PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33727228-9 2021 Decreased tyrosine phosphorylation of key sites in the phosphatase SHP2 suggests its inhibition, resulting in subsequent inhibition of RAS/MAPK and activation of PI3K/AKT pathways. Tyrosine 10-18 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 67-71 33732417-5 2021 By Co-immunoprecipitation (Co-IP) and in vitro dephosphorylation assays, we identified that Shp2 negatively controlled sEV biogenesis by directly dephosphorylating tyrosine 46 of Syntenin, which has been reported as a molecular switch in sEV biogenesis. Tyrosine 164-172 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 92-96 33582386-2 2021 SHP2 protein is a non-receptor tyrosine phosphatase encoded by PTPN11 gene, and it is widely expressed in various tissues and cells. Tyrosine 31-39 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 33582386-2 2021 SHP2 protein is a non-receptor tyrosine phosphatase encoded by PTPN11 gene, and it is widely expressed in various tissues and cells. Tyrosine 31-39 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 63-69 33562835-0 2021 Polyphyllin D Shows Anticancer Effect through a Selective Inhibition of Src Homology Region 2-Containing Protein Tyrosine Phosphatase-2 (SHP2). Tyrosine 113-121 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 137-141 33113413-1 2020 PTPN11 (coding the gene of SHP2), a classic non-receptor protein tyrosine phosphatase, is implicated in multiple cell signaling pathway. Tyrosine 65-73 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-6 33413561-14 2021 SHP2 enhanced Ras activation by dephosphorylating its inhibitory tyrosine 32, thus triggering the MAPK cascade. Tyrosine 65-73 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 33113413-1 2020 PTPN11 (coding the gene of SHP2), a classic non-receptor protein tyrosine phosphatase, is implicated in multiple cell signaling pathway. Tyrosine 65-73 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 27-31 32391629-6 2020 Mechanistically, MB blocks interaction between Y248-phosphorylated immunoreceptor tyrosine-based switch motif (ITSM) of human PD-1 and SHP2. Tyrosine 82-90 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 135-139 33002410-1 2020 The non-receptor protein tyrosine phosphatase (PTP) SHP2, encoded by PTPN11, plays an essential role in RAS-mitogen-activated protein kinase (MAPK) signaling during normal development. Tyrosine 25-33 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 52-56 33002410-1 2020 The non-receptor protein tyrosine phosphatase (PTP) SHP2, encoded by PTPN11, plays an essential role in RAS-mitogen-activated protein kinase (MAPK) signaling during normal development. Tyrosine 25-33 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 69-75 32545165-2 2020 SHP2 is a protein phosphatase that binds, through its two SH2 domains, specific consensus sequences presenting a phosphorylated tyrosine located on the disordered tail of Gab2. Tyrosine 128-136 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 32765928-3 2020 The most frequently reported mutations in LS patients are in the protein tyrosine phosphatase nonreceptor type 11 gene, PTPN11 . Tyrosine 73-81 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 120-126 32910655-1 2020 SHP2 is a nonreceptor protein tyrosine phosphatase encoded by the PTPN11 gene and is involved in cell growth and differentiation via the MAPK signaling pathway. Tyrosine 30-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 32910655-1 2020 SHP2 is a nonreceptor protein tyrosine phosphatase encoded by the PTPN11 gene and is involved in cell growth and differentiation via the MAPK signaling pathway. Tyrosine 30-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 66-72 32921395-1 2020 SHP2 is a non-receptor protein tyrosine phosphatase encoded by the PTPN11 gene in human. Tyrosine 31-39 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 32921395-1 2020 SHP2 is a non-receptor protein tyrosine phosphatase encoded by the PTPN11 gene in human. Tyrosine 31-39 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 67-73 32460492-1 2020 SHP2 (Src homology-2 domain-containing protein tyrosine phosphatase-2) is a non-receptor protein tyrosine phosphatase that removes tyrosine phosphorylation. Tyrosine 47-55 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 32460492-1 2020 SHP2 (Src homology-2 domain-containing protein tyrosine phosphatase-2) is a non-receptor protein tyrosine phosphatase that removes tyrosine phosphorylation. Tyrosine 97-105 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 32460492-1 2020 SHP2 (Src homology-2 domain-containing protein tyrosine phosphatase-2) is a non-receptor protein tyrosine phosphatase that removes tyrosine phosphorylation. Tyrosine 97-105 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 6-69 32236803-0 2020 1H, 13C, 15N chemical shift assignments of SHP2 SH2 domains in complex with PD-1 immune-tyrosine motifs. Tyrosine 88-96 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 43-47 32236803-4 2020 Activation of PD-1 leads to phosphorylation of two signaling motifs located in its cytoplasmic domain, the immune tyrosine inhibitory motif (ITIM) and immune tyrosine switch motif (ITSM), which recruit and activate protein tyrosine phosphatase SHP2. Tyrosine 114-122 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 244-248 32236803-4 2020 Activation of PD-1 leads to phosphorylation of two signaling motifs located in its cytoplasmic domain, the immune tyrosine inhibitory motif (ITIM) and immune tyrosine switch motif (ITSM), which recruit and activate protein tyrosine phosphatase SHP2. Tyrosine 158-166 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 244-248 32061959-1 2020 Src homology 2 (SH2)-containing protein tyrosine phosphatase 2 (SHP2), encoded by PTPN11, regulates cell proliferation, differentiation, apoptosis and survival via releasing intramolecular autoinhibition and modulating various signaling pathways, such as mitogen-activated protein kinase (MAPK) pathway. Tyrosine 40-48 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 64-68 32467571-0 2020 Loss of tyrosine phosphatase SHP2 activity promotes growth of colorectal carcinoma HCT-116 cells. Tyrosine 8-16 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 29-33 32363035-0 2020 SHP2-Independent Tyrosine Dephosphorylation of Cortactin and Vinculin during Infection with Helicobacter pylori. Tyrosine 17-25 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 32061959-1 2020 Src homology 2 (SH2)-containing protein tyrosine phosphatase 2 (SHP2), encoded by PTPN11, regulates cell proliferation, differentiation, apoptosis and survival via releasing intramolecular autoinhibition and modulating various signaling pathways, such as mitogen-activated protein kinase (MAPK) pathway. Tyrosine 40-48 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 82-88 31954180-2 2020 The Src-homology 2 domain-containing phosphatase 2 (SHP2), encoded by PTPN11, has been reported oncogenic tyrosine phosphatase associated with various tumors and played critical roles in many cell signaling events. Tyrosine 106-114 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 52-56 32024694-7 2020 A phosphorylated form of this peptide inhibits SHP2 activity in vitro and EGFR and HER2 signaling in cells, suggesting inhibition of SHP2 protein tyrosine phosphatase activity by this peptide. Tyrosine 146-154 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 47-51 32024694-7 2020 A phosphorylated form of this peptide inhibits SHP2 activity in vitro and EGFR and HER2 signaling in cells, suggesting inhibition of SHP2 protein tyrosine phosphatase activity by this peptide. Tyrosine 146-154 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 133-137 31954180-2 2020 The Src-homology 2 domain-containing phosphatase 2 (SHP2), encoded by PTPN11, has been reported oncogenic tyrosine phosphatase associated with various tumors and played critical roles in many cell signaling events. Tyrosine 106-114 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 70-76 30573803-6 2019 This suggests that this missense change not only weakens tyrosine kinase autoinhibition, but also influences substrate binding, as both PTPN11 tyrosines (Tyr542 and Tyr580) usually are phosphorylated upon PDGFR activation. Tyrosine 143-152 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 136-142 31953320-1 2020 The non-receptor protein tyrosine phosphatase (PTP) SHP2 is encoded by the proto-oncogene PTPN11 and is a ubiquitously expressed key regulator of cell signaling, acting on a number of cellular processes and components, including the Ras/Raf/Erk, PI3K/Akt, and JAK/STAT pathways and immune check point receptors. Tyrosine 25-33 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 52-56 31953320-1 2020 The non-receptor protein tyrosine phosphatase (PTP) SHP2 is encoded by the proto-oncogene PTPN11 and is a ubiquitously expressed key regulator of cell signaling, acting on a number of cellular processes and components, including the Ras/Raf/Erk, PI3K/Akt, and JAK/STAT pathways and immune check point receptors. Tyrosine 25-33 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 90-96 31838080-1 2020 Src homology-2-containing protein tyrosine phosphatase 2 (SHP2) is a major phosphatase involved in several cellular processes. Tyrosine 34-42 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 58-62 31784318-1 2020 SHP2, a non-receptor protein tyrosine phosphatase encoded by PTPN11 gene, plays an important role in the cell growth and proliferation. Tyrosine 29-37 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 31784318-1 2020 SHP2, a non-receptor protein tyrosine phosphatase encoded by PTPN11 gene, plays an important role in the cell growth and proliferation. Tyrosine 29-37 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 61-67 31562133-1 2019 SHP2, encoded by the PTPN11 gene, is a ubiquitous protein tyrosine phosphatase that is a critical regulator of signal transduction. Tyrosine 58-66 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 31562133-1 2019 SHP2, encoded by the PTPN11 gene, is a ubiquitous protein tyrosine phosphatase that is a critical regulator of signal transduction. Tyrosine 58-66 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 21-27 31373232-4 2019 Notably, SHP2 activation was found in KRAS-mutant NSCLC cells with TKIs treatment, as judged by the increase of tyrosine 542 phosphorylation (pSHP2 Y542), which activates the RAS/MEK/ERK pathway. Tyrosine 112-120 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 9-13 31184863-3 2019 Upon FGFR activation, FRS2alpha undergoes phosphorylation on multiple tyrosines, triggering recruitment of the adaptor Grb2 and the tyrosine phosphatase Shp2, resulting in stimulation of PI3K/AKT and MAPK signaling pathways. Tyrosine 70-79 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 153-157 31978797-3 2020 In this experiment, protein tyrosine phosphatase 2 (Shp2), which was encoded by the PTPN11 gene, was highly expressed in BMSCs of the newly diagnosed and the recurrent B-ALL patients. Tyrosine 28-36 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 52-56 31978797-3 2020 In this experiment, protein tyrosine phosphatase 2 (Shp2), which was encoded by the PTPN11 gene, was highly expressed in BMSCs of the newly diagnosed and the recurrent B-ALL patients. Tyrosine 28-36 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 84-90 32076487-1 2020 SHP2 mediates RAS activation downstream of multiple receptor tyrosine kinases (RTKs) and cancer cell lines dependent on RTKs are in general dependent on SHP2. Tyrosine 61-69 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 31561841-2 2020 Two such important Non-Receptor protein tyrosine phosphatases, SHP-1 and SHP-2, have been found to be expressed in immune cells and reported to be key regulators of immune cell development, functions, and differentiation by modulating the duration and amplitude of the downstream cascade transduced via receptors. Tyrosine 40-48 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 73-78 31807022-1 2019 Purpose: The aim of this study was to investigate the effects of gain-of-function (GOF) E76K-mutant Src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2) on the biological behaviors of glioblastoma (GBM) cells, and explore the molecular mechanisms of GBM progression. Tyrosine 141-149 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 165-169 30696956-3 2019 The protein tyrosine phosphatase SHP2 counteracted the Src effects on VIF tyrosine phosphorylation and organization. Tyrosine 12-20 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 33-37 30129165-8 2018 The results indicated that the primary variances between SHP2-WT and SHP2-E76K were the different interactions between Glu/Lys 76 and Arg 265, Tyr 80 and Leu 77, Leu 77 and Tyr 81, Thr 73 and Glu 258, Ala 75 and Cys 259, Phe 71 and Tyr 81, Ala 75 and Glu 258, and Tyr 73 and Glu/Lys 76. Tyrosine 143-146 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 57-61 30688462-1 2019 SHP2 is a nonreceptor protein tyrosine phosphatase within the mitogen-activated protein kinase (MAPK) pathway controlling cell growth, differentiation, and oncogenic transformation. Tyrosine 30-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 30047735-3 2018 SHP2 binds to Gab2 through its SH2 domains, which recognize specific regions of Gab2 characterized by the presence of a phosphorylated tyrosine. Tyrosine 135-143 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 30129165-8 2018 The results indicated that the primary variances between SHP2-WT and SHP2-E76K were the different interactions between Glu/Lys 76 and Arg 265, Tyr 80 and Leu 77, Leu 77 and Tyr 81, Thr 73 and Glu 258, Ala 75 and Cys 259, Phe 71 and Tyr 81, Ala 75 and Glu 258, and Tyr 73 and Glu/Lys 76. Tyrosine 173-176 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 57-61 30129165-8 2018 The results indicated that the primary variances between SHP2-WT and SHP2-E76K were the different interactions between Glu/Lys 76 and Arg 265, Tyr 80 and Leu 77, Leu 77 and Tyr 81, Thr 73 and Glu 258, Ala 75 and Cys 259, Phe 71 and Tyr 81, Ala 75 and Glu 258, and Tyr 73 and Glu/Lys 76. Tyrosine 173-176 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 69-73 30129165-8 2018 The results indicated that the primary variances between SHP2-WT and SHP2-E76K were the different interactions between Glu/Lys 76 and Arg 265, Tyr 80 and Leu 77, Leu 77 and Tyr 81, Thr 73 and Glu 258, Ala 75 and Cys 259, Phe 71 and Tyr 81, Ala 75 and Glu 258, and Tyr 73 and Glu/Lys 76. Tyrosine 173-176 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 57-61 30129165-8 2018 The results indicated that the primary variances between SHP2-WT and SHP2-E76K were the different interactions between Glu/Lys 76 and Arg 265, Tyr 80 and Leu 77, Leu 77 and Tyr 81, Thr 73 and Glu 258, Ala 75 and Cys 259, Phe 71 and Tyr 81, Ala 75 and Glu 258, and Tyr 73 and Glu/Lys 76. Tyrosine 173-176 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 69-73 30129165-8 2018 The results indicated that the primary variances between SHP2-WT and SHP2-E76K were the different interactions between Glu/Lys 76 and Arg 265, Tyr 80 and Leu 77, Leu 77 and Tyr 81, Thr 73 and Glu 258, Ala 75 and Cys 259, Phe 71 and Tyr 81, Ala 75 and Glu 258, and Tyr 73 and Glu/Lys 76. Tyrosine 143-146 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 69-73 30129165-8 2018 The results indicated that the primary variances between SHP2-WT and SHP2-E76K were the different interactions between Glu/Lys 76 and Arg 265, Tyr 80 and Leu 77, Leu 77 and Tyr 81, Thr 73 and Glu 258, Ala 75 and Cys 259, Phe 71 and Tyr 81, Ala 75 and Glu 258, and Tyr 73 and Glu/Lys 76. Tyrosine 173-176 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 57-61 30129165-8 2018 The results indicated that the primary variances between SHP2-WT and SHP2-E76K were the different interactions between Glu/Lys 76 and Arg 265, Tyr 80 and Leu 77, Leu 77 and Tyr 81, Thr 73 and Glu 258, Ala 75 and Cys 259, Phe 71 and Tyr 81, Ala 75 and Glu 258, and Tyr 73 and Glu/Lys 76. Tyrosine 173-176 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 69-73 30374120-2 2018 Upon delivery into gastric epithelial cells via type IV secretion, the cagA-encoded CagA interacts with and thereby perturbs the pro-oncogenic phosphatase SHP2 and the polarity-regulating kinase PAR1b via the tyrosine-phosphorylated EPIYA-C/D segment and the CM sequence, respectively. Tyrosine 209-217 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 155-159 28768764-6 2017 In this regard, we report that phosphorylation of Shp2 at tyrosine 542 and its translocation to the postsynaptic compartment are integral processes in synaptic scaling. Tyrosine 58-66 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 50-54 29408202-3 2018 In addition, we found that H2O2-mediated SHP2 inhibition leads to tyrosine phosphorylation and inactivation of PP2A by LPS, which in turn, accounts for increased NFkappaB activation and ICAM1 and VCAM1 expression facilitating EC-monocyte interactions and all these LPS-mediated responses were reduced by RvD1. Tyrosine 66-74 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 41-45 29282323-9 2018 Mechanistically, SAP opposed PD-1 function by acting as a molecular shield of key tyrosine residues that are targets for the tyrosine phosphatase SHP2, which mediates PD-1 inhibitory properties. Tyrosine 82-90 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 146-150 28804122-6 2018 SHP2, and specifically, its SH2 domains, PTP activity and C-terminal tyrosines, are essential for BCR-ABL1+, but not WT, pre-B-cell proliferation. Tyrosine 69-78 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 30333625-5 2018 Here we use mouse models and human cells to show that LILRB4, an immunoreceptor tyrosine-based inhibition motif-containing receptor and a marker of monocytic leukaemia, supports tumour cell infiltration into tissues and suppresses T cell activity via a signalling pathway that involves APOE, LILRB4, SHP-2, uPAR and ARG1 in acute myeloid leukaemia (AML) cells. Tyrosine 80-88 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 300-305 30018082-3 2018 We investigated the signaling upstream of PTPN11 in JMML and AML cells and found that PTPN11 was activated by the nonreceptor tyrosine/serine/threonine kinase TNK2 and that PTPN11-mutant JMML and AML cells were sensitive to TNK2 inhibition. Tyrosine 126-134 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 42-48 30018082-3 2018 We investigated the signaling upstream of PTPN11 in JMML and AML cells and found that PTPN11 was activated by the nonreceptor tyrosine/serine/threonine kinase TNK2 and that PTPN11-mutant JMML and AML cells were sensitive to TNK2 inhibition. Tyrosine 126-134 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 86-92 30018082-3 2018 We investigated the signaling upstream of PTPN11 in JMML and AML cells and found that PTPN11 was activated by the nonreceptor tyrosine/serine/threonine kinase TNK2 and that PTPN11-mutant JMML and AML cells were sensitive to TNK2 inhibition. Tyrosine 126-134 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 86-92 30227954-2 2018 Here we report that the YAP/TAZ activities are stimulated upon complex formation with Parafibromin, which undergoes tyrosine phosphorylation and dephosphorylation by kinases such as PTK6 and phosphatases such as SHP2, respectively. Tyrosine 116-124 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 212-216 28208810-10 2017 Moreover, by using Shp2 phosphatase mutants, phosphor-tyrosine mimicking, and deficiency mutants, we provided evidence that the phosphatase activity of Shp2 and its tyrosine phosphorylation, are necessary for the IL-6-induced downregulation of E-cadherin and the phosphorylation of Erk1/2. Tyrosine 54-62 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 152-156 28332308-2 2017 The immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing isoforms of this molecule which possess a long cytoplasmic tail (CEACAM1-L) generally play inhibitory roles in cell function by interacting with Src homology 2 domain-containing tyrosine phosphatase (SHP)-1 and/or SHP-2. Tyrosine 19-27 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 283-288 28883531-3 2017 A prototype that can detect tyrosine phosphorylation and immediately activate auto-inhibited Shp2 phosphatase, Shp2-iSNAP, is designed through modular assembly. Tyrosine 28-36 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 93-97 28883531-3 2017 A prototype that can detect tyrosine phosphorylation and immediately activate auto-inhibited Shp2 phosphatase, Shp2-iSNAP, is designed through modular assembly. Tyrosine 28-36 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 111-115 28209599-6 2017 Similarly, Western blot studies showed increased tyrosine phosphorylation of (p-tyrosine) SHP2, indicative of its activation. Tyrosine 49-57 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 90-94 28209599-6 2017 Similarly, Western blot studies showed increased tyrosine phosphorylation of (p-tyrosine) SHP2, indicative of its activation. Tyrosine 77-88 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 90-94 28209599-10 2017 In the cells overexpressing constitutively active SHP2, SERT polypeptide showed complete loss of p-tyrosine. Tyrosine 97-107 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 50-54 28208810-10 2017 Moreover, by using Shp2 phosphatase mutants, phosphor-tyrosine mimicking, and deficiency mutants, we provided evidence that the phosphatase activity of Shp2 and its tyrosine phosphorylation, are necessary for the IL-6-induced downregulation of E-cadherin and the phosphorylation of Erk1/2. Tyrosine 165-173 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 19-23 28208810-10 2017 Moreover, by using Shp2 phosphatase mutants, phosphor-tyrosine mimicking, and deficiency mutants, we provided evidence that the phosphatase activity of Shp2 and its tyrosine phosphorylation, are necessary for the IL-6-induced downregulation of E-cadherin and the phosphorylation of Erk1/2. Tyrosine 165-173 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 152-156 27530552-7 2016 This event led to tyrosine phosphorylation at Tyr627 domain of GAB1 that regulated EGFR signaling by recruiting SHP2. Tyrosine 18-26 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 112-116 27696702-3 2017 However, IDO1 also harbours immunoreceptor tyrosine-based inhibitory motifs, (ITIM1 and ITIM2), that, once phosphorylated, bind protein tyrosine phosphatases, (SHP-1 and SHP-2), and thus trigger an immunoregulatory signalling in DCs. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 170-175 26316256-6 2016 By an iTRAQ based strategy coupled to mass spectrometry, we have identified 63 phosphorylated tyrosine residues in 53 different proteins whose phosphorylation is affected by SHP-2 activity. Tyrosine 94-102 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 174-179 27092521-3 2016 Here we show that NS1 can induce an efficient translocation of Crk proteins from the cytoplasm into the nucleus, which results in an altered pattern of nuclear protein tyrosine phosphorylation. Tyrosine 168-176 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 18-21 26359300-5 2015 Whereas EGF promoted SHP2 binding to tyrosine phosphorylated GAB1, which promotes SHP2 activity, TGFbeta did not induce SHP2 association with phosphotyrosine-containing proteins. Tyrosine 37-45 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 21-25 27078017-10 2016 The interaction between chondroitin 4-sulfate and SHP2 is a novel intersection between sulfation and phosphorylation, by which decline in ARSB and increased chondroitin 4-sulfation can inhibit SHP2, thereby regulating downstream tyrosine phosphorylations by sustained phosphorylations with associated activation of signaling and transcriptional events. Tyrosine 229-237 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 50-54 27078017-10 2016 The interaction between chondroitin 4-sulfate and SHP2 is a novel intersection between sulfation and phosphorylation, by which decline in ARSB and increased chondroitin 4-sulfation can inhibit SHP2, thereby regulating downstream tyrosine phosphorylations by sustained phosphorylations with associated activation of signaling and transcriptional events. Tyrosine 229-237 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 193-197 26337637-5 2016 All patients had a mutation in the protein tyrosine phosphatase catalytic domain of the PTPN11 gene; two unrelated patients had the p.Thr468Met mutation, while the family consisting of two affected individuals harboured the p.Thr279Cys mutation. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 88-94 26527736-8 2016 Phosphorylation of this tyrosine residue of TXNIP diminished the binding capability of PPxY motifs of TXNIP to Itch, whereas this phosphorylation is a prerequisite to the binding activity of TXNIP to SHP2 [SH2 (Src homology 2) domain-containing protein tyrosine phosphatase 2] and their roles in stabilizing the phosphorylation and activation of CSK (c-Src tyrosine kinase). Tyrosine 24-32 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 200-204 27572445-4 2016 Tyrosine-phosphorylated CagA binds to the pro-oncogenic protein tyrosine phosphatase SHP2 and thereby deregulates the phosphatase activity(11,12), which has been considered to play an important role in gastric carcinogenesis(13). Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 85-89 30695496-3 2016 This leads to activation of tyrosine kinase JAK2, which phosphory- lates tyrosine-containing sites located in the cytoplasmic domain of the receptor, resulting in stimulation of activity of phosphatidylinositol-3-kinase, the transcription factors STAT3 and STAT5, phosphatase SHP2, and mitogen-activated protein kinase. Tyrosine 28-36 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 276-280 26755576-8 2016 Further mechanistic analyses reveal that GOF mutant Shp2 hyperactivates the Polo-like kinase 1 (Plk1) kinase by enhancing c-Src kinase-mediated tyrosine phosphorylation of Plk1. Tyrosine 144-152 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 52-56 25531430-11 2014 Leukemia-associated, constitutively active mutants of Shp2 block cytokine-induced tyrosine phosphorylation of HoxA9 and HoxA10. Tyrosine 82-90 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 54-58 26385178-1 2015 Src homology-2 domain-containing phosphatase (SHP) 2, an oncogenic phosphatase, inhibits type II immune interferon (IFN)-gamma signaling by subverting signal transducers and activators of transcription 1 tyrosine phosphorylation and activation. Tyrosine 204-212 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 46-52 25317600-2 2015 Inhibition of the protein tyrosine phosphorylase SH2 domain-containing protein tyrosine phosphatase 2 (SHP2) increases tyrosine phosphorylation of vascular endothelial cadherin and beta-catenin, resulting in disruption of the endothelial monolayer and edema formation in the pulmonary endothelium. Tyrosine 26-34 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 103-107 25969544-3 2015 We explored how dynamics in the interactions among the epidermal growth factor (EGF) receptor (EGFR), GRB2-associated binder protein 1 (GAB1), and SH2 domain-containing phosphatase 2 (SHP2) affected EGFR signaling output, specifically SHP2 binding to tyrosine-phosphorylated GAB1, which relieves the autoinhibition of SHP2. Tyrosine 251-259 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 184-188 25805816-9 2015 We conclude that WNK4 is a substrate of SFKs and that the association of c-Src and PTP-1D with WNK4 at Tyr(1092) and Tyr(1143) plays an important role in modulating the inhibitory effect of WNK4 on ROMK. Tyrosine 103-106 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 83-89 25805816-9 2015 We conclude that WNK4 is a substrate of SFKs and that the association of c-Src and PTP-1D with WNK4 at Tyr(1092) and Tyr(1143) plays an important role in modulating the inhibitory effect of WNK4 on ROMK. Tyrosine 117-120 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 83-89 25672415-5 2015 Moreover, deletion of the N-SH2 domain of SHP-2 affected H2O2-mediated ERK phosphorylation and Src phosphorylation at Tyr 419 in primary astrocytes, suggesting that N-SH2 domain of SHP-2 is responsible for the binding of caveolin-1 and contributes to the regulation of Src phosphorylation and activation following ROS-induced oxidative stress in brain astrocytes. Tyrosine 118-121 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 42-47 23822953-7 2013 Biochemical validation showed that SHP-2 tyrosine phosphorylation is dependent on DDR2 kinase activity. Tyrosine 41-49 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 35-40 23946508-5 2013 Tyrosine-phosphorylated hnRNP Q was directly bound to SHP2 in vivo and in vitro, and dephosphorylated by SHP2 in vitro. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 54-58 23946508-5 2013 Tyrosine-phosphorylated hnRNP Q was directly bound to SHP2 in vivo and in vitro, and dephosphorylated by SHP2 in vitro. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 105-109 24632723-5 2014 In the presence of CSK siRNA, binding between caveolin-1 and SHP-2 was enhanced by H2O2 treatment, which led to reduced Src phosphorylation at tyrosine (Tyr) 530 and enhanced Src phosphorylation at Tyr 419. Tyrosine 143-151 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 61-66 24632723-5 2014 In the presence of CSK siRNA, binding between caveolin-1 and SHP-2 was enhanced by H2O2 treatment, which led to reduced Src phosphorylation at tyrosine (Tyr) 530 and enhanced Src phosphorylation at Tyr 419. Tyrosine 153-156 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 61-66 24632723-5 2014 In the presence of CSK siRNA, binding between caveolin-1 and SHP-2 was enhanced by H2O2 treatment, which led to reduced Src phosphorylation at tyrosine (Tyr) 530 and enhanced Src phosphorylation at Tyr 419. Tyrosine 198-201 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 61-66 24632723-6 2014 In contrast, siRNA targeting of SHP-2 facilitated H2O2-mediated interaction between caveolin-1 and CSK and enhanced Src phosphorylation at Tyr 530, leading to subsequent decrease in Src downstream signaling, such as focal adhesion kinase (FAK) and extracellular signal-related kinase (ERK). Tyrosine 139-142 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 32-37 23822953-8 2013 Targeted proteomic profiling of a panel of lung SCC (squamous cell carcinoma) DDR2 mutants demonstrated that SHP-2 is tyrosine-phosphorylated by the L63V and G505S mutants. Tyrosine 118-126 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 109-114 23822953-9 2013 In contrast, the I638F kinase domain mutant exhibited diminished DDR2 and SHP-2 tyrosine phosphorylation levels which have an inverse relationship with clonogenic potential. Tyrosine 80-88 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 74-79 23612964-3 2013 Using dominant negative GAB1 mutants lacking canonical tyrosine residues for SHP2 and PI3K interactions or lentiviral shRNA that targets GAB1, we demonstrate that GAB1 phosphorylation is required for ERBB2 mutant-induced cell signaling, cell transformation, and tumorigenesis. Tyrosine 55-63 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 77-81 23980151-8 2013 Inhibition of either N-SH2 or C-SH2 was sufficient to inhibit two tyrosine phosphorylation events that are critical for SHP2 catalytic activity and to block ERK activation. Tyrosine 66-74 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 120-124 23922991-9 2013 By employing the well characterized dynamin inhibitor, dynasore, we established that PDGF-induced SHP-2 phosphorylation primarily occurs within endosomal compartments, the same compartments in which LRP1 is tyrosine phosphorylated by activated PDGFRbeta. Tyrosine 207-215 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 98-103 22711529-5 2012 Most mutations affecting Tyr(63) exerted an unpredicted disrupting effect on the structure of the N-SH2 phosphopeptide-binding cleft mediating the interaction of SHP2 with signaling partners. Tyrosine 25-28 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 162-166 23545499-6 2013 A predicted dynamic interaction between the SH2 domains of the tyrosine phosphatase SHP2 and the phosphorylated tyrosine in the extracellular signal-regulated kinase activation loop was validated by experiments in living cells. Tyrosine 63-71 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 84-88 23192641-1 2013 Src homology 2 domain-containing tyrosine phosphatase-2 (SHP-2) is an important regulator of cell signaling because of its ability to dephosphorylate receptors of growth factors as well as the cytokines and tyrosine-phosphorylated proteins associated with these receptors. Tyrosine 33-41 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 57-62 23233201-6 2013 We also demonstrate by using a substrate trapping mutant of SHP2 that tyrosine phosphorylated PECAM-1 binds SHP2 and is a major substrate for this tyrosine phosphatase in BCR/ABL-expressing cells. Tyrosine 82-90 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 72-76 23233201-6 2013 We also demonstrate by using a substrate trapping mutant of SHP2 that tyrosine phosphorylated PECAM-1 binds SHP2 and is a major substrate for this tyrosine phosphatase in BCR/ABL-expressing cells. Tyrosine 82-90 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 132-136 23178938-7 2013 SHP2 selectively suppressed the tyrosine phosphorylation of Tks5, a scaffolding protein required for podosome formation. Tyrosine 32-40 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 22956765-7 2012 Moreover, on thrombin challenge, we find prolonged elevation in tyrosine phosphorylation levels of VE-cadherin-associated beta-catenin in SHP2-depleted cells. Tyrosine 64-72 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 138-142 22851227-5 2012 We show that both Gab1 and Gab2 were tyrosine phosphorylated in IL-22-stimulated HaCaT cells and human primary epidermal keratinocytes and contributed to the activation of Extracellular signal regulated kinase 1/2 (Erk1/2) through interaction with Shp2. Tyrosine 37-45 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 248-252 23258536-6 2013 Specifically, Src family kinases, NCK1 and Vav1, bound to the Tyr(P)(120) site, PLCgamma2 and the SHP2 phosphatase bound to the Tyr(P)(129) motif, and the p85alpha subunit of PI3K associated with either motif. Tyrosine 128-131 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 98-102 23431498-3 2013 Gab proteins lack the enzymatic activity themselves; however, when phosphorylated on tyrosine residues, they provide binding sites for multiple Src homology-2 (SH2) domain-containing proteins, such as SH2-containing protein tyrosine phosphatase 2 (SHP2), phosphatidylinositol 3-kinase regulatory subunit p85, phospholipase Cgamma, Crk, and GC-GAP. Tyrosine 85-93 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 248-252 22806893-4 2012 Importantly, a single tyrosine at position 719 in oncogenic KIT is sufficient to develop MPD by recruiting p85alpha, SHP2, and Gab2 complex to oncogenic KIT. Tyrosine 22-30 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 117-121 22628433-3 2012 METHODS AND RESULTS: In human umbilical vein-derived endothelial cells, treatment with insulin (100 nmol/L) increased Tyr(542) phosphorylation, activity, and subsequently expression of SHP2. Tyrosine 118-121 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 185-189 22641100-6 2012 PECAM-1 is also tyrosine-phosphorylated, an event associated with recruitment of the phosphatase SHP-2 (Src homology 2 domain-containing protein phosphatase) to PECAM-1, beta-catenin release from PECAM-1, and reassociation of beta-catenin with the AJ. Tyrosine 16-24 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 97-102 22609512-9 2012 Moreover, tyrosine phosphorylation sites were identified in several MAP kinases and a protein tyrosine phosphatase, SHPTP2. Tyrosine 10-18 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 116-122 22629427-7 2012 CONCLUSIONS: These results identify FGF-dependent maintenance of SHP2 as an important new mechanism controlling the extent of VE-cadherin tyrosine phosphorylation, thereby regulating its presence in adherens junctions and endothelial permeability. Tyrosine 138-146 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 65-69 22537350-6 2012 Tyrosine phosphorylation of the CD300a ITIMs created docking sites for both src homology 2 domain containing protein tyrosine phosphatase (SHP)-1 and SHP-2. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 150-155 22306001-4 2012 Shp2 knockdown increased IFN-alpha2b-stimulated STAT1 Tyr-701 phosphorylation and ISRE-luciferase activity even though it did not affect STAT2 Tyr-690 phosphorylation in A375 cells. Tyrosine 54-57 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 21627633-9 2012 This results in phosphorylation of two immunoreceptor tyrosine-based inhibitory motifs (ITIM) in OX(1)R and subsequent recruitment by OX(1)R of the phosphotyrosine phosphatase SHP-2, which is activated thereby. Tyrosine 54-62 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 176-181 21726809-6 2011 We found that, on tyrosine dephosphorylation by SHP2, parafibromin acquires the ability to stably bind beta-catenin. Tyrosine 18-26 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 48-52 21663700-8 2011 Changes in the complex"s PLCbeta1 tyr-phosphorylation and SHP-2"s tyr-phosphorylation as well as SHP-2-PLCbeta1 complex formation are the result of Ang II type 1 receptor activation with changes in complex associated PLCbeta1 tyr-phosphorylation requiring RGS-2. Tyrosine 66-69 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 58-63 21663700-5 2011 Complex PLCbeta1 is tyr-phosphorylated basally and Ang II increased SHP-2-PLCbeta1 complexes and caused complex associated PLCbeta1 tyr-phosphorylation to decline while complex associated SHP-2"s tyr-phosphorylation increased and did so via the Ang II type 1 receptors as shown by Ang II type 1 receptor blocker losartan"s effects. Tyrosine 20-23 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 68-73 21531714-7 2011 Finally, we found two tyrosine residues on SPRED1 that are required, when phosphorylated, to inhibit Ras/ERK activation and identified Tyr-420 as a specific dephosphorylation target of SHP2. Tyrosine 22-30 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 185-189 21531714-7 2011 Finally, we found two tyrosine residues on SPRED1 that are required, when phosphorylated, to inhibit Ras/ERK activation and identified Tyr-420 as a specific dephosphorylation target of SHP2. Tyrosine 135-138 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 185-189 21531714-8 2011 The evidence obtained indicates that SPRED1 is a likely substrate of SHP2, whose tyrosine dephosphorylation is required to attenuate the inhibitory action of SPRED1 in the Ras/ERK pathway. Tyrosine 81-89 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 69-73 21663700-5 2011 Complex PLCbeta1 is tyr-phosphorylated basally and Ang II increased SHP-2-PLCbeta1 complexes and caused complex associated PLCbeta1 tyr-phosphorylation to decline while complex associated SHP-2"s tyr-phosphorylation increased and did so via the Ang II type 1 receptors as shown by Ang II type 1 receptor blocker losartan"s effects. Tyrosine 20-23 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 188-193 21663700-8 2011 Changes in the complex"s PLCbeta1 tyr-phosphorylation and SHP-2"s tyr-phosphorylation as well as SHP-2-PLCbeta1 complex formation are the result of Ang II type 1 receptor activation with changes in complex associated PLCbeta1 tyr-phosphorylation requiring RGS-2. Tyrosine 66-69 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 58-63 21663700-5 2011 Complex PLCbeta1 is tyr-phosphorylated basally and Ang II increased SHP-2-PLCbeta1 complexes and caused complex associated PLCbeta1 tyr-phosphorylation to decline while complex associated SHP-2"s tyr-phosphorylation increased and did so via the Ang II type 1 receptors as shown by Ang II type 1 receptor blocker losartan"s effects. Tyrosine 132-135 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 68-73 21663700-5 2011 Complex PLCbeta1 is tyr-phosphorylated basally and Ang II increased SHP-2-PLCbeta1 complexes and caused complex associated PLCbeta1 tyr-phosphorylation to decline while complex associated SHP-2"s tyr-phosphorylation increased and did so via the Ang II type 1 receptors as shown by Ang II type 1 receptor blocker losartan"s effects. Tyrosine 132-135 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 188-193 21047965-0 2011 The Kaposi"s sarcoma-associated herpesvirus G protein-coupled receptor contains an immunoreceptor tyrosine-based inhibitory motif that activates Shp2. Tyrosine 98-106 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 145-149 21663700-5 2011 Complex PLCbeta1 is tyr-phosphorylated basally and Ang II increased SHP-2-PLCbeta1 complexes and caused complex associated PLCbeta1 tyr-phosphorylation to decline while complex associated SHP-2"s tyr-phosphorylation increased and did so via the Ang II type 1 receptors as shown by Ang II type 1 receptor blocker losartan"s effects. Tyrosine 132-135 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 68-73 21663700-5 2011 Complex PLCbeta1 is tyr-phosphorylated basally and Ang II increased SHP-2-PLCbeta1 complexes and caused complex associated PLCbeta1 tyr-phosphorylation to decline while complex associated SHP-2"s tyr-phosphorylation increased and did so via the Ang II type 1 receptors as shown by Ang II type 1 receptor blocker losartan"s effects. Tyrosine 132-135 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 188-193 21272002-4 2011 We show that the D(1) R interacts with Shp-2, that D(1) R stimulation results in Shp-2 tyrosine phosphorylation and activation in primary striatal neuronal cultures and that D(1) R/Shp-2 interaction is required for transmitting D(1) R-dependent signaling to Erk1/2 activation. Tyrosine 87-95 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 81-86 21272002-4 2011 We show that the D(1) R interacts with Shp-2, that D(1) R stimulation results in Shp-2 tyrosine phosphorylation and activation in primary striatal neuronal cultures and that D(1) R/Shp-2 interaction is required for transmitting D(1) R-dependent signaling to Erk1/2 activation. Tyrosine 87-95 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 81-86 21123182-6 2011 Ultimately a variety of in vitro and in vivo approaches were used to verify the prediction that the tyrosine phosphorylation levels of five high-ranking substrates, PLC-gamma1, Gab1, SHP2, EGFR, and SHP1, are indeed specifically modulated by PTP1B. Tyrosine 100-108 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 183-187 21047965-2 2011 We show that vGPCR contains a bona fide immunoreceptor tyrosine-based inhibitory motif (ITIM) that binds and constitutively activates Shp2. Tyrosine 55-63 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 134-138 20631249-4 2010 We observed that the levels of PECAM-1 tyrosine phosphorylation and SHP-2 association with PECAM-1 were significantly increased in cells expressing a phosphatase-inactive SHP-2 mutant, suggesting that the level of PECAM-1 tyrosine phosphorylation, and thus SHP-2 binding are regulated in part by bound, catalytically active SHP-2. Tyrosine 222-230 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 171-176 20723025-7 2010 We therefore propose that PECAM-1-mediated inhibition of GPVI-dependent platelet responses result, at least in part, from recruitment of SHP-2-p85 complexes to tyrosine-phosphorylated PECAM-1, which diminishes the association of PI3K with activatory signaling molecules, such as Gab1 and LAT. Tyrosine 160-168 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 137-142 21085662-4 2010 H5N1 NS1 reduces IFN-inducible tyrosine phosphorylation of STAT1, STAT2 and STAT3 and inhibits the nuclear translocation of phospho-STAT2 and the formation of IFN-inducible STAT1:1-, STAT1:3- and STAT3:3- DNA complexes. Tyrosine 31-39 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 5-8 20682772-3 2010 Here we have identified the protein-tyrosine phosphatase SHP2 as a novel direct interactor of RET and the first effector known to bind to phosphorylated Tyr(687) in the juxtamembrane region of the receptor. Tyrosine 153-156 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 57-61 20682772-4 2010 We show that SHP2 is recruited to RET upon ligand binding in a cooperative fashion, such that both interaction with Tyr(687) and association with components of the Tyr(1062) signaling complex are required for stable recruitment of SHP2 to the receptor. Tyrosine 116-119 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 13-17 20682772-4 2010 We show that SHP2 is recruited to RET upon ligand binding in a cooperative fashion, such that both interaction with Tyr(687) and association with components of the Tyr(1062) signaling complex are required for stable recruitment of SHP2 to the receptor. Tyrosine 164-167 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 13-17 20631249-4 2010 We observed that the levels of PECAM-1 tyrosine phosphorylation and SHP-2 association with PECAM-1 were significantly increased in cells expressing a phosphatase-inactive SHP-2 mutant, suggesting that the level of PECAM-1 tyrosine phosphorylation, and thus SHP-2 binding are regulated in part by bound, catalytically active SHP-2. Tyrosine 222-230 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 171-176 20631249-4 2010 We observed that the levels of PECAM-1 tyrosine phosphorylation and SHP-2 association with PECAM-1 were significantly increased in cells expressing a phosphatase-inactive SHP-2 mutant, suggesting that the level of PECAM-1 tyrosine phosphorylation, and thus SHP-2 binding are regulated in part by bound, catalytically active SHP-2. Tyrosine 222-230 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 171-176 21442024-9 2010 Tyrosine phosphoproteomic analysis of H292 tumor tissues showed that Shp2 could both up- and down-regulate tyrosine phosphorylation on cellular proteins. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 69-73 21442024-10 2010 Among other changes, Shp2 inhibition increased phosphorylation of Src Tyr-530 and Cdk1 Thr-14/Tyr-15 and decreased phosphorylation of Erk1 and Erk2 activating sites in the tumors. Tyrosine 94-97 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 21-25 21442024-13 2010 Shp2 Tyr-62/Tyr-63 phosphorylation was observed in tumor tissues, indicating that Shp2 is activated in the tumors. Tyrosine 5-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 21442024-13 2010 Shp2 Tyr-62/Tyr-63 phosphorylation was observed in tumor tissues, indicating that Shp2 is activated in the tumors. Tyrosine 5-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 82-86 21442024-9 2010 Tyrosine phosphoproteomic analysis of H292 tumor tissues showed that Shp2 could both up- and down-regulate tyrosine phosphorylation on cellular proteins. Tyrosine 107-115 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 69-73 21442024-13 2010 Shp2 Tyr-62/Tyr-63 phosphorylation was observed in tumor tissues, indicating that Shp2 is activated in the tumors. Tyrosine 12-15 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 82-86 21442024-10 2010 Among other changes, Shp2 inhibition increased phosphorylation of Src Tyr-530 and Cdk1 Thr-14/Tyr-15 and decreased phosphorylation of Erk1 and Erk2 activating sites in the tumors. Tyrosine 70-73 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 21-25 20004456-6 2010 We find that vGPCR activity results in phosphorylation of regulatory tyrosines in Shp2 and that in turn, Shp2 is required for vGPCR-mediated activation of MEK, NFkappaB, and AP-1. Tyrosine 69-78 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 82-86 20671117-4 2010 The results show that IL-22 induces IL-22R1 phosphorylation, and Shp2 is recruited to the tyrosine phosphorylated IL-22R1 upon IL-22 stimulation. Tyrosine 90-98 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 65-69 20398180-7 2010 These results suggest that calpain-dependent cleavage of SHP-1 and SHP-2 may contribute to protein tyrosine dephosphorylation in Jurkat T cell death induced by E. histolytica. Tyrosine 99-107 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 67-72 20004456-6 2010 We find that vGPCR activity results in phosphorylation of regulatory tyrosines in Shp2 and that in turn, Shp2 is required for vGPCR-mediated activation of MEK, NFkappaB, and AP-1. Tyrosine 69-78 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 105-109 19661287-3 2009 OX1R is equipped with a tyrosine-based inhibitory motif ITIM, which is tyrosine-phosphorylated on receptor activation, allowing the recruitment and activation of the tyrosine phosphatase SHP-2, leading to apoptosis. Tyrosine 24-32 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 187-192 19881549-4 2010 It is interesting to note that the binding of the tyrosine phosphatase SHP2 to the Y627 antagonized the effect of c-Src on the phosphorylation of the other four tyrosine residues. Tyrosine 50-58 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 71-75 19661287-3 2009 OX1R is equipped with a tyrosine-based inhibitory motif ITIM, which is tyrosine-phosphorylated on receptor activation, allowing the recruitment and activation of the tyrosine phosphatase SHP-2, leading to apoptosis. Tyrosine 71-79 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 187-192 19410646-6 2009 The FGF7/FGFR2 pair caused tyrosine phosphorylation of multiple proteins that have been implicated in the growth stimulating activities of FGFR1 that included multi-substrate organizers FRS2alpha and IRS4, ERK2 and phosphatases SHP2 and SHIP2. Tyrosine 27-35 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 228-232 19622105-3 2009 The molecular basis for the activation of SHP-2 is also unique: In the basal state, the NH(2)-terminal SH2 domain of SHP-2 interacts with the PTP domain, resulting in autoinhibition of PTP activity; the binding of SHP-2 via its SH2 domains to tyrosine-phosphorylated growth factor receptors or docking proteins, however, results in disruption of this intramolecular interaction, leading to exposure of the PTP domain and catalytic activation. Tyrosine 243-251 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 42-47 19622105-3 2009 The molecular basis for the activation of SHP-2 is also unique: In the basal state, the NH(2)-terminal SH2 domain of SHP-2 interacts with the PTP domain, resulting in autoinhibition of PTP activity; the binding of SHP-2 via its SH2 domains to tyrosine-phosphorylated growth factor receptors or docking proteins, however, results in disruption of this intramolecular interaction, leading to exposure of the PTP domain and catalytic activation. Tyrosine 243-251 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 117-122 19622105-3 2009 The molecular basis for the activation of SHP-2 is also unique: In the basal state, the NH(2)-terminal SH2 domain of SHP-2 interacts with the PTP domain, resulting in autoinhibition of PTP activity; the binding of SHP-2 via its SH2 domains to tyrosine-phosphorylated growth factor receptors or docking proteins, however, results in disruption of this intramolecular interaction, leading to exposure of the PTP domain and catalytic activation. Tyrosine 243-251 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 117-122 19805366-6 2009 BG1 encodes an Ig-superfamily type I transmembrane receptor-like protein that contains an immunoreceptor tyrosine-based inhibition motif (ITIM), which undergoes phosphorylation and is recognized by Src homology 2 domain-containing protein tyrosine phosphatase (SHP-2). Tyrosine 105-113 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 261-266 19463892-14 2009 We propose that NO mediated inhibition of protein tyrosine phosphatases SH-PTP-1 and SH-PTP-2 leads to increased tyrosine phosphorylation and activation of Src kinase in the cerebral cortex of newborn piglets. Tyrosine 50-58 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 85-93 19233262-3 2009 Here, we show that Gab2 is tyrosine phosphorylated in a Grb2-dependent manner downstream of activated VEGF receptor-2 (VEGFR2), and that it associates with signalling proteins including PI3K and SHP2, but apparently not with the receptor. Tyrosine 27-35 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 195-199 19509291-7 2009 Because the amino acid sequence surrounding tyrosine 453 is similar to the immunoreceptor tyrosine-based inhibitory motif, Shp2, a positive regulator of Erk, binds to GAREM in this phosphorylation-dependent manner. Tyrosine 44-52 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 123-127 19509291-7 2009 Because the amino acid sequence surrounding tyrosine 453 is similar to the immunoreceptor tyrosine-based inhibitory motif, Shp2, a positive regulator of Erk, binds to GAREM in this phosphorylation-dependent manner. Tyrosine 90-98 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 123-127 19509418-2 2009 Approximately 50% of NS patients have germline gain-of-function mutations in PTPN11, which encodes the protein-tyrosine phosphatase, Shp2. Tyrosine 111-119 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 77-83 19509418-2 2009 Approximately 50% of NS patients have germline gain-of-function mutations in PTPN11, which encodes the protein-tyrosine phosphatase, Shp2. Tyrosine 111-119 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 133-137 19509418-5 2009 Biochemical and functional analyses demonstrate that activated Shp2 is able to down-regulate Tyr(P)-Stat3 and that constitutively active Stat3 rescues activating mutant Shp2-induced granulocyte-macrophage colony-stimulating factor hypersensitivity in bone marrow cells. Tyrosine 93-96 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 63-67 19509418-5 2009 Biochemical and functional analyses demonstrate that activated Shp2 is able to down-regulate Tyr(P)-Stat3 and that constitutively active Stat3 rescues activating mutant Shp2-induced granulocyte-macrophage colony-stimulating factor hypersensitivity in bone marrow cells. Tyrosine 93-96 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 169-173 19275884-4 2009 SHP-2 inhibits tyrosine phosphorylation of Cas-L, and associates with Cas-L to form a complex in a tyrosine phosphorylation-dependent manner. Tyrosine 15-23 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 19275884-4 2009 SHP-2 inhibits tyrosine phosphorylation of Cas-L, and associates with Cas-L to form a complex in a tyrosine phosphorylation-dependent manner. Tyrosine 99-107 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 19275884-0 2009 SHP-2 inhibits tyrosine phosphorylation of Cas-L and regulates cell migration. Tyrosine 15-23 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 19275884-2 2009 In this report, we demonstrated that SHP-2 inhibits tyrosine phosphorylation of Crk-associated substrate lymphocyte type (Cas-L), a docking protein which mediates cell migration, and found that SHP-2 negatively regulates migration of A549 lung adenocarcinoma cells induced by fibronectin (FN). Tyrosine 52-60 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 37-42 19275884-6 2009 These results suggest that SHP-2 regulates tyrosine phosphorylation of Cas-L, hence opposing the effect of kinases, and SHP-2 is a negative regulator of cell migration mediated by Cas-L. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 27-32 19275884-2 2009 In this report, we demonstrated that SHP-2 inhibits tyrosine phosphorylation of Crk-associated substrate lymphocyte type (Cas-L), a docking protein which mediates cell migration, and found that SHP-2 negatively regulates migration of A549 lung adenocarcinoma cells induced by fibronectin (FN). Tyrosine 52-60 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 194-199 19047464-6 2008 Fer or SHP-2 depletion results in elevated tyrosine phosphorylation of beta-catenin. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 7-12 19290926-5 2009 The signaling pathways propagated by these tyrosine kinases can be further upregulated by the Tec kinase Bruton"s tyrosine kinase and downregulated by the actions of the tyrosine Src homology 2 domain-containing phosphatase 1 (SHP-1) and SHP-2. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 238-243 19271114-4 2009 Tyrosine-phosphorylated CagA then acquires the ability to interact with and deregulate SHP-2 phosphatase, a bona-fide oncoprotein, deregulation of which is involved in a variety of human malignancies. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 87-92 19066472-0 2008 Tyrosine phosphatase SHP-2 is a regulator of p27(Kip1) tyrosine phosphorylation. Tyrosine 55-63 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 21-26 19066472-5 2008 Using a catalytically inactive form of SHP-2 and siRNA directed against SHP-2, we could demonstrate the involvement of SHP-2 in tyrosine dephosphorylation of p27(Kip1). Tyrosine 128-136 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 39-44 19066472-5 2008 Using a catalytically inactive form of SHP-2 and siRNA directed against SHP-2, we could demonstrate the involvement of SHP-2 in tyrosine dephosphorylation of p27(Kip1). Tyrosine 128-136 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 72-77 19066472-5 2008 Using a catalytically inactive form of SHP-2 and siRNA directed against SHP-2, we could demonstrate the involvement of SHP-2 in tyrosine dephosphorylation of p27(Kip1). Tyrosine 128-136 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 72-77 19066472-8 2008 Taken together, our results demonstrate that SHP-2 is a key regulator of p27(Kip1) tyrosine phosphorylation. Tyrosine 83-91 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 45-50 18832710-0 2008 Inhibition of IFN-gamma-induced STAT1 tyrosine phosphorylation by human CMV is mediated by SHP2. Tyrosine 38-46 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 91-95 18829466-13 2008 Ablation of Shp-2 expression led only to an increased tyrosine phosphorylation of TERTwt, but not of TERT(Y707F). Tyrosine 54-62 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 12-17 18829466-15 2008 In conclusion, Shp-2 retains TERT in the nucleus by regulating tyrosine 707 phosphorylation. Tyrosine 63-71 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 15-20 18832710-4 2008 Src homology region 2 domain-containing phosphatase 2 (SHP2) is a ubiquitous phosphatase involved in the regulation of IFN-gamma-mediated tyrosine phosphorylation. Tyrosine 138-146 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 55-59 18832710-12 2008 Our data suggest that SHP2 activation induced by HCMV infection is responsible for the down-regulation of IFN-gamma-induced STAT1 tyrosine phosphorylation. Tyrosine 130-138 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 22-26 18322230-5 2008 Separate experiments using affinity binding with a tyrosine-phosphorylated peptide containing an ITIM (ICAM-1 residues 480-488) showed binding to Shp2 phosphatase and GMRbeta. Tyrosine 51-59 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 146-150 18568953-2 2008 PZR interacts with Src homology 2 domain-containing tyrosine phosphatase (SHP-2) via its tyrosine-phosphorylated ITIMs, for which c-Src is a putative kinase. Tyrosine 52-60 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 74-79 18473914-7 2008 Evidence is also presented indicating that the inhibitory effect of this extract may be mediated through enhancement of tyrosine phosphorylation of SHP2 tyrosine phosphatase. Tyrosine 120-128 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 148-152 18593565-2 2008 CD95L-induced caspase activation leads to degradation of gp130, thereby suppressing IL-6-induced phosphorylation of STAT3 (Tyr(705)) and of tyrosine phosphatase SHP2 (Tyr(580)). Tyrosine 167-170 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 161-165 18519587-4 2008 The stimulation-dependent ubiquitination of gp130 was mediated by c-Cbl, an E3 ligase, which was recruited to gp130 in a tyrosine-phosphorylated SHP2-dependent manner. Tyrosine 121-129 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 145-149 18320059-6 2008 In addition, reduced phosphorylation of Src at tyrosine 416 and p-SHP2 at tyrosine 542 was observed in these downregulated cell lines. Tyrosine 74-82 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 66-70 17936057-8 2008 Importantly, a higher level of tyrosine phosphorylation of eEF1A2 as compared to eEF1A1 was demonstrated in several independent experiments and its importance for interaction of eEF1A2 with Shp2 in vitro was revealed. Tyrosine 31-39 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 190-194 18097101-2 2008 PILRalpha can suppress the functions of such immune cells because it has the immunoreceptor tyrosine-based inhibitory motif (ITIM) in the intracellular region, which recruits the phosphatase Src homology-2 (SH2) domain-containing protein tyrosine phosphatase 2 (SHP-2) to inhibit phosphorylations induced by activation signals. Tyrosine 92-100 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 262-267 17483340-5 2007 In primary lymphomas, antibodies against the phosphorylated tyrosine Y542 of Shp2 mainly stained ALK-positive cells. Tyrosine 60-68 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 77-81 17714694-5 2007 Here, we show that FP induces a dose- and time-dependent phosphorylation of tyrosine 8 and 21 of Band 3, as confirmed by the recruitment of SHP2 phosphatase to the membrane. Tyrosine 76-84 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 140-144 17679554-3 2007 We found that Shp2 became tyrosine phosphorylated following PDGF treatment. Tyrosine 26-34 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 14-18 17311996-1 2007 The G6B cell-surface receptor, which contains a single Ig-like domain, has been shown to bind to SHP-1 and SHP-2 after phosphorylation of 2 immunoreceptor tyrosine-based inhibitory motifs (ITIMs) in its cytoplasmic tail, classifying this protein as a new member of the family of inhibitory receptors. Tyrosine 155-163 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 107-112 18253061-6 2008 Of interest to note is that tyrosine-phosphorylated neogenin and uncoordinated 5 H2 (Unc5H2) not only bind to the Src homology 2 (SH2) domains of Fyn and SHP2, but also interact with the SH2 domain of SHIP1, suggesting a differential signaling between DCC and neogenin/Unc5H2. Tyrosine 28-36 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 154-158 17717529-7 2007 Virus attachment also induced tyrosine phosphorylation of PVR; this permitted the association of PVR with SHP-2, a protein tyrosine phosphatase whose activation was required for entry and infection. Tyrosine 30-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 106-111 17678728-1 2007 The G6b-B gene encodes a novel cell surface receptor of the immunoglobulin superfamily that activates inhibitory signaling pathways by triggering SHP-1/SHP-2 via immunoreceptor tyrosine-based inhibitory motifs (ITIM) in its cytoplasmic domain. Tyrosine 177-185 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 152-157 17664338-4 2007 NOMA-GAP binds directly to the NGF receptor, TrkA, and becomes tyrosine phosphorylated upon receptor activation, thus enabling recruitment and activation of the tyrosine phosphatase SHP2. Tyrosine 63-71 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 182-186 17483340-8 2007 Shp2 knock down by specific shRNA decreased the phosphorylation of extracellular signal-regulated kinase 1/2 and of the tyrosine residue Y416 in the activation loop of Src, resulting in impaired ALCL cell proliferation and growth disadvantage. Tyrosine 120-128 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 17027227-6 2007 We found that the N-terminal SH2 domain of SHP-2 binds Jak2 predominantly, but not exclusively at tyrosine 201. Tyrosine 98-106 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 43-48 16920701-8 2006 Incubation of immunoprecipitated FAK, in vitro, with glutathione-S-transferase-ShP2 fusion protein resulted in tyrosine dephosphorylation of FAK in a concentration-dependent manner. Tyrosine 111-119 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 79-83 17404032-9 2007 We hypothesize that the presence of both SHP-2 and SHP-1 ensures band 3 dephosphorylation in different conditions: SHP-2, through interaction of its SH2 domain/s to P-Tyr protein, is regulated by the band 3 Tyr-phosphorylation level; SHP-1 may be involved by simple membrane rearrangement. Tyrosine 167-170 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 41-46 17404032-9 2007 We hypothesize that the presence of both SHP-2 and SHP-1 ensures band 3 dephosphorylation in different conditions: SHP-2, through interaction of its SH2 domain/s to P-Tyr protein, is regulated by the band 3 Tyr-phosphorylation level; SHP-1 may be involved by simple membrane rearrangement. Tyrosine 167-170 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 115-120 17404032-9 2007 We hypothesize that the presence of both SHP-2 and SHP-1 ensures band 3 dephosphorylation in different conditions: SHP-2, through interaction of its SH2 domain/s to P-Tyr protein, is regulated by the band 3 Tyr-phosphorylation level; SHP-1 may be involved by simple membrane rearrangement. Tyrosine 207-210 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 41-46 17404032-9 2007 We hypothesize that the presence of both SHP-2 and SHP-1 ensures band 3 dephosphorylation in different conditions: SHP-2, through interaction of its SH2 domain/s to P-Tyr protein, is regulated by the band 3 Tyr-phosphorylation level; SHP-1 may be involved by simple membrane rearrangement. Tyrosine 207-210 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 115-120 17158954-3 2006 We found that activation of the Met receptor for hepatocyte growth factor results in the tyrosine phosphorylation of beta4, which is instrumental for integrin-mediated recruitment of the tyrosine phosphatase Shp2. Tyrosine 89-97 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 208-212 17008544-2 2007 CD33 contains a cytoplasmic immunoreceptor tyrosine-based inhibitory motif (ITIM), which can recruit SHP-1 and SHP-2. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 111-116 17003374-1 2007 SHP-2 phosphatase forms a stable protein complex with and is heavily tyrosine-phosphorylated by the oncogenic tyrosine kinase Bcr-Abl. Tyrosine 69-77 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 17118755-6 2006 CagA binds to and activates SHP-2 in a tyrosine phosphorylation-dependent manner, thereby provoking abnormal activation of Erk MAP kinase while inducing elevated cell motility. Tyrosine 39-47 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 28-33 16767162-0 2006 Modulation of alpha-catenin Tyr phosphorylation by SHP2 positively effects cell transformation induced by the constitutively active FGFR3. Tyrosine 28-31 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 51-55 16767162-5 2006 We show that alpha-catenin becomes Tyr phosphorylated in intercellular adhesion-dependent manner and this event is counteracted by SHP2. Tyrosine 35-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 131-135 16702953-1 2006 The membrane-linked docking protein SNT-2/FRS2beta/FRS3 becomes tyrosine phosphorylated in response to fibroblast growth factors (FGFs) and neurotrophins and serves as a platform for recruitment of multiple signaling proteins, including Grb2 and Shp2, to FGF receptors or neurotrophin receptors. Tyrosine 64-72 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 246-250 16762922-9 2006 The interaction of SHP-1 with Gab1 is mediated by SHP-2 because it was abrogated by knockdown of SHP-2, and SHP-2, but not SHP-1, binds directly to tyrosine-phosphorylated Gab1. Tyrosine 148-156 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 50-55 16762922-9 2006 The interaction of SHP-1 with Gab1 is mediated by SHP-2 because it was abrogated by knockdown of SHP-2, and SHP-2, but not SHP-1, binds directly to tyrosine-phosphorylated Gab1. Tyrosine 148-156 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 97-102 16762922-9 2006 The interaction of SHP-1 with Gab1 is mediated by SHP-2 because it was abrogated by knockdown of SHP-2, and SHP-2, but not SHP-1, binds directly to tyrosine-phosphorylated Gab1. Tyrosine 148-156 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 97-102 16725108-2 2006 We previously identified two tyrosine-containing signaling motifs in the cytoplasmic domain of BTLA that interact with the SHP-1 and SHP-2 phosphatases. Tyrosine 29-37 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 133-138 16702225-4 2006 These studies reveal that binding of a pY peptide to the N-SH2 domain of SHP-2 is greatly enhanced by a large hydrophobic residue (Trp, Tyr, Met, or Phe) at the pY+4 and/or pY+5 positions, whereas binding to SHP-1 N-SH2 domain is enhanced by either hydrophobic or positively charged residues (Arg, Lys, or His) at these positions. Tyrosine 136-139 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 73-78 16631468-1 2006 The PTPN11 gene encodes SHP-2, a widely expressed cytoplasmic protein tyrosine phosphatase functioning as a signaling transducer. Tyrosine 70-78 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 4-10 16611743-4 2006 Expression of catalytically inactive SHP-2 in DDR1-transfected cells restored the tyrosine phosphorylation of Stat3 and cell migration. Tyrosine 82-90 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 37-42 16611743-5 2006 We demonstrated that the Src homology-2 (SH2)-SH2 and phosphotyrosyl phosphatase (PTP) domains of SHP-2 were responsible for interaction with DDR1 and that both tyrosine phosphorylation sites 703 and 796 of DDR1 were essential for it to bind with SHP-2. Tyrosine 161-169 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 98-103 16611743-5 2006 We demonstrated that the Src homology-2 (SH2)-SH2 and phosphotyrosyl phosphatase (PTP) domains of SHP-2 were responsible for interaction with DDR1 and that both tyrosine phosphorylation sites 703 and 796 of DDR1 were essential for it to bind with SHP-2. Tyrosine 161-169 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 247-252 16611743-7 2006 Together, these results demonstrate that SHP-2 is required for the DDR1-induced suppression of Stat1 and Stat3 tyrosine phosphorylation, cell migration, and branching tubulogenesis. Tyrosine 111-119 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 41-46 16195423-9 2006 IGF-I also elicited time-dependent recruitment of protein tyrosine phosphatase SHP-2 that coincided with dephosphorylation of the tyrosine phosphorylated IGF-I receptor tyrosine kinase. Tyrosine 58-66 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 79-84 16698585-3 2006 Sirpalpha1 can bind SHP-2 in the form of tyrosine phosphorylation by SH2 effect and negatively regulate growth factor, oncogene, or insulin-induced responses as its substrate. Tyrosine 41-49 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 20-25 16573649-12 2006 Moreover, the PTB association motif of TrkB containing tyrosine 484 is required for the BDNF-induced association of Shp2 with FRS2 and the phosphorylation of Shp2. Tyrosine 55-63 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 116-120 16573649-12 2006 Moreover, the PTB association motif of TrkB containing tyrosine 484 is required for the BDNF-induced association of Shp2 with FRS2 and the phosphorylation of Shp2. Tyrosine 55-63 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 158-162 16631468-1 2006 The PTPN11 gene encodes SHP-2, a widely expressed cytoplasmic protein tyrosine phosphatase functioning as a signaling transducer. Tyrosine 70-78 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 24-29 16250012-9 2006 IL-1beta-induced tyrosine phosphorylation of SHP-2 on residue Y542 promoted focal adhesion maturation. Tyrosine 17-25 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 45-50 16250012-11 2006 We conclude that IL-1beta mediated maturation of focal adhesions is dependent on tyrosine phosphorylation of SHP-2 at Y542, leading to recruitment of Gab1, a process that may influence the downstream activation of ERK. Tyrosine 81-89 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 109-114 16306077-7 2006 Substitution for these tyrosines in p85 resulted in loss of SHP-2 recruitment and was associated with a reduction in association of the p85/p110 complex with insulin receptor substrate-1. Tyrosine 23-32 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 60-65 16360206-1 2006 Proteins that bear immunoreceptor tyrosine based inhibitory motifs (ITIM) are believed to participate in the repression of cell activation via phosphatases such as SHP-1, SHP-2 and/or SHIP-1. Tyrosine 34-42 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 171-176 16306077-10 2006 The findings indicate that tyrosines 528 and 556 in p85 are required for SHP-2 association. Tyrosine 27-36 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 73-78 15985475-2 2005 Half the individuals with Noonan syndrome carry a heterozygous mutation of the nonreceptor-type protein tyrosine phosphatase, Src homology region 2-domain phosphatase-2 (SHP-2), encoded by PTPN11, which has a role in GH receptor signaling. Tyrosine 104-112 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 170-175 16030196-5 2005 Notably, the majority of Shp2 was preferentially localized to the plasma membrane and was constitutively phosphorylated on tyrosine in leukemia cells, and also in normal hematopoietic cells following mitogenic stimulation. Tyrosine 123-131 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 25-29 16020478-10 2005 These data suggest that phosphorylation of Ser1223 dampens association of IRS-1 with SHP-2, thereby increasing net insulin-stimulated tyrosine phosphorylation. Tyrosine 134-142 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 85-90 16365455-2 2006 In this study, we show that ligation of CD28 by its natural ligand B7-1/CD80, induces tyrosine phosphorylation of Gab2 and its coassociation with Src homology phosphatase (SHP)-2 and class IA PI3K in Jurkat cells. Tyrosine 86-94 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 146-178 15985475-2 2005 Half the individuals with Noonan syndrome carry a heterozygous mutation of the nonreceptor-type protein tyrosine phosphatase, Src homology region 2-domain phosphatase-2 (SHP-2), encoded by PTPN11, which has a role in GH receptor signaling. Tyrosine 104-112 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 189-195 16308275-5 2005 However, since both Syk, and Lyn kinases, and SHP-2 phosphatase, mostly implicated in the band 3 P-Tyr level regulation, are alike in content and activity in normal and patient erythrocytes, an alteration in the membrane organization is likely the cause of the anomalous response to the oxidant. Tyrosine 99-102 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 46-51 15888547-6 2005 Preincubation of cells with a peptide that contains a phospho-tyrosine binding motif sequence derived from SHPS-1 inhibited IGF-I-stimulated SHP-2 transfer to SHPS-1, the association of Shc with SHPS-1, and IGF-I-dependent Shc phosphorylation. Tyrosine 62-70 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 141-146 15985432-8 2005 Flow significantly increased tyrosine phosphorylation of both Tie2 and PECAM1 and their association with SHP2. Tyrosine 29-37 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 105-109 15769739-4 2005 Tyrosine phosphorylation of Siglec-5 led to recruitment of the tyrosine phosphatases SHP-1 and SHP-2, as seen in both pull-down assays and microscopy. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 95-100 15601262-0 2005 Interferon-gamma-dependent tyrosine phosphorylation of MEKK4 via Pyk2 is regulated by annexin II and SHP2 in keratinocytes. Tyrosine 27-35 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 101-105 15194502-3 2004 The ITIM was tyrosine-phosphorylated upon binding of anti-CD155 monoclonal antibody D171, poliovirus, and DNAM-1 (CD226) to human CD155alpha, and recruited SH2-domain-containing tyrosine phosphatase-2 (SHP-2). Tyrosine 13-21 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 156-200 15683731-2 2005 Gp130 contains a crucial motif around tyrosine Y759, which mediates negative regulation through the feedback inhibitor SOCS3 and the protein tyrosine phosphatase SHP2. Tyrosine 38-46 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 162-166 15574420-10 2005 Gab1 constructs mutated on Tyr(317) were severely affected in RasGAP binding and were the most active in compensating for Ras-defective activation and blocking RasGAP redistribution induced by SHP2 inactivation. Tyrosine 27-30 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 193-197 15574420-11 2005 We have thus localized on Gab1 a Ras-negative regulatory tyrosine phosphorylation site involved in RasGAP binding and showed that an important SHP2 function is to down-regulate its phosphorylation to disengage RasGAP and sustain Ras activation. Tyrosine 57-65 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 143-147 15351743-2 2004 We previously reported that tyrosine 1062 in RET receptor tyrosine kinase activated by glial cell line-derived neurotrophic factor (GDNF) represents a binding site for the Shc-Grb2-Gab1 complex, and that the p85 subunit of phosphatidylinositol 3-kinase (PI3K) and SHP2 tyrosine phosphatase is associated with Gab1 in GDNF-treated cells. Tyrosine 28-36 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 264-268 15356145-4 2004 Indeed, ERK phosphorylated Gab2 on a consensus phosphorylation site at serine 623, a residue located between tyrosine 614 and tyrosine 643 that are responsible for Gab2/Src homology 2 domain-containing tyrosine phosphatase (SHP)-2 interaction. Tyrosine 126-134 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 202-230 15356145-5 2004 We report that pretreatment of Kit 225 cells with U0126 increased Gab2/SHP-2 association and tyrosine phosphorylation of SHP-2 in response to IL-2, suggesting that ERK phosphorylation of serine 623 regulates the interaction between Gab2 and SHP-2, and consequently the activity of SHP-2. Tyrosine 93-101 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 121-126 15356145-5 2004 We report that pretreatment of Kit 225 cells with U0126 increased Gab2/SHP-2 association and tyrosine phosphorylation of SHP-2 in response to IL-2, suggesting that ERK phosphorylation of serine 623 regulates the interaction between Gab2 and SHP-2, and consequently the activity of SHP-2. Tyrosine 93-101 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 121-126 15356145-5 2004 We report that pretreatment of Kit 225 cells with U0126 increased Gab2/SHP-2 association and tyrosine phosphorylation of SHP-2 in response to IL-2, suggesting that ERK phosphorylation of serine 623 regulates the interaction between Gab2 and SHP-2, and consequently the activity of SHP-2. Tyrosine 93-101 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 121-126 15170389-1 2004 Gab2 (Grb2-associated binder-2), a member of the IRS (insulin receptor substrate)/Gab family of adapter proteins, undergoes tyrosine phosphorylation in response to cytokine or growth factor stimulation and serves as a docking platform for many signal transduction effectors, including the tyrosine phosphatase SHP-2 [SH2 (Src homology 2)-domain-containing tyrosine phosphatase]. Tyrosine 124-132 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 310-315 15170389-2 2004 Here, we report that, following IL-2 (interleukin-2) stimulation of human T lymphocytes, SHP-2 binds tyrosine residues 614 and 643 of human Gab2 through its N- and C-terminal SH2 domains respectively. Tyrosine 101-109 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 89-94 15170389-4 2004 Expression of the Gab2 Tyr-614-->Phe (Y614F) mutant, defective in SHP-2 association, prevents ERK (extracellular-signal-regulated kinase) activation and expression of a luciferase reporter plasmid driven by the c-fos SRE (serum response element), indicating that interaction of SHP-2 with Gab2 is required for ERK activation in response to IL-2. Tyrosine 23-26 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 69-74 15170389-4 2004 Expression of the Gab2 Tyr-614-->Phe (Y614F) mutant, defective in SHP-2 association, prevents ERK (extracellular-signal-regulated kinase) activation and expression of a luciferase reporter plasmid driven by the c-fos SRE (serum response element), indicating that interaction of SHP-2 with Gab2 is required for ERK activation in response to IL-2. Tyrosine 23-26 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 281-286 15349900-4 2004 Treatment of Huh7 transfectants with EGF or HGF induced tyrosine phosphorylation of SIRPalpha1 and its association with SHP-2, which were accompanied by reduced ERK1 activation. Tyrosine 56-64 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 120-125 15240681-0 2004 SHP-1 and SHP-2 associate with immunoreceptor tyrosine-based switch motif of programmed death 1 upon primary human T cell stimulation, but only receptor ligation prevents T cell activation. Tyrosine 46-54 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 10-15 16181551-3 2005 The tyrosine phosphorylation of SHP2 was examined by immunoprecipitation. Tyrosine 4-12 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 32-36 15528274-8 2005 Ligand occupancy of alphaVbeta3 stimulates tyrosine phosphorylation of the beta3-subunit, resulting in recruitment of SHP-2. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 118-123 15528274-11 2005 This transfer requires IGF-I receptor-mediated tyrosine phosphorylation of SHPS-1, which contains two YXXL motifs that mediate SHP-2 binding. Tyrosine 47-55 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 127-132 15557178-6 2004 We then show by site-directed mutagenesis that the membrane-proximal tyrosine motif is essential for the inhibitory function of both Siglec-7 and -9, and is also required for tyrosine phosphorylation and recruitment of SHP-1 and SHP-2 phosphatases. Tyrosine 69-77 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 229-234 15272025-6 2004 The activated SHP-2 then dephosphorylated IRS-1 Tyr(P)-895, resulting in blockade of the pathways from IRS-1/Grb2/Sos to the ERK and p38 MAPK. Tyrosine 48-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 14-19 15194502-3 2004 The ITIM was tyrosine-phosphorylated upon binding of anti-CD155 monoclonal antibody D171, poliovirus, and DNAM-1 (CD226) to human CD155alpha, and recruited SH2-domain-containing tyrosine phosphatase-2 (SHP-2). Tyrosine 13-21 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 202-207 15039022-1 2004 The phosphorylation of tyrosine residues of human red blood cell (RBC) band 3 is regulated in vivo by constitutively active tyrosine-kinases (PTKs) and phosphotyrosine-phosphatases (PTPs), identified so far as, respectively, p72(syk) and p56/53(lyn), and PTP1B and SHPTP-2. Tyrosine 23-31 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 265-272 12972546-6 2003 Notably, Fer induced tyrosine phosphorylation of SHP-2, which is known to bind to the immunoreceptor tyrosine-based inhibitory motif of PECAM-1, and Fer also induced tyrosine phosphorylation of Gab1 (Grb2-associated binder-1). Tyrosine 21-29 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 49-54 14749507-3 2004 LRb initiates signaling via three major mechanisms: 1) Tyr(985) of LRb recruits SH2-containing tyrosine phosphatase (SHP-2); 2) Tyr(1138) of LRb recruits signal transducer and activator of transcription 3 (STAT3); and 3) tyrosine phosphorylation sites on the receptor-associated Jak2 likely recruit numerous undefined signaling proteins. Tyrosine 55-58 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 117-122 14749507-3 2004 LRb initiates signaling via three major mechanisms: 1) Tyr(985) of LRb recruits SH2-containing tyrosine phosphatase (SHP-2); 2) Tyr(1138) of LRb recruits signal transducer and activator of transcription 3 (STAT3); and 3) tyrosine phosphorylation sites on the receptor-associated Jak2 likely recruit numerous undefined signaling proteins. Tyrosine 95-103 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 117-122 14749507-4 2004 The Tyr(985) --> SHP-2 pathway is a major regulator of extracellular signal-regulated kinase (ERK) activation during leptin signaling in cultured cells, while the Tyr(1138) --> STAT3 pathway induces the feedback inhibitor, suppressor of cytokine signaling 3 (SOCS3), as well as important positive effectors of leptin action. Tyrosine 4-7 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 20-25 12923167-7 2003 Immunoblot analyses confirm that Tyr-542 and Tyr-580 are the major sites of Shp2 tyrosyl phosphorylation and that Tyr-542 is the major Grb2 binding site. Tyrosine 33-36 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 76-80 12923167-7 2003 Immunoblot analyses confirm that Tyr-542 and Tyr-580 are the major sites of Shp2 tyrosyl phosphorylation and that Tyr-542 is the major Grb2 binding site. Tyrosine 45-48 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 76-80 12923167-7 2003 Immunoblot analyses confirm that Tyr-542 and Tyr-580 are the major sites of Shp2 tyrosyl phosphorylation and that Tyr-542 is the major Grb2 binding site. Tyrosine 45-48 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 76-80 12791772-0 2003 Tyrosine phosphorylation of the beta3-subunit of the alphaVbeta3 integrin is required for embrane association of the tyrosine phosphatase SHP-2 and its further recruitment to the insulin-like growth factor I receptor. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 138-143 14967142-6 2004 In Shp2-deficient cells, SFK inhibitory C-terminal tyrosines are hyperphosphorylated, and the tyrosyl phosphorylation of multiple SFK substrates, including Plcgamma1, is decreased. Tyrosine 51-60 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 3-7 14732700-3 2004 We show that the ITIM of Ly49Q can recruit SHP-2 and SHP-1 in a tyrosine phosphorylation-dependent manner. Tyrosine 64-72 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 43-48 14522994-2 2003 We report that SHP-2 dephosphorylates tyrosine (Tyr-1007) of Jak2 kinase, a critical recruitment site for the ubiquitin ligase-associated inhibitory protein suppressor of cytokine signaling-1 (SOCS-1), thereby contributing to Jak2 stability. Tyrosine 38-46 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 15-20 14522994-2 2003 We report that SHP-2 dephosphorylates tyrosine (Tyr-1007) of Jak2 kinase, a critical recruitment site for the ubiquitin ligase-associated inhibitory protein suppressor of cytokine signaling-1 (SOCS-1), thereby contributing to Jak2 stability. Tyrosine 48-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 15-20 14522994-3 2003 Inactivation of SHP-2 function by blocking receptor/SHP-2 association or by using a catalytically inactive mutant of SHP-2 led to a marked increase in Jak2 ubiquitination/degradation, Jak2 phosphorylation on Tyr-1007, and Jak2/SOCS-1 association. Tyrosine 208-211 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 16-21 14652006-10 2003 Thus, similar to the bisphosphoryl tyrosine-based activation motif (BTAM) by which the Grb-2 associated binder (Gab1), PDGF receptor, and PECAM-1 recruit SHP-2, BTLA also relies on dual ITIMs for its association with the phosphatases SHP-1 and SHP-2. Tyrosine 35-43 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 154-159 14652006-10 2003 Thus, similar to the bisphosphoryl tyrosine-based activation motif (BTAM) by which the Grb-2 associated binder (Gab1), PDGF receptor, and PECAM-1 recruit SHP-2, BTLA also relies on dual ITIMs for its association with the phosphatases SHP-1 and SHP-2. Tyrosine 35-43 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 244-249 12893640-3 2003 The recent demonstration that PECAM-1 tyrosine phosphorylation occurs in cells exposed to the reactive oxygen species hydrogen peroxide (H2O2) suggested that this form of oxidative stress may also support PECAM-1/SHP-2 complex formation. Tyrosine 38-46 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 213-218 12893640-4 2003 In the present study, we show that PECAM-1 tyrosine phosphorylation in response to exposure of cells to H2O2 is reversible, involves a shift in the balance between kinase and phosphatase activities, and supports binding of SHP-2 and recruitment of this phosphatase to cell-cell borders. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 223-228 12893640-6 2003 Finally, we provide evidence that PECAM-1 tyrosine phosphorylation and SHP-2 binding in endothelial cells requires exposure to an "oxidative burst" of H2O2, but that exposure of these cells to sufficiently high concentrations of H2O2 for a sufficiently long period of time abrogates binding of SHP-2 to tyrosine-phosphorylated PECAM-1. Tyrosine 303-311 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 71-76 12972546-6 2003 Notably, Fer induced tyrosine phosphorylation of SHP-2, which is known to bind to the immunoreceptor tyrosine-based inhibitory motif of PECAM-1, and Fer also induced tyrosine phosphorylation of Gab1 (Grb2-associated binder-1). Tyrosine 101-109 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 49-54 12972546-6 2003 Notably, Fer induced tyrosine phosphorylation of SHP-2, which is known to bind to the immunoreceptor tyrosine-based inhibitory motif of PECAM-1, and Fer also induced tyrosine phosphorylation of Gab1 (Grb2-associated binder-1). Tyrosine 101-109 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 49-54 12972574-4 2003 Surface plasmon resonance and mutation analyses revealed that SHP-2 directly associated with phosphorylated tyrosine 228 and 312, which are located in sst2 ITIMs (immunoreceptor tyrosine-based inhibitory motifs). Tyrosine 108-116 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 62-67 12972574-4 2003 Surface plasmon resonance and mutation analyses revealed that SHP-2 directly associated with phosphorylated tyrosine 228 and 312, which are located in sst2 ITIMs (immunoreceptor tyrosine-based inhibitory motifs). Tyrosine 178-186 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 62-67 12697669-3 2003 Ligand occupancy of these three proteins influences the recruitment of the phosphatase SHP-2 to the IGF-I receptor and thereby modulates the duration of IGF-I receptor tyrosine phosphorylation. Tyrosine 168-176 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 87-92 12731888-0 2003 Chemical dissection of the effects of tyrosine phosphorylation of SHP-2. Tyrosine 38-46 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 66-71 12731888-1 2003 The regulation of the protein tyrosine phosphatase (PTPase) SHP-2 by tyrosine phosphorylation has been difficult to elucidate because of the intrinsic instability of the phosphoprotein. Tyrosine 30-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 60-65 12731888-2 2003 In the past, expressed protein ligation has been used to site-specifically incorporate the phosphotyrosine mimic Pmp (phosphonomethylene phenylalanine) into the two tyrosine phosphorylation sites (542, 580) of SHP-2 one at a time to analyze the effects on catalytic behavior. Tyrosine 98-106 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 210-215 12721296-5 2003 Using a combination of immunoblotting, immunoprecipitation, and immunostaining we show that SHP-2 is present in nascent focal adhesions and undergoes phosphorylation on tyrosine 542 in response to IL-1 stimulation. Tyrosine 169-177 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 92-97 12615921-4 2003 Using tyrosine-phosphorylated peptides derived from Stat5A, we were able to purify protein-tyrosine phosphatase Shp-2 from cell lysates. Tyrosine 6-14 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 112-117 12615921-5 2003 Shp-2, but not Shp-1, specifically interacted with Stat5A in vivo, and the interaction was tyrosine phosphorylation-dependent. Tyrosine 91-99 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 12687608-8 2003 The strategy was succesfully applied to the model protein SHP2 tyrosine phosphatase interacting with an immunoreceptor tyrosine-based inhibitory motif sequence of the sst2 somatostatin receptor. Tyrosine 63-71 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 58-62 12684038-1 2003 PZR is an immunoglobulin superfamily protein that specifically binds tyrosine phosphatase SHP-2 through its intracellular immunoreceptor tyrosine-based inhibitory motifs (ITIMs). Tyrosine 69-77 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 90-95 12410637-6 2003 The PZR intracellular domain contains two SHP-2 binding immunoreceptor tyrosine-based inhibitory motifs (VIY(246)AQL and VVY(263)ADI) which are not present in PZRa and PZRb. Tyrosine 71-79 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 42-47 12522132-12 2003 In summary, Tyr-319 of the AT1 receptor is phosphorylated in response to Ang II and plays a key role in mediating Ang II-induced transactivation of EGFR and cell proliferation, possibly through its interaction with SHP-2 and EGFR. Tyrosine 12-15 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 215-220 12444928-3 2003 Tyr-568 has previously been identified as the binding site of the Src family of tyrosine kinases, the Csk-homologous kinase CHK, and the protein tyrosine phosphatase SHP-2. Tyrosine 0-3 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 166-171 12531430-1 2003 SHP-2, a cytosolic protein tyrosine phosphatase with two SH2 domains and multiple tyrosine phosphorylation sites, contributes to signal transduction as an enzyme and/or adaptor molecule. Tyrosine 27-35 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 12531430-5 2003 The recruitment of p29 to SHP-2 requires the carboxy-terminal tyrosine residues of SHP-2 (Y(546) and Y(584)). Tyrosine 62-70 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 26-31 12531430-5 2003 The recruitment of p29 to SHP-2 requires the carboxy-terminal tyrosine residues of SHP-2 (Y(546) and Y(584)). Tyrosine 62-70 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 83-88 12650772-2 2003 Similar to mammalian Gab protein, tyrosine-phosphorylated CagA recruits and activates SHP-2 phosphatase at the plasma membrane, thereby inducing a growth factor-like effect. Tyrosine 34-42 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 86-91 12403768-0 2003 SHP2 and SOCS3 contribute to Tyr-759-dependent attenuation of interleukin-6 signaling through gp130. Tyrosine 29-32 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 12535670-4 2003 We found that PECAM-1 is dephosphorylated on tyrosine 686 during endothelial migration, resulting in diffuse dispersal of PECAM-1 and SHP-2. Tyrosine 45-53 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 134-139 12535670-9 2003 Thus homophilically engaged, tyrosine-phosphorylated PECAM-1 locally activates SHP-2 at cell-cell junctions; with disruption of the endothelial monolayer, selective dephosphorylation of PECAM-1 leads to redistribution of SHP-2 and pro-migratory changes in phosphorylation of cytoskeletal and focal contact components. Tyrosine 29-37 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 79-84 12535670-9 2003 Thus homophilically engaged, tyrosine-phosphorylated PECAM-1 locally activates SHP-2 at cell-cell junctions; with disruption of the endothelial monolayer, selective dephosphorylation of PECAM-1 leads to redistribution of SHP-2 and pro-migratory changes in phosphorylation of cytoskeletal and focal contact components. Tyrosine 29-37 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 221-226 12552462-3 2003 Tyrosine-phosphorylated CagA and CagA-coimmunoprecipitated SHP-2 were detected in gastric mucosa from H. pylori-positive patients with atrophic gastritis and in noncancerous tissues from H. pylori-positive patients with early gastric cancer. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 59-64 12403768-3 2003 Because this site is known to be a recruitment motif for the protein-tyrosine phosphatase SHP2, it has been suggested that SHP2 is the mediator of tyrosine 759-dependent signal attenuation. Tyrosine 69-77 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 90-94 12403768-3 2003 Because this site is known to be a recruitment motif for the protein-tyrosine phosphatase SHP2, it has been suggested that SHP2 is the mediator of tyrosine 759-dependent signal attenuation. Tyrosine 69-77 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 123-127 12220227-1 2002 Signalling by the insulin receptor substrate (IRS) proteins is critically dependent on the tyrosine phosphorylation of specific binding sites that recruit Src homology 2 (SH2)-domain-containing proteins, such as the p85 subunit of phosphoinositide 3-kinase (PI 3-kinase), the tyrosine phosphatase SHP-2 and the adapter protein Grb2. Tyrosine 91-99 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 297-302 12119038-1 2002 Suppressor of cytokine signaling-3 (SOCS-3) and the protein tyrosine phosphatase SHP-2 both regulate signaling by cytokines of the interleukin-6 family, and this is dependent upon recruitment to tyrosine 757 in the shared cytokine receptor subunit gp130. Tyrosine 60-68 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 81-86 12270932-9 2002 Our findings demonstrate that SHP-2 is a dual-specificity protein phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues and plays an important role in modulating STAT function in gene regulation. Tyrosine 122-130 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 30-35 12177047-5 2002 When PECAM-1 is tyrosine phosphorylated by FSS or osmotic changes, SHP-2 binds to it. Tyrosine 16-24 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 67-72 12270932-0 2002 SHP-2 is a dual-specificity phosphatase involved in Stat1 dephosphorylation at both tyrosine and serine residues in nuclei. Tyrosine 84-92 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 12270932-7 2002 Consistently, purified GST-SHP-2 dephosphorylated Stat1 at both tyrosine and serine residues when immunoprecipitated phospho-Stat1 or a peptide corresponding to the sequence surrounding Tyr(P)(701) or Ser(P)(727) of Stat1 was used as the substrate. Tyrosine 64-72 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 27-32 12270932-7 2002 Consistently, purified GST-SHP-2 dephosphorylated Stat1 at both tyrosine and serine residues when immunoprecipitated phospho-Stat1 or a peptide corresponding to the sequence surrounding Tyr(P)(701) or Ser(P)(727) of Stat1 was used as the substrate. Tyrosine 186-189 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 27-32 12177051-5 2002 Using surface plasmon resonance analysis, we observed that an immunoreceptor tyrosine-based inhibitory motif (ITIM) located in the C-terminal part of the B2 receptor interacted specifically with the protein-tyrosine phosphatase SHP-2. Tyrosine 77-85 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 228-233 12207897-0 2002 Nitration of PECAM-1 ITIM tyrosines abrogates phosphorylation and SHP-2 binding. Tyrosine 26-35 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 66-71 12207897-1 2002 Platelet-endothelial cell adhesion molecule-1 (PECAM-1) is a cell adhesion molecule with a cytoplasmic immunoreceptor tyrosine-based inhibitory motif (ITIM) that, when phosphorylated, binds Src homology 2 domain-containing protein-tyrosine phosphatase (SHP-2). Tyrosine 118-126 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 253-258 12060651-3 2002 In addition, overexpression studies indicate that the carboxyl-terminal SH2 domain of SHP-2 is required to maintain tyrosine phosphorylation of Stat5 and its interaction with SHP-2. Tyrosine 116-124 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 86-91 12060651-3 2002 In addition, overexpression studies indicate that the carboxyl-terminal SH2 domain of SHP-2 is required to maintain tyrosine phosphorylation of Stat5 and its interaction with SHP-2. Tyrosine 116-124 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 175-180 11896055-7 2002 Furthermore, overexpression of a catalytically inactive form of SHP2 or pretreatment with pervanadate markedly increased EGF-stimulated Gab1 tyrosine phosphorylation. Tyrosine 141-149 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 64-68 12124436-0 2002 Shp-2 positively regulates brain-derived neurotrophic factor-promoted survival of cultured ventral mesencephalic dopaminergic neurons through a brain immunoglobulin-like molecule with tyrosine-based activation motifs/Shp substrate-1. Tyrosine 184-192 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 12070037-3 2002 In this study, we show that Tyr phosphorylation of band 3, elicited by pervanadate, N-ethylmaleimide, or diamide, greatly increases band-3 interaction with the tyrosine phosphatase SHP-2 in parallel with the translocation of SHP-2 to erythrocyte membranes. Tyrosine 28-31 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 181-186 12070037-3 2002 In this study, we show that Tyr phosphorylation of band 3, elicited by pervanadate, N-ethylmaleimide, or diamide, greatly increases band-3 interaction with the tyrosine phosphatase SHP-2 in parallel with the translocation of SHP-2 to erythrocyte membranes. Tyrosine 28-31 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 225-230 12070037-4 2002 These events seem to be mediated by Src-like catalyzed phosphorylation of band 3 because both SHP-2 translocation to cellular membranes and its interaction with Tyr-phosphorylated protein are greatly counteracted by PP2, a specific inhibitor of Src kinases. Tyrosine 161-164 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 94-99 12070037-7 2002 Experiments performed with intact erythrocytes in the presence of the SHP-2 inhibitor calpeptin suggest that, once recruited to Tyr-phosphorylated band 3, the tyrosine phosphatase dephosphorylates the protein. Tyrosine 128-131 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 70-75 11602579-7 2001 Tyrosine 603 plays an important role in mediating the association of E-selectin with SHP2, and the catalytic domain of SHP2 is, in turn, critical for E-selectin-dependent ERK1/2 activation. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 85-89 12051764-6 2002 Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 173-178 11751924-5 2002 Tyrosine phosphorylation of PZR was accompanied by recruitment of SHP-2 and was inhibited by PP1, a selective inhibitor of the Src family tyrosine kinases. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 66-71 11830491-6 2002 Activation of the c-fos SRE transcriptional activity by Gab2 required tyrosine 604, which is a SHP2 docking site on Gab2, and the SHP2 tyrosine phosphatase activity. Tyrosine 70-78 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 95-99 11602579-7 2001 Tyrosine 603 plays an important role in mediating the association of E-selectin with SHP2, and the catalytic domain of SHP2 is, in turn, critical for E-selectin-dependent ERK1/2 activation. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 119-123 11733002-10 2001 Further experiments with cell extracts suggest that SHP-1 interacts with Y667 and SHP-2 interacts with Y667 in addition to another tyrosine. Tyrosine 131-139 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 82-87 11695994-10 2001 Taken together, our data indicate that PI 3-kinase and Src-family tyrosine kinases regulate ET-1-induced Gab1 tyrosine phosphorylation, which, in turn, induces ERK1 activation via PI 3-kinase- and SHP-2-dependent pathways. Tyrosine 66-74 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 197-202 11704759-0 2001 Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Tyrosine 42-50 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 13-19 11704759-0 2001 Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Tyrosine 42-50 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 63-68 11328818-6 2001 Upon tyrosine phosphorylation, S2V recruits both Src homology 2 (SH2) domain-containing protein-tyrosine phosphatases SHP-1 and SHP-2, two important inhibitory regulators of immunoreceptor signal transduction. Tyrosine 5-13 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 128-133 11544253-11 2001 Mutagenesis studies showed that phosphorylation of tyrosine 211 is critical for the interaction of G6b with SHP-1 and SHP-2. Tyrosine 51-59 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 118-123 11533026-5 2001 Indeed, the NH2-terminal SH2 domain of the Shp2 tyrosine phosphatase bound specifically to a Tyr(568) RCM phosphopeptide. Tyrosine 93-96 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 43-47 11533026-8 2001 These results suggest that netrin-stimulated phosphorylation of RCM Tyr(568) recruits Shp2 to the cell membrane where it can potentially modify RCM phosphorylation and function. Tyrosine 68-71 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 86-90 11335710-7 2001 Expression of Deltap85 led to a reduction in SHP2 tyrosine phosphorylation and its ability to interact with Grb2 and Gab2 but increased overall tyrosine phosphorylation of Gab2. Tyrosine 50-58 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 45-49 11684012-0 2001 Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling. Tyrosine 40-48 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 104-109 11684012-1 2001 The regulation of protein tyrosine phosphatase (PTPase) SHP-2 is proposed to involve tyrosine phosphorylation on two tail tyrosine residues. Tyrosine 26-34 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 56-61 11684012-1 2001 The regulation of protein tyrosine phosphatase (PTPase) SHP-2 is proposed to involve tyrosine phosphorylation on two tail tyrosine residues. Tyrosine 85-93 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 56-61 11684012-4 2001 Microinjection experiments indicate that a single phosphorylation of Tyr-542 of SHP-2 is sufficient to activate the MAP kinase pathway in living cells. Tyrosine 69-72 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 80-85 11323411-0 2001 Phosphotyrosines 627 and 659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) conferring binding and activation of SHP2. Tyrosine 7-15 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 140-144 11323411-4 2001 We found that both Tyr-627 and Tyr-659 of Gab1 were required for SHP2 binding to Gab1 and for ERK2 activation by EGF. Tyrosine 19-22 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 65-69 11323411-4 2001 We found that both Tyr-627 and Tyr-659 of Gab1 were required for SHP2 binding to Gab1 and for ERK2 activation by EGF. Tyrosine 31-34 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 65-69 11323411-5 2001 Far Western blot analysis suggested that the tandem SH2 domains of SHP2 bind to Gab1 in a specific orientation, in which the N-SH2 domain binds to phosphotyrosine (Tyr(P))-627 and the C-SH2 domain binds to Tyr(P)-659. Tyrosine 164-167 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 67-71 11323411-5 2001 Far Western blot analysis suggested that the tandem SH2 domains of SHP2 bind to Gab1 in a specific orientation, in which the N-SH2 domain binds to phosphotyrosine (Tyr(P))-627 and the C-SH2 domain binds to Tyr(P)-659. Tyrosine 206-209 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 67-71 11402314-1 2001 In this study, we show that upon thrombopoietin (Tpo) stimulation the two adapter proteins Gab1 and Gab2 are strongly tyrosine phosphorylated and associated with Shc, SHP2, PI 3-kinase and Grb2 in mpl-expressing UT7 cells. Tyrosine 118-126 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 167-171 11323411-6 2001 When assayed with peptide substrates, SHP2 PTPase was activated by a bisphosphopeptide containing both Tyr(P)-627 and Tyr(P)-659, but not by monophosphopeptides containing Tyr(P)-627 or Tyr(P)-659 or a mixture of these monophosphopeptides. Tyrosine 103-106 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 38-42 11323411-6 2001 When assayed with peptide substrates, SHP2 PTPase was activated by a bisphosphopeptide containing both Tyr(P)-627 and Tyr(P)-659, but not by monophosphopeptides containing Tyr(P)-627 or Tyr(P)-659 or a mixture of these monophosphopeptides. Tyrosine 118-121 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 38-42 11323411-6 2001 When assayed with peptide substrates, SHP2 PTPase was activated by a bisphosphopeptide containing both Tyr(P)-627 and Tyr(P)-659, but not by monophosphopeptides containing Tyr(P)-627 or Tyr(P)-659 or a mixture of these monophosphopeptides. Tyrosine 118-121 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 38-42 11323411-6 2001 When assayed with peptide substrates, SHP2 PTPase was activated by a bisphosphopeptide containing both Tyr(P)-627 and Tyr(P)-659, but not by monophosphopeptides containing Tyr(P)-627 or Tyr(P)-659 or a mixture of these monophosphopeptides. Tyrosine 118-121 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 38-42 11323411-7 2001 These results suggest that Tyr(P)-627 and Tyr(P)-659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) that binds and activates SHP2. Tyrosine 27-30 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 152-156 11323411-7 2001 These results suggest that Tyr(P)-627 and Tyr(P)-659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) that binds and activates SHP2. Tyrosine 42-45 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 152-156 11323411-7 2001 These results suggest that Tyr(P)-627 and Tyr(P)-659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) that binds and activates SHP2. Tyrosine 88-96 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 152-156 11433379-3 2001 Indeed, it has recently been demonstrated that SIT inducibly interacts with the SH2-containing protein tyrosine phosphatase 2 (SHP2) via an immunoreceptor tyrosine-based inhibition motif (ITIM). Tyrosine 103-111 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 127-131 11388808-4 2001 The cytoplasmic domain of PECAM-1 contains an immunoreceptor tyrosine-based inhibitory motif that, upon tyrosine phosphorylation, supports recruitment of the Src homology 2 domain-containing protein tyrosine phosphatase, SHP-2. Tyrosine 61-69 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 221-226 11294897-6 2001 Addition of a single tyrosine residue, Y724, restored its ability to stimulate cellular transformation, phosphatidylinositol 3-kinase activation, and phosphorylation of Shp2, MAPK, Stat1, and Stat3. Tyrosine 21-29 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 169-173 11342028-1 2001 Signalling through the leptin receptor has been shown to activate the SH2 domain-containing tyrosine phosphatase SHP-2 through tyrosine phosphorylation. Tyrosine 92-100 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 113-118 11268587-7 2001 Phosphorylation of 985- and 1138-tyrosine of long-form leptin receptor activates SHP-2 and STAT3, respectively. Tyrosine 33-41 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 81-86 11085989-4 2001 SHP-2, lacking two C-terminal tyrosine residues, partially inhibits ERK phosphorylation. Tyrosine 30-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 11085989-9 2001 The phosphatase activity of SHP-2 is required for both pathways, whereas activation of ERK via Tyr-985 of ObRb also requires tyrosine phosphorylation of SHP-2. Tyrosine 95-98 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 28-33 11085989-9 2001 The phosphatase activity of SHP-2 is required for both pathways, whereas activation of ERK via Tyr-985 of ObRb also requires tyrosine phosphorylation of SHP-2. Tyrosine 95-98 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 153-158 11085989-9 2001 The phosphatase activity of SHP-2 is required for both pathways, whereas activation of ERK via Tyr-985 of ObRb also requires tyrosine phosphorylation of SHP-2. Tyrosine 125-133 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 28-33 11085989-9 2001 The phosphatase activity of SHP-2 is required for both pathways, whereas activation of ERK via Tyr-985 of ObRb also requires tyrosine phosphorylation of SHP-2. Tyrosine 125-133 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 153-158 11342028-5 2001 Only the leptin receptor-derived peptide corresponding to tyrosine 974 was dephosphorylated by recombinant purified SHP-2. Tyrosine 58-66 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 116-121 11157475-6 2001 Further studies revealed that SDF-1alpha stimulation induced robust tyrosine phosphorylation in the SH2-containing phosphatase SHP2. Tyrosine 68-76 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 127-131 10991949-0 2000 Recruitment of the protein-tyrosine phosphatase SHP-2 to the C-terminal tyrosine of the prolactin receptor and to the adaptor protein Gab2. Tyrosine 27-35 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 48-53 11018044-2 2000 Phosphorylated Tyr(1138) binds STAT3 to mediate its tyrosine phosphorylation and transcriptional activation, while phosphorylated Tyr(985) binds the tyrosine phosphatase SHP-2 and reportedly mediates both activation of ERK kinases and inhibition of LRb-mediated STAT3 activation. Tyrosine 130-133 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 170-175 10991949-6 2000 Together, these studies suggest the presence of dual recruitment sites for SHP-2; the first is to the C-terminal tyrosine of the PRLR and the second is to the adaptor protein Gab2. Tyrosine 113-121 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 75-80 11196191-12 2001 On IL-6 stimulation, SHP-2 and Gab1 were recruited to the gp130 subunit of the IL-6 receptor and tyrosine phosphorylated, allowing downstream signaling to the MAPK and PI3K pathways. Tyrosine 97-105 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 21-26 11027663-4 2000 They interact with tyrosine-phosphorylated Shp-2, p85, Grb2, and Shc. Tyrosine 19-27 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 43-48 10995764-7 2000 Ligand stimulation of neuronal cells induced the assembly of a large protein complex containing c-Ret, Grb2, and tyrosine-phosphorylated forms of Shc, p85(PI3K), the adaptor Gab2, and the protein-tyrosine phosphatase SHP-2. Tyrosine 113-121 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 217-222 10995764-9 2000 These results indicate that upon ligand stimulation, at least two distinct protein complexes assemble on phosphorylated Tyr-1062 of c-Ret via Shc, one leading to activation of the Ras/Erk pathway through recruitment of Grb2/Sos and another to the PI3K/Akt pathway through recruitment of Grb2/Gab2 followed by p85(PI3K) and SHP-2. Tyrosine 120-123 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 323-328 10880513-6 2000 We demonstrate that RAFTK is a direct substrate of SHP2 both in vitro and in vivo, and that Tyr(906) in the C-terminal domain of RAFTK mediates its interaction with SHP2. Tyrosine 92-95 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 165-169 10864922-2 2000 In our studies, the ligation of Fg to ICAM-1 on tumor necrosis factor-alpha-stimulated endothelial cells resulted in the tyrosine phosphorylation of Src homology domain 2 (SH2)-containing phosphatase-2 (SHP-2). Tyrosine 121-129 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 203-208 10864922-3 2000 The ICAM-1 cytoplasmic sequence IKKYRLQ conforms poorly to the concensus immunoreceptor tyrosine-based inhibition motifs found in receptors that bind SHP-2. Tyrosine 88-96 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 150-155 10864922-4 2000 Nevertheless, the tyrosine phosphorylated sequence (IKKpYRLQ) bound specifically to the SH2 domain proximal to the NH(2)-terminal of SHP-2 (SHP-2-N) but not to the SH2 domain proximal on the COOH-terminal side (SHP-2-C). Tyrosine 18-26 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 133-138 10864922-4 2000 Nevertheless, the tyrosine phosphorylated sequence (IKKpYRLQ) bound specifically to the SH2 domain proximal to the NH(2)-terminal of SHP-2 (SHP-2-N) but not to the SH2 domain proximal on the COOH-terminal side (SHP-2-C). Tyrosine 18-26 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 140-147 10864922-4 2000 Nevertheless, the tyrosine phosphorylated sequence (IKKpYRLQ) bound specifically to the SH2 domain proximal to the NH(2)-terminal of SHP-2 (SHP-2-N) but not to the SH2 domain proximal on the COOH-terminal side (SHP-2-C). Tyrosine 18-26 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 140-145 11035084-2 2000 Previous studies concluded that inhibitory signal transduction by FcgammaRIIB is mediated solely by its immunoreceptor tyrosine-based inhibition motif (ITIM) that, when phosphorylated, recruits the SH2-containing inositol 5"- phosphatase SHIP and the SH2-containing tyrosine phosphatases SHP-1 and SHP-2. Tyrosine 119-127 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 298-303 10849428-5 2000 We further demonstrate that phosphorylation of both Gab2 and SHP-2 is largely dependent upon tyrosine 338 of the IL-2 receptor beta chain. Tyrosine 93-101 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 61-66 10946280-1 2000 Stimulation of the IL-6R complex leads to Src homology domain containing tyrosine phosphatase 2 (SHP2) recruitment to the receptor subunit gp130 and its subsequent tyrosine phosphorylation. Tyrosine 73-81 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 97-101 10946280-8 2000 Interestingly, one SHP2-recruiting phosphotyrosine motif in a single chain of the gp130 dimer is sufficient to mediate SHP2 association to the gp130 receptor subunit and its tyrosine phosphorylation as well as to attenuate IL-6-dependent gene induction. Tyrosine 42-50 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 19-23 10946280-8 2000 Interestingly, one SHP2-recruiting phosphotyrosine motif in a single chain of the gp130 dimer is sufficient to mediate SHP2 association to the gp130 receptor subunit and its tyrosine phosphorylation as well as to attenuate IL-6-dependent gene induction. Tyrosine 42-50 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 119-123 10946280-4 2000 Tyrosine 759 of gp130, the signal transducing subunit of the IL-6R complex, is essential for the phosphorylation of SHP2. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 116-120 10946280-7 2000 We also tested whether the tyrosine 759 motifs in both subunits of the gp130 dimer are required for SHP2 association and tyrosine phosphorylation. Tyrosine 27-35 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 100-104 10833515-7 2000 Further, stimulation of untransformed cells with H(2)O(2) or pervanadate increased tyrosine phosphorylation of each of the most prominent known substrates of BCR/ABL, including c-ABL, c-CBL, SHC, and SHP-2. Tyrosine 83-91 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 200-205 10887109-3 2000 When phosphorylated, these tyrosines could function as docking sites for the phosphatases, SHP-1 and/or SHP-2, enabling CD33 to function as an inhibitory receptor. Tyrosine 27-36 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 104-109 10887109-4 2000 Here we demonstrate that CD33 is tyrosine phosphorylated in the presence of the phosphatase inhibitor, pervanadate, and recruits SHP-1 and SHP-2. Tyrosine 33-41 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 139-144 10764798-8 2000 In the present study we demonstrate that in addition to STAT3, also tyrosine phosphorylation of STAT1, signal transducer gp130, and phosphotyrosine-phosphatase SHP2 underlies negative regulation by MAP kinases. Tyrosine 68-76 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 160-164 10800945-2 2000 gp130 and LIFR contain consensus binding motifs for the protein tyrosine phosphatase SHP-2 surrounding tyrosines 118 and 115 (Y118 and Y115) of their cytoplasmic domains, respectively. Tyrosine 103-112 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 85-90 10842319-3 2000 Some signaling molecules such as Src homology 2 protein tyrosine phosphatase 2 (SHP-2) and the p85 subunit of phosphatidylinositol 3 kinase (PI3 kinase) associate with phosphorylated tyrosine residue Y-165, through Src homology 2 (SH2) domains. Tyrosine 56-64 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 80-85 10800945-6 2000 Mutation of Y115 of the cytoplasmic domain of LIFR eliminates receptor-mediated tyrosine phosphorylation of SHP-2. Tyrosine 80-88 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 108-113 10777583-6 2000 Furthermore, we show that tyrosine 759 in gp130 is essential for both SHP2 and SOCS3 but not for SOCS1 to exert their inhibitory activities on interleukin-6 signal transduction. Tyrosine 26-34 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 70-74 10722671-10 2000 Thus, the balance of Pyk2 tyrosine phosphorylation in response to Ang II is controlled by Yes kinase and by a tyrosine phosphatase SHP-2 in endothelial cells. Tyrosine 26-34 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 131-136 10655627-7 2000 The present approach will thus become a general method for screening agonists for one specific pathway in tyrosine phosphorylation of IRS-1 in insulin signaling, which is regulated by specific protein-protein interaction between a phosphorylated tyrosine in IRS-1 and its corresponding SH2 domain-containing protein such as PI-3 kinase, Grb2-Sos, or SHP2. Tyrosine 106-114 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 350-354 10681592-4 2000 Thrombin treatment of human umbilical vein endothelial cells promotes SHP2 tyrosine phosphorylation and dissociation from VE-cadherin complexes. Tyrosine 75-83 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 70-74 10681592-5 2000 The loss of SHP2 from the cadherin complexes correlates with a dramatic increase in the tyrosine phosphorylation of beta-catenin, gamma-catenin, and p120-catenin complexed with VE-cadherin. Tyrosine 88-96 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 12-16 10681592-6 2000 We propose that thrombin regulates the tyrosine phosphorylation of VE-cadherin-associated beta-catenin, gamma-catenin, and p120-catenin by modulating the quantity of SHP2 associated with VE-cadherin complexes. Tyrosine 39-47 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 166-170 10623804-2 2000 In vitro peptide binding experiments using phosphotyrosine-containing sequences derived from the immunoreceptor tyrosine-based inhibitory motif (ITIM) known to mediate Fc gamma RIIB1 effects suggest that the receptor uses SH2-containing inositol phosphatase (SHIP) and SH2-containing phosphotyrosine phosphatase (SHP)-1, as well as SHP-2 as effectors. Tyrosine 50-58 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 332-337 10650943-3 2000 Shp-2 becomes activated upon binding through one or both SH2 domains to tyrosine phosphorylated molecules such as Shc or insulin receptor substrates. Tyrosine 72-80 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 10650943-4 2000 We were interested in finding a new molecule(s), tyrosine phosphorylated by the insulin receptor (IR), that could interact with Shp-2. Tyrosine 49-57 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 128-133 10650943-15 2000 Moreover, in intact cells insulin stimulates tyrosine phosphorylation of FRS2 and its subsequent association with Shp-2. Tyrosine 45-53 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 114-119 10617656-10 2000 Furthermore, tyrosine-phosphorylated STAT5 associates with the substrate-trapping mutant (Cys --> Ser) of SHP-2 but not SHP-1. Tyrosine 13-21 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 109-114 10949653-6 2000 However, on formation the endodomain physically associates with a number of tyrosine phosphorylated signalling intermediates including the tyrosine phosphatase and adaptor protein SHP2. Tyrosine 76-84 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 180-184 10655627-7 2000 The present approach will thus become a general method for screening agonists for one specific pathway in tyrosine phosphorylation of IRS-1 in insulin signaling, which is regulated by specific protein-protein interaction between a phosphorylated tyrosine in IRS-1 and its corresponding SH2 domain-containing protein such as PI-3 kinase, Grb2-Sos, or SHP2. Tyrosine 246-254 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 350-354 10542280-6 1999 Furthermore, the tyrosine phosphorylation and activities of the SHP-1 and SHP-2 tyrosine phosphatases, enzymes that regulate Ang II-induced JAK2 tyrosine phosphorylation, are altered by HG. Tyrosine 17-25 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 74-79 10542280-6 1999 Furthermore, the tyrosine phosphorylation and activities of the SHP-1 and SHP-2 tyrosine phosphatases, enzymes that regulate Ang II-induced JAK2 tyrosine phosphorylation, are altered by HG. Tyrosine 80-88 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 74-79 10508911-0 1999 Thrombin-induced association of SHP-2 with multiple tyrosine-phosphorylated proteins in human platelets. Tyrosine 52-60 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 32-37 10514514-3 1999 In the present study, we show that besides STAT1 also the tyrosine phosphatase SHP2 became tyrosine-phosphorylated upon hyperosmolarity. Tyrosine 58-66 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 79-83 10514514-6 1999 Accordingly, overexpression of dominant negative mutants of p38 and MKK6 largely decreased hyperosmotic STAT1 activation and tyrosine phosphorylation of SHP2. Tyrosine 125-133 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 153-157 10514514-7 1999 Furthermore, we provide evidence that a genistein-sensitive tyrosine kinase different from Jak1 is involved in stress-activation of STAT1 and tyrosine phosphorylation of SHP2. Tyrosine 60-68 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 170-174 10497192-2 1999 These events are preceded by the ligand-induced tyrosine phosphorylation of the receptor and its association with SH2-containing signaling enzymes including Src family members (Src), the phosphotyrosine phosphatase SHP-2, phosphatidylinositol 3-kinase (PI3K), and phospholipase C-gamma1 (PLCgamma). Tyrosine 48-56 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 215-220 10515388-10 1999 Tyrosine-phosphorylated CD31 complexed with SHP2 and other unidentified phosphoproteins. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 44-48 10449753-7 1999 After cotransfection of Ob-Rb, Janus kinase 2 (JAK2), and SHP-2 into 293T cells, leptin results in direct binding of SHP-2 to the phosphorylated Tyr 985. Tyrosine 145-148 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 58-63 10455108-3 1999 In the present study we provide evidence that the recently cloned IRS-related proteins, Gab1 and Gab2, of the Gab family of proteins, are rapidly phosphorylated on tyrosine during erythropoietin treatment of erythropoietin-responsive cells and provide docking sites for the engagement of the SHP2 phosphatase and the p85 subunit of the phosphatidylinositol 3"-kinase. Tyrosine 164-172 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 292-296 10449753-7 1999 After cotransfection of Ob-Rb, Janus kinase 2 (JAK2), and SHP-2 into 293T cells, leptin results in direct binding of SHP-2 to the phosphorylated Tyr 985. Tyrosine 145-148 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 117-122 10449753-8 1999 The bound SHP-2 is itself tyrosine phosphorylated after leptin treatment. Tyrosine 26-34 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 10-15 10350061-1 1999 Recent studies have shown that, in addition to its role as an adhesion receptor, platelet endothelial cell adhesion molecule 1/CD31 becomes phosphorylated on tyrosine residues Y663 and Y686 and associates with protein tyrosine phosphatases SHP-1 and SHP-2. Tyrosine 158-166 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 250-255 10407071-10 1999 These findings indicate that amphiphilic and hydrophilic PTPases different from PTP1B, PTP1C, PTP1D or RPTPalpha, with higher sedimentation coefficients and with higher activity when O-phosphotyrosine or a synthetic peptide phosphorylated on tyrosine were used as substrates, are present in platelets. Tyrosine 192-200 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 94-99 10457220-3 1999 In another approach, using the entire cytoplasmic domain of the Ly49A receptor, we found that SHP2 also interacted with the tyrosine-phosphorylated form of the Ly49A cytoplasmic tail. Tyrosine 124-132 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 94-98 10457220-4 1999 Using BIACORE(R)2000 analysis, we determined that both SHP1 and SHP2 bound to the tyrosine-phosphorylated cytoplasmic tail of Ly49A with affinities in the nanomolar range, whilst SHIP showed no binding. Tyrosine 82-90 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 64-68 10395658-3 1999 The PECAM-1 cytoplasmic domain contains an immunoreceptor tyrosine-based inhibitory motif (ITIM) that, when appropriately engaged, becomes phosphorylated on tyrosine residues, creating docking sites for nontransmembrane, Src homology 2 domain-bearing protein tyrosine phosphatase (SHP)-1 and SHP-2. Tyrosine 58-66 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 292-297 10382761-6 1999 Moreover, P-ITIM-bound SHP-2 dephosphorylates synthetic peptides corresponding to the sites of tyrosine phosphorylation on SHIP and Shc, indicating that these proteins are its potential substrates. Tyrosine 95-103 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 23-28 10318871-1 1999 SHP-2 is a ubiquitously expressed Src homology-2-containing cytosolic tyrosine phosphatase that binds to and becomes tyrosine-phosphorylated by the activated platelet-derived growth factor receptor-beta (PDGFR-beta). Tyrosine 70-78 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 10329850-8 1999 Adding back each tyrosine to Fall revealed that (1) Tyr577 was necessary and sufficient for Shc phosphorylation; (2) Tyr577, Tyr612, and Tyr695 were involved in activation of SHP-2, the Raf/ERK cascade, and c-fos transcription; and (3) all tyrosines, but particularly Tyr612, Tyr695, Tyr750, and Tyr806, facilitated STAT5 activation. Tyrosine 17-25 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 175-180 10329850-8 1999 Adding back each tyrosine to Fall revealed that (1) Tyr577 was necessary and sufficient for Shc phosphorylation; (2) Tyr577, Tyr612, and Tyr695 were involved in activation of SHP-2, the Raf/ERK cascade, and c-fos transcription; and (3) all tyrosines, but particularly Tyr612, Tyr695, Tyr750, and Tyr806, facilitated STAT5 activation. Tyrosine 240-249 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 175-180 10206955-7 1999 The first CD33 phosphotyrosine motif is dominant in CD33-SHP-1/SHP-2 interactions, since mutating tyrosine 340 in a CD33-cytoplasmic tail fusion protein significantly reduced binding to SHP-1 and SHP-2 in THP-1 lysates, while mutation of tyrosine 358 had no effect. Tyrosine 22-30 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 63-68 10206955-7 1999 The first CD33 phosphotyrosine motif is dominant in CD33-SHP-1/SHP-2 interactions, since mutating tyrosine 340 in a CD33-cytoplasmic tail fusion protein significantly reduced binding to SHP-1 and SHP-2 in THP-1 lysates, while mutation of tyrosine 358 had no effect. Tyrosine 22-30 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 196-201 10206955-7 1999 The first CD33 phosphotyrosine motif is dominant in CD33-SHP-1/SHP-2 interactions, since mutating tyrosine 340 in a CD33-cytoplasmic tail fusion protein significantly reduced binding to SHP-1 and SHP-2 in THP-1 lysates, while mutation of tyrosine 358 had no effect. Tyrosine 98-106 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 63-68 10206955-7 1999 The first CD33 phosphotyrosine motif is dominant in CD33-SHP-1/SHP-2 interactions, since mutating tyrosine 340 in a CD33-cytoplasmic tail fusion protein significantly reduced binding to SHP-1 and SHP-2 in THP-1 lysates, while mutation of tyrosine 358 had no effect. Tyrosine 98-106 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 196-201 10206955-8 1999 Furthermore, the NH2-terminal Src homology 2 domain of SHP-1 and SHP-2, believed to be essential for phosphatase activation, selectively bound a CD33 phosphopeptide containing tyrosine 340 but not one containing tyrosine 358. Tyrosine 176-184 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 65-70 10372132-4 1999 Mutation of each of the 8 tyrosine residues in the cytoplasmic domain of the human GMR beta to phenylalanine (GMR beta-F8) reduced tyrosine phosphorylation of GMR beta, SHP2 and SHC, but not JAK2 or STAT5. Tyrosine 26-34 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 169-173 10206955-8 1999 Furthermore, the NH2-terminal Src homology 2 domain of SHP-1 and SHP-2, believed to be essential for phosphatase activation, selectively bound a CD33 phosphopeptide containing tyrosine 340 but not one containing tyrosine 358. Tyrosine 212-220 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 65-70 10350061-6 1999 These results suggest that overlapping immunoreceptor tyrosine-based inhibition motif/immunoreceptor tyrosine-based activation motif-like motifs within platelet endothelial cell adhesion molecule 1 mediate differential interactions between the Src homology 2 containing signalling proteins SHP-1, SHP-2, SHIP and PLC-gamma1. Tyrosine 54-62 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 297-302 9804835-4 1998 Moreover, tyrosine phosphorylation of Gab1 correlated with the binding of several SH2-containing signaling proteins to Gab1 including Shc, Grb2, phosphatidylinositol 3-kinase, and the SHP-2 tyrosine phosphatase. Tyrosine 10-18 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 184-189 10209036-4 1999 After tyrosine phosphorylation by src and possibly syk protein tyrosine kinases SIT recruits the SH2 domain-containing tyrosine phosphatase SHP2 via an immunoreceptor tyrosine-based inhibition motif. Tyrosine 6-14 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 140-144 10209036-4 1999 After tyrosine phosphorylation by src and possibly syk protein tyrosine kinases SIT recruits the SH2 domain-containing tyrosine phosphatase SHP2 via an immunoreceptor tyrosine-based inhibition motif. Tyrosine 63-71 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 140-144 9923452-7 1999 Both IL-4 and IL-9 stimulated tyrosine phosphorylation of SHP-2, whereas the 90-kD tyrosine phosphorylated protein induced by IL-9 stimulation is Stat3. Tyrosine 30-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 58-63 9867848-6 1999 Association of Bgp1 and SHP-2 involves the Tyr residues within the Bgp1 ITIM sequences, Val at position +3 relative to the second Tyr (Tyr-515), and the SHP-2 N-terminal SH2 domain. Tyrosine 43-46 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 24-29 9867848-6 1999 Association of Bgp1 and SHP-2 involves the Tyr residues within the Bgp1 ITIM sequences, Val at position +3 relative to the second Tyr (Tyr-515), and the SHP-2 N-terminal SH2 domain. Tyrosine 130-133 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 24-29 9867848-6 1999 Association of Bgp1 and SHP-2 involves the Tyr residues within the Bgp1 ITIM sequences, Val at position +3 relative to the second Tyr (Tyr-515), and the SHP-2 N-terminal SH2 domain. Tyrosine 130-133 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 24-29 10080542-8 1999 We found that SHP-2, but not SHP-1, is tyrosine-phosphorylated by FL stimulation. Tyrosine 39-47 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 14-19 9931295-3 1999 The catalytically active forms of SHP-2 decreased the tyrosine phosphorylation of the receptor, whereas the catalytically inactive forms increased the phosphorylation. Tyrosine 54-62 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 34-39 9890893-8 1999 Fifty percent of the identified radioactivity was incorporated in tyrosine Y657 as the predominant peak in HPLC analysis, a site exhibiting features of a potential Syp (PTP1D) binding site. Tyrosine 66-74 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 169-174 9867848-7 1999 In addition, our results indicate that residues +4, +5, and +6 relative to Tyr-515 in the Bgp1 cytoplasmic domain play a significant role in these interactions, as their deletion reduced Bgp1 Tyr phosphorylation and association with SHP-1 and SHP-2 by as much as 80%. Tyrosine 75-78 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 243-248 9886492-5 1999 Thus, tyrosine-phosphorylated p115 and p105 may provide a novel platform recruiting p85, which may simultaneously bind to SHP-2. Tyrosine 6-14 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 122-127 9886492-6 1999 In contrast, tyrosine phosphorylation of p115 or p 105 was undetectable by immunoblot with IGF-I stimulation, and PI 3-kinase activity was mediated via IRS-1 phosphorylated with IGF-I stimulation, little of which was associated with SHP-2. Tyrosine 13-21 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 233-238 9832615-7 1998 These results indicate that the opposite regulation of Cas phosphorylation by insulin and IGF-I may be mediated through different properties of their receptors, and that the interaction of the insulin receptor with SHP-2 may play an important role in determining the tyrosine-phosphorylation state of Cas. Tyrosine 267-275 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 215-220 9804835-5 1998 Far Western analysis showed that the SH2 domains of Shc, SHP-2, and the p85 subunit of phosphatidylinositol 3-kinase could bind directly to tyrosine-phosphorylated Gab1 isolated from activated RAMOS cells. Tyrosine 140-148 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 57-62 9794795-8 1998 This phosphorylation depends on Tyr-759 in the cytoplasmatic domain of gp130, since a Tyr-759-->Phe exchange abrogates SHP2 activation and in turn leads to elevated and prolonged STAT3 and STAT1 activation as well as enhanced acute-phase protein gene induction. Tyrosine 32-35 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 122-126 9794795-8 1998 This phosphorylation depends on Tyr-759 in the cytoplasmatic domain of gp130, since a Tyr-759-->Phe exchange abrogates SHP2 activation and in turn leads to elevated and prolonged STAT3 and STAT1 activation as well as enhanced acute-phase protein gene induction. Tyrosine 86-89 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 122-126 9794795-2 1998 Ligand binding to the receptor complex leads to tyrosine phosphorylation and activation of Janus kinases (Jak), phosphorylation of the signal transducing subunit gp130, followed by recruitment and phosphorylation of the signal transducer and activator of transcription factors STAT3 and STAT1 and the src homology domain (SH2)-containing protein tyrosine phosphatase (SHP2). Tyrosine 48-56 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 368-372 9774457-8 1998 These data suggest that in hematopoietic cells such as platelets, PECAM-1 cellular signaling is regulated by the selective recruitment and activation of two distinct protein-tyrosine phosphatases, SHP-1 and SHP-2, via a common immunoreceptor tyrosine-based inhibitory-like motif. Tyrosine 174-182 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 207-212 9794795-7 1998 It is concluded that Jak1 is required for the tyrosine phosphorylation of SHP2. Tyrosine 46-54 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 74-78 9774457-3 1998 In this report, we demonstrate that both protein-tyrosine phosphatases SHP-1 and SHP-2 physically associate with different kinetics of assembly with tyrosine-phosphorylated human PECAM-1 during integrin alphaIIbbeta3-mediated platelet aggregation. Tyrosine 49-57 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 81-86 9730901-2 1998 PIR-B bears immunoreceptor tyrosine-based inhibitory motif (ITIM) sequences in its cytoplasmic domain that recruit Src homology (SH)2 domain-containing tyrosine phosphatases SHP-1 and SHP-2, leading to inhibition of B and mast cell activation. Tyrosine 27-35 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 184-189 9774457-4 1998 Peptido-precipitation analysis revealed that tyrosine-phosphorylated peptides encompassing residues 658-668 and 681-691 of PECAM-1 bound specifically to both protein-tyrosine phosphatases SHP-1 and SHP-2. Tyrosine 45-53 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 198-203 9712716-3 1998 While signaling molecules such as SHP-2 and the p85 subunit of PI3 kinase associate with this tyrosine residue through SH2 domains upon phosphorylation, the adapter complex AP-2 interacts with the same tyrosine when dephosphorylated, leading to clathrin-mediated endocytosis of CTLA-4. Tyrosine 94-102 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 34-39 9677359-5 1998 The addition of hGM-CSF to WT19 cell lines containing the hbetac627 subunit stimulated the phosphorylation of ERK (extracellular signal-regulated kinase) and induced the tyrosine-phosphorylation of SHP-2 and STAT5, suggesting that the activation of these molecules is insufficient to mediate the induction of differentiation. Tyrosine 170-178 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 198-203 9658397-4 1998 In this report, using a modified version of the yeast two-hybrid system, we localized which Gab1 phospho-tyrosine residues are required for its interaction with phosphatidylinositol 3-kinase and with SHP-2. Tyrosine 105-113 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 200-205 9660791-0 1998 A new tyrosine-phosphorylated 97-kDa adaptor protein mediates interleukin-2-induced association of SHP-2 with p85-phosphatidylinositol 3-kinase in human T lymphocytes. Tyrosine 6-14 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 99-104 9658397-5 1998 Our results demonstrate that to interact with p85 or SHP-2 SH2 domains, Gab1 must be tyrosine phosphorylated by IR. Tyrosine 85-93 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 53-58 9658397-7 1998 Concerning Gab1/SHP-2 interaction, only mutation of tyrosine 627 prevents binding of Gab1 to SHP-2 SH2 domains, suggesting the occurrence of a monovalent binding event. Tyrosine 52-60 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 16-21 9658397-7 1998 Concerning Gab1/SHP-2 interaction, only mutation of tyrosine 627 prevents binding of Gab1 to SHP-2 SH2 domains, suggesting the occurrence of a monovalent binding event. Tyrosine 52-60 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 93-98 9582366-0 1998 Integrin-mediated tyrosine phosphorylation of SHPS-1 and its association with SHP-2. Tyrosine 18-26 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 78-83 9600917-4 1998 Herein we report that activation of ObR induces the tyrosine phosphorylation of the tyrosine phosphatase SH2-containing phosphatase 2 (SHP-2) and demonstrate that Tyr986 within the ObR cytoplasmic domain is essential to mediate phosphorylation of SHP-2 and binding of SHP-2 to ObR. Tyrosine 52-60 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 105-133 9600917-4 1998 Herein we report that activation of ObR induces the tyrosine phosphorylation of the tyrosine phosphatase SH2-containing phosphatase 2 (SHP-2) and demonstrate that Tyr986 within the ObR cytoplasmic domain is essential to mediate phosphorylation of SHP-2 and binding of SHP-2 to ObR. Tyrosine 52-60 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 135-140 9582366-3 1998 Cell adhesion to extracellular matrix proteins such as fibronectin and laminin also induced the tyrosine phosphorylation of SHPS-1 and its association with SHP-2. Tyrosine 96-104 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 156-161 9505191-6 1998 JAK tyrosine kinase is a key molecule that can initiate multiple signal-transduction pathways by inducing the tyrosine-phosphorylation of the cytokine receptor, gp130 in the case of IL-6, on which several signaling molecules are recruited, including STAT, a signal transducer and activator of transcription, and SHP-2, which links to the Ras-MAP kinase pathway. Tyrosine 4-12 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 312-317 9565634-5 1998 Inactive SHP-2 was targeted to membranes resulting in the selective increase in tyrosine phosphorylation of three membrane-associated candidate SHP-2 substrates of 110 kD, 55-60 kD, and 36 kD, respectively. Tyrosine 80-88 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 9-14 9565634-5 1998 Inactive SHP-2 was targeted to membranes resulting in the selective increase in tyrosine phosphorylation of three membrane-associated candidate SHP-2 substrates of 110 kD, 55-60 kD, and 36 kD, respectively. Tyrosine 80-88 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 144-149 9673410-3 1998 The phosphorylated tyrosine at 1009 is a binding site for Syp/PTP1D, an adaptor molecule mediating Grb2/RAS signalling. Tyrosine 19-27 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 62-67 9528773-6 1998 We conclude that the initial burst of Src activity is required for efficient tyrosine phosphorylation of receptor-associated proteins such as PLCgamma, RasGAP, Shc, and SHP-2 and for maximal activation of Erk. Tyrosine 77-85 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 169-174 9497348-2 1998 SHP-2 has more recently been shown to be tyrosine phosphorylated and recruited to the gp130 component of the ciliary neurotrophic factor (CNTF) receptor complex upon stimulation with CNTF. Tyrosine 41-49 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 9538215-4 1998 Tyrosine-phosphorylated, but not nonphosphorylated, synthetic peptides matching the third ITIM and the fourth ITIM-like sequences, respectively, found in the cytoplasmic portion of p91A, the sole inhibitory-type p91, were associated with the tyrosine phosphatases, SHP-1 and SHP-2. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 275-280 9597134-5 1998 Upon ligand binding and activation, the inhibitory NK cell receptors become tyrosine phosphorylated and recruit tyrosine phosphatases, SHP-1 and possibly SHP-2, resulting in inhibition of NK cell-mediated cytotoxicity and cytokine expression. Tyrosine 76-84 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 154-159 9600074-0 1998 Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2. Tyrosine 0-8 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 58-63 9693956-2 1998 Upon activation of cells with different stimuli, SHP-2 is recruited to the plasma membrane where it can associate with a number of tyrosine phosphorylated molecules, including receptor tyrosine kinases (e.g. growth factor receptors), multisite adapter proteins and cell adhesion molecules. Tyrosine 131-139 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 49-54 9535915-4 1998 In addition, mutation of either Tyr449 or Tyr473 abolished the insulin-induced tyrosine phosphorylation of SHPS-1 and its association with SHP-2. Tyrosine 79-87 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 139-144 9544991-8 1998 The dominant negative mutant of SHP-2 was found to inhibit the induction of tyrosine phosphorylation and DNA-binding activity of m-Stat5a, m-Stat5b, and the carboxyl-terminal deletion variant m-Stat5adelta749, as well as the transactivation potential of m-Stat5a and m-Stat5b. Tyrosine 76-84 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 32-37 9544991-11 1998 We propose that SHP-2 relieves an inhibitory tyrosine phosphorylation event in Jak2 required for Jak2 activity, Stat5 phosphorylation, and transcriptional induction. Tyrosine 45-53 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 16-21 9488729-8 1998 Comparing the ability of these two receptors to initiate tyrosine phosphorylation of signaling molecules indicated that both receptors mediated phosphorylation of the receptor itself, phospholipase Cgamma 1, and SHP-2 to similar levels. Tyrosine 57-65 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 212-217 9442080-6 1998 A reciprocal binding assay using IM-9 cells as a source of SHP-1 and SHP-2 revealed specific association of SHP-2 (but not SHP-1) with a glutathione S-transferase fusion incorporating GHR cytoplasmic domain residues 485-620, but only if the fusion was first rendered tyrosine-phosphorylated. Tyrosine 267-275 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 108-113 9312087-1 1997 Recent studies have shown that the Src homology-2 (SH2) domain-containing protein-tyrosine phosphatase, SHP-2, associates with the cytoplasmic domain of PECAM-1 as it becomes tyrosine-phosphorylated during platelet aggregation: a process that can be mimicked in part by small synthetic phosphopeptides corresponding to the cytoplasmic domain of PECAM-1 encompassing tyrosine residues Tyr-663 or Tyr-686. Tyrosine 82-90 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 104-109 9393882-5 1997 Both phosphatases in the complex were tyrosine phosphorylated, and the amount of SHIP coprecipitating with SHP-2 was inversely related to the amount of SHIP coprecipitating with SHC. Tyrosine 38-46 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 107-112 9312087-6 1997 Finally, peptido-precipitation analysis showed that the NH2-terminal SH2 domain of SHP-2 reacted preferentially with the Tyr-663 PECAM-1 phosphopeptide, while the Tyr-686 phosphopeptide associated only with the COOH-terminal SH2 domain of the phosphatase. Tyrosine 121-124 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 83-88 9312087-1 1997 Recent studies have shown that the Src homology-2 (SH2) domain-containing protein-tyrosine phosphatase, SHP-2, associates with the cytoplasmic domain of PECAM-1 as it becomes tyrosine-phosphorylated during platelet aggregation: a process that can be mimicked in part by small synthetic phosphopeptides corresponding to the cytoplasmic domain of PECAM-1 encompassing tyrosine residues Tyr-663 or Tyr-686. Tyrosine 175-183 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 104-109 9312087-6 1997 Finally, peptido-precipitation analysis showed that the NH2-terminal SH2 domain of SHP-2 reacted preferentially with the Tyr-663 PECAM-1 phosphopeptide, while the Tyr-686 phosphopeptide associated only with the COOH-terminal SH2 domain of the phosphatase. Tyrosine 163-166 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 83-88 9312087-1 1997 Recent studies have shown that the Src homology-2 (SH2) domain-containing protein-tyrosine phosphatase, SHP-2, associates with the cytoplasmic domain of PECAM-1 as it becomes tyrosine-phosphorylated during platelet aggregation: a process that can be mimicked in part by small synthetic phosphopeptides corresponding to the cytoplasmic domain of PECAM-1 encompassing tyrosine residues Tyr-663 or Tyr-686. Tyrosine 384-387 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 104-109 9312087-1 1997 Recent studies have shown that the Src homology-2 (SH2) domain-containing protein-tyrosine phosphatase, SHP-2, associates with the cytoplasmic domain of PECAM-1 as it becomes tyrosine-phosphorylated during platelet aggregation: a process that can be mimicked in part by small synthetic phosphopeptides corresponding to the cytoplasmic domain of PECAM-1 encompassing tyrosine residues Tyr-663 or Tyr-686. Tyrosine 395-398 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 104-109 9299490-0 1997 SHP2 associates directly with tyrosine phosphorylated p90 (SNT) protein in FGF-stimulated cells. Tyrosine 30-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 9299490-1 1997 In a number of cell lines responsive to basic fibroblast growth factor (bFGF), two major tyrosine phosphorylated proteins, of molecular weights around 120kDa and 90kDa, are precipitated along with the tyrosine phosphatase SHP2 from the lysates of stimulated cells. Tyrosine 89-97 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 222-226 9299490-4 1997 The two SH2 domains of SHP2 bind directly and synergistically to tyrosine phosphorylated SNT. Tyrosine 65-73 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 23-27 9295037-7 1997 In addition, we show that point mutation of the amino acid residue in position tyrosine-2 of Fc gammaRIIB and KIR ITIM abolihes their binding to SHP-1 and SHP-2, but leaves intact the association of SHIP with Fc gammaRIIB ITIM. Tyrosine 79-87 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 155-160 9285712-1 1997 Ciliary neurotrophic factor, along with other neuropoietic cytokines, signals through the shared receptor subunit gp130 [1-3], leading to the tyrosine phosphorylation of a number of substrates [4,5], including the transcription factors STAT1 and STAT3 and the protein tyrosine phosphatase SHP-2 [6,7] [8]. Tyrosine 142-150 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 289-294 9285712-5 1997 Inhibition of SHP-2, either by mutating the tyrosine residue in gp130 that mediates the SHP-2 interaction, or by expression of dominant-negative SHP-2, resulted in dramatic increases in gp130-dependent gene expression, through the VIP CyRE and more specifically through multimerized STAT-binding sites. Tyrosine 44-52 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 14-19 9254654-5 1997 We found that IL-5 produced a rapid activation and tyrosine phosphorylation of SHPTP2 within 1 min. Tyrosine 51-59 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 79-85 9254654-6 1997 The tyrosine phosphorylated SHPTP2 was complexed with the adapter protein Grb2 in IL-5-stimulated eosinophils. Tyrosine 4-12 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 28-34 9254654-8 1997 The association of SHPTP2 with IL-5betacR was reconstituted using a synthetic phosphotyrosine-containing peptide, betac 605-624, encompassing tyrosine (Y)612. Tyrosine 85-93 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 19-25 9254654-10 1997 Only SHPTP2 antisense oligonucleotides, but not sense SHPTP2, could inhibit tyrosine phosphorylation of microtubule-associated protein kinase, and reverse the eosinophil survival advantage provided by IL-5. Tyrosine 76-84 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 5-11 9285712-5 1997 Inhibition of SHP-2, either by mutating the tyrosine residue in gp130 that mediates the SHP-2 interaction, or by expression of dominant-negative SHP-2, resulted in dramatic increases in gp130-dependent gene expression, through the VIP CyRE and more specifically through multimerized STAT-binding sites. Tyrosine 44-52 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 88-93 9285712-5 1997 Inhibition of SHP-2, either by mutating the tyrosine residue in gp130 that mediates the SHP-2 interaction, or by expression of dominant-negative SHP-2, resulted in dramatic increases in gp130-dependent gene expression, through the VIP CyRE and more specifically through multimerized STAT-binding sites. Tyrosine 44-52 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 88-93 9242692-3 1997 We have previously demonstrated that a single carboxyl-terminal tyrosine residue, Tyr489, is essential for efficient transformation of Fr3T3 fibroblasts by Tpr-Met and forms a multisubstrate binding site for Grb2, phosphatidylinositol 3" kinase, phospholipase Cgamma, SHP2, and an unknown protein of 110 kDa. Tyrosine 64-72 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 268-272 9129156-4 1997 The IL-2-induced tyrosine phosphorylation of SHP-2 required the acidic region within the IL-2Rbeta chain where Src-family PTKs interact. Tyrosine 17-25 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 45-50 9162089-0 1997 SHP1 and SHP2 protein-tyrosine phosphatases associate with betac after interleukin-3-induced receptor tyrosine phosphorylation. Tyrosine 22-30 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 9-13 9188788-3 1997 PECAM-1 was coimmunoprecipitated by anti-SH-PTP2 from EC extracts as a major binding protein, and the level of association increased when PECAM-1 was tyrosine phosphorylated. Tyrosine 150-158 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 41-48 9129156-0 1997 Interleukin-2 induces tyrosine phosphorylation of SHP-2 through IL-2 receptor beta chain. Tyrosine 22-30 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 50-55 9129156-6 1997 In COS-7 cells, co-expression of SHP-2 with Lyn resulted in increased tyrosine phosphorylation levels of SHP-2, whereas co-expression of SHP-2 with Fyn failed to alter the levels significantly. Tyrosine 70-78 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 33-38 9129156-2 1997 Here, we report that stimulation through the IL-2R induced tyrosine phosphorylation of the SH2-containing protein-tyrosine phosphatase SHP-2 in F7, a hematopoietic BAF-B03 transfectant clone expressing the IL-2Rbeta chain. Tyrosine 59-67 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 135-140 9129156-6 1997 In COS-7 cells, co-expression of SHP-2 with Lyn resulted in increased tyrosine phosphorylation levels of SHP-2, whereas co-expression of SHP-2 with Fyn failed to alter the levels significantly. Tyrosine 70-78 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 105-110 9129156-3 1997 The tyrosine phosphorylation of SHP-2 was specific since another protein-tyrosine phosphatase SHP-1, which is structurally homologous to SHP-2, was not tyrosine phosphorylated. Tyrosine 4-12 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 32-37 9129156-6 1997 In COS-7 cells, co-expression of SHP-2 with Lyn resulted in increased tyrosine phosphorylation levels of SHP-2, whereas co-expression of SHP-2 with Fyn failed to alter the levels significantly. Tyrosine 70-78 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 105-110 9129156-3 1997 The tyrosine phosphorylation of SHP-2 was specific since another protein-tyrosine phosphatase SHP-1, which is structurally homologous to SHP-2, was not tyrosine phosphorylated. Tyrosine 4-12 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 137-142 9129156-3 1997 The tyrosine phosphorylation of SHP-2 was specific since another protein-tyrosine phosphatase SHP-1, which is structurally homologous to SHP-2, was not tyrosine phosphorylated. Tyrosine 73-81 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 32-37 9129156-8 1997 Furthermore, the IL-2 stimulation also induced tyrosine phosphorylation of SHP-2 in the human IL-2-dependent T-cell line ILT-Mat. Tyrosine 47-55 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 75-80 9020117-7 1997 Tyr(P)992 receptors were associated with more SOS, Ras-GTPase activating protein, phosphatidylinositol 3-kinase, and SHPTP2/syp, but less Grb2, than receptors in the general population, and these receptors were more heavily phosphorylated than the general population of active receptors. Tyrosine 0-3 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 117-123 9054456-4 1997 One of the tyrosine-phosphorylated proteins was identified as an Src homology-2 domain-containing protein-tyrosine phosphatase, SHP2. Tyrosine 11-19 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 128-132 9054456-5 1997 The stimulatory effect of the agonist peptide on early gene transcription was markedly blocked by pertussis toxin treatment whereas the induced tyrosine phosphorylation of SHP2 was completely abolished by the drug. Tyrosine 144-152 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 172-176 9062191-3 1997 To investigate its mechanism of action we purified a tyrosine-phosphorylated glycoprotein which in different cell types associates tightly with SHP-2 and appears to serve as its substrate. Tyrosine 53-61 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 144-149 9062191-6 1997 The transmembrane polypeptide SIRP alpha1 is a substrate of activated RTKs and in its tyrosine-phosphorylated form binds SHP-2 through SH2 interactions and acts as its substrate. Tyrosine 86-94 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 121-126 8978277-4 1997 EPO, IL-2, and IL-15 activated the tyrosine phosphorylation of the adaptor protein, Shp2, and the association of Shp2/Grb2/cytokine receptor complexes. Tyrosine 35-43 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 84-88 9039769-2 1997 Recent advances indicate that immunoreceptor tyrosine-based inhibitory motifs in the cytoplasmic domains of the killer cell inhibitory receptors and Ly-49 receptors recruit the SH2-containing protein tyrosine phosphatases, SHP-1 and SHP-2, resulting in inhibition of natural-killer- and T-cell-mediated cytotoxicity and cytokine secretion. Tyrosine 45-53 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 233-238 8959326-0 1996 Multiple in vivo phosphorylated tyrosine phosphatase SHP-2 engages binding to Grb2 via tyrosine 584. Tyrosine 32-40 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 53-58 8978300-3 1997 IL-6 induced transient tyrosine phosphorylation of the IL-6-receptor signal-transducing subunit gp130, the gp130-associated protein tyrosine kinases Jak1,Jak2, and Tyk2, the phosphotyrosine phosphatase PTP1D/Syp, the adaptor protein Shc and the mitogen-activated protein kinase Erk2, and accumulation of GTP-bound p21ras. Tyrosine 23-31 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 202-207 8978300-4 1997 Prior treatment of U266 cells with IFN-beta downregulated IL-6-induced tyrosine phosphorylation of gp130, Jak2, PTP1D/Syp, Shc, and Erk2, and GTP-loading of p21ras. Tyrosine 71-79 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 112-117 8978300-5 1997 Further analysis indicated that treatment with IFN-beta disrupted IL-6-induced binding of PTP1D/Syp to gp130 and the adaptor protein Grb2; IFN-beta pretreatment also interfered with IL-6-induced interaction of Shc with Grb2 and a 145-kD tyrosine-phosphorylated protein. Tyrosine 237-245 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 90-95 8959326-2 1996 Upon growth factor stimulation, SHP-2 becomes tyrosine phosphorylated, thereby increasing its catalytic activity. Tyrosine 46-54 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 32-37 8959326-3 1996 Here, we identified SHP-2 to be phosphorylated on multiple tyrosine residues in response to different stimuli and unmasked the carboxyl-terminal tyrosine 584 as a major phosphorylation site in human cell lines. Tyrosine 59-67 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 20-25 8959326-3 1996 Here, we identified SHP-2 to be phosphorylated on multiple tyrosine residues in response to different stimuli and unmasked the carboxyl-terminal tyrosine 584 as a major phosphorylation site in human cell lines. Tyrosine 145-153 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 20-25 8959326-5 1996 We show here that mutation of tyrosine 584, but not tyrosine 546, to phenylalanine totally abolished the binding of Grb2 to SHP-2. Tyrosine 30-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 124-129 8959326-6 1996 By using a systematic mutagenesis approach, phosphorylation of additional tyrosines in each of the SH2 domains of SHP-2 was detected after coexpression of epidermal growth factor receptor, but not after coexpression of platelet-derived growth factor receptor, whereas tyrosine 263 located in the interspace between SH2 and catalytic domain appears to be exclusively recognized by platelet-derived growth factor receptor. Tyrosine 74-83 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 114-119 8959326-6 1996 By using a systematic mutagenesis approach, phosphorylation of additional tyrosines in each of the SH2 domains of SHP-2 was detected after coexpression of epidermal growth factor receptor, but not after coexpression of platelet-derived growth factor receptor, whereas tyrosine 263 located in the interspace between SH2 and catalytic domain appears to be exclusively recognized by platelet-derived growth factor receptor. Tyrosine 74-82 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 114-119 8959326-7 1996 Immunoprecipitation of SHP-2 from a panel of mammary carcinoma cell lines copurifies several tyrosine phosphorylated proteins; the most prominent band has an apparent molecular weight of M(r) 115,000. Tyrosine 93-101 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 23-28 9052869-3 1996 These receptors recruit the protein tyrosine phosphatases (PTPase), SHP-1 and SHP-2, upon tyrosine phosphorylation of immunoreceptor tyrosine-based inhibition motif (ITIM) expressed in both human and mouse KIR. Tyrosine 36-44 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 78-83 9052869-3 1996 These receptors recruit the protein tyrosine phosphatases (PTPase), SHP-1 and SHP-2, upon tyrosine phosphorylation of immunoreceptor tyrosine-based inhibition motif (ITIM) expressed in both human and mouse KIR. Tyrosine 90-98 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 78-83 8943348-0 1996 Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation. Tyrosine 19-27 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 121-126 8943348-7 1996 SHP-2 bound the alphaPDGFR directly, whereas Grb2 associated indirectly, most probably via SHP-2, as Grb2 and SHP-2 coimmunoprecipitated when SHP-2 was tyrosine phosphorylated. Tyrosine 152-160 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 91-96 8943348-7 1996 SHP-2 bound the alphaPDGFR directly, whereas Grb2 associated indirectly, most probably via SHP-2, as Grb2 and SHP-2 coimmunoprecipitated when SHP-2 was tyrosine phosphorylated. Tyrosine 152-160 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 91-96 8943348-1 1996 Following binding of platelet-derived growth factor (PDGF), the PDGF alpha receptor (alphaPDGFR) becomes tyrosine phosphorylated and associates with a number of signal transduction molecules, including phospholipase Cgamma-1 (PLCgamma-1), phosphatidylinositol 3-kinase (PI3K), the phosphotyrosine phosphatase SHP-2, Grb2, and Src. Tyrosine 105-113 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 309-314 8943348-5 1996 In addition, mutating Y720 to phenylalanine dramatically reduced PDGF-dependent tyrosine phosphorylation of SHP-2. Tyrosine 80-88 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 108-113 8943348-7 1996 SHP-2 bound the alphaPDGFR directly, whereas Grb2 associated indirectly, most probably via SHP-2, as Grb2 and SHP-2 coimmunoprecipitated when SHP-2 was tyrosine phosphorylated. Tyrosine 152-160 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 91-96 8895367-3 1996 We found that a catalytically inactive SHP-2 is able to bind to tyrosine-phosphorylated IR beta-subunit and IGF-I R beta-subunit. Tyrosine 64-72 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 39-44 8895367-5 1996 Further, our results demonstrate that tyrosine 1322 of the IR, and the corresponding tyrosine 1316 of the IGF-I R are implicated in the interaction with the SHP-2 SH2 domain. Tyrosine 38-46 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 157-162 8895367-5 1996 Further, our results demonstrate that tyrosine 1322 of the IR, and the corresponding tyrosine 1316 of the IGF-I R are implicated in the interaction with the SHP-2 SH2 domain. Tyrosine 85-93 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 157-162 8934572-3 1996 The second tyrosine (from the membrane) of gp130, which was required for the tyrosine phosphorylation of SHP-2, its association with GRB2, and activation of a MAP kinase, was essential for mitogenesis, but not for anti-apoptosis. Tyrosine 11-19 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 105-110 8934572-3 1996 The second tyrosine (from the membrane) of gp130, which was required for the tyrosine phosphorylation of SHP-2, its association with GRB2, and activation of a MAP kinase, was essential for mitogenesis, but not for anti-apoptosis. Tyrosine 77-85 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 105-110 8809054-0 1996 Insulin-induced tyrosine dephosphorylation of paxillin and focal adhesion kinase requires active phosphotyrosine phosphatase 1D. Tyrosine 16-24 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 97-127 8810330-0 1996 Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule. Tyrosine 22-30 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 43-50 8810330-5 1996 SH-PTP2 and BIT were coimmunoprecipitated from phosphorylated rat brain lysate, and BIT was a major tyrosine-phosphorylated protein associated with SH-PTP2 in this lysate. Tyrosine 100-108 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 148-155 8810330-8 1996 Our findings suggest that the tyrosine phosphorylation of BIT results in stimulation of the signal transduction pathway promoted by SH-PTP2 and that BIT is probably a major receptor molecule in the brain located just upstream of SH-PTP2. Tyrosine 30-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 132-139 8810330-8 1996 Our findings suggest that the tyrosine phosphorylation of BIT results in stimulation of the signal transduction pathway promoted by SH-PTP2 and that BIT is probably a major receptor molecule in the brain located just upstream of SH-PTP2. Tyrosine 30-38 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 229-236 8598196-2 1996 We report that PTP1D, a cytoplasmic protein tyrosine phosphatase containing two Src homology 2 (SH2) domains, physically associates with the PRLR-Jak2 complex and is tyrosine-phosphorylated upon stimulation with prolactin. Tyrosine 44-52 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 15-20 9183644-8 1996 Cas-L is directly associated with FAk-C-terminal region in an integrin stimulation-dependent manner, and tyrosine phosphorylated Cas-L binds to the SH2 domains of Crk, Nck and SHPTP2. Tyrosine 105-113 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 176-182 8663536-3 1996 We now show that the SH2 domain containing tyrosine phosphatase PTP1D (also designated as SHPTP2, SHPTP3, PTP2C, or Syp) is constitutively associated with the IFNalpha/beta receptor and becomes tyrosine-phosphorylated in response to ligand. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 64-69 8663536-3 1996 We now show that the SH2 domain containing tyrosine phosphatase PTP1D (also designated as SHPTP2, SHPTP3, PTP2C, or Syp) is constitutively associated with the IFNalpha/beta receptor and becomes tyrosine-phosphorylated in response to ligand. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 90-96 8663536-3 1996 We now show that the SH2 domain containing tyrosine phosphatase PTP1D (also designated as SHPTP2, SHPTP3, PTP2C, or Syp) is constitutively associated with the IFNalpha/beta receptor and becomes tyrosine-phosphorylated in response to ligand. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 98-104 8663536-3 1996 We now show that the SH2 domain containing tyrosine phosphatase PTP1D (also designated as SHPTP2, SHPTP3, PTP2C, or Syp) is constitutively associated with the IFNalpha/beta receptor and becomes tyrosine-phosphorylated in response to ligand. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 106-111 8647120-3 1996 We have found that one of the two T-cell-expressed SH2-domain-containing PTPases, SHPTP2, is rapidly phosphorylated on tyrosine upon addition of anti-CD3 mAbs. Tyrosine 119-127 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 82-88 8647120-5 1996 Concomitantly with tyrosine phosphorylation, SHPTP2 co-immunoprecipitated with two unphosphorylated cellular proteins; phosphatidylinositol 3-kinase p85 and Grb2. Tyrosine 19-27 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 45-51 8647120-8 1996 Our results indicate that SHPTP2 participates actively at an early stage in TCR signaling and that its phosphorylation on tyrosine may direct a Grb2-dependent association with selected substrates. Tyrosine 122-130 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 26-32 8601424-7 1996 Immunofluorescence examination revealed that PTP2C colocalized with actin, the PDGF receptors, and hyper-tyrosine- phosphorylated protein(s). Tyrosine 105-113 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 45-50 7588273-5 1995 To address this issue, we constructed different rat IRS-1 mutants containing mutations in the tyrosine residues that interact with the SH2 domains of PI3-K and PTP2C in vitro. Tyrosine 94-102 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 160-165 7588273-8 1995 Furthermore, we found that mutation of tyrosines 1172 and 1222 totally prevents the insulin-induced association of IRS-1 with the SH2 domains of PTP2C, demonstrating that both tyrosines 1172 and 1222 are key elements in the binding sites for the SH2 domains of PTP2C. Tyrosine 39-48 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 145-150 7588273-4 1995 In this report, we examined which tyrosine residues of IRS-1 are required for the interactions of IRS-1 with PI3-K and PTP2C. Tyrosine 34-42 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 119-124 7588273-8 1995 Furthermore, we found that mutation of tyrosines 1172 and 1222 totally prevents the insulin-induced association of IRS-1 with the SH2 domains of PTP2C, demonstrating that both tyrosines 1172 and 1222 are key elements in the binding sites for the SH2 domains of PTP2C. Tyrosine 39-48 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 261-266 7588273-8 1995 Furthermore, we found that mutation of tyrosines 1172 and 1222 totally prevents the insulin-induced association of IRS-1 with the SH2 domains of PTP2C, demonstrating that both tyrosines 1172 and 1222 are key elements in the binding sites for the SH2 domains of PTP2C. Tyrosine 176-185 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 145-150 21597824-4 1995 Furthermore, most of the gastric carcinomas displayed higher levels of tyrosine-phosphorylated form of SH-PTP2, while non-neoplastic mucosas tended to express unphosphorylated SH-PTP2 protein. Tyrosine 71-79 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 103-110 21597824-5 1995 These results suggest that the increased expression and tyrosine-phosphorylation of SH-PTP2 may participate in stomach carcinogenesis. Tyrosine 56-64 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 84-91 7935386-7 1994 Recombinant SH-PTP2 specifically dephosphorylated a synthetic phosphopeptide corresponding to the sequence surrounding Tyr-1172 of IRS-1, a putative binding site for SH-PTP2. Tyrosine 119-122 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 12-19 7549895-5 1995 IRS-1 and 4PS possess a number of tyrosine phosphorylation sites that are within motifs that bind specific SH2-containing molecules known to be involved in mitogenic signaling such as PI-3 kinase, SHPTP-2 (Syp) and Grb-2. Tyrosine 34-42 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 197-204 7531337-1 1995 SHPTP2 is a ubiquitously expressed tyrosine-specific protein phosphatase that contains two amino-terminal Src homology 2 (SH2) domains responsible for its association with tyrosine-phosphorylated proteins. Tyrosine 35-43 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-6 7531337-5 1995 These data demonstrate that SHPTP2 functions as a positive regulator of insulin action and that insulin signaling results in the dephosphorylation of tyrosine-phosphorylated pp125FAK. Tyrosine 150-158 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 28-34 7935386-7 1994 Recombinant SH-PTP2 specifically dephosphorylated a synthetic phosphopeptide corresponding to the sequence surrounding Tyr-1172 of IRS-1, a putative binding site for SH-PTP2. Tyrosine 119-122 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 166-173 7629070-0 1995 Identification of the major SHPTP2-binding protein that is tyrosine-phosphorylated in response to insulin. Tyrosine 59-67 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 28-34 7629070-1 1995 Immunoprecipitation of the cytosolic Src homology 2 domain-containing protein-tyrosine phosphatase, SHPTP2, from insulin-stimulated 3T3L1 adipocytes or Chinese hamster ovary cells expressing the human insulin receptor resulted in the coimmunoprecipitation of a diffuse tyrosine-phosphorylated band in the 115-kDa protein region on SDS-polyacrylamide gels. Tyrosine 78-86 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 100-106 7629070-3 1995 SHPTP2 was also associated with tyrosine-phosphorylated insulin receptor substrate-1, but this only accounted for < 2% of the total immunoreactive SHPTP2 protein. Tyrosine 32-40 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-6 7629070-4 1995 Similarly, only a small fraction of the total amount of tyrosine-phosphorylated insulin receptor substrate-1 (< 4%) was associated with SHPTP2. Tyrosine 56-64 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 139-145 7629070-6 1995 Furthermore, expression of the catalytically inactive SHPTP2 mutant resulted in a marked enhancement in the amount of coimmunoprecipitated tyrosine-phosphorylated pp115 compared with the expression of wild-type SHPTP2. Tyrosine 139-147 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 54-60 7629070-6 1995 Furthermore, expression of the catalytically inactive SHPTP2 mutant resulted in a marked enhancement in the amount of coimmunoprecipitated tyrosine-phosphorylated pp115 compared with the expression of wild-type SHPTP2. Tyrosine 139-147 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 211-217 7629070-7 1995 These data indicate that the insulin-stimulated tyrosine-phosphorylated 115-kDa protein is the predominant in vivo SHPTP2-binding protein and that pp115 may function as a physiological substrate for the SHPTP2 protein-tyrosine phosphatase. Tyrosine 48-56 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 115-121 7629070-7 1995 These data indicate that the insulin-stimulated tyrosine-phosphorylated 115-kDa protein is the predominant in vivo SHPTP2-binding protein and that pp115 may function as a physiological substrate for the SHPTP2 protein-tyrosine phosphatase. Tyrosine 48-56 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 203-209 7541031-2 1995 In contrast, activation of the EGF receptor resulted in a relatively low level (< 1%) of the total SHPTP2 pool associated with the tyrosine-autophosphorylated EGF receptor itself. Tyrosine 134-142 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 102-108 7541031-5 1995 In comparison, activation of Jurkat cells with a T cell receptor agonist monoclonal antibody resulted in the co-immunoprecipitation of a 120-kDa tyrosine-phosphorylated protein with Grb2 and a 105-kDa protein with SHPTP2. Tyrosine 145-153 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 214-220 7540003-1 1995 In order to determine whether the tyrosine phosphatase PTP2C dephosphorylates insulin-elicited phosphotyrosine proteins in vivo, we have compared the patterns of protein tyrosine phosphorylation and its reversal in the kidney 293 cell line with those in 293 cell lines overexpressing PTP2C and a catalytically inactive point mutant of PTP2C. Tyrosine 34-42 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 55-60 7744825-4 1995 Expression of the latter caused hyperphosphorylation on tyrosine of a 43-kDa protein, which was coimmunoprecipitated and co-partitioned in the plasma membrane fraction with the inactive PTP2C mutant. Tyrosine 56-64 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 186-191 7515062-2 1994 Our previous study revealed that Tyr(P) IRS-1 binds to the widely distributed tyrosine phosphatase PTP2C through the src homology 2 (SH2) domains of the latter. Tyrosine 33-36 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 99-104 7522233-3 1994 The Src homology 2 (SH2) domain of the adaptor protein Grb2 bound with high affinity to tyrosine-phosphorylated SHPTP2 following treatment of cells with IL-3 or GM-CSF, but not IL-4. Tyrosine 88-96 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 112-118 7515062-5 1994 PTP2C rapidly dephosphorylated Tyr(P) IRS-1; dephosphorylation by delta PTP2C was approximately one-third as fast. Tyrosine 31-34 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-5 7515062-7 1994 These results indicate that the binding of Tyr(P) residues on IRS-1 to the SH2 domain(s) of PTP2C enhances its activity toward IRS-1 and suggest that PTP2C is the phosphatase responsible for the dephosphorylation of IRS-1 in vivo. Tyrosine 43-46 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 92-97 7515062-7 1994 These results indicate that the binding of Tyr(P) residues on IRS-1 to the SH2 domain(s) of PTP2C enhances its activity toward IRS-1 and suggest that PTP2C is the phosphatase responsible for the dephosphorylation of IRS-1 in vivo. Tyrosine 43-46 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 150-155 8216283-9 1993 The identification of SH-PTP2 along with PTP1C and corkscrew protein suggest that there exist a family of nonreceptor PTP containing SH2-domain which will participate in specific signal transduction pathways involving tyrosine phosphorylation-dephosphorylation. Tyrosine 218-226 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 22-29 7513703-1 1994 The cytoplasmic insulin receptor substrate-1 (IRS-1), which is multiply phosphorylated in vivo on tyrosine residues, is a known binding protein for the tandem src homology 2 (SH2) domain-containing protein tyrosine phosphatase, SH-PTP2. Tyrosine 98-106 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 228-235 8264620-9 1994 The protein tyrosine phosphatase Syp/PTP1D/SHPTP2/PTP2C is approximately 70 kDa, binds to the PDGF receptor via Tyr-1009, and contains several YXNX sequences. Tyrosine 112-115 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 37-42 8264620-9 1994 The protein tyrosine phosphatase Syp/PTP1D/SHPTP2/PTP2C is approximately 70 kDa, binds to the PDGF receptor via Tyr-1009, and contains several YXNX sequences. Tyrosine 112-115 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 43-49 8264620-9 1994 The protein tyrosine phosphatase Syp/PTP1D/SHPTP2/PTP2C is approximately 70 kDa, binds to the PDGF receptor via Tyr-1009, and contains several YXNX sequences. Tyrosine 112-115 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 50-55 7504175-7 1993 By contrast, the SH2 domain in GRB2 and the amino-terminal SH2 domain in SHPTP2 (Syp) specifically bind to Tyr(P)-895 and Tyr(P)-1172, respectively. Tyrosine 107-110 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 73-79 7504175-7 1993 By contrast, the SH2 domain in GRB2 and the amino-terminal SH2 domain in SHPTP2 (Syp) specifically bind to Tyr(P)-895 and Tyr(P)-1172, respectively. Tyrosine 122-125 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 73-79 7691811-8 1993 Addition of a phosphotyrosyl peptide comprising the region around Tyr-1009 stimulates SH-PTP2 activity 5-10-fold, whereas other phosphotyrosyl peptides from the platelet-derived growth factor receptor have no stimulatory effect. Tyrosine 66-69 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 86-93 34338914-1 2021 SHP2 is a protein tyrosine phosphatase (PTP) that can regulate the tyrosine phosphorylation level. Tyrosine 67-75 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 0-4 33777680-3 2021 The established method can effectively exclude the false positive SHP2 inhibitors with fluorescence interference and was also successfully employed to identify new protein tyrosine phosphatase domain of SHP2 (SHP2-PTP) and allosteric inhibitors. Tyrosine 172-180 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 66-70 33777680-3 2021 The established method can effectively exclude the false positive SHP2 inhibitors with fluorescence interference and was also successfully employed to identify new protein tyrosine phosphatase domain of SHP2 (SHP2-PTP) and allosteric inhibitors. Tyrosine 172-180 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 203-207 33777680-3 2021 The established method can effectively exclude the false positive SHP2 inhibitors with fluorescence interference and was also successfully employed to identify new protein tyrosine phosphatase domain of SHP2 (SHP2-PTP) and allosteric inhibitors. Tyrosine 172-180 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 203-207 1281790-5 1992 As with other SH2 domains in src-family kinases, the SH2 domains of SH-PTP3 may play a crucial role in interactions with tyrosine phosphorylated signaling proteins, including itself and protein tyrosine kinases (PTKs), to regulate targets" enzyme activity. Tyrosine 121-129 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 68-75 35154156-7 2022 Siglec-8 inhibition was dependent on both cytoplasmic immunoreceptor tyrosine-based inhibitory motifs (ITIMs) that interact with the SH2 containing protein phosphatase Shp-2 upon Siglec-8 phosphorylation. Tyrosine 69-77 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 168-173 35439551-0 2022 The down-regulation of tyrosine phosphatase SHP2 activity is involved in the removal of surface AMPA receptors in long term depression. Tyrosine 23-31 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 44-48 35439551-2 2022 Effective activity and synaptic content of tyrosine phosphatase SHP2 are required for AMPA receptor trafficking during LTP. Tyrosine 43-51 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 64-68 34310951-3 2022 We further show that CLEC12B recruits SHP2 phosphatase through its immunoreceptor tyrosine-based inhibition motif domain, inactivates signal transducer and activator of transcription 1/3/5, increases p53/p21/p27 expression/activity, and modulates melanoma cell proliferation. Tyrosine 82-90 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 38-42