Annotation of structural and un-structural regions in the human proteome.
| Project/Area Number |
20510195
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
ゲノム情報科学
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| Research Institution | National Institute of Genetics |
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Principal Investigator |
FUKUCHI Satoshi National Institute of Genetics, DDBJ・生命情報研究センター, 助教 (70360336)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2010: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2009: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2008: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 生体生命情報学 / 蛋白質 / 天然変性タンパク質 / 生命情報学 / アノテーショ / 構造予測 / アノテーション |
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| Research Abstract |
We estimated the fraction of intrinsically disordered (ID) regions in the human proteome by using bioinforamtics technique. Because it is still difficult to conduct an experimental verification of ID regions in a genome wide scale, bioinformatics is expected to make an answer to this question. Although ID prediction programs generally output only potentail ID regions, our system, DICHOT, can divid an amino acid sequence into two categories, structural domains (SDs) and ID regions. With this unique feature, we can firstly estimate SD/ID fractions in the human proteome to obtain 35% of ID region, 52% of SD with similarity to PDB structures, and 13% of SD without similarity to PDB structures in residue base. The last 13% is the regions, which have not known in 3D structure, thus, can be targets of the structural genomics. Several functional sites such as trans-activation, phpsphorylation, and O-linked glycosylation were estimated on ID regions. The ID fractions differ between protein's sub-cellular locations, where nuclear proteins have the highest and mitochondrial ones do the lowest. Interestingly, phosphorylation and O-linked glycosylation occur in ID regions in secreted proteins, which have less ID regions. Comparison of ID fractions between the proteomes from several model organisms suggest that high fractions of ID regions in the human proteome is common in eukaryotes, but in bacteria, which is agree with the ID distributions by the cellular locations.
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Report
(4 results)
Research Products
(21 results)
