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http://purl.uniprot.org/citations/2123345http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2123345http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2123345http://www.w3.org/2000/01/rdf-schema#comment"smg p21A and -B are small GTP-binding proteins that share putative effector and consensus C-terminal sequences with ras p21 proteins. In the present report, we showed that human platelet smg p21B became labeled when intact platelets were incubated with exogenous [3H]mevalonolactone and when a purified preparation of smg p21B was incubated with bovine brain membranes and S-adenosyl-L-[methyl-3H]methionine. In addition, we demonstrated by gas chromatography/mass spectrometry that treatment of smg p21B with Raney nickel released a geranylgeranyl moiety in a molar ratio of about 1:1. In contrast, treatment of smg p21B with NH2OH or KOH yielded no evidence for the presence of a palmitoyl thioester. Extensive digestion of smg p21B with Achromobacter protease I yielded two C-terminal tripeptides that contained serine and cysteine in a molar ratio of 2:1. Both peptides were modified by a thioether-linked geranylgeranyl group. One of the peptides comigrated with a 3H-labeled proteolytic product of methylated smg p21B on reverse-phase HPLC and this peptide appeared at the same retention time as that of the other peptide after being treated with KOH. Since the cDNA-predicted C-terminal sequence of smg p21B contains a unique Ser-Ser-Cys peptide within its C-terminal domain, -Lys-Lys-Ser-Ser-Cys-Gln-Leu-Leu184, these results indicate that smg p21B is posttranslationally modified by geranylgeranylation of Cys-181 and suggest that further modifications cause proteolytic removal of the three predicted C-terminal amino acids followed by partial methylation of the cysteinyl carboxyl group."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.org/dc/terms/identifier"doi:10.1073/pnas.87.22.8960"xsd:string
http://purl.uniprot.org/citations/2123345http://purl.org/dc/terms/identifier"doi:10.1073/pnas.87.22.8960"xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Takai Y."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Takai Y."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Yoshida Y."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Yoshida Y."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Gelb M.H."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Gelb M.H."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Kawata M."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Kawata M."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Farnsworth C.C."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Farnsworth C.C."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Glomset J.A."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/author"Glomset J.A."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/pages"8960-8964"xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/pages"8960-8964"xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/title"Posttranslationally processed structure of the human platelet protein smg p21B: evidence for geranylgeranylation and carboxyl methylation of the C-terminal cysteine."xsd:string
http://purl.uniprot.org/citations/2123345http://purl.uniprot.org/core/title"Posttranslationally processed structure of the human platelet protein smg p21B: evidence for geranylgeranylation and carboxyl methylation of the C-terminal cysteine."xsd:string
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