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TERF1/TRF1  Protein, Antibody, ELISA Kit, cDNA Clone

TERF1/TRF1 Related Pathways

TERF1/TRF1 Related Protein, Antibody, cDNA Gene, and ELISA Kits

TERF1/TRF1 Summary & Protein Information

TERF1/TRF1 Background

Gene Summary: TERF1 gene encodes a telomere specific protein which is a component of the telomere nucleoprotein complex. This protein is present at telomeres throughout the cell cycle and functions as an inhibitor of telomerase, acting in cis to limit the elongation of individual chromosome ends. The protein structure contains a C-terminal Myb motif, a dimerization domain near its N-terminus and an acidic N-terminus. Two transcripts of TERF1 gene are alternatively spliced products. [provided by RefSeq, Jul 2008]
General information above from NCBI
Subunit structure: Homodimer; can contain both isoforms. Found in a complex with POT1; TINF2 and TNKS1. Interacts with ATM, TINF2, TNKS1, TNKS2, PINX1, NEK2 and MAPRE1. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with RLIM (via N-terminus). Interacts with FBXO4. Interaction with TINF2 protects against interaction with FBXO4 and subsequent polyubiquitination and proteasomal degradation. Interacts with GNL3L; this interaction promotes homodimerization. Interacts with TIN2. Interactions with GNL3L and TIN2 are mutually exclusive (By similarity).
Domain: The acidic N-terminal domain binds to the ankyrin repeats of TNKS1 and TNKS2. The C-terminal domain binds microtubules.
The TRFH dimerization region mediates the interaction with TINF2.
The HTH domain is an independent structural unit and mediates binding to telomeric DNA.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, telomere. Note=Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle.
Tissue specificity: Highly expressed and ubiquitous. Isoform Pin2 predominates.
Induction: Expression is tightly regulated during the cell cycle; levels are low in G1 and S phase and increase during G2 phase and mitosis.
Post-translational: Phosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage.
ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind to telomeric DNA.
Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex, leading to its degradation by the proteasome.
Sequence similarity: Contains 1 HTH myb-type DNA-binding domain.
General information above from UniProt

Telomeric repeat binding factor 1 (TRF1), also known as TERF1, the shelterin complex, which modulates the telomere structures. TRF1 protein structure contains a C-terminal Myb motif, a dimerization domain near its N-terminus and an acidic N-terminus. Pin2/TRF1 was originally identified as a protein bound to telomeric DNA (TRF1) and as a protein involved in mitotic regulation (Pin2). Pin2/TRF1 negatively regulates telomere length and importantly, its function is tightly regulated during the cell cycle, acting as an important regulator of mitosis. TRF1 can be bound and modulated by two nucleolar GTP-binding proteins, nucleostemin (NS) and guanine nucleotide binding protein-like 3-like (GNL3L), which exhibit apparently opposite effects on the protein degradation of TRF1. TRF1/TERF1 may has association with cancer. TRF1 may play a significant role in cell differentiation in non-small cell lung cancer (NSCLC). The expression level of TRF1 protein is significantly reduced in kidney cancer and the level is negatively correlated with malignant degree of the cancer. TRF1 expression in malignant gliomas cells, may play a role in the malignant progression of astroglial brain tumors.

TERF1/TRF1 Alternative Name

TERF1/TRF1 Related Studies

  • Tsai RY. (2009) Nucleolar modulation of TRF1: a dynamic way to regulate telomere and cell cycle by nucleostemin and GNL3L. Cell Cycle. 8(18):2912-6.
  • Chen YC, et al. (2009) Phosphorylation of telomeric repeat binding factor 1 (TRF1) by Akt causes telomere shortening. Cancer Invest. 27(1): 24-8.
  • Hu J, et al. (2006) Expression of telomeric repeat binding factor 1 in non-small cell lung cancer. J Surg Oncol. 93(1): 62-7.
  • La Torre D, et al. (2005) Expression of telomeric repeat binding factor-1 in astroglial brain tumors. Neurosurgery. 56(4): 802-10.
  • Shi JM, et al. (2004) Expression of telomere repeat binding factor 1 (TRF1) protein in kidney cancer. Zhejiang Da Xue Xue Bao Yi Xue Ban. 33(6): 496-9, 508.
  • Zhou XZ, et al. (2003) Role of Pin2/TRF1 in telomere maintenance and cell cycle control. J Cell Biochem. 89(1): 19-37.