Telomeres are DNA-protein structures that protect the ends of linear chromosomes and help maintain genomic stability and cell phenotype. Mammalian telomeric proteins consist of TRF1 (telomeric repeat binding factor), TRF2, tankyrase, and TIN2, which have no recognized orthologs in the budding yeast, Saccharomyces cerevisiae, and RAP1, which is an ortholog to the yeast telomeric protein scRap1. Like scRap1, mammalian RAP1 regulates telomere elongation. RAP1 interacts with two proteins, Rif1 and Rif2, which contribute to telomere length homeostasis. Unlike scRap1, which binds telomeric DNA directly, RAP1 is recruited to telomeres by TRF2. The functional and structural similarities of scRap1 to mammalian RAP1 suggest that the budding yeast preserved RAP1 at telomeres, but lost the TRF component. The telomeric protein TRF1 requires TIN2 to control telomere length in human cells.