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2013 Fiscal Year Final Research Report

Characterization of the ubiquitin code

Research Project

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Project/Area Number 23657112
Research Category

Grant-in-Aid for Challenging Exploratory Research

Allocation TypeMulti-year Fund
Research Field Molecular biology
Research InstitutionNational 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)

Project Period (FY) 2011 – 2012
Keywordsユビキチン / 翻訳後修飾 / 蛋白質
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.

  • Research Products

    (1 results)

All 2012

All Journal Article (1 results) (of which Peer Reviewed: 1 results)

  • [Journal Article] JMJD5, a JmjC-domain-containing protein, negatively regulates osteoclastogenesis through facilitating NFATc1 protein degradation2012

    • Author(s)
      Youn MY, 他
    • Journal Title

      J Biol Chem

      Volume: 287 Pages: 12994-13004

    • DOI

      10.1074

    • Peer Reviewed

URL: 

Published: 2015-06-25  

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