PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27255182-10 2016 Breast cancer cell lines MCF10A and MDA-MB-231 grown in methionine-restricted cysteine-depleted media for 24 h also up-regulated P21 and P27 gene expression, and MDA-MB-231 cells had decreased proliferation. Cysteine 78-86 H3 histone pseudogene 16 Homo sapiens 129-132 17320764-5 2007 The results of LC-MS/MS analysis of tryptic peptides of p21ras treated with ONOO(-) showed that ICAT labeling of Cys(118) was decreased by 47%, whereas Cys(80) was not significantly affected and was thereby shown to be less reactive. Cysteine 113-116 H3 histone pseudogene 16 Homo sapiens 56-59 17314138-6 2007 Conversely, its interaction with a key cysteine residue on p21(ras), led to its activation, an obligatory activity for AS101-induced neuronal differentiation. Cysteine 39-47 H3 histone pseudogene 16 Homo sapiens 59-62 17320764-5 2007 The results of LC-MS/MS analysis of tryptic peptides of p21ras treated with ONOO(-) showed that ICAT labeling of Cys(118) was decreased by 47%, whereas Cys(80) was not significantly affected and was thereby shown to be less reactive. Cysteine 152-155 H3 histone pseudogene 16 Homo sapiens 56-59 15323418-5 2004 Each cysteine mutant can increase endogenous p21 level, and also increased mortality rate of 293 cells when exposed to H2O2. Cysteine 5-13 H3 histone pseudogene 16 Homo sapiens 45-48 16415107-8 2006 These results indicate that peroxynitrite arising from NO donors or pathological stimuli such as oxLDL triggers direct S-glutathiolation of p21ras Cys-118, which increases p21ras activity and mediates downstream signaling. Cysteine 147-150 H3 histone pseudogene 16 Homo sapiens 140-143 1501882-1 1992 rap1/Krev-1/smg p21 (smg p21), a member of the small GTP-binding protein (G protein) superfamily, has a geranylgeranylated cysteine residue and clustered basic amino acids in the C-terminal region. Cysteine 123-131 H3 histone pseudogene 16 Homo sapiens 16-19 7494090-2 1995 FTase catalyzes the transfer of a farnesyl group from farnesylpyrophosphate (FPP) to cysteine 185/186 at the carboxyl terminal end of ras proteins (ras p21), a reaction essential for the localization of ras p21 to the plasma membrane for their cellular functions including cell transformation in case of oncogenic ras p21. Cysteine 85-93 H3 histone pseudogene 16 Homo sapiens 152-155 7494090-2 1995 FTase catalyzes the transfer of a farnesyl group from farnesylpyrophosphate (FPP) to cysteine 185/186 at the carboxyl terminal end of ras proteins (ras p21), a reaction essential for the localization of ras p21 to the plasma membrane for their cellular functions including cell transformation in case of oncogenic ras p21. Cysteine 85-93 H3 histone pseudogene 16 Homo sapiens 207-210 7494090-2 1995 FTase catalyzes the transfer of a farnesyl group from farnesylpyrophosphate (FPP) to cysteine 185/186 at the carboxyl terminal end of ras proteins (ras p21), a reaction essential for the localization of ras p21 to the plasma membrane for their cellular functions including cell transformation in case of oncogenic ras p21. Cysteine 85-93 H3 histone pseudogene 16 Homo sapiens 207-210 8175645-9 1994 Furthermore, Cys-3-AMBA-Met and Cys-4-ABA-Met are true inhibitors of p21ras FTase since they are not farnesylated by this enzyme, in contrast to Cys-Val-Ile-Met, which inhibits the enzyme by acting as alternative substrate. Cysteine 13-16 H3 histone pseudogene 16 Homo sapiens 69-72 12510823-7 2002 This key post-translational modification is catalyzed by the enzyme Ras famesyltransferase (FTase), which transfers a famesyl group from farnesylpyrophosphate to the C-terminal cysteine of the Ras protein. Cysteine 177-185 H3 histone pseudogene 16 Homo sapiens 68-71 12510823-7 2002 This key post-translational modification is catalyzed by the enzyme Ras famesyltransferase (FTase), which transfers a famesyl group from farnesylpyrophosphate to the C-terminal cysteine of the Ras protein. Cysteine 177-185 H3 histone pseudogene 16 Homo sapiens 193-196 1501280-4 1992 Fractionation of radiolabeled oocyte extracts on 10 to 60% sucrose gradients revealed that Cys-minus core proteins resolved into the nonparticulate and capsid forms seen for wild-type p21.5. Cysteine 91-94 H3 histone pseudogene 16 Homo sapiens 184-187 1501280-8 1992 However, Cys residues stabilize isolated p21.5 structures, as evidenced by the marked reduction in stability of Cys-minus dimers and capsids (i) in nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis and (ii) upon protease digestion. Cysteine 9-12 H3 histone pseudogene 16 Homo sapiens 41-44 1501882-4 1992 Moreover, smg p21 is phosphorylated by cyclic AMP- and cyclic GMP-dependent protein kinases at the serine residue between the polybasic region and the prenylated cysteine residue, and this phosphorylation initiates the smg GDS-induced smg p21 activation. Cysteine 162-170 H3 histone pseudogene 16 Homo sapiens 14-17 1501882-1 1992 rap1/Krev-1/smg p21 (smg p21), a member of the small GTP-binding protein (G protein) superfamily, has a geranylgeranylated cysteine residue and clustered basic amino acids in the C-terminal region. Cysteine 123-131 H3 histone pseudogene 16 Homo sapiens 25-28 1939117-1 1991 smg p21B, a member of the ras p21-like small GTP-binding protein superfamily, undergoes post-translational modifications, which are geranylgeranylation of the cysteine residue in the C-terminal region followed by removal of the three C-terminal amino acids (QLL) and the subsequent carboxyl methylation of the exposed prenylated cysteine residue. Cysteine 159-167 H3 histone pseudogene 16 Homo sapiens 4-7 1939117-1 1991 smg p21B, a member of the ras p21-like small GTP-binding protein superfamily, undergoes post-translational modifications, which are geranylgeranylation of the cysteine residue in the C-terminal region followed by removal of the three C-terminal amino acids (QLL) and the subsequent carboxyl methylation of the exposed prenylated cysteine residue. Cysteine 329-337 H3 histone pseudogene 16 Homo sapiens 4-7 1900364-3 1991 Two ras-related human genes rap1A and rap1B encode 95% homologous 21-kDa proteins that share with Ras p21 the same effector domain and a similar C-terminal Cys-Ali-Ali-Xaa sequence (where Ali is an aliphatic amino acid; also known as a CAAX sequence). Cysteine 156-159 H3 histone pseudogene 16 Homo sapiens 102-105 1924354-6 1991 These observations indicate that the amino acid occupying the terminal position (Xaa) in the Cys-Ali-Ali-Xaa motif constitutes a key structural feature by which Ha-ras p21 and other proteins with ras-like COOH-terminal isoprenylation sites are distinguished as substrates for farnesyl- or geranylgeranyltransferases. Cysteine 93-96 H3 histone pseudogene 16 Homo sapiens 168-171 3330790-6 1987 These data identify the first base of codon 13 as a novel mutation site in ras genes and indicate that cysteine at position 13 of the ras p21 is a transforming substitution. Cysteine 103-111 H3 histone pseudogene 16 Homo sapiens 138-141 2567085-6 1989 Since one would anticipate that the valine/cysteine substitution at position 12 of the ras p21 would occur at only low frequencies in human tumors, our results with DWP are consistent with this hypothesis. Cysteine 43-51 H3 histone pseudogene 16 Homo sapiens 91-94 6096811-2 1984 The oncogene of PR371 was found to present a mutation at codon 12 of the first coding exon which substitutes cysteine for glycine in the encoded p21 protein. Cysteine 109-117 H3 histone pseudogene 16 Homo sapiens 145-148 3333361-7 1986 p21 appears to have a small membrane binding domain at the C-terminus, which contains a palmitylation site at cysteine-186, four amino acid residues from the end. Cysteine 110-118 H3 histone pseudogene 16 Homo sapiens 0-3