Protein Post-translational Modification

Protein Post-Translational Modification (PTM) plays an essential role in cellular control mechanisms that adjust protein physical and chemical properties, folding, conformation, stability and activity, thus also altering protein function.

Four articles in this field were published in Nucleic Acids Research. dbPTM is a comprehensive information repository of protein post-translational modification (PTM) (Nucl Acids Res, 2006). Furthermore, we developed KinasePhos [1.0, 2.0], which is a web tool for identifying protein kinase-specific phosphorylation site (Nucl Acids Res, 2005, 2007, J. Comp Chem 2005). Besides, ProKware was designed as an integrated software for presenting protein structural properties in protein tertiary structures (Nucl Acids Res, 2006). These database and tools were totally cited more than 90 times during last three years.

Post-Transcriptional Regulation

  • SpliceInfo an information repository for the modes of mRNA alternative splicing in human genome (Nucl Acids Res, 2005)

  • ProSplicer an alternative splicing database based on protein, mRNA, and EST sequences (Genome Biology, 2003)

We coperate with...

  • N-Ace: using solvent accessibility and physicochemical properties to identify protein N-Acetylation sites.

    Lee TY, Hsu JBK, Lin FM, Chang WC, Hsu PC, & Huang HD
    Journal of Computational Chemistry 31, 2759-2771.

    PUBMED: 19460868

  • A Comprehensive Resource for Integrating and Displaying Protein Post-Translational Modifications

    T.Y. Lee, J.B.K. Hsu, W.C. Chang, T.Y. Wang, P.C. Hsu, and H.D. Huang*
    BMC Research Notes, 2(1):111, 2009

  • dbPTM: An information repository of protein post-translational modification

    T.Y. Lee?, H.D. Huang?, * (? joint first authorship), J.H. Hung, Y.S. Yang, and T.H. Wang*.
    Nucleic Acids Research, Vol. 34, D622-D627, 2006.