TERF1 interacting nuclear factor 2
Last updated 18 Aug 2020
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The TINF2 gene provides instructions for making part of the shelterin protein complex. This complex consists of a group of proteins that work together to help maintain structures known as telomeres, which are found at the ends of chromosomes. Telomeres help protect chromosomes from abnormally sticking together or breaking down (degrading).
Normal function
The TINF2 gene provides instructions for making part of the shelterin protein complex. This complex consists of a group of proteins that work together to help maintain structures known as telomeres, which are found at the ends of chromosomes. Telomeres help protect chromosomes from abnormally sticking together or breaking down (degrading).
The shelterin complex helps protect telomeres from the cell's DNA repair process. Without the protection of shelterin, the repair mechanism would sense the chromosome ends as abnormal breaks in the DNA sequence and either attempt to join the ends together or initiate cellular self-destruction (apoptosis).
Conditions referring to this gene or chromosome
Other names
(TRF1)-interacting nuclear factor 2 variant 1
TERF1 (TRF1)-interacting nuclear factor 2
TERF1-interacting nuclear factor 2
TERF1-interacting nuclear factor 2 isoform 1
TERF1-interacting nuclear factor 2 isoform 2
TIN2
TINF2_HUMAN
TRF1-interacting nuclear protein 2
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Further reading and references
- TERF1 interacting nuclear factor 2; MedlinePlus, National Library of Medicine.
- Ballew BJ, Savage SA. Updates on the biology and management of dyskeratosis congenita and related telomere biology disorders. Expert Rev Hematol. 2013 Jun;6(3):327-37. doi: 10.1586/ehm.13.23.
- Baran I, Nalcaci R, Kocak M. Dyskeratosis congenita: clinical report and review of the literature. Int J Dent Hyg. 2010 Feb;8(1):68-74. doi: 10.1111/j.1601-5037.2009.00364.x.
- Calado RT, Young NS. Telomere maintenance and human bone marrow failure. Blood. 2008 May 1;111(9):4446-55. doi: 10.1182/blood-2007-08-019729. Epub 2008 Jan 31.
- Calado RT. Telomeres and marrow failure. Hematology Am Soc Hematol Educ Program. 2009:338-43. doi: 10.1182/asheducation-2009.1.338.
- Chan SS, Chang S. Defending the end zone: studying the players involved in protecting chromosome ends. FEBS Lett. 2010 Sep 10;584(17):3773-8. doi: 10.1016/j.febslet.2010.06.016. Epub 2010 Jun 19.
- Kirwan M, Dokal I. Dyskeratosis congenita, stem cells and telomeres. Biochim Biophys Acta. 2009 Apr;1792(4):371-9. doi: 10.1016/j.bbadis.2009.01.010. Epub 2009 Feb 7.
- Nishio N, Kojima S. Recent progress in dyskeratosis congenita. Int J Hematol. 2010 Oct;92(3):419-24. doi: 10.1007/s12185-010-0695-5. Epub 2010 Oct 1.
- Sasa GS, Ribes-Zamora A, Nelson ND, Bertuch AA. Three novel truncating TINF2 mutations causing severe dyskeratosis congenita in early childhood. Clin Genet. 2012 May;81(5):470-8. doi: 10.1111/j.1399-0004.2011.01658.x. Epub 2011 Apr 7.
- Savage SA, Giri N, Baerlocher GM, Orr N, Lansdorp PM, Alter BP. TINF2, a component of the shelterin telomere protection complex, is mutated in dyskeratosis congenita. Am J Hum Genet. 2008 Feb;82(2):501-9. doi: 10.1016/j.ajhg.2007.10.004. Epub 2008 Jan 31.
- Walne AJ, Dokal I. Advances in the understanding of dyskeratosis congenita. Br J Haematol. 2009 Apr;145(2):164-72. doi: 10.1111/j.1365-2141.2009.07598.x. Epub 2009 Feb 4.
- Walne AJ, Vulliamy T, Beswick R, Kirwan M, Dokal I. TINF2 mutations result in very short telomeres: analysis of a large cohort of patients with dyskeratosis congenita and related bone marrow failure syndromes. Blood. 2008 Nov 1;112(9):3594-600. doi: 10.1182/blood-2008-05-153445. Epub 2008 Jul 30.
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