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Verfasst von:Minguez, Pablo [VerfasserIn]   i
 Mende, Daniel Richard [VerfasserIn]   i
 Gavin, Anne-Claude [VerfasserIn]   i
 Bork, Peer [VerfasserIn]   i
Titel:Deciphering a global network of functionally associated post-translational modifications
Verf.angabe:Pablo Minguez, Luca Parca, Francesca Diella, Daniel R Mende, Runjun Kumar, Manuela Helmer-Citterich, Anne-Claude Gavin, Vera van Noort and Peer Bork
E-Jahr:2012
Jahr:2012 Jul 17
Umfang:14 S.
Teil:volume:8
 year:2012
 elocationid:599
 extent:14
Fussnoten:Gesehen am 23.10.2018
Titel Quelle:Enthalten in: Molecular systems biology
Ort Quelle:Heidelberg : EMBO Press, 2005
Jahr Quelle:2012
Band/Heft Quelle:8(2012), Artikel-ID 599
ISSN Quelle:1744-4292
Abstract:Various post-translational modifications (PTMs) fine-tune the functions of almost all eukaryotic proteins, and co-regulation of different types of PTMs has been shown within and between a number of proteins. Aiming at a more global view of the interplay between PTM types, we collected modifications for 13 frequent PTM types in 8 eukaryotes, compared their speed of evolution and developed a method for measuring PTM co-evolution within proteins based on the co-occurrence of sites across eukaryotes. As many sites are still to be discovered, this is a considerable underestimate, yet, assuming that most co-evolving PTMs are functionally associated, we found that PTM types are vastly interconnected, forming a global network that comprise in human alone >50,000 residues in about 6000 proteins. We predict substantial PTM type interplay in secreted and membrane-associated proteins and in the context of particular protein domains and short-linear motifs. The global network of co-evolving PTM types implies a complex and intertwined post-translational regulation landscape that is likely to regulate multiple functional states of many if not all eukaryotic proteins.
DOI:doi:10.1038/msb.2012.31
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: http://dx.doi.org/10.1038/msb.2012.31
 Volltext: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3421446/
 DOI: https://doi.org/10.1038/msb.2012.31
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1582185832
Verknüpfungen:→ Zeitschrift

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