DESCRIBE <http://purl.uniprot.org/citations/19933165>

Subject	Predicate	Object
http://purl.uniprot.org/citations/19933165	http://www.w3.org/1999/02/22-rdf-syntax-ns#type	http://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19933165	http://www.w3.org/1999/02/22-rdf-syntax-ns#type	http://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19933165	http://www.w3.org/2000/01/rdf-schema#comment	" Unlabelled Using sensitive sequence profile analysis, we identify a hitherto uncharacterized cysteine-rich, transmembrane (TM) module, CYSTM, found in a wide range of tail-anchored membrane proteins across eukaryotes. This superfamily includes Schizosaccharomyces Uvi15, Arabidopsis PCC1, Digtaria CDT1 and Saccharomyces proteins YDL012C and YDR210W, which have all been implicated in resistance/response to stress or pathogens. Based on the pattern of conserved cysteines and data from different chemical genetics studies, we suggest that CYSTM proteins might have critical role in responding to deleterious compounds at the plasma membrane via chelation or redox-based mechanisms. Thus, CYSTM proteins are likely to be part of a novel cellular protective mechanism that is widely active in eukaryotes, including humans. Supplementary information Supplementary data are available at Bioinformatics online."xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.org/dc/terms/identifier	"doi:10.1093/bioinformatics/btp647"xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.org/dc/terms/identifier	"doi:10.1093/bioinformatics/btp647"xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/author	"Aravind L."xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/author	"Aravind L."xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/author	"Venancio T.M."xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/author	"Venancio T.M."xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/date	"2010"xsd:gYear
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/date	"2010"xsd:gYear
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/name	"Bioinformatics"xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/name	"Bioinformatics"xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/pages	"149-152"xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/pages	"149-152"xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/title	"CYSTM, a novel cysteine-rich transmembrane module with a role in stress tolerance across eukaryotes."xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/title	"CYSTM, a novel cysteine-rich transmembrane module with a role in stress tolerance across eukaryotes."xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/volume	"26"xsd:string
http://purl.uniprot.org/citations/19933165	http://purl.uniprot.org/core/volume	"26"xsd:string
http://purl.uniprot.org/citations/19933165	http://www.w3.org/2004/02/skos/core#exactMatch	http://purl.uniprot.org/pubmed/19933165
http://purl.uniprot.org/citations/19933165	http://www.w3.org/2004/02/skos/core#exactMatch	http://purl.uniprot.org/pubmed/19933165
http://purl.uniprot.org/citations/19933165	http://xmlns.com/foaf/0.1/primaryTopicOf	https://pubmed.ncbi.nlm.nih.gov/19933165
http://purl.uniprot.org/citations/19933165	http://xmlns.com/foaf/0.1/primaryTopicOf	https://pubmed.ncbi.nlm.nih.gov/19933165
http://purl.uniprot.org/uniprot/Q94C26	http://purl.uniprot.org/core/citation	http://purl.uniprot.org/citations/19933165
http://purl.uniprot.org/uniprot/Q94C26#attribution-57B168A7321FA410D20B6F35E20E178B	http://purl.uniprot.org/core/source	http://purl.uniprot.org/citations/19933165