PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21067594-5 2010 RESULTS: In this study, we investigated redox regulation of PTEN, namely S-nitrosylation, a covalent modification of cysteine residues by nitric oxide (NO), and H2O2-mediated oxidation. Cysteine 117-125 phosphatase and tensin homolog Homo sapiens 60-64 21953448-0 2011 Hydrogen sulfide and L-cysteine increase phosphatidylinositol 3,4,5-trisphosphate (PIP3) and glucose utilization by inhibiting phosphatase and tensin homolog (PTEN) protein and activating phosphoinositide 3-kinase (PI3K)/serine/threonine protein kinase (AKT)/protein kinase Czeta/lambda (PKCzeta/lambda) in 3T3l1 adipocytes. Cysteine 21-31 phosphatase and tensin homolog Homo sapiens 159-163 22095074-13 2012 The mutation in cysteine 124 present in the catalytic domain of PTEN abolished cis-GS-induced HO-1 expression as well as Akt phosphorylation. Cysteine 16-24 phosphatase and tensin homolog Homo sapiens 64-68 21067594-9 2010 S-nitrosylation and oxidation occur on overlapping and distinct Cys residues of PTEN. Cysteine 64-67 phosphatase and tensin homolog Homo sapiens 80-84 17324556-2 2007 Herein, we demonstrate that the PTEN-catalysed PIP(3) dephosphorylation reaction involves two-steps: (i) formation of a phosphoenzyme intermediate (PE) in which Cys-124 in the active site is thiophosphorylated, and (ii) hydrolysis of PE. Cysteine 161-164 phosphatase and tensin homolog Homo sapiens 32-36 20685300-1 2010 Missense PTEN mutations of the active site residues Asp-92, Cys-124 and Gly-129 contribute to Cowden syndrome. Cysteine 60-63 phosphatase and tensin homolog Homo sapiens 9-13 20685300-4 2010 Our data suggest that PTEN catalysis of phosphoprotein dephosphorylation follows a two-step mechanism with Cys-124 transiently phosphorylated to form the phosphoenzyme intermediate. Cysteine 107-110 phosphatase and tensin homolog Homo sapiens 22-26 17941496-6 2007 The authors report the case of a 17-year-old girl who had a severe cyanotic cardiac malformation for which surgery was not advised and a heterozygous missense mutation (c.406T>C) in exon 5 of PTEN resulting in the substitution of cysteine for arginine (p.Cysl36Arg) in the protein, which was also found in her mother and sister. Cysteine 233-241 phosphatase and tensin homolog Homo sapiens 195-199 15313215-6 2004 Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain. Cysteine 148-151 phosphatase and tensin homolog Homo sapiens 87-91 15890001-3 2005 The CBPs, which include protein tyrosine phosphatases (PTPs), dual-specificity phosphatases, low-molecular-weight PTPs, and the lipid phosphatase PTEN, all contain a nucleophilic catalytic cysteine within a conserved motif that enables these enzymes to dephosphorylate phosphoproteins or phospholipids. Cysteine 189-197 phosphatase and tensin homolog Homo sapiens 146-150 15967877-3 2005 Because S-nitrosothiols are known to modify enzymes containing reactive cysteines, we hypothesized that S-nitrosothiols would oxidize PTEN and inhibit its phosphatase activity. Cysteine 72-81 phosphatase and tensin homolog Homo sapiens 134-138 15313215-6 2004 Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain. Cysteine 169-172 phosphatase and tensin homolog Homo sapiens 87-91 15313215-6 2004 Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain. Cysteine 169-172 phosphatase and tensin homolog Homo sapiens 198-202 15313215-6 2004 Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain. Cysteine 169-172 phosphatase and tensin homolog Homo sapiens 198-202 35216667-4 2022 Mechanistically, fumarate directly reacts with PTEN at cysteine 211 (C211) to form S-(2-succino)-cysteine. Cysteine 55-63 phosphatase and tensin homolog Homo sapiens 47-51 15534200-4 2004 We also show that a small fraction of PTEN molecules is transiently inactivated as a result of oxidation of the essential cysteine residue of this phosphatase in various cell types stimulated with epidermal growth factor, platelet-derived growth factor, or insulin. Cysteine 122-130 phosphatase and tensin homolog Homo sapiens 38-42 15017976-4 2004 Among these redox-regulated PTPs, PTEN, Cdc25 and low molecular weight PTP are known to form a disulfide bond between two cysteines, one in the active site and the other nearby, during oxidation by H(2)O(2). Cysteine 122-131 phosphatase and tensin homolog Homo sapiens 34-38 11916965-3 2002 Analysis of various cysteine mutants, including mass spectrometry of tryptic peptides, indicated that the essential Cys(124) residue in the active site of PTEN specifically forms a disulfide with Cys(71) during oxidation by H(2)O(2). Cysteine 20-28 phosphatase and tensin homolog Homo sapiens 155-159 11916965-3 2002 Analysis of various cysteine mutants, including mass spectrometry of tryptic peptides, indicated that the essential Cys(124) residue in the active site of PTEN specifically forms a disulfide with Cys(71) during oxidation by H(2)O(2). Cysteine 116-119 phosphatase and tensin homolog Homo sapiens 155-159 11916965-3 2002 Analysis of various cysteine mutants, including mass spectrometry of tryptic peptides, indicated that the essential Cys(124) residue in the active site of PTEN specifically forms a disulfide with Cys(71) during oxidation by H(2)O(2). Cysteine 196-199 phosphatase and tensin homolog Homo sapiens 155-159 12549040-7 2000 One of the base-pair substitution in exon 8 is a missense mutation, which changed codon 304 of PTEN protein from Cys to Gly. Cysteine 113-116 phosphatase and tensin homolog Homo sapiens 95-99 32413744-2 2020 Cellular PTEN activity is restrained by the oxidation of active-site cysteine by reactive oxygen species (ROS). Cysteine 69-77 phosphatase and tensin homolog Homo sapiens 9-13 25637034-5 2015 Formation of oxidized PTEN was abolished when the active site Cys(124) or nearby Cys(71) was replaced with Ser suggesting that Cys(124) and Cys(71) are involved in the formation of an intramolecular disulfide bond. Cysteine 62-65 phosphatase and tensin homolog Homo sapiens 22-26 30959964-7 2019 We demonstrate that ANXA2 via its reactive Cys-8 residue, binds to PTEN and that the co-expression of PTEN and ANXA2, but not ANXA2 Cys-8-Ala mutant, inhibits AKT phosphorylation on Ser 473. Cysteine 43-46 phosphatase and tensin homolog Homo sapiens 67-71 30959964-7 2019 We demonstrate that ANXA2 via its reactive Cys-8 residue, binds to PTEN and that the co-expression of PTEN and ANXA2, but not ANXA2 Cys-8-Ala mutant, inhibits AKT phosphorylation on Ser 473. Cysteine 43-46 phosphatase and tensin homolog Homo sapiens 102-106 30959964-7 2019 We demonstrate that ANXA2 via its reactive Cys-8 residue, binds to PTEN and that the co-expression of PTEN and ANXA2, but not ANXA2 Cys-8-Ala mutant, inhibits AKT phosphorylation on Ser 473. Cysteine 132-135 phosphatase and tensin homolog Homo sapiens 102-106 29550515-0 2018 15-Deoxy-Delta12,14-prostaglandin J2 activates PI3K-Akt signaling in human breast cancer cells through covalent modification of the tumor suppressor PTEN at cysteine 136. Cysteine 157-165 phosphatase and tensin homolog Homo sapiens 149-153 29550515-5 2018 A mass spectrometric analysis by using recombinant and endogenous PTEN protein revealed that the cysteine 136 residue (Cys136) of PTEN is covalently modified upon treatment with 15d-PGJ2. Cysteine 97-105 phosphatase and tensin homolog Homo sapiens 66-70 29550515-5 2018 A mass spectrometric analysis by using recombinant and endogenous PTEN protein revealed that the cysteine 136 residue (Cys136) of PTEN is covalently modified upon treatment with 15d-PGJ2. Cysteine 97-105 phosphatase and tensin homolog Homo sapiens 130-134 29550515-7 2018 The present study demonstrates for the first time that electrophilic 15d-PGJ2 directly binds to cysteine 136 of PTEN and provides new insight into PTEN loss in cancer progression associated with chronic inflammation. Cysteine 96-104 phosphatase and tensin homolog Homo sapiens 112-116 25637034-5 2015 Formation of oxidized PTEN was abolished when the active site Cys(124) or nearby Cys(71) was replaced with Ser suggesting that Cys(124) and Cys(71) are involved in the formation of an intramolecular disulfide bond. Cysteine 81-84 phosphatase and tensin homolog Homo sapiens 22-26 25637034-5 2015 Formation of oxidized PTEN was abolished when the active site Cys(124) or nearby Cys(71) was replaced with Ser suggesting that Cys(124) and Cys(71) are involved in the formation of an intramolecular disulfide bond. Cysteine 81-84 phosphatase and tensin homolog Homo sapiens 22-26 23872024-9 2013 Subsequent LC/MS/MS analysis of 4-HNE-modified recombinant human PTEN identified Michael addition adducts of 4-HNE on Cys(71), Cys(136), Lys(147), Lys(223), Cys(250), Lys(254), Lys(313), Lys(327), and Lys(344). Cysteine 118-121 phosphatase and tensin homolog Homo sapiens 65-69 24759986-11 2014 Hence, we hypothesize that zinc signals affect the IL-2-dependent PI3K/Akt pathway by inhibiting the negative regulator PTEN through binding with a sub-nanomolar affinity to cysteine residues that are essential for its catalytic activity. Cysteine 174-182 phosphatase and tensin homolog Homo sapiens 120-124 25446078-3 2015 PTEN is a target of nitric oxide (NO) or hydrogen peroxide, and the oxidative modification of cysteine (Cys) residue(s) attenuates its enzymatic activity. Cysteine 94-102 phosphatase and tensin homolog Homo sapiens 0-4 25446078-3 2015 PTEN is a target of nitric oxide (NO) or hydrogen peroxide, and the oxidative modification of cysteine (Cys) residue(s) attenuates its enzymatic activity. Cysteine 104-107 phosphatase and tensin homolog Homo sapiens 0-4 25378175-6 2014 Here, we report that PTEN phosphatase activity is inhibited via a transnitrosylation reaction [i.e., transfer of a nitric oxide (NO) group from the cysteine residue of one protein to another]. Cysteine 148-156 phosphatase and tensin homolog Homo sapiens 21-25 25378175-6 2014 Here, we report that PTEN phosphatase activity is inhibited via a transnitrosylation reaction [i.e., transfer of a nitric oxide (NO) group from the cysteine residue of one protein to another]. Cysteine 148-156 phosphatase and tensin homolog Homo sapiens 26-37 23872024-9 2013 Subsequent LC/MS/MS analysis of 4-HNE-modified recombinant human PTEN identified Michael addition adducts of 4-HNE on Cys(71), Cys(136), Lys(147), Lys(223), Cys(250), Lys(254), Lys(313), Lys(327), and Lys(344). Cysteine 127-130 phosphatase and tensin homolog Homo sapiens 65-69 23872024-9 2013 Subsequent LC/MS/MS analysis of 4-HNE-modified recombinant human PTEN identified Michael addition adducts of 4-HNE on Cys(71), Cys(136), Lys(147), Lys(223), Cys(250), Lys(254), Lys(313), Lys(327), and Lys(344). Cysteine 127-130 phosphatase and tensin homolog Homo sapiens 65-69