Telomere is an essential DNA-protein complex composed of repetitive DNA and binding proteins to protect the chromosomal ends in eukaryotes. Telomere length is regulated by a specialized RNA-dependent DNA polymerase, telomerase and associated proteins. We show here a potential role of STEP1 that was previously isolated by affinity chromatography in controlling telomere length. While STEP1 requires both RNA-binding domains for telomere binding and subsequent DNA protection, it requires only one RBD to interact with telomerase. The differential telomerase inhibitory activity depending on STEP1 concentrations may suggest that STEP1 contributes to controlling telomere length homeostasis, likely by limiting the accessibility of nuclease or telomerase to telomeric DNA.