TRF 2 | TTAGGG repeat binding factor 2

Telomeric repeat-binding factor 2 also known as TRF2 is a 500 amino acid containing telomere specific protein. This nuclear protein with a HTH myb-type DNA-binding domain is a component of the telomere nucleoprotein complex. Usually present at telomeres in metaphase of the cell cycle, TRF2 is a second negative regulator of telomere length where it protects against end-to-end fusion of chromosomes by binding to the telomeric double-stranded TTAGGG repeat. Absence of TRF2 leads to damage of telomeres which are now no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Thus it plays a role in successful progression through the cell division cycle. TRF2 shows ubiquitous expression in most of the tissues with high expression in spleen, thymus, prostate, uterus, testis, small intestine, colon and peripheral blood leukocytes. A component of the shelterin complex (telosome), TRF2 differs from TERF1 in that its N terminus is basic rather than acidic.