TERF2

From Wikipedia, the free encyclopedia
Telomeric repeat binding factor 2

PDB rendering based on 1h6p.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsTERF2; TRBF2; TRF2
External IDsOMIM: 602027 MGI: 1195972 HomoloGene: 4133 GeneCards: TERF2 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez701421750
EnsemblENSG00000132604ENSMUSG00000031921
UniProtQ15554O35144
RefSeq (mRNA)NM_005652NM_001083118
RefSeq (protein)NP_005643NP_001076587
Location (UCSC)Chr 16:
69.39 – 69.44 Mb
Chr 8:
107.07 – 107.1 Mb
PubMed search

Telomeric repeat-binding factor 2 is a protein that is also known as TRF2 and TRBF2. It is in humans encoded by the TERF2 gene.[1][2]

This gene encodes a telomere specific protein, TERF2, which is a component of the telomere nucleoprotein complex. This protein is present at telomeres in metaphase of the cell cycle, is a second negative regulator of telomere length and plays a key role in the protective activity of telomeres. While having similar telomere binding activity and domain organization, TERF2 differs from TERF1 in that its N terminus is basic rather than acidic.[3]

Interactions

TERF2 has been shown to interact with Ku70,[4] TERF2IP,[5][6][7] Werner syndrome ATP-dependent helicase,[8] Rad50,[5][7] Nibrin[7] and MRE11A.[7]

References

  1. Broccoli D, Smogorzewska A, Chong L, de Lange T (November 1997). "Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2". Nat Genet 17 (2): 231–5. doi:10.1038/ng1097-231. PMID 9326950. 
  2. Sakaguchi AY, Padalecki SS, Mattern V, Rodriguez A, Leach RJ, McGill JR, Chavez M, Giambernardi TA (May 1999). "Chromosomal sublocalization of the transcribed human telomere repeat binding factor 2 gene and comparative mapping in the mouse". Somat Cell Mol Genet 24 (3): 157–63. doi:10.1023/B:SCAM.0000007118.47691.d7. PMID 10226653. 
  3. "Entrez Gene: TERF2 telomeric repeat binding factor 2". 
  4. Song, K; Jung D, Jung Y, Lee S G, Lee I (September 2000). "Interaction of human Ku70 with TRF2". FEBS Lett. (NETHERLANDS) 481 (1): 81–5. doi:10.1016/S0014-5793(00)01958-X. ISSN 0014-5793. PMID 10984620. 
  5. 5.0 5.1 O'Connor, Matthew S; Safari Amin, Liu Dan, Qin Jun, Songyang Zhou (July 2004). "The human Rap1 protein complex and modulation of telomere length". J. Biol. Chem. (United States) 279 (27): 28585–91. doi:10.1074/jbc.M312913200. ISSN 0021-9258. PMID 15100233. 
  6. Li, B; Oestreich S, de Lange T (May 2000). "Identification of human Rap1: implications for telomere evolution". Cell (UNITED STATES) 101 (5): 471–83. doi:10.1016/S0092-8674(00)80858-2. ISSN 0092-8674. PMID 10850490. 
  7. 7.0 7.1 7.2 7.3 Zhu, X D; Küster B, Mann M, Petrini J H, de Lange T (July 2000). "Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres". Nat. Genet. (UNITED STATES) 25 (3): 347–52. doi:10.1038/77139. ISSN 1061-4036. PMID 10888888. 
  8. Opresko, Patricia L; von Kobbe Cayetano, Laine Jean-Philippe, Harrigan Jeanine, Hickson Ian D, Bohr Vilhelm A (October 2002). "Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases". J. Biol. Chem. (United States) 277 (43): 41110–9. doi:10.1074/jbc.M205396200. ISSN 0021-9258. PMID 12181313. 


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