Recombinant technology allows engineering and production of proteins with desirable properties. Human serum albumin has been developed with recombinant technology, and thus plays an increasing role as a drug carrier in the clinical setting. Genetic variations usually occur on the surface of the protein, and do not impose significant effects on the conformation of albumin. However, binding of fatty acids by genetic variants is affected according to the location of the mutation. Albumin undergoes three major posttranslational modifications, namely, oxidation, glycation, and S-nitrosylation. This review gives an account of the different posttranslational modifications that should be taken into consideration when designing albumin mutant analogues with desirable pharmaceutical properties.