Mammalian Elongin C is a ∼15 kDa protein that binds the von Hippel-Lindau (VHL) tumor suppressor and to Elongin A, the transcriptionally active subunit of the RNA polymerase II elongation factor, SIII. Although Elongin C was named for its role as a positive regulator of the transcription factor Elongin A, several lines of evidence indicate that the essential role of Elongin C, in the tumor suppressor function of the VHL complex, is unrelated to transcription. The overall objective of this work is to add insight into the biological function(s) of Elongin C by examining the highly conserved S. cerevisiae homolog, Elc1. Elc1 was identified by a BLAST search of the yeast genome. Characterization of yeast ELC1 revealed that the gene is non-essential, and the mRNA is expressed constitutively at low levels. The only other yeast protein identified with significant homology to Elc1 is Skp1, yet these proteins do not likely share overlapping functions. Strains containing mutations in both genes do not demonstrate synthetic lethality, nor does Skp1 interact with the same subset of proteins as Elc1. To gain further insight into the function of Elongin C, a two-hybrid screen using yeast Elc1 as the bait was conducted. The data indicate that Elc1 interacts strongly and specifically with several yeast proteins including Snf4, Pc16, Yap4/6, and Mdj1. The only obvious overlap between these gene products is a role in the regulation of protein stability. Thus, Elc1 may be involved in protein modulation. This hypothesis is supported by the observation that mammalian Elongin C is also found in complexes thought to be involved in the regulation of protein stability. The emerging theme in the mammalian and yeast systems supports a role for Elongin C as a fine-tuning regulator through involvement in complexes that both target specific proteins for degradation and increase the stability of other proteins