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TERF2 (telomeric repeat binding factor 2)

Written2013-02Molly L Bristol, Claire P Bailey, Lynne W Elmore
Department of Pathology, Virginia Commonwealth University, Richmond, Virginia, USA

(Note : for Links provided by Atlas : click)

Identity

Alias_namesTRBF2
Alias_symbol (synonym)TRF2
Other alias
HGNC (Hugo) TERF2
LocusID (NCBI) 7014
Atlas_Id 42522
Location 16q22.1  [Link to chromosome band 16q22]
Location_base_pair Starts at 69355561 and ends at 69385988 bp from pter ( according to hg19-Feb_2009)  [Mapping TERF2.png]
Fusion genes
(updated 2016)
COG8 (16q22.1) / TERF2 (16q22.1)CYTH1 (17q25.3) / TERF2 (16q22.1)TERF2 (16q22.1) / COG4 (16q22.1)
TERF2 (16q22.1) / NNMT (11q23.2)

DNA/RNA

 
  Human TERF2 is alternatively spliced, resulting in 8 protein encoding transcripts. Figure adapted from Flicek et al. 2012.
Description The human TERF2 gene spans a length of 53011 bp. The TERF2 structural gene is composed of 10 exons.
Transcription Human TERF2 is alternatively spliced, resulting in 12 transcripts, 8 of which are protein encoding.
TERF2-001: 2951 bp in length, with a translational length of 500 residues.
TERF2-002: 1112 bp in length, with a translational length of 251 residues.
TERF2-003: 554 bp in length, with no protein product.
TERF2-004: 556 bp in length, with no protein product.
TERF2-005: 513 bp in length, with a translational length of 60 residues; transcript undergoes nonsense-mediated decay.
TERF2-006: 917 bp in length, with a translational length of 283 residues.
TERF2-008: 791 bp in length, with a translational length of 49 residues.
TERF2-009: 573 bp in length, with a translational length of 99 residues; transcript undergoes nonsense mediated decay.
TERF2-010: 316 bp in length, with no protein product.
TERF2-011: 1107 bp in length, with no protein product.
TERF2-012: 431 bp in length, with a translational length of 144 residues.
TERF2-013: 669 bp in length, with a translational length of 206 residues.
(Flicek et al., 2012).
Pseudogene This gene has a pseudogene, TERF2IPP1, telomeric repeat binding factor 2 interacting protein pseudogene 1, located on chromosome 22q11.2 (Seal et al., 2011).

Protein

 
  Homodimer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TIN2, TPP1, RAP1 and POT1. Figure adapted from de Lange 2005, and Oeseburg et al. 2010.
Description Of the 12 TERF2 transcripts, 8 encode for proteins, and 2 of these are subject to nonsense-mediated decay. Among splice variants: isoform 1 is 500 aa in length, mass 55.6 kDa; isoform 2 is 251 aa in length, mass 28.3 kDa; isoform 6 is 283 aa in length, mass 31.5 kDa; and isoform 13 is 206 aa in length, mass 22.9 kDa (Uhlen et al., 2010).
Expression Ubiquitous. There are high levels of TERF2 expression in spleen, thymus, prostate, uterus, testes, brain, kidney, lung, liver, small intestine, colon, and peripheral blood leukocytes (Jung et al., 2004; Sugiura et al., 2003; UniProt, 2012).
Localisation TERF2 colocalizes with telomeric DNA in the nucleus of cells at interphase, and is located at telomeres on chromosome ends during metaphase (Ye et al., 2010). TERF2 has also been found in peripheral nerve axons (Jung et al., 2004).
Function TERF2 is a component of the telomere-specific protein complex called shelterin or telosome, which coats mammalian telomeric DNA (Kim et al., 2009). TERF2 is a homodimer, which binds to the double-stranded 5'-TTAGGG-3' repeat in telomeres (van Steensel et al., 1998). Its primary role is the maintenance of telomere length, structure, and protection against end-to-end fusion of chromosomes. TERF2 induces the formation of telomere-loops (t-loops); without its protection, telomeres are no longer hidden from DNA repair pathways and these ends could be subject to non-homologous end joining (NHEJ) of chromosomes during metaphase (Wang et al., 2004). TERF2 causes the 3' single-stranded overhang to tuck under the double stranded TTAGGG repeat, thus shielding chromosomes from incorrect processing. TERF2 also works together with the exonuclease Apollo as a negative regulator of telomere length (Ye et al., 2010). TERF2 differs from TERF1 in that its N terminus is basic rather than acidic (provided by RefSeq, Jul 2008).
Homology Significant TERF2 sequence homology is shared among human (H.sapiens), chimpanzee (P.troglodytes), Rhesus monkey (M.mulatta), dog (C.lupus), cow (B.taurus), mouse (M.musculus), and rat (R.norvegicus). Conserved domains in protein sequences include: the Telomeric Repeat binding Factor domain, the RAP1 binding motif of telomere repeat binding factor, and the 'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains, which consist of repeats containing the G/C rich motif (Geer et al., 2010).

Mutations

Note According to the January 2013, NCBI dbSNP database, there are 488 known SNPs in the human TERF2 gene. SNPs associated with TERF2 affect telomere length and chromosomal stability by influencing gene expression or protein configuration at telomeres.

Implicated in

Note
  
Entity Various pathological conditions
Note The dysregulation of TERF2 has been implicated in the susceptibility of a number of human diseases and pathological disorders. Such implications include age- and cancer-related conditions.
  
  
Entity Adult T-cell leukemia
Note TERF2 was found to be overexpressed in T-cell leukemia cell lines. TERF2 expression levels were found to be highest in primary leukemia cells from patients with M0 and M1 subtypes of acute myelogenous leukemia (AML) compared with normal controls and other subtypes of AML (Chen et al., 2008; Jiao et al., 2007).
Prognosis Increased TERF2 expression levels were found in T-cell leukemia cell lines and AML patients with poor prognosis, suggesting that TRF2 expression might be related to the prognosis of leukemia (Chen et al., 2008; Jiao et al., 2007).
  
  
Entity Breast cancer
Note In vitro models suggest that expression of TERF2 protein increases during mammary cancer progression. However, some data indicate that elevated expression of TERF2 is not a frequent occurrence during the transformation of breast cancer cells in vivo. Conversely, higher levels of TERF2 protein may protect advanced cancer cells with critically short telomeres, and shorter telomeres in breast cancer cells correlate with a higher TNM stage (Diehl et al., 2011).
Prognosis Shorter telomeres correlate with advanced stages in breast cancer. Furthermore, elevated TERF2 levels are found in advanced breast cancer with short telomeres, suggesting TERF2 levels may correlate with breast cancer progression and prognosis (Diehl et al., 2011).
  
  
Entity Werner syndrome
Note Telomere dysfunction has been proposed to contribute to the pathogenesis of Werner syndrome. The Werner syndrome protein (WRN) is a nuclear protein with helicase and exonuclease activities, whose loss-of-function mutations are associated with the premature aging and the cancer-prone disease, Werner syndrome. WRN functions at telomeres and interacts with TERF2. TERF2 has an N-terminal domain which plays a key role in the prevention of telomere shortening. Expression of TRF2(DeltaB), lacks this key domain, and leads to the formation of telomeric circles, telomere shortening, and cell senescence. The TRF2(DeltaB) pathway requires WRN helicase (Jog et al., 2011; Li et al., 2008).
Prognosis Expression of TRF2(DeltaB) leads to excessive telomere shortening and cellular senescence, thus contributing to the pathogenesis of Werner syndrome (Jog et al., 2011; Li et al., 2008).
  
  
Entity Lung and bronchial cancer
Note Telomere shortening is an early event in lung and bronchial carcinogenesis, leading to DNA damage responses (DDR). As telomere attrition occurs, genetic instability increases, thus facilitating malignant progression. When telomeres reach a critical length, expression of TERF2 increases progressively and correlates with progression from dysplasia to squamous invasive carcinoma and from atypical alveolar hyperplasia to invasive adenocarcinoma (Frias et al., 2008; Hosgood et al., 2009; Lantuejoul et al., 2010).
Prognosis Telomere attrition occurs at an early stage of lung carcinogenesis as an initiating event and is preceded by TERF2 overexpression for telomere stabilization. Evidence suggests that telomere length and genetic variance of TERF2 and other telomere maintenance genes may be associated with an increased risk of developing lung cancer and a poorer prognosis (Frias et al., 2008; Hosgood et al., 2009; Lantuejoul et al., 2010).
  
  
Entity Colorectal cancer
Note Overexpression of TERF2 protein has been observed in colorectal carcinoma tissue. Experimental data suggests that siRNA silencing of TERF2 expression significantly inhibited SW480 cell proliferation and colony formation; moreover, defective TERF2 induced apoptosis and increased chromosomal instability in SW480 cells (Dong et al., 2009).
Prognosis TERF2 is overexpressed in colorectal carcinoma and siRNA TERF2 inhibition reduced tumorigenesis of colorectal cancer, suggesting a new target for the development of anti-cancer therapy for colorectal carcinoma (Dong et al., 2009).
  
  
Entity Age-dependent telomere shortening
Note TERF2 alterations permit the progressive reduction in the length of telomeres at the termini of eukaryotic chromosomes, which occur as part of cellular aging.
Prognosis Shortening of telomeres can initiate DNA damage response mechanisms, leading to cell cycle arrest, cell death, or cellular senescence whereby normal cells irreversibly lose their ability to divide (De Boeck et al., 2009; Mikhelson and Gamaley, 2012).
  
  
Entity Type 2 - Diabetes mellitus
Note Leukocyte telomere length shortening has recently been associated with type 2 diabetes mellitus (T2D). tSNPs within TERF2 were associated with T2D risk (Zee et al., 2011).
  

Bibliography

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J Pathol. 2009 Feb;217(3):327-44. doi: 10.1002/path.2500. (REVIEW)
PMID 19142887
 
Elevated TRF2 in advanced breast cancers with short telomeres.
Diehl MC, Idowu MO, Kimmelshue KN, York TP, Jackson-Cook CK, Turner KC, Holt SE, Elmore LW.
Breast Cancer Res Treat. 2011 Jun;127(3):623-30. doi: 10.1007/s10549-010-0988-7. Epub 2010 Jul 13.
PMID 20625812
 
Sp1 upregulates expression of TRF2 and TRF2 inhibition reduces tumorigenesis in human colorectal carcinoma cells.
Dong W, Shen R, Wang Q, Gao Y, Qi X, Jiang H, Yao J, Lin X, Wu Y, Wang L.
Cancer Biol Ther. 2009 Nov;8(22):2166-74. Epub 2009 Nov 21.
PMID 19783902
 
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Telomere shortening is associated with poor prognosis and telomerase activity correlates with DNA repair impairment in non-small cell lung cancer.
Frias C, Garcia-Aranda C, De Juan C, Moran A, Ortega P, Gomez A, Hernando F, Lopez-Asenjo JA, Torres AJ, Benito M, Iniesta P.
Lung Cancer. 2008 Jun;60(3):416-25. Epub 2008 Feb 20.
PMID 18077053
 
TRF2 controls telomeric nucleosome organization in a cell cycle phase-dependent manner.
Galati A, Magdinier F, Colasanti V, Bauwens S, Pinte S, Ricordy R, Giraud-Panis MJ, Pusch MC, Savino M, Cacchione S, Gilson E.
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The NCBI BioSystems database.
Geer LY, Marchler-Bauer A, Geer RC, Han L, He J, He S, Liu C, Shi W, Bryant SH.
Nucleic Acids Res. 2010 Jan;38(Database issue):D492-6. doi: 10.1093/nar/gkp858. Epub 2009 Oct 23.
PMID 19854944
 
Genetic variation in telomere maintenance genes, telomere length, and lung cancer susceptibility.
Hosgood HD 3rd, Cawthon R, He X, Chanock S, Lan Q.
Lung Cancer. 2009 Nov;66(2):157-61. doi: 10.1016/j.lungcan.2009.02.005. Epub 2009 Mar 13.
PMID 19285750
 
Telomere attrition and chromosome instability via downregulation of TRF2 contributes to arsenic trioxide-induced apoptosis of human T-Cell leukemia cell line molt-4 cells.
Jiao Y, Zhang W, Liu J, Ni W, Xu W, Jin J, Qian W.
Cancer Biol Ther. 2007 Aug;6(8):1186-92. Epub 2007 May 4.
PMID 17643074
 
Cell cycle-regulated association between the Werner syndrome protein and its molecular partners.
Jog SP, Reddy S, Comai L.
Cell Cycle. 2011 Jun 15;10(12):2038-40. Epub 2011 Jun 15.
PMID 21558813
 
TRF2 is in neuroglial cytoplasm and induces neurite-like processes.
Jung Y, Lee S, Bang S, Kim S, Choi K, Lee C, Lee SG, Kim CJ, Song K, Lee I.
FEBS Lett. 2004 Jan 16;557(1-3):129-32.
PMID 14741354
 
TRF2 functions as a protein hub and regulates telomere maintenance by recognizing specific peptide motifs.
Kim H, Lee OH, Xin H, Chen LY, Qin J, Chae HK, Lin SY, Safari A, Liu D, Songyang Z.
Nat Struct Mol Biol. 2009 Apr;16(4):372-9. doi: 10.1038/nsmb.1575. Epub 2009 Mar 15.
PMID 19287395
 
Telomere maintenance and DNA damage responses during lung carcinogenesis.
Lantuejoul S, Raynaud C, Salameire D, Gazzeri S, Moro-Sibilot D, Soria JC, Brambilla C, Brambilla E.
Clin Cancer Res. 2010 Jun 1;16(11):2979-88. doi: 10.1158/1078-0432.CCR-10-0142. Epub 2010 Apr 19.
PMID 20404006
 
WRN controls formation of extrachromosomal telomeric circles and is required for TRF2DeltaB-mediated telomere shortening.
Li B, Jog SP, Reddy S, Comai L.
Mol Cell Biol. 2008 Mar;28(6):1892-904. doi: 10.1128/MCB.01364-07. Epub 2008 Jan 22.
PMID 18212065
 
Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins.
Liu D, O'Connor MS, Qin J, Songyang Z.
J Biol Chem. 2004 Dec 3;279(49):51338-42. Epub 2004 Sep 20.
PMID 15383534
 
Telomere shortening is a sole mechanism of aging in mammals.
Mikhelson VM, Gamaley IA.
Curr Aging Sci. 2012 Dec;5(3):203-8.
PMID 23387887
 
Telomere biology in healthy aging and disease.
Oeseburg H, de Boer RA, van Gilst WH, van der Harst P.
Pflugers Arch. 2010 Jan;459(2):259-68. doi: 10.1007/s00424-009-0728-1. Epub 2009 Sep 10. (REVIEW)
PMID 19756717
 
genenames.org: the HGNC resources in 2011.
Seal RL, Gordon SM, Lush MJ, Wright MW, Bruford EA.
Nucleic Acids Res. 2011 Jan;39(Database issue):D514-9. doi: 10.1093/nar/gkq892. Epub 2010 Oct 6.
PMID 20929869
 
Expression of a testis-specific form of TBP-related factor 2 (TRF2) mRNA during mouse spermatogenesis.
Sugiura S, Kashiwabara S, Iwase S, Baba T.
J Reprod Dev. 2003 Feb;49(1):107-11.
PMID 14967955
 
Towards a knowledge-based Human Protein Atlas.
Uhlen M, Oksvold P, Fagerberg L, Lundberg E, Jonasson K, Forsberg M, Zwahlen M, Kampf C, Wester K, Hober S, Wernerus H, Bjorling L, Ponten F.
Nat Biotechnol. 2010 Dec;28(12):1248-50. doi: 10.1038/nbt1210-1248.
PMID 21139605
 
Homologous recombination generates T-loop-sized deletions at human telomeres.
Wang RC, Smogorzewska A, de Lange T.
Cell. 2004 Oct 29;119(3):355-68.
PMID 15507207
 
TRF2 and apollo cooperate with topoisomerase 2alpha to protect human telomeres from replicative damage.
Ye J, Lenain C, Bauwens S, Rizzo A, Saint-Leger A, Poulet A, Benarroch D, Magdinier F, Morere J, Amiard S, Verhoeyen E, Britton S, Calsou P, Salles B, Bizard A, Nadal M, Salvati E, Sabatier L, Wu Y, Biroccio A, Londono-Vallejo A, Giraud-Panis MJ, Gilson E.
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PMID 20655466
 
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PMID 21665207
 
Shelterin: the protein complex that shapes and safeguards human telomeres.
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PMID 16166375
 
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Citation

This paper should be referenced as such :
Bristol, ML ; Bailey, CP ; Elmore, LW
TERF2 (telomeric repeat binding factor 2)
Atlas Genet Cytogenet Oncol Haematol. 2013;17(8):539-542.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/TERF2ID42522ch16q22.html


External links

Nomenclature
HGNC (Hugo)TERF2   11729
Cards
AtlasTERF2ID42522ch16q22
Entrez_Gene (NCBI)TERF2  7014  telomeric repeat binding factor 2
AliasesTRBF2; TRF2
GeneCards (Weizmann)TERF2
Ensembl hg19 (Hinxton)ENSG00000132604 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000132604 [Gene_View]  chr16:69355561-69385988 [Contig_View]  TERF2 [Vega]
ICGC DataPortalENSG00000132604
TCGA cBioPortalTERF2
AceView (NCBI)TERF2
Genatlas (Paris)TERF2
WikiGenes7014
SOURCE (Princeton)TERF2
Genetics Home Reference (NIH)TERF2
Genomic and cartography
GoldenPath hg38 (UCSC)TERF2  -     chr16:69355561-69385988 -  16q22.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)TERF2  -     16q22.1   [Description]    (hg19-Feb_2009)
EnsemblTERF2 - 16q22.1 [CytoView hg19]  TERF2 - 16q22.1 [CytoView hg38]
Mapping of homologs : NCBITERF2 [Mapview hg19]  TERF2 [Mapview hg38]
OMIM602027   
Gene and transcription
Genbank (Entrez)AF002999 BC024890 BX090758 CB216181 HY046320
RefSeq transcript (Entrez)NM_005652
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)TERF2
Cluster EST : UnigeneHs.63335 [ NCBI ]
CGAP (NCI)Hs.63335
Alternative Splicing GalleryENSG00000132604
Gene ExpressionTERF2 [ NCBI-GEO ]   TERF2 [ EBI - ARRAY_EXPRESS ]   TERF2 [ SEEK ]   TERF2 [ MEM ]
Gene Expression Viewer (FireBrowse)TERF2 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)7014
GTEX Portal (Tissue expression)TERF2
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ15554   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ15554  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ15554
Splice isoforms : SwissVarQ15554
PhosPhoSitePlusQ15554
Domaine pattern : Prosite (Expaxy)HTH_MYB (PS51294)   
Domains : Interpro (EBI)Homeobox-like    Myb_dom    SANT/Myb    Telomere_rpt-bd_fac_dimer_dom    TERF2    TERF2_RBM   
Domain families : Pfam (Sanger)Myb_DNA-binding (PF00249)    TERF2_RBM (PF16772)    TRF (PF08558)   
Domain families : Pfam (NCBI)pfam00249    pfam16772    pfam08558   
Domain families : Smart (EMBL)SANT (SM00717)  
Domain structure : Prodom (Prabi Lyon)Telomere_repeat-bd_fac_dimer (PD014243)   
Conserved Domain (NCBI)TERF2
DMDM Disease mutations7014
Blocks (Seattle)TERF2
PDB (SRS)1H6P    1VF9    1VFC    1W0U    1XG1    3BU8    3BUA    3K6G    3SJM    4M7C    4RQI   
PDB (PDBSum)1H6P    1VF9    1VFC    1W0U    1XG1    3BU8    3BUA    3K6G    3SJM    4M7C    4RQI   
PDB (IMB)1H6P    1VF9    1VFC    1W0U    1XG1    3BU8    3BUA    3K6G    3SJM    4M7C    4RQI   
PDB (RSDB)1H6P    1VF9    1VFC    1W0U    1XG1    3BU8    3BUA    3K6G    3SJM    4M7C    4RQI   
Structural Biology KnowledgeBase1H6P    1VF9    1VFC    1W0U    1XG1    3BU8    3BUA    3K6G    3SJM    4M7C    4RQI   
SCOP (Structural Classification of Proteins)1H6P    1VF9    1VFC    1W0U    1XG1    3BU8    3BUA    3K6G    3SJM    4M7C    4RQI   
CATH (Classification of proteins structures)1H6P    1VF9    1VFC    1W0U    1XG1    3BU8    3BUA    3K6G    3SJM    4M7C    4RQI   
SuperfamilyQ15554
Human Protein AtlasENSG00000132604
Peptide AtlasQ15554
HPRD03610
IPIIPI00024214   IPI00216552   
Protein Interaction databases
DIP (DOE-UCLA)Q15554
IntAct (EBI)Q15554
FunCoupENSG00000132604
BioGRIDTERF2
STRING (EMBL)TERF2
ZODIACTERF2
Ontologies - Pathways
QuickGOQ15554
Ontology : AmiGOtelomere maintenance  chromosome, telomeric region  nuclear telomere cap complex  nuclear chromosome, telomeric region  double-stranded telomeric DNA binding  double-stranded telomeric DNA binding  telomerase activity  protein binding  nucleus  nucleoplasm  RNA-dependent DNA biosynthetic process  cell cycle  protein C-terminus binding  positive regulation of gene expression  negative regulation of gene expression  telomere capping  telomere capping  telomere capping  nuclear body  enzyme binding  Mre11 complex  telomeric loop formation  protection from non-homologous end joining at telomere  protection from non-homologous end joining at telomere  regulation of telomere maintenance  negative regulation of telomere maintenance  negative regulation of telomere maintenance via recombination  negative regulation of telomere maintenance via recombination  regulation of telomere maintenance via telomerase  regulation of telomere maintenance via telomerase  negative regulation of telomere maintenance via telomerase  negative regulation of telomere maintenance via telomerase  negative regulation of telomere maintenance via telomerase  negative regulation of telomere maintenance via semi-conservative replication  telomeric DNA binding  protein homodimerization activity  macromolecular complex binding  positive regulation of nitric-oxide synthase activity  telomeric D-loop disassembly  shelterin complex  shelterin complex  shelterin complex  protein localization to chromosome, telomeric region  cellular senescence  G-rich strand telomeric DNA binding  negative regulation of beta-galactosidase activity  negative regulation of telomere single strand break repair  negative regulation of telomere capping  negative regulation of telomere maintenance via telomere lengthening  negative regulation of t-circle formation  negative regulation of t-circle formation  negative regulation of exonuclease activity  negative regulation of telomeric D-loop disassembly  negative regulation of cellular senescence  
Ontology : EGO-EBItelomere maintenance  chromosome, telomeric region  nuclear telomere cap complex  nuclear chromosome, telomeric region  double-stranded telomeric DNA binding  double-stranded telomeric DNA binding  telomerase activity  protein binding  nucleus  nucleoplasm  RNA-dependent DNA biosynthetic process  cell cycle  protein C-terminus binding  positive regulation of gene expression  negative regulation of gene expression  telomere capping  telomere capping  telomere capping  nuclear body  enzyme binding  Mre11 complex  telomeric loop formation  protection from non-homologous end joining at telomere  protection from non-homologous end joining at telomere  regulation of telomere maintenance  negative regulation of telomere maintenance  negative regulation of telomere maintenance via recombination  negative regulation of telomere maintenance via recombination  regulation of telomere maintenance via telomerase  regulation of telomere maintenance via telomerase  negative regulation of telomere maintenance via telomerase  negative regulation of telomere maintenance via telomerase  negative regulation of telomere maintenance via telomerase  negative regulation of telomere maintenance via semi-conservative replication  telomeric DNA binding  protein homodimerization activity  macromolecular complex binding  positive regulation of nitric-oxide synthase activity  telomeric D-loop disassembly  shelterin complex  shelterin complex  shelterin complex  protein localization to chromosome, telomeric region  cellular senescence  G-rich strand telomeric DNA binding  negative regulation of beta-galactosidase activity  negative regulation of telomere single strand break repair  negative regulation of telomere capping  negative regulation of telomere maintenance via telomere lengthening  negative regulation of t-circle formation  negative regulation of t-circle formation  negative regulation of exonuclease activity  negative regulation of telomeric D-loop disassembly  negative regulation of cellular senescence  
REACTOMEQ15554 [protein]
REACTOME PathwaysR-HSA-2559586 [pathway]   
NDEx NetworkTERF2
Atlas of Cancer Signalling NetworkTERF2
Wikipedia pathwaysTERF2
Orthology - Evolution
OrthoDB7014
GeneTree (enSembl)ENSG00000132604
Phylogenetic Trees/Animal Genes : TreeFamTERF2
HOVERGENQ15554
HOGENOMQ15554
Homologs : HomoloGeneTERF2
Homology/Alignments : Family Browser (UCSC)TERF2
Gene fusions - Rearrangements
Fusion : MitelmanCOG8/TERF2 [16q22.1/16q22.1]  [t(16;16)(q22;q22)]  
Fusion : MitelmanTERF2/COG4 [16q22.1/16q22.1]  [t(16;16)(q22;q22)]  
Fusion: TCGATERF2 16q22.1 COG4 16q22.1 BRCA
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerTERF2 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TERF2
dbVarTERF2
ClinVarTERF2
1000_GenomesTERF2 
Exome Variant ServerTERF2
ExAC (Exome Aggregation Consortium)TERF2 (select the gene name)
Genetic variants : HAPMAP7014
Genomic Variants (DGV)TERF2 [DGVbeta]
DECIPHERTERF2 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisTERF2 
Mutations
ICGC Data PortalTERF2 
TCGA Data PortalTERF2 
Broad Tumor PortalTERF2
OASIS PortalTERF2 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICTERF2  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDTERF2
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch TERF2
DgiDB (Drug Gene Interaction Database)TERF2
DoCM (Curated mutations)TERF2 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)TERF2 (select a term)
intoGenTERF2
NCG5 (London)TERF2
Cancer3DTERF2(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM602027   
Orphanet
MedgenTERF2
Genetic Testing Registry TERF2
NextProtQ15554 [Medical]
TSGene7014
GENETestsTERF2
Target ValidationTERF2
Huge Navigator TERF2 [HugePedia]
snp3D : Map Gene to Disease7014
BioCentury BCIQTERF2
ClinGenTERF2
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD7014
Chemical/Pharm GKB GenePA36446
Clinical trialTERF2
Miscellaneous
canSAR (ICR)TERF2 (select the gene name)
Probes
Litterature
PubMed198 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineTERF2
EVEXTERF2
GoPubMedTERF2
iHOPTERF2
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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