Akhilesh Pandey
733 N.Broadway Street, Broadway Research Building,
Room 527, Baltimore, Maryland 21205
Tanzania
Research Article
Identification of Novel Phosphorylation Motifs Through an Integrative Computational and Experimental Analysis of the Human Phosphoproteome
Author(s): Ramars Amanchy, Kumaran Kandasamy, Suresh Mathivanan, Balamurugan Periaswamy, Raghunath Reddy, Wan-Hee Yoon, Jos Joore, Michael A Beer, Leslie Cope and Akhilesh PandeyRamars Amanchy, Kumaran Kandasamy, Suresh Mathivanan, Balamurugan Periaswamy, Raghunath Reddy, Wan-Hee Yoon, Jos Joore, Michael A Beer, Leslie Cope and Akhilesh Pandey
Protein phosphorylation occurs in certain sequence/structural contexts that are still incompletely understood. The amino acids surrounding the phosphorylated residues are important in determining the binding of the kinase to the protein sequence. Upon phosphorylation these sequences also determine the binding of certain domains that specifically bind to phosphorylated sequences. Thus far, such 'motifs' have been identified through alignment of a limited number of well identified kinase substrates. Results: Experimentally determined phosphorylation sites from Human Protein Reference Database were used to identify 1,167 novel serine/threonine or tyrosine phosphorylation motifs using a computational approach. We were able to statistically validate a number of these novel motifs based on their enrichment in known phosphopeptides datasets over phosphoserine / threonine/tyrosine peptides in.. View More»
DOI: 10.4172/jpb.1000163
