The ubiquitin fusion technique, developed in 1986, is still the method of choice for producing a desired N-terminal residue in a protein of interest in vivo. This technique is also used as a tool for protein expression. Over the past two decades, several otherwise unrelated methods were invented that have in common the use of ubiquitin fusions as a component of design. I describe the original ubiquitin fusion technique, its current applications, and other methods that use the properties of ubiquitin fusions.