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Systematic Decoding of Deubiquitylase-Regulated Signaling Networks

Total Cost €


EC-Contrib. €






Project "DUB-DECODE" data sheet

The following table provides information about the project.


Organization address
address: NORREGADE 10
postcode: 1165

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Denmark [DK]
 Total cost 1˙972˙570 €
 EC max contribution 1˙972˙570 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2014-CoG
 Funding Scheme ERC-COG
 Starting year 2015
 Duration (year-month-day) from 2015-10-01   to  2020-09-30


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    KOBENHAVNS UNIVERSITET DK (KOBENHAVN) coordinator 1˙972˙570.00


 Project objective

Cellular processes are largely governed by sophisticated protein posttranslational modification (PTM)-dependent signaling networks, and a systematic understanding of regulatory PTM-based networks is a key goal in modern biology. Ubiquitin is a small, evolutionarily conserved signaling protein that acts as a PTM after being covalently conjugated to other proteins. Reversible ubiquitylation forms the most versatile and largest eukaryote-exclusive signaling system, and regulates the stability and function of almost all proteins in cells. Deubiquitylases (DUBs) are ubiquitin-specific proteases that remove substrate-conjugated ubiquitin, and thereby regulate virtually all ubiquitylation-dependent signaling. Because of their central role in ubiquitin signaling, DUBs have essential functions in mammalian physiology and development, and the dysregulated expression and mutation of DUBs is frequently associated with human diseases. Despite their vital functions, very little is known about the proteins and ubiquitylation sites that are regulated by DUBs and this knowledge gap is hampering our understanding of the molecular mechanisms by which DUBs control diverse biological processes. Recently, we developed a mass spectrometry-based proteomics approach that allowed unbiased and site-specific quantification of ubiquitylation on a systems-wide scale. Here we propose to comprehensively investigate DUB-regulated ubiquitin signaling in human cells. We will integrate interdisciplinary approaches to develop next-generation cell models and innovative proteomic technologies to systematically decode DUB function in human cells. This will enable a novel and detailed understanding of DUB-regulated signaling networks, and open up new avenues for further research into the mechanisms and biological functions of ubiquitylation and of ubiquitin-like modifiers.


year authors and title journal last update
List of publications.
2016 Sebastian A Wagner, Shankha Satpathy, Petra Beli, Chunaram Choudhary
SPATA2 links CYLD to the TNF‐α receptor signaling complex and modulates the receptor signaling outcomes
published pages: 1868-1884, ISSN: 0261-4189, DOI: 10.15252/embj.201694300
The EMBO Journal 35/17 2019-06-06
2018 Rajat Gupta, Kumar Somyajit, Takeo Narita, Elina Maskey, Andre Stanlie, Magdalena Kremer, Dimitris Typas, Michael Lammers, Niels Mailand, Andre Nussenzweig, Jiri Lukas, Chunaram Choudhary
DNA Repair Network Analysis Reveals Shieldin as a Key Regulator of NHEJ and PARP Inhibitor Sensitivity
published pages: 972-988.e23, ISSN: 0092-8674, DOI: 10.1016/j.cell.2018.03.050
Cell 173/4 2019-06-06
2018 Thomas Wild, Magda Budzowska, Susanne Hellmuth, Susana Eibes, Gopal Karemore, Marin Barisic, Olaf Stemmann, Chunaram Choudhary
Deletion of APC7 or APC16 Allows Proliferation of Human Cells without the Spindle Assembly Checkpoint
published pages: 2317-2328.e5, ISSN: 2211-1247, DOI: 10.1016/j.celrep.2018.10.104
Cell Reports 25/9 2019-02-25

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