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  Dual Coordination of Post Translational Modifications in Human Protein Networks

Woodsmith, J., Kamburov, A., & Stelzl, U. (2013). Dual Coordination of Post Translational Modifications in Human Protein Networks. PLoS Computational Biology, 9(3), e1002933-e1002933. doi:10.1371/journal.pcbi.1002933.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0018-F3D3-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-0F21-4
Genre: Journal Article

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2013
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2013 Woodsmith et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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 Creators:
Woodsmith, J.1, Author              
Kamburov, A.2, Author              
Stelzl, U.1, Author              
Affiliations:
1Molecular Interaction Networks (Ulrich Stelzl), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479660              
2Bioinformatics (Ralf Herwig), Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479648              

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Free keywords: posttranslational modifications lysine acetylation web server phosphorylation cancer methylation ubiquitin genome database kinases
 Abstract: Post-translational modifications (PTMs) regulate protein activity, stability and interaction profiles and are critical for cellular functioning. Further regulation is gained through PTM interplay whereby modifications modulate the occurrence of other PTMs or act in combination. Integration of global acetylation, ubiquitination and tyrosine or serine/threonine phosphorylation datasets with protein interaction data identified hundreds of protein complexes that selectively accumulate each PTM, indicating coordinated targeting of specific molecular functions. A second layer of PTM coordination exists in these complexes, mediated by PTM integration (PTMi) spots. PTMi spots represent very dense modification patterns in disordered protein regions and showed an equally high mutation rate as functional protein domains in cancer, inferring equivocal importance for cellular functioning. Systematic PTMi spot identification highlighted more than 300 candidate proteins for combinatorial PTM regulation. This study reveals two global PTM coordination mechanisms and emphasizes dataset integration as requisite in proteomic PTM studies to better predict modification impact on cellular signaling.

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Language(s): eng - English
 Dates: 2013-03-072013
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1371/journal.pcbi.1002933
ISSN: 1553-7358
 Degree: -

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Title: PLoS Computational Biology
Source Genre: Journal
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Publ. Info: San Francisco, CA : Public Library of Science
Pages: - Volume / Issue: 9 (3) Sequence Number: - Start / End Page: e1002933 - e1002933 Identifier: ISSN: 1553-734X
CoNE: /journals/resource/1000000000017180_1