Characterization of the ubiquitin code
Project/Area Number |
23657112
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Research Category |
Grant-in-Aid for Challenging Exploratory Research
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Allocation Type | Multi-year Fund |
Research Field |
Molecular biology
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Research Institution | National Institute of Health Sciences (2012-2013) The University of Tokyo (2011) |
Principal Investigator |
OHTAKE Fumiaki 国立医薬品食品衛生研究所, 毒性部, 主任研究官 (60447373)
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Project Period (FY) |
2011 – 2012
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Project Status |
Completed (Fiscal Year 2013)
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Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2011: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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Keywords | ユビキチン / 翻訳後修飾 / 蛋白質 / 質量分析 |
Research Abstract |
Post-translational modifications (PTMs) govern many aspects of biological systems. Ubiquitylation is a versatile PTM whose functional diversity has not been fully understood. In this study, we investigated a possibility that ubiquitin, itself a source of PTM, is functionally regulated by another PTM. Our research identified ubiquitin phosphorylation sites from cellular ubiquitin conjugated to substrates.
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Report
(4 results)
Research Products
(4 results)
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[Journal Article] JMJD5, a JmjC-domain-containing protein, negatively regulates osteoclastogenesis through facilitating NFATc1 protein degradation.2012
Author(s)
Youn MY, Yokoyama A, Fujiyama-Nakamura S, Ohtake F, Minehata KI, Yasuda H, Suzuki T, Kato S, *Imai Y.
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Journal Title
J Biol Chem
Volume: 287
Pages: 12994-3004
Related Report
Peer Reviewed
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