Bioinformatics Analysis of Functional Associations of PTMs.
Post-translational modifications (PTMs) are an important source of protein regulation; they fine-tune the function, localization, and interaction with other molecules of the majority of proteins and are partially responsible for their multifunctionality. Usually, proteins have several potential modification sites, and their patterns of occupancy are associated with certain functional states. These patterns imply cross talk among PTMs within and between proteins, the majority of which are still to be discovered. Several methods detect associations between PTMs; these have recently combined into a global resource, the PTMcode database, which contains already known and predicted functional associations between pairs of PTMs from more than 45,000 proteins in 19 eukaryotic species.
Department of Genetics and Genomics, Instituto de Investigacion Sanitaria-University Hospital Fundacion Jimenez Diaz (IIS-FJD), Avda. Reyes Católicos 2, 28040, Madrid, Spain. pablo.minguez@quironsalud.es.
Pablo
P
Minguez
European Molecular Biology Laboratory, Structural and Computational Biology Unit, 69117, Heidelberg, Germany.|Max Delbrück Centre for Molecular Medicine, 13125, Berlin, Germany.
Peer
P
Bork
D019295:Computational Biology / Q000379:methods*; D030562:Databases, Protein; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D040901:Proteomics / Q000379:methods; D021281:Quantitative Structure-Activity Relationship; D012984:Software; D049490:Systems Biology / Q000379:methods; D014584:User-Computer Interface; D064878:Web Browser
D011506:Proteins
Post-translational modifications; Protein regulation; Protein–protein interactions; Proteomics; Systems biology