pubmed-article:11914276 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11914276 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:11914276 | lifeskim:mentions | umls-concept:C0751973 | lld:lifeskim |
pubmed-article:11914276 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
pubmed-article:11914276 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:11914276 | pubmed:dateCreated | 2002-3-26 | lld:pubmed |
pubmed-article:11914276 | pubmed:abstractText | Protein localization data are a valuable information resource helpful in elucidating eukaryotic protein function. Here, we report the first proteome-scale analysis of protein localization within any eukaryote. Using directed topoisomerase I-mediated cloning strategies and genome-wide transposon mutagenesis, we have epitope-tagged 60% of the Saccharomyces cerevisiae proteome. By high-throughput immunolocalization of tagged gene products, we have determined the subcellular localization of 2744 yeast proteins. Extrapolating these data through a computational algorithm employing Bayesian formalism, we define the yeast localizome (the subcellular distribution of all 6100 yeast proteins). We estimate the yeast proteome to encompass approximately 5100 soluble proteins and >1000 transmembrane proteins. Our results indicate that 47% of yeast proteins are cytoplasmic, 13% mitochondrial, 13% exocytic (including proteins of the endoplasmic reticulum and secretory vesicles), and 27% nuclear/nucleolar. A subset of nuclear proteins was further analyzed by immunolocalization using surface-spread preparations of meiotic chromosomes. Of these proteins, 38% were found associated with chromosomal DNA. As determined from phenotypic analyses of nuclear proteins, 34% are essential for spore viability--a percentage nearly twice as great as that observed for the proteome as a whole. In total, this study presents experimentally derived localization data for 955 proteins of previously unknown function: nearly half of all functionally uncharacterized proteins in yeast. To facilitate access to these data, we provide a searchable database featuring 2900 fluorescent micrographs at http://ygac.med.yale.edu. | lld:pubmed |
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pubmed-article:11914276 | pubmed:language | eng | lld:pubmed |
pubmed-article:11914276 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11914276 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11914276 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11914276 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11914276 | pubmed:month | Mar | lld:pubmed |
pubmed-article:11914276 | pubmed:issn | 0890-9369 | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:VoasRR | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:KumarAnujA | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:CheungKei-Hoi... | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:MillerPerryP | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:SnyderMichael... | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:JansenRonaldR | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:GersteinMarkM | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:RoederG... | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:AgarwalSeemaS | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:HeymanJohn... | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:MatsonSandraS | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:HeidtmanMatth... | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:PiccirilloSta... | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:UmanskyLaraL | lld:pubmed |
pubmed-article:11914276 | pubmed:author | pubmed-author:DrawidAmarA | lld:pubmed |
pubmed-article:11914276 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11914276 | pubmed:day | 15 | lld:pubmed |
pubmed-article:11914276 | pubmed:volume | 16 | lld:pubmed |
pubmed-article:11914276 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11914276 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11914276 | pubmed:pagination | 707-19 | lld:pubmed |
pubmed-article:11914276 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:11914276 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:11914276 | pubmed:articleTitle | Subcellular localization of the yeast proteome. | lld:pubmed |
pubmed-article:11914276 | pubmed:affiliation | Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA. | lld:pubmed |
pubmed-article:11914276 | pubmed:publicationType | Journal Article | lld:pubmed |