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2.1.9: A9. In Vivo Post Translational Modification of Amino Acids

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    Amino acids in naturally occurring proteins are also subjected to chemical modification within cells. These modifications alter the properties of the amino acid that is modified, which can alter the structure and function of the protein. Most chemical modifications made to proteins within cells occur after the protein is synthesized in a process called translation. The resulting chemical changes are termed post-translational modifications.

    Figure: Post-translational modification of proteins

    posttransmod.gif

    Here is a list of post-translational modification from the Swiss Institute of Bioinformatics:

    • PDOC00001 1 N-glycosylation site

    • PDOC00004 1 cAMP- and cGMP-dependent protein kinase phosphorylation site

    • PDOC00005 1 Protein kinase C phosphorylation site

    • PDOC00006 1 Casein kinase II phosphorylation site

    • PDOC00007 1 Tyrosine kinase phosphorylation site

    • PDOC00008 1 N-myristoylation site

    • PDOC00009 1 Amidation site

    • PDOC00010 1 Aspartic acid and asparagine hydroxylation site

    • PDOC00012 1 Phosphopantetheine attachment site

    • PDOC00013 1 Prokaryotic membrane lipoprotein lipid attachment site

    • PDOC00342 1 Prokaryotic N-terminal methylation site

    • PDOC00266 1 Prenyl group binding site (CAAX box)

    • PDOC00687 2 Intein N- and C-terminal splicing motif profiles


    This page titled 2.1.9: A9. In Vivo Post Translational Modification of Amino Acids is shared under a CC BY-NC-SA license and was authored, remixed, and/or curated by Henry Jakubowski.

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