TERF2

Telomeric repeat binding factor 2

PDB rendering based on 1h6p.

Available structures
PDB	1H6P, 1VF9, 1VFC, 1W0U, 1XG1, 3BU8, 3BUA, 3K6G

Identifiers

Symbols

TERF2; TRBF2; TRF2

External IDs

OMIM: 602027 MGI: 1195972 HomoloGene: 4133 GeneCards: TERF2 Gene

Gene Ontology
Molecular function	• DNA binding • double-stranded telomeric DNA binding • protein binding • protein C-terminus binding • telomeric DNA binding • protein homodimerization activity
Cellular component	• chromosome, telomeric region • nuclear telomere cap complex • male germ cell nucleus • nucleus • nucleoplasm • nucleoplasm • chromosome • nucleolus • cytoplasm • Golgi apparatus • Mre11 complex
Biological process	• telomere maintenance • telomere maintenance • age-dependent telomere shortening • in utero embryonic development • regulation of transcription, DNA-dependent • telomere maintenance via telomerase • cell cycle • telomere maintenance via telomere shortening • telomere capping • telomeric loop formation • protection from non-homologous end joining at telomere • negative regulation of telomere maintenance • positive regulation of telomere maintenance • negative regulation of telomere maintenance via semi-conservative replication • protein localization to chromosome, telomeric region • cellular senescence
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 16:
69.39 – 69.42 Mb

Chr 8:
109.59 – 109.62 Mb

PubMed search

[1]

[2]

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

^ Broccoli D, Smogorzewska A, Chong L, de Lange T (Nov 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.
^ 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.
^ "Entrez Gene: TERF2 telomeric repeat binding factor 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7014.
^ Song, K; Jung D, Jung Y, Lee S G, Lee I (Sep. 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.
^ ^a ^b O'Connor, Matthew S; Safari Amin, Liu Dan, Qin Jun, Songyang Zhou (Jul. 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.
^ 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.
^ ^a ^b ^c ^d Zhu, X D; Küster B, Mann M, Petrini J H, de Lange T (Jul. 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.
^ Opresko, Patricia L; von Kobbe Cayetano, Laine Jean-Philippe, Harrigan Jeanine, Hickson Ian D, Bohr Vilhelm A (Oct. 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.

Bilaud T, Koering CE, Binet-Brasselet E, et al. (1996). "The telobox, a Myb-related telomeric DNA binding motif found in proteins from yeast, plants and human.". Nucleic Acids Res. 24 (7): 1294–303. doi:10.1093/nar/24.7.1294. PMC 145771. PMID 8614633. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=145771.
Bilaud T, Brun C, Ancelin K, et al. (1997). "Telomeric localization of TRF2, a novel human telobox protein.". Nat. Genet. 17 (2): 236–9. doi:10.1038/ng1097-236. PMID 9326951.
van Steensel B, Smogorzewska A, de Lange T (1998). "TRF2 protects human telomeres from end-to-end fusions.". Cell 92 (3): 401–13. doi:10.1016/S0092-8674(00)80932-0. PMID 9476899.
Griffith JD, Comeau L, Rosenfield S, et al. (1999). "Mammalian telomeres end in a large duplex loop.". Cell 97 (4): 503–14. doi:10.1016/S0092-8674(00)80760-6. PMID 10338214.
Teichmann M, Wang Z, Martinez E, et al. (2000). "Human TATA-binding protein-related factor-2 (hTRF2) stably associates with hTFIIA in HeLa cells.". Proc. Natl. Acad. Sci. U.S.A. 96 (24): 13720–5. doi:10.1073/pnas.96.24.13720. PMC 24131. PMID 10570139. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=24131.
Smogorzewska A, van Steensel B, Bianchi A, et al. (2000). "Control of human telomere length by TRF1 and TRF2.". Mol. Cell. Biol. 20 (5): 1659–68. doi:10.1128/MCB.20.5.1659-1668.2000. PMC 85349. PMID 10669743. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85349.
Li B, Oestreich S, de Lange T (2000). "Identification of human Rap1: implications for telomere evolution.". Cell 101 (5): 471–83. doi:10.1016/S0092-8674(00)80858-2. PMID 10850490.
Zhu XD, Küster B, Mann M, et al. (2000). "Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres.". Nat. Genet. 25 (3): 347–52. doi:10.1038/77139. PMID 10888888.
Song K, Jung D, Jung Y, et al. (2000). "Interaction of human Ku70 with TRF2.". FEBS Lett. 481 (1): 81–5. doi:10.1016/S0014-5793(00)01958-X. PMID 10984620.
Song K, Jung Y, Jung D, Lee I (2001). "Human Ku70 interacts with heterochromatin protein 1alpha.". J. Biol. Chem. 276 (11): 8321–7. doi:10.1074/jbc.M008779200. PMID 11112778.
Fairall L, Chapman L, Moss H, et al. (2001). "Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2.". Mol. Cell 8 (2): 351–61. doi:10.1016/S1097-2765(01)00321-5. PMID 11545737.
Bailey SM, Cornforth MN, Kurimasa A, et al. (2001). "Strand-specific postreplicative processing of mammalian telomeres.". Science 293 (5539): 2462–5. doi:10.1126/science.1062560. PMID 11577237.
Karlseder J, Smogorzewska A, de Lange T (2002). "Senescence induced by altered telomere state, not telomere loss.". Science 295 (5564): 2446–9. doi:10.1126/science.1069523. PMID 11923537.
Mignon-Ravix C, Depetris D, Delobel B, et al. (2002). "A human interstitial telomere associates in vivo with specific TRF2 and TIN2 proteins.". Eur. J. Hum. Genet. 10 (2): 107–12. doi:10.1038/sj.ejhg.5200775. PMID 11938440.
Ancelin K, Brunori M, Bauwens S, et al. (2002). "Targeting assay to study the cis functions of human telomeric proteins: evidence for inhibition of telomerase by TRF1 and for activation of telomere degradation by TRF2.". Mol. Cell. Biol. 22 (10): 3474–87. doi:10.1128/MCB.22.10.3474-3487.2002. PMC 133804. PMID 11971978. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=133804.
Opresko PL, von Kobbe C, Laine JP, et al. (2002). "Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases.". J. Biol. Chem. 277 (43): 41110–9. doi:10.1074/jbc.M205396200. PMID 12181313.
Chagnon P, Michaud J, Mitchell G, et al. (2003). "A missense mutation (R565W) in cirhin (FLJ14728) in North American Indian childhood cirrhosis.". Am. J. Hum. Genet. 71 (6): 1443–9. doi:10.1086/344580. PMC 378590. PMID 12417987. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=378590.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.

PDB gallery

1h6p: DIMERISTION DOMAIN FROM HUMAN TRF2

1vf9: Solution Structure Of Human Trf2

1vfc: Solution Structure Of The DNA Complex Of Human Trf2

1w0u: HTRF2 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.

1xg1: Solution structure of Myb-domain of human TRF2