TERF1

Telomeric repeat binding factor (NIMA-interacting) 1

PDB rendering based on 1ba5.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsTERF1 ; PIN2; TRBF1; TRF; TRF1; hTRF1-AS; t-TRF1
External IDsOMIM: 600951 MGI: 109634 HomoloGene: 7570 GeneCards: TERF1 Gene
Orthologs
SpeciesHumanMouse
Entrez701321749
EnsemblENSG00000147601ENSMUSG00000025925
UniProtP54274P70371
RefSeq (mRNA)NM_003218NM_001286628
RefSeq (protein)NP_003209NP_001273557
Location (UCSC)Chr 8:
73.92 – 73.96 Mb		Chr 1:
15.81 – 15.84 Mb
PubMed search

Telomeric repeat-binding factor 1 is a protein that in humans is encoded by the TERF1 gene.[1][2]

Function

This gene encodes a telomere specific protein which is a component of the shelterin 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 this gene are alternatively spliced products.[2]

Interactions

TERF1 has been shown to interact with:

References

  1. ↑ Shen M, Haggblom C, Vogt M, Hunter T, Lu KP (January 1998). "Characterization and cell cycle regulation of the related human telomeric proteins Pin2 and TRF1 suggest a role in mitosis". Proc. Natl. Acad. Sci. U.S.A. 94 (25): 13618–23. doi:10.1073/pnas.94.25.13618. PMC 28355. PMID 9391075. Check date values in: |year= / |date= mismatch (help)
  2. ↑ 2.0 2.1 "Entrez Gene: TERF1 telomeric repeat binding factor (NIMA-interacting) 1".
  3. ↑ 3.0 3.1 Kishi S, Zhou XZ, Ziv Y, Khoo C, Hill DE, Shiloh Y et al. (August 2001). "Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks". J. Biol. Chem. 276 (31): 29282–91. doi:10.1074/jbc.M011534200. PMID 11375976.
  4. ↑ Nakamura M, Zhou XZ, Kishi S, Lu KP (March 2002). "Involvement of the telomeric protein Pin2/TRF1 in the regulation of the mitotic spindle". FEBS Lett. 514 (2-3): 193–8. doi:10.1016/s0014-5793(02)02363-3. PMID 11943150.
  5. ↑ Nosaka K, Kawahara M, Masuda M, Satomi Y, Nishino H (February 1998). "Association of nucleoside diphosphate kinase nm23-H2 with human telomeres". Biochem. Biophys. Res. Commun. 243 (2): 342–8. doi:10.1006/bbrc.1997.8097. PMID 9480811.
  6. ↑ Zhou XZ, Lu KP (November 2001). "The Pin2/TRF1-interacting protein PinX1 is a potent telomerase inhibitor". Cell 107 (3): 347–59. doi:10.1016/s0092-8674(01)00538-4. PMID 11701125.
  7. ↑ Netzer C, Rieger L, Brero A, Zhang CD, Hinzke M, Kohlhase J et al. (Dec 2001). "SALL1, the gene mutated in Townes-Brocks syndrome, encodes a transcriptional repressor which interacts with TRF1/PIN2 and localizes to pericentromeric heterochromatin". Hum. Mol. Genet. 10 (26): 3017–24. doi:10.1093/hmg/10.26.3017. PMID 11751684.
  8. ↑ Liu D, Safari A, O'Connor MS, Chan DW, Laegeler A, Qin J et al. (July 2004). "PTOP interacts with POT1 and regulates its localization to telomeres". Nat. Cell Biol. 6 (7): 673–80. doi:10.1038/ncb1142. PMID 15181449.
  9. ↑ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H et al. (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
  10. ↑ Kim SH, Kaminker P, Campisi J (Dec 1999). "TIN2, a new regulator of telomere length in human cells". Nat. Genet. 23 (4): 405–12. doi:10.1038/70508. PMID 10581025.
  11. ↑ 11.0 11.1 Cook BD, Dynek JN, Chang W, Shostak G, Smith S (January 2002). "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres". Mol. Cell. Biol. 22 (1): 332–42. doi:10.1128/mcb.22.1.332-342.2002. PMC 134233. PMID 11739745.
  12. ↑ Chi NW, Lodish HF (Dec 2000). "Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles". J. Biol. Chem. 275 (49): 38437–44. doi:10.1074/jbc.M007635200. PMID 10988299.
  13. ↑ 13.0 13.1 Sbodio JI, Lodish HF, Chi NW (February 2002). "Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)". Biochem. J. 361 (Pt 3): 451–9. doi:10.1042/0264-6021:3610451. PMC 1222327. PMID 11802774.
  14. ↑ Seimiya H, Smith S (April 2002). "The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)". J. Biol. Chem. 277 (16): 14116–26. doi:10.1074/jbc.M112266200. PMID 11854288.
  15. ↑ Sbodio JI, Chi NW (August 2002). "Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner". J. Biol. Chem. 277 (35): 31887–92. doi:10.1074/jbc.M203916200. PMID 12080061.
  16. ↑ Smith S, Giriat I, Schmitt A, de Lange T (November 1998). "Tankyrase, a poly(ADP-ribose) polymerase at human telomeres". Science 282 (5393): 1484–7. doi:10.1126/science.282.5393.1484. PMID 9822378.

Further reading