Dr1 is a nuclear protein of 19 kDa that exists in the nucleoplasm as a homotetramer. By binding to TBP (the DNA-binding subunit of TFIID, and also a subunit of SL1 and TFIIIB), the protein blocks class II and class III preinitiation complex assembly, thus repressing the activity of the corresponding promoters. Since transcription of class I genes is unaffected by Drl, it has been proposed that the protein may coordinate the expression of class I, class II and class III genes. By somatic cell genetics and fluorescence in situ hybridization, we have localized the gene (DRl), present in the genome of higher eukaryotes as a single copy, to human chromosome region 1p21→p13. The nucleotide sequence conservation of the coding segment of the gene, as determined by Noah’s ark blot analysis, and its ubiquitous transcription suggest that Drl has an important biological role, which could be related to the negative control of cell proliferation.