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Current Protein & Peptide Science


ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

Computational Analysis of Phosphoproteomics: Progresses and Perspectives

Author(s): Jian Ren, Xinjiao Gao, Zexian Liu, Jun Cao, Qian Ma and Yu Xue

Volume 12, Issue 7, 2011

Page: [591 - 601] Pages: 11

DOI: 10.2174/1389203711109070591

Price: $65


Phosphorylation is one of the most essential post-translational modifications (PTMs) of proteins, regulates a variety of cellular signaling pathways, and at least partially determines the biological diversity. Recent progresses in phosphoproteomics have identified more than 100,000 phosphorylation sites, while this number will easily exceed one million in the next decade. In this regard, how to extract useful information from flood of phosphoproteomics data has emerged as a great challenge. In this review, we summarized the leading edges on computational analysis of phosphoproteomics, including discovery of phosphorylation motifs from phosphoproteomics data, systematic modeling of phosphorylation network, analysis of genetic variation that influences phosphorylation, and phosphorylation evolution. Based on existed knowledge, we also raised several perspectives for further studies. We believe that integration of experimental and computational analyses will propel the phosphoproteomics research into a new phase.

Keywords: Post-translational modification, phosphorylation, phosphorylation motif, phosphorylation network, phosGV, phosphorylation evolution, PTMs, PKs, HTP-MS, BRCT

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