PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30062411-3 2018 S-glutathionylation, the adduction of glutathione to cysteine residues in Rac1, is a redox-dependent thiol modification and is generally associated with oxidative/nitrosative stress, representing a novel mechanism of GTPase regulation. Cysteine 53-61 Rac family small GTPase 1 Homo sapiens 74-78 27693992-10 2016 Glutathionylation of Rac1 on cysteine 81 and 157 located adjacent to guanine nucleotide binding site was required for the metabolic stress to inhibit Rac1 activity and promote endothelial hyperpermeability. Cysteine 29-37 Rac family small GTPase 1 Homo sapiens 21-25 27693992-10 2016 Glutathionylation of Rac1 on cysteine 81 and 157 located adjacent to guanine nucleotide binding site was required for the metabolic stress to inhibit Rac1 activity and promote endothelial hyperpermeability. Cysteine 29-37 Rac family small GTPase 1 Homo sapiens 150-154 25289457-14 2015 Our results suggest that Rac1 oxidation at Cys(18) is a novel posttranslational modification that upregulates Rac1 activity. Cysteine 43-46 Rac family small GTPase 1 Homo sapiens 110-114 25289457-5 2015 Herein, we show that Rac1 contains a redox-sensitive cysteine (Cys(18)) that can be selectively oxidized at physiological pH because of its lowered pKa. Cysteine 53-61 Rac family small GTPase 1 Homo sapiens 21-25 25289457-5 2015 Herein, we show that Rac1 contains a redox-sensitive cysteine (Cys(18)) that can be selectively oxidized at physiological pH because of its lowered pKa. Cysteine 63-66 Rac family small GTPase 1 Homo sapiens 21-25 25289457-7 2015 Oxidation of Cys(18) by glutathione greatly perturbs Rac1 guanine nucleotide binding and promotes nucleotide exchange. Cysteine 13-16 Rac family small GTPase 1 Homo sapiens 53-57 25289457-8 2015 As aspartate substitutions have been previously used to mimic cysteine oxidation, we characterized the biochemical properties of Rac1(C18D). Cysteine 62-70 Rac family small GTPase 1 Homo sapiens 129-133 25289457-14 2015 Our results suggest that Rac1 oxidation at Cys(18) is a novel posttranslational modification that upregulates Rac1 activity. Cysteine 43-46 Rac family small GTPase 1 Homo sapiens 25-29 25677088-6 2015 Rac1 activity has recently been shown to be modulated by glutathiolation or S-nitrosation via an active site cysteine residue. Cysteine 109-117 Rac family small GTPase 1 Homo sapiens 0-4 22157745-4 2012 We show that Rac1 can incorporate palmitate at cysteine 178 and that this post-translational modification targets Rac1 for stabilization at actin cytoskeleton-linked ordered membrane regions. Cysteine 47-55 Rac family small GTPase 1 Homo sapiens 13-17 22157762-3 2012 This study shows that Rac1 is localized in the mitochondria of alveolar macrophages from asbestosis patients, and mitochondrial import requires the C-terminal cysteine of Rac1 (Cys-189), which is post-translationally modified by geranylgeranylation. Cysteine 159-167 Rac family small GTPase 1 Homo sapiens 22-26 22157762-3 2012 This study shows that Rac1 is localized in the mitochondria of alveolar macrophages from asbestosis patients, and mitochondrial import requires the C-terminal cysteine of Rac1 (Cys-189), which is post-translationally modified by geranylgeranylation. Cysteine 159-167 Rac family small GTPase 1 Homo sapiens 171-175 22157762-3 2012 This study shows that Rac1 is localized in the mitochondria of alveolar macrophages from asbestosis patients, and mitochondrial import requires the C-terminal cysteine of Rac1 (Cys-189), which is post-translationally modified by geranylgeranylation. Cysteine 177-180 Rac family small GTPase 1 Homo sapiens 22-26 22157762-3 2012 This study shows that Rac1 is localized in the mitochondria of alveolar macrophages from asbestosis patients, and mitochondrial import requires the C-terminal cysteine of Rac1 (Cys-189), which is post-translationally modified by geranylgeranylation. Cysteine 177-180 Rac family small GTPase 1 Homo sapiens 171-175 22157762-4 2012 Furthermore, H(2)O(2) generation mediated by mitochondrial Rac1 requires electron transfer from cytochrome c to a cysteine residue on Rac1 (Cys-178). Cysteine 114-122 Rac family small GTPase 1 Homo sapiens 59-63 22157762-4 2012 Furthermore, H(2)O(2) generation mediated by mitochondrial Rac1 requires electron transfer from cytochrome c to a cysteine residue on Rac1 (Cys-178). Cysteine 114-122 Rac family small GTPase 1 Homo sapiens 134-138 22157762-4 2012 Furthermore, H(2)O(2) generation mediated by mitochondrial Rac1 requires electron transfer from cytochrome c to a cysteine residue on Rac1 (Cys-178). Cysteine 140-143 Rac family small GTPase 1 Homo sapiens 59-63 22157762-4 2012 Furthermore, H(2)O(2) generation mediated by mitochondrial Rac1 requires electron transfer from cytochrome c to a cysteine residue on Rac1 (Cys-178). Cysteine 140-143 Rac family small GTPase 1 Homo sapiens 134-138 21060846-3 2010 Analyses of different chimeras revealed that nuclear accumulation of C. albicans Rac1 requires the NLS-motifs at its carboxyl-terminus, which are blocked by prenylation of the adjacent cysteine residue. Cysteine 185-193 Rac family small GTPase 1 Homo sapiens 81-85 18589439-3 2008 The structure of the Vav1 DH-PH-CRD/Rac1 complex to 2.6 A resolution reveals a unique intramolecular network of contacts between the Vav1 cysteine-rich domain (CRD) and the C-terminal helix of the Vav1 Dbl homology (DH) domain. Cysteine 138-146 Rac family small GTPase 1 Homo sapiens 36-40 17275330-2 2007 Vav1 is also a unique member of the GEF family in that it contains a cysteine-rich domain (CRD) that is critical for Rac1 binding and maximal guanine nucleotide exchange activity, and thus may provide a unique protein-protein interface compared to other GEF/GTPase pairs. Cysteine 69-77 Rac family small GTPase 1 Homo sapiens 117-121 17128987-2 2006 We now show that the reaction of RhoA with redox agents leads to different functional consequences from that of Rac1 and Cdc42 due to the presence of an additional cysteine (GXXXCGK(S/T)C) in the RhoA redox-active motif. Cysteine 164-172 Rac family small GTPase 1 Homo sapiens 112-116 16709244-7 2006 Mutations in the Dbl homology, pleckstrin homology, or cysteine-rich domains of Vav1Y3F abolished Rac1 or ERK activation in the absence of EGF and blocked the migration-promoting activity of Vav1Y3F. Cysteine 55-63 Rac family small GTPase 1 Homo sapiens 98-102 16091733-3 2005 Hypoxia or the counteradhesive matricellular protein SPARC/BM-40 (SPARC: secreted protein acidic rich in cysteine) overexpressed during cancer progression also commutated PAR-1 to cellular invasion through the cGMP/protein kinase G (PKG) cascade, RhoA inactivation, and Rac1-dependent or -independent signaling. Cysteine 105-113 Rac family small GTPase 1 Homo sapiens 270-274 12006387-2 2002 Here, we investigated the role of isoprenylcysteine carboxyl methyltransferase (ICMTase), which methylates isoprenylated CAAX (where C indicates cysteine; A, aliphatic amino acids; and X, almost any other amino acid) proteins, including Rac1, a component of superoxide-generating NAD(P)H oxidase, in the expression of VCAM-1. Cysteine 43-51 Rac family small GTPase 1 Homo sapiens 237-241 1464587-2 1992 rac1 and rac2 p21s have a Cys-A-A-Leu (A = aliphatic amino acid) structure in their C-terminal region which may undergo post-translational processing including prenylation, proteolysis, and carboxyl methylation. Cysteine 26-29 Rac family small GTPase 1 Homo sapiens 0-4 1903399-8 1991 Site-directed mutagenesis established that the isoprenylated cysteines in the rac1, rac2, and ralA proteins were located in the fourth position from the carboxyl terminus. Cysteine 61-70 Rac family small GTPase 1 Homo sapiens 78-82 1903399-10 1991 The isoprenylation of rac1 (CSLL), ralA (CCIL), and the site-directed mutants rac1 (CRLL) and ralA (CSIL), demonstrates that the amino acid adjacent to the cysteine need not be aliphatic. Cysteine 156-164 Rac family small GTPase 1 Homo sapiens 22-26 1903399-10 1991 The isoprenylation of rac1 (CSLL), ralA (CCIL), and the site-directed mutants rac1 (CRLL) and ralA (CSIL), demonstrates that the amino acid adjacent to the cysteine need not be aliphatic. Cysteine 156-164 Rac family small GTPase 1 Homo sapiens 78-82 2119580-3 1990 A similar COOH-terminal amino acid sequence, Cys-Xaa-Ali-Xaa, exists in the ras-related GTP-binding proteins rac 1 and rac 2. Cysteine 45-48 Rac family small GTPase 1 Homo sapiens 109-114 2119580-5 1990 We report here that both rac 1 and rac 2 are post-translationally modified by addition of an isoprenoid group, the likely site of which is the COOH-terminal cysteine. Cysteine 157-165 Rac family small GTPase 1 Homo sapiens 25-30 31609245-4 2019 Rac1 activation requires a posttranslational modification, geranylgeranylation, of the C-terminal cysteine residue. Cysteine 98-106 Rac family small GTPase 1 Homo sapiens 0-4