Post-translational modification of the major human surfactant-associated proteins

Computational Prediction of Post-Translational Modification Sites in Proteins

The last several decades have witnessed rapid progresses in identification and functional analysis of post-translational modifications (PTMs) in proteins. Through temporal and spatial modification of proteins by covalent attachment of additional chemical groups and other small proteins, proteolytic cleavage or intein splicing, PTMs greatly expand the proteome diversity and play important roles ...

Post-translational modification of PII signal transduction proteins

The PII proteins constitute one of the most widely distributed families of signal transduction proteins in nature. They are pivotal players in the control of nitrogen metabolism in bacteria and archaea, and are also found in the plastids of plants. Quite remarkably PII proteins control the activities of a diverse range of enzymes, transcription factors and membrane transport proteins, and in al...

Post-translational modification and folding of secreted proteins.

The production of a functional protein does not end with the termination of the growing polypeptide chain. This, while clearly true of all proteins, is particularly obvious in the case of secretory proteins. While all proteins must fold to a functional conformation, and many must assemble into some supramolecular structure, secretory proteins must also make their way across membranes and throug...

Post-translational modification of exogenous proteins in Xenopus laevis oocytes.

ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins

Interpretation of genetic variation is needed for deciphering genotype-phenotype associations, mechanisms of inherited disease, and cancer driver mutations. Millions of single nucleotide variants (SNVs) in human genomes are known and thousands are associated with disease. An estimated 21% of disease-associated amino acid substitutions corresponding to missense SNVs are located in protein sites ...