page_title: TERF2
section_title: Interactions
hierarchical_section_title: TERF2 / Interactions
caption_attribution_description: English: Describes TERF2 functionality with client proteins and recruitment specificity
context_page_description: Telomeric repeat-binding factor 2 is a protein that is present at telomeres throughout the cell cycle. It is also known as TERF2, TRF2, and TRBF2, and is encoded in humans by the TERF2 gene. It is a component of the shelterin nucleoprotein complex and a second negative regulator of telomere length, playing a key role in the protective activity of telomeres. It was first reported in 1997 in the lab of Titia de Lange, where a DNA sequence similar, but not identical, to TERF1 was discovered, with respect to the Myb-domain. De Lange isolated the new Myb-containing protein sequence and called it TERF2.
context_section_description: TERF2 is also known to recruit certain client proteins, also known as accessory factors. These client proteins are often recruited to TERF2 for a specific function at a specific time, often temporarily. The TRFH domain contains a F120 residue, which is the binding site of TERF2 where it recruits client proteins. These client proteins also contain a TRFH binding motif, which consists of a conserved 6-amino acid sequence of the following formula: YxLxP, where "x" can be any amino acid substituted. The above-mentioned Apollo nuclease (one of many TERF2's client proteins) also contains the formulaic motif; its specific motif sequence is YLLTP.
  TERF1 also demonstrates similar client protein recruitment mechanism as TERF2, except that it diverges at two concepts: 1) the TRFH of TERF1 contains a F142 residue, 2) the client proteins specific for TERF1 contain the TRFH binding motif sequence of FxLxP, where the amino acid Y (tyrosine) is replaced with F (phenylalanine).
  TERF2 has also been shown to interact with:
  Ku70,
  MRE11A,
  Nibrin and
  Rad50,
  RE1-silencing transcription factor,
  TERF2IP,
  Werner syndrome ATP-dependent helicase.
caption: Client proteins have a distinctive YxLxP motif (where "x" can be any amino acid) that bind to TERF2.[16]
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