dephosphorylation tests, confirm and extend earlier findings that ptp-1b and t-cell ptp are physiological enzymes for the insulin receptor kinase.

Publications:

8

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-254704	Tyr1189	RDIYETDyYRKGGKG	in vitro
pmid	sentence
25624455	PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity.

Identifier	Residue	Sequence	Organism
SIGNOR-254705	Tyr1190	DIYETDYyRKGGKGL	in vitro
pmid	sentence
25624455	PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity.

Identifier	Residue	Sequence	Organism
SIGNOR-254703	Tyr999	YASSNPEyLSASDVF	in vitro
pmid	sentence
25624455	PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248385	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens	HEK-293 Cell
pmid	sentence
12612081	In this study, we investigated the downregulation of insulin receptor (IR) signaling by TCPTP. In response to insulin stimulation, the TC48-D182A and TC45-D182A substrate-trapping mutants formed stable complexes with the endogenous tyrosine-phosphorylated IR beta-subunit in 293 cells.\|IR β-subunit phosphorylated on tyrosine and specifically on tyrosines 1162 and 1163 could be coimmunoprecipitated with the TC48-D182A and TC45-D182A mutants but not the wild-type TC48 or TC45 in response to insulin

Identifier	Residue	Sequence	Organism
SIGNOR-248386	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
12612081	In this study, we investigated the downregulation of insulin receptor (IR) signaling by TCPTP. In response to insulin stimulation, the TC48-D182A and TC45-D182A substrate-trapping mutants formed stable complexes with the endogenous tyrosine-phosphorylated IR beta-subunit in 293 cells.\|IR β-subunit phosphorylated on tyrosine and specifically on tyrosines 1162 and 1163 could be coimmunoprecipitated with the TC48-D182A and TC45-D182A mutants but not the wild-type TC48 or TC45 in response to insulin

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276956	Tyr1189	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
30230471	In keeping with the overall improvement in insulin sensitivity we found that insulin-induced IR Y1162/Y1163 tyrosine phosphorylation and activation and downstream PI3K/AKT signaling in the liver (as monitored by AKT Ser-473 phosphorylation) were dramatically enhanced by POMC TCPTP deficiency (Figure 4h).\|This would suggest that TCPTP deletion, or decreased TCPTP in POMC neurons in response to feeding, represses HGP by enhancing IR signaling and permitting POMC neurons to be activated by insulin.

Identifier	Residue	Sequence	Organism
SIGNOR-276957	Tyr1190	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
30230471	In keeping with the overall improvement in insulin sensitivity we found that insulin-induced IR Y1162/Y1163 tyrosine phosphorylation and activation and downstream PI3K/AKT signaling in the liver (as monitored by AKT Ser-473 phosphorylation) were dramatically enhanced by POMC TCPTP deficiency (Figure 4h).\|This would suggest that TCPTP deletion, or decreased TCPTP in POMC neurons in response to feeding, represses HGP by enhancing IR signaling and permitting POMC neurons to be activated by insulin.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236752	Tyr1229	SSEDLSAyASISFQK	Cricetulus griseus	CHO Cell
pmid	sentence
7651388	Therefore, during insulin stimulation irs-1 undergoes tyrosine phosphorylation, and a portion of tyrosine phosphorylated irs-1 associated with the insulin receptor. The insulin receptor substrate-1 (irs-1) is rapidly phosphorylated on several tyrosine residues by the activated insulin receptor. Insulin signals are mediated through tyrosine phosphorylation of specific proteins such as insulin receptor substrate 1 (irs-1) and shc by the activated insulin receptor (ir).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235983	Tyr1229	SSEDLSAyASISFQK	Homo sapiens	Adipocyte
pmid	sentence
12220227	Here we show that stimulation by insulin of freshly isolated primary adipocytes resulted in the expected rapid tyrosine phosphorylation of the insulin receptor, IRS-1 and IRS-3. Inhibition of PI 3-kinase enhanced the insulin-stimulated phosphorylation of IRS-1 on (i) Tyr(612) and Tyr(941) (p85 binding sites), concomitant with an increased association of the p85 subunit of PI 3-kinase; (ii) Tyr(896) (a Grb2 binding site); and (iii) Tyr(1229) (an SHP-2 binding site), although little or no binding of SHP-2 to IRS-1 was detectable under any conditions.

Identifier	Residue	Sequence	Organism
SIGNOR-236713	Tyr465	GEEELSNyICMGGKG	Rattus norvegicus
pmid	sentence
7651388	All known IRS proteins contain multiple YXXM motifs that upon phosphorylation by activated insulin receptors A previous study using phosphopeptides suggested that tyrosine-phosphorylated YXXM motifs at positions 608 and 939 in rat IRS-1 bind with high affinity to SH2 domains of p85, and motifs at positions 460 and 987 bind with lower affinity (10).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236756	Tyr612	TLHTDDGyMPMSPGV	Cricetulus griseus	CHO Cell
pmid	sentence
7651388	Therefore, during insulin stimulation irs-1 undergoes tyrosine phosphorylation, and a portion of tyrosine phosphorylated irs-1 associated with the insulin receptor. The insulin receptor substrate-1 (irs-1) is rapidly phosphorylated on several tyrosine residues by the activated insulin receptor. Insulin signals are mediated through tyrosine phosphorylation of specific proteins such as insulin receptor substrate 1 (irs-1) and shc by the activated insulin receptor (ir).

Identifier	Residue	Sequence	Organism
SIGNOR-235971	Tyr612	TLHTDDGyMPMSPGV	Rattus norvegicus
pmid	sentence
11416002	All known IRS proteins contain multiple YXXM motifs that upon phosphorylation by activated insulin re- ceptors Tyr(612) and Tyr(632) in human insulin receptor substrate-1 are important for full activation of insulin-stimulated phosphatidylinositol 3-kinase activity and translocation of GLUT4 in adipose cells

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236741	Tyr632	GRKGSGDyMPMSPKS	Cricetulus griseus	CHO Cell
pmid	sentence
7651388	Therefore, during insulin stimulation irs-1 undergoes tyrosine phosphorylation, and a portion of tyrosine phosphorylated irs-1 associated with the insulin receptor. The insulin receptor substrate-1 (irs-1) is rapidly phosphorylated on several tyrosine residues by the activated insulin receptor. Insulin signals are mediated through tyrosine phosphorylation of specific proteins such as insulin receptor substrate 1 (irs-1) and shc by the activated insulin receptor (ir).

Identifier	Residue	Sequence	Organism
SIGNOR-236709	Tyr632	GRKGSGDyMPMSPKS	Rattus norvegicus
pmid	sentence
11416002	All known IRS proteins contain multiple YXXM motifs that upon phosphorylation by activated insulin re- ceptors Tyr(612) and Tyr(632) in human insulin receptor substrate-1 are important for full activation of insulin-stimulated phosphatidylinositol 3-kinase activity and translocation of GLUT4 in adipose cells

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236745	Tyr896	EPKSPGEyVNIEFGS	Cricetulus griseus	CHO Cell
pmid	sentence
7651388	Therefore, during insulin stimulation irs-1 undergoes tyrosine phosphorylation, and a portion of tyrosine phosphorylated irs-1 associated with the insulin receptor. The insulin receptor substrate-1 (irs-1) is rapidly phosphorylated on several tyrosine residues by the activated insulin receptor. Insulin signals are mediated through tyrosine phosphorylation of specific proteins such as insulin receptor substrate 1 (irs-1) and shc by the activated insulin receptor (ir).

Identifier	Residue	Sequence	Organism
SIGNOR-236725	Tyr896	EPKSPGEyVNIEFGS	Homo sapiens
pmid	sentence
12220227	Here we show that stimulation by insulin of freshly isolated primary adipocytes resulted in the expected rapid tyrosine phosphorylation of the insulin receptor, IRS-1 and IRS-3. Inhibition of PI 3-kinase enhanced the insulin-stimulated phosphorylation of IRS-1 on (i) Tyr(612) and Tyr(941) (p85 binding sites), concomitant with an increased association of the p85 subunit of PI 3-kinase; (ii) Tyr(896) (a Grb2 binding site); and (iii) Tyr(1229) (an SHP-2 binding site), although little or no binding of SHP-2 to IRS-1 was detectable under any conditions.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235975	Tyr941	EETGTEEyMKMDLGP	Rattus norvegicus	Adipocyte
pmid	sentence
7651388	All known IRS proteins contain multiple YXXM motifs that upon phosphorylation by activated insulin receptors A previous study using phosphopeptides suggested that tyrosine-phosphorylated YXXM motifs at positions 608 and 939 in rat IRS-1 bind with high affinity to SH2 domains of p85, and motifs at positions 460 and 987 bind with lower affinity (10).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235979	Tyr989	VPSSRGDyMTMQMSC	Rattus norvegicus	Adipocyte
pmid	sentence
7651388	All known IRS proteins contain multiple YXXM motifs that upon phosphorylation by activated insulin receptors A previous study using phosphopeptides suggested that tyrosine-phosphorylated YXXM motifs at positions 608 and 939 in rat IRS-1 bind with high affinity to SH2 domains of p85, and motifs at positions 460 and 987 bind with lower affinity (10).

Publications:

11

Organism:

Cricetulus Griseus, Homo Sapiens, Rattus Norvegicus

Pathways:

Adipogenesis, AMPK Signaling, Insulin Signaling, Luminal Breast Cancer, Leptin Signaling, mTOR in cancer, MTOR Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251299	Tyr132	CVIAVDRyFAITSPF	Cricetulus griseus	CHO Cell
pmid	sentence
8557631	Insulin (10 nM)-stimulated rIR-catalyzed phosphorylation of β2-adrenergic receptor peptides was found prominently in peptides L339 (Tyr350 and Tyr354), T362 (Tyr364), and to a lesser extent peptides Y132 (Tyr132 and Tyr141), and I135 (Tyr141). G-protein-linked receptors and intrinsic tyrosine-kinase growth receptors represent two prominent modalities in cell signaling. Cross-regulation among members of both receptor superfamilies has been reported, including the counter-regulatory effects of insulin on β-adrenergic catecholamine action. Cells stimulated by insulin show loss of function and increased phosphotyrosine content of β2-adrenergic receptors.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251300	Tyr141	AITSPFKyQSLLTKN	Cricetulus griseus	CHO Cell
pmid	sentence
8557631	Insulin (10 nM)-stimulated rIR-catalyzed phosphorylation of β2-adrenergic receptor peptides was found prominently in peptides L339 (Tyr350 and Tyr354), T362 (Tyr364), and to a lesser extent peptides Y132 (Tyr132 and Tyr141), and I135 (Tyr141). G-protein-linked receptors and intrinsic tyrosine-kinase growth receptors represent two prominent modalities in cell signaling. Cross-regulation among members of both receptor superfamilies has been reported, including the counter-regulatory effects of insulin on β-adrenergic catecholamine action. Cells stimulated by insulin show loss of function and increased phosphotyrosine content of β2-adrenergic receptors.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251301	Tyr350	RRSSLKAyGNGYSSN	Cricetulus griseus	CHO Cell
pmid	sentence
8557631	Insulin (10 nM)-stimulated rIR-catalyzed phosphorylation of β2-adrenergic receptor peptides was found prominently in peptides L339 (Tyr350 and Tyr354), T362 (Tyr364), and to a lesser extent peptides Y132 (Tyr132 and Tyr141), and I135 (Tyr141). G-protein-linked receptors and intrinsic tyrosine-kinase growth receptors represent two prominent modalities in cell signaling. Cross-regulation among members of both receptor superfamilies has been reported, including the counter-regulatory effects of insulin on β-adrenergic catecholamine action. Cells stimulated by insulin show loss of function and increased phosphotyrosine content of β2-adrenergic receptors.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251302	Tyr354	LKAYGNGySSNGNTG	Cricetulus griseus	CHO Cell
pmid	sentence
8557631	Insulin (10 nM)-stimulated rIR-catalyzed phosphorylation of β2-adrenergic receptor peptides was found prominently in peptides L339 (Tyr350 and Tyr354), T362 (Tyr364), and to a lesser extent peptides Y132 (Tyr132 and Tyr141), and I135 (Tyr141). G-protein-linked receptors and intrinsic tyrosine-kinase growth receptors represent two prominent modalities in cell signaling. Cross-regulation among members of both receptor superfamilies has been reported, including the counter-regulatory effects of insulin on β-adrenergic catecholamine action. Cells stimulated by insulin show loss of function and increased phosphotyrosine content of β2-adrenergic receptors.

Publications:

4

Organism:

Cricetulus Griseus

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-276471	Tyr174	TIPSQRRyVYYYSYL	in vitro
pmid	sentence
23995781	Our results show that the kinase region of IRβ subunit physically binds to PTEN and phosphorylates on Y27 and Y174. In the current study, we discovered that IR also downregulates PTEN through tyrosine phosphorylation and suggest that Y27 and 174 are the two key tyrosines.

Identifier	Residue	Sequence	Organism
SIGNOR-276470	Tyr27	GFDLDLTyIYPNIIA	in vitro
pmid	sentence
23995781	Our results show that the kinase region of IRβ subunit physically binds to PTEN and phosphorylates on Y27 and Y174. In the current study, we discovered that IR also downregulates PTEN through tyrosine phosphorylation and suggest that Y27 and 174 are the two key tyrosines.

Publications:

2

Organism:

In Vitro

Pathways:

Insulin Signaling, Luminal Breast Cancer, MTOR Signaling

Identifier	Residue	Sequence
SIGNOR-275514	Tyr198	EERKEDQyMKMTVCL
pmid	sentence
15870194	Human BVR (hBVR) also reduces the hemeoxygenase activity product biliverdin to bilirubin and is directly activated by insulin receptor kinase (IRK).\|in addition to Y198 in the YMKM motif, 2 other tyrosines, Y228 in the YLSF motif and Y291 in the C-terminus of the protein, are directly phosphorylated by IRK

Identifier	Residue	Sequence
SIGNOR-275515	Tyr228	PGLKRNRyLSFHFKS
pmid	sentence
15870194	Human BVR (hBVR) also reduces the hemeoxygenase activity product biliverdin to bilirubin and is directly activated by insulin receptor kinase (IRK).\|in addition to Y198 in the YMKM motif, 2 other tyrosines, Y228 in the YLSF motif and Y291 in the C-terminus of the protein, are directly phosphorylated by IRK

Identifier	Residue	Sequence
SIGNOR-275516	Tyr291	LAEEIQKyCCSRK
pmid	sentence
15870194	Human BVR (hBVR) also reduces the hemeoxygenase activity product biliverdin to bilirubin and is directly activated by insulin receptor kinase (IRK).\|in addition to Y198 in the YMKM motif, 2 other tyrosines, Y228 in the YLSF motif and Y291 in the C-terminus of the protein, are directly phosphorylated by IRK

Publications:

3

Identifier	Residue	Sequence	Organism
SIGNOR-251309	Tyr20	SSENFDDyMKEVGVG	in vitro
pmid	sentence
1648089	Adipocyte lipid-binding protein is phosphorylated on tyrosine 19 in an insulin-stimulated fashion by the insulin receptor

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-251310	Tyr242	FFQQQMIyDSPPSRA	Mus musculus
pmid	sentence
10978177	HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin

Identifier	Residue	Sequence	Organism
SIGNOR-251311	Tyr285	TEADGELyVFNTPSG	Mus musculus
pmid	sentence
10978177	HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin

Identifier	Residue	Sequence	Organism
SIGNOR-251312	Tyr373	ASDTDSSyCIPTAGM	Mus musculus
pmid	sentence
10978177	HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin

Identifier	Residue	Sequence	Organism
SIGNOR-251313	Tyr447	SEELDENyVPMNPNS	Mus musculus
pmid	sentence
10978177	HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin

Identifier	Residue	Sequence	Organism
SIGNOR-251314	Tyr472	EPIQEANyVPMTPGT	Mus musculus
pmid	sentence
10978177	HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251315	Tyr589	SHDSEENyVPMNPNL	Mus musculus	NIH-3T3 Cell
pmid	sentence
10978177	HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251316	Tyr627	KGDKQVEyLDLDLDS	Mus musculus	NIH-3T3 Cell
pmid	sentence
10978177	HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251317	Tyr659	VADERVDyVVVDQQK	Mus musculus	NIH-3T3 Cell
pmid	sentence
10978177	HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin

Publications:

8

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-28791	Tyr341	NEDADENyFINEEDE	Homo sapiens
pmid	sentence
7542745	This pattern of 32p-tyr release unambiguously identified tyr-341 in p55pik as a major in vitro phosphorylation site.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain, Kidney

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251307	Tyr362	DPKEDPIyDEPEGLA	Cricetulus griseus	CHO Cell
pmid	sentence
11551902	Insulin receptor-mediated p62dok tyrosine phosphorylation at residues 362 and 398. p62(dok) is a direct substrate for the IR tyrosine kinase and that phosphorylation at Tyr(362) and Tyr(398) plays an essential role for p62(dok) to interact with its effectors and negatively regulate the insulin signaling pathway.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251308	Tyr398	ARVKEEGyELPYNPA	Cricetulus griseus	CHO Cell
pmid	sentence
11551902	Insulin receptor-mediated p62dok tyrosine phosphorylation at residues 362 and 398. p62(dok) is a direct substrate for the IR tyrosine kinase and that phosphorylation at Tyr(362) and Tyr(398) plays an essential role for p62(dok) to interact with its effectors and negatively regulate the insulin signaling pathway.

Publications:

2

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251320	Tyr368	STKMHGDyTLTLRKG	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
8385099	The alpha-type 85-kDa subunit of phosphatidylinositol 3-kinase is phosphorylated at tyrosines 368, 580, and 607 by the insulin receptor.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251321	Tyr580	LRKTRDQyLMWLTQK	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
8385099	The alpha-type 85-kDa subunit of phosphatidylinositol 3-kinase is phosphorylated at tyrosines 368, 580, and 607 by the insulin receptor.

Identifier	Residue	Sequence	Organism
SIGNOR-251322	Tyr607	NENTEDQySLVEDDE	Chlorocebus aethiops
pmid	sentence
8385099	The alpha-type 85-kDa subunit of phosphatidylinositol 3-kinase is phosphorylated at tyrosines 368, 580, and 607 by the insulin receptor.

Publications:

3

Organism:

Chlorocebus Aethiops

Pathways:

MTOR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-252692	Tyr368	STKMHGDyTLTLRKG	Chlorocebus aethiops
pmid	sentence
8385099	The alpha-type 85-kDa subunit of phosphatidylinositol 3-kinase is phosphorylated at tyrosines 368, 580, and 607 by the insulin receptor.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252691	Tyr580	LRKTRDQyLMWLTQK	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
8385099	The alpha-type 85-kDa subunit of phosphatidylinositol 3-kinase is phosphorylated at tyrosines 368, 580, and 607 by the insulin receptor.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252693	Tyr607	NENTEDQySLVEDDE	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
8385099	The alpha-type 85-kDa subunit of phosphatidylinositol 3-kinase is phosphorylated at tyrosines 368, 580, and 607 by the insulin receptor.

Publications:

3

Organism:

Chlorocebus Aethiops

Pathways:

FAP: Insulin-mediated adipogenesis, Leptin Signaling, mTOR in cancer

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251304	Tyr371	TQEQYELyCEMGSTF	Mus musculus	NIH-3T3 Cell
pmid	sentence
11997497	Insulin receptor phosphorylates Cbl on tyrosines 371, 700, and 774 in the presence of APS. This phosphorylation event is required for the recruitment of Crk to the CAP/Cbl complex and for the subsequent activation of GLUT4 translocation.

Identifier	Residue	Sequence	Organism
SIGNOR-251305	Tyr700	EGEEDTEyMTPSSRP	Mus musculus
pmid	sentence
11997497	Insulin receptor phosphorylates Cbl on tyrosines 371, 700, and 774 in the presence of APS. This phosphorylation event is required for the recruitment of Crk to the CAP/Cbl complex and for the subsequent activation of GLUT4 translocation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251306	Tyr774	SENEDDGyDVPKPPV	Mus musculus	NIH-3T3 Cell
pmid	sentence
11997497	Insulin receptor phosphorylates Cbl on tyrosines 371, 700, and 774 in the presence of APS. This phosphorylation event is required for the recruitment of Crk to the CAP/Cbl complex and for the subsequent activation of GLUT4 translocation.

Publications:

3

Organism:

Mus Musculus

Identifier	Residue	Sequence
SIGNOR-251325	Tyr427	ELFDDPSyVNVQNLD
pmid	sentence
11075717	Insulin predominantly phosphorylates the Shc Tyr-317 residue. Phosphorylated Shc binds to Grb2 which forms a complex with Sos guanine nucleotide exchange factor for p21ras.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-26870	Tyr536	QKGQESEyGNITYPP	Homo sapiens
pmid	sentence
7512963	Insulin stimulates the phosphorylation of tyr538 and the catalytic activity of ptp1c, a protein tyrosine phosphatase with src homology-2 domains. these results suggest that ptp1c is a target protein for the insulin receptor tyrosine kinase

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251323	Tyr576	RYMEDSTyYKASKGK	in vitro
pmid	sentence
9507031	P125(Fak) sequence comprising amino acids 568-582, which contains tyrosines 576 and 577 of the kinase domain regulatory loop, is phosphorylated by the insulin receptor. p125(Fak) phosphorylation by the receptor results in its activation.

Identifier	Residue	Sequence	Organism
SIGNOR-251324	Tyr577	YMEDSTYyKASKGKL	in vitro
pmid	sentence
9507031	P125(Fak) sequence comprising amino acids 568-582, which contains tyrosines 576 and 577 of the kinase domain regulatory loop, is phosphorylated by the insulin receptor. p125(Fak) phosphorylation by the receptor results in its activation.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-251318	Tyr628	PKVAYHPyPEDYGDI	in vitro
pmid	sentence
9195949	Tyr624 and Tyr628 are involved in the interaction between the IR and the KRLB domain of IRS-2, including tyrosine phosphorylation, and Tyr628 seems to be more important than Tyr624 in this process. the binding between the insulin receptor and the KRLB domain of IRS-2 results in tyrosine phosphorylation of the KRLB domain, and this leads to decreased binding of IRS-2 to the insulin receptor.

Identifier	Residue	Sequence	Organism
SIGNOR-251319	Tyr632	YHPYPEDyGDIEIGS	in vitro
pmid	sentence
9195949	Tyr624 and Tyr628 are involved in the interaction between the IR and the KRLB domain of IRS-2, including tyrosine phosphorylation, and Tyr628 seems to be more important than Tyr624 in this process. the binding between the insulin receptor and the KRLB domain of IRS-2 results in tyrosine phosphorylation of the KRLB domain, and this leads to decreased binding of IRS-2 to the insulin receptor.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-174065		Homo sapiens
pmid	sentence
21659604	Grb10 negatively regulates growth factor signaling. It binds the insulin and insulin-like growth factor 1 (igf-1) receptors;mice without grb10 are larger and exhibit enhanced insulin sensitivity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-216619		Homo sapiens
pmid	sentence
22207502	Ampk phosphorylates and activates theinsulinreceptor, providing a direct link between ampk and theinsulin pathway.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Pathways:

AMPK Signaling, Leptin Signaling, MTOR Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264873
pmid	sentence
24535599	Growth factor receptor-bound protein 14 (Grb14) interacts with insulin receptor (IR) through the between PH and SH2 (BPS) domain. Grb14-IR complex formation is initiated by insulin stimulation, and the binding event results in the inhibition of insulin signalling.

Publications:

1

Identifier	Residue	Organism	Cell Line
SIGNOR-260365		Homo sapiens	LoVo Cell
pmid	sentence
25527501	Here we demonstrate that the two IR isoforms are similarly cleaved by furin, but when this furin-dependent maturation is inefficient, IR proforms move to the cell surface where the proprotein convertase PACE4 selectively supports IRB maturation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-194895		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-50719		Homo sapiens
pmid	sentence
9281335	Therefore, these results provide genetic evidence that the growth-promoting function of igf-ii during mouse embryogenesis is mediated in part by signaling through the insulin receptor.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-109688		Homo sapiens
pmid	sentence
11498022	Aps couples c-cbl to theinsulinreceptor, resulting in ubiquitination of theinsulinreceptor

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-77153		Homo sapiens
pmid	sentence
10803466	Insulin induces the ir-grb7 interaction in cells expressing physiological levels of the proteins, suggesting that grb7 is implicated in insulin signaling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-236803		Homo sapiens
pmid	sentence
10909964	In skeletal muscle, insulin activates glycogen synthase by reducing phosphorylation at both NH2- and COOH-terminal sites of the enzyme and by elevating the levels of glucose-6-phosphate, an allosteric activator of glycogen synthase.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Pathways:

Insulin Signaling

Identifier	Residue	Organism
SIGNOR-195324		Homo sapiens
pmid	sentence
22207502	Ampk phosphorylates and activates theinsulinreceptor, providing a direct link between ampk and theinsulin pathway.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Organism
SIGNOR-109694		Homo sapiens
pmid	sentence
11498022	APS couples c-Cbl to the insulin receptor, resulting in ubiquitination of the insulin receptor.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Ovary

Identifier	Residue	Organism
SIGNOR-280045		Homo sapiens
pmid	sentence
26584640	Both recombinant mTOR and immunoprecipitated mTORC2 phosphorylate IGF-IR and InsR on Tyr1131/1136 and Tyr1146/1151, respectively.\|Here we show that mTOR possesses unexpected tyrosine kinase activity and activates IGF-IR and InsR.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Leptin Signaling, MTOR Signaling

Identifier	Residue	Organism
SIGNOR-101005		Homo sapiens
pmid	sentence
12730241	Irs5/dok4 and irs6/dok5 represent two new signaling proteins with potential roles in insulin and igf-1 action.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle, Kidney

Identifier	Residue	Organism
SIGNOR-217897		Mus musculus
pmid	sentence
25905389	The binding of insulin to the subunit of IR not only concentrates insulin at its site of action, but also induces conformational changes in the receptor, which in turn stimulates the tyrosine kinase activity intrinsic to the _ subunit of the IR and triggers the signaling cascades (Fig. 3). Insulin receptors trans phosphorylate several immediate substrates (on Tyr residues) including IRS1-4, Shc, and Gab 1, Cbl, APS, and P60dok.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-23001		Homo sapiens
pmid	sentence
2550426	Our previous studies indicated that amino acid residues 240-250 in the cysteine-rich region of the human insulin receptor alpha-subunit constitute a site in which insulin binds.

Identifier	Residue	Organism
SIGNOR-236748		Cricetulus griseus
pmid	sentence
16956584	Insulin binds to the alpha subunit of the insulin receptor (IR) on the cell surface.

Publications:

2

Organism:

Homo Sapiens, Cricetulus Griseus

Pathways:

Adipogenesis, AMPK Signaling, FAP: Insulin-mediated adipogenesis, Insulin Signaling, Luminal Breast Cancer, Leptin Signaling, mTOR in cancer, MTOR Signaling

Identifier	Residue	Organism
SIGNOR-101038		Homo sapiens
pmid	sentence
12730241	Irs5/dok4 and irs6/dok5 represent two new signaling proteins with potential roles in insulin and igf-1 action

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle, Kidney

Identifier	Residue	Organism
SIGNOR-190458		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-192883		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-278819		Homo sapiens
pmid	sentence
27577745	MARCH1 ubiquitinates INSR to decrease cell surface INSR levels, but unlike other INSR ubiquitin ligases, MARCH1 acts in the basal state rather than after insulin stimulation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-260366		Homo sapiens	LoVo Cell
pmid	sentence
25527501	Here we demonstrate that the two IR isoforms are similarly cleaved by furin, but when this furin-dependent maturation is inefficient, IR proforms move to the cell surface where the proprotein convertase PACE4 selectively supports IRB maturation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-84251		Homo sapiens
pmid	sentence
11075717	The npxy motif around 960-tyr residue of the insulin receptor binds to the n-terminal ptb domain of shc.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-253604		Chlorocebus aethiops
pmid	sentence
7629118	Tyrosine phosphorylation of insulin receptor substrate-1 in vivo depends upon the presence of its pleckstrin homology region.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Organism
SIGNOR-252190		Homo sapiens
pmid	sentence
10615944	Plasma cell membrane glycoprotein-1 (PC-1) inhibits insulin receptor (IR) tyrosine kinase activity and subsequent cellular signaling. PC-1 may inhibit the IR by interacting directly with a specific region in the IR alpha-subunit.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-262029		Mus musculus
pmid	sentence
24712877	Effects of the antitumor drug OSI-906, a dual inhibitor of IGF-1 receptor and insulin receptor, on the glycemic control, β-cell functions, and β-cell proliferation in male mice

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-190446		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-192871		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-278945		Homo sapiens
pmid	sentence
10650943	We found that insulin receptor can directly phosphorylate FRS2.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Luminal Breast Cancer

Identifier	Residue	Organism	Cell Line
SIGNOR-262026		Homo sapiens	Rhabdomyosarcoma Cell
pmid	sentence
19996272	BMS-754807, a small molecule inhibitor of insulin-like growth factor-1R/IR

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-278946		Homo sapiens
pmid	sentence
11604231	Thus, Tyr phosphorylation of Sam68 by IR could modulate its association with the splicing machinery in a similar way to that described for p59 fyn, and this way, it could influence splice site selection.

Publications:

1

Organism:

Homo Sapiens

Name	INSR View Modifications
Full Name	Insulin receptor
Synonyms	IR
Primary ID	P06213
Links	- -
Type	protein
Relations	163
Pathways	Adipogenesis, AMPK Signaling, FAP: In vitro induction of adipogenesis, FAP: Insulin-mediated adipogenesis, FAP: INSR, GLP-1 and GIP receptor signaling in PDAC, Insulin Signaling, Luminal Breast Cancer, Leptin Signaling, mTOR in cancer, MTOR Signaling, Pericyte: In vitro induction of adipogenesis
Inhibitors	NVP-AEW541; BMS-554417; N-(2,6-difluorophenyl)-5-[3-[2-[5-ethyl-2-methoxy-4-[4-(4-methylsulfonyl-1-piperazinyl)-1-piperidinyl]anilino]-4-pyrimidinyl]-2-imidazo[1,2-a]pyridinyl]-2-methoxybenzamide; Linsitinib; 4-[[(2S)-2-(3-chlorophenyl)-2-hydroxyethyl]amino]-3-[4-methyl-6-(4-morpholinyl)-1,3-dihydrobenzimidazol-2-ylidene]-2-pyridinone; 2-[[2-[[1-[2-(dimethylamino)-1-oxoethyl]-5-methoxy-2,3-dihydroindol-6-yl]amino]-7H-pyrrolo[2,3-d]pyrimidin-4-yl]amino]-6-fluoro-N-methylbenzamide; BMS-754807
Function	Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosine residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways

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