HUMAN:TERF2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	TERF2 (synonyms: TRBF2, TRF2)
Protein Name(s)	Telomeric repeat-binding factor 2 TTAGGG repeat-binding factor 2 Telomeric DNA-binding protein
External Links
UniProt	Q15554
EMBL	AC026464 BC024890 AF002999 U95970 X93512
CCDS	CCDS10879.2
PIR	S67923
RefSeq	NP_005643.2
UniGene	Hs.63335
PDB	1H6P 1VF9 1VFC 1W0U 1XG1 3BU8 3BUA 3K6G 3SJM 4M7C
PDBsum	1H6P 1VF9 1VFC 1W0U 1XG1 3BU8 3BUA 3K6G 3SJM 4M7C
ProteinModelPortal	Q15554
SMR	Q15554
BioGrid	112873
DIP	DIP-34052N
IntAct	Q15554
MINT	MINT-2831307
STRING	9606.ENSP00000254942
PhosphoSite	Q15554
DMDM	21542277
MaxQB	Q15554
PaxDb	Q15554
PRIDE	Q15554
Ensembl	ENST00000254942 ENST00000567296
GeneID	7014
KEGG	hsa:7014
UCSC	uc002exd.4
CTD	7014
GeneCards	GC16M069389
HGNC	HGNC:11729
HPA	CAB010451 HPA001907 HPA002735
MIM	602027
neXtProt	NX_Q15554
PharmGKB	PA36446
eggNOG	NOG44337
GeneTree	ENSGT00530000063796
HOGENOM	HOG000154547
HOVERGEN	HBG108560
InParanoid	Q15554
KO	K11111
OMA	ITKKQKW
OrthoDB	EOG7DFXCF
TreeFam	TF333209
Reactome	REACT_169185 REACT_75792 REACT_7963
ChiTaRS	TERF2
EvolutionaryTrace	Q15554
GeneWiki	TERF2
GenomeRNAi	7014
NextBio	27401
PRO	PR:Q15554
Proteomes	UP000005640
Bgee	Q15554
CleanEx	HS_TERF2
ExpressionAtlas	Q15554
Genevestigator	Q15554
GO	GO:0000781 GO:0005737 GO:0005794 GO:0001673 GO:0000783 GO:0005654 GO:0005634 GO:0003682 GO:0003691 GO:0008022 GO:0042803 GO:0042162 GO:0001309 GO:0007049 GO:0090398 GO:0001701 GO:0032205 GO:0032214 GO:0032206 GO:0031848 GO:0070198 GO:0016233 GO:0000723 GO:0007004 GO:0031627
Gene3D	1.10.10.60 1.25.40.210
InterPro	IPR009057 IPR017930 IPR001005 IPR017357 IPR013867
Pfam	PF00249 PF08558
PIRSF	PIRSF038016
ProDom	PD014243
SMART	SM00717
SUPFAM	SSF46689 SSF63600
PROSITE	PS51294

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0032204	regulation of telomere maintenance	PMID:22536324^[1]	ECO:0000315			P		Fig. 1	complete CACAO 9092
	0003677		PMID:26856421^[2]	ECO:0000314					Fg. 4d 4e: shows DNA binding	complete CACAO 11750
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:19274049^[3]	ECO:0000255	match to sequence model evidence used in manual assertion	InterPro:IPR001005 InterPro:IPR009057	F		Seeded From UniProt	complete
part_of	GO:0000781	chromosome, telomeric region	PMID:24012755^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003691	double-stranded telomeric DNA binding	PMID:18812185^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1905778	negative regulation of exonuclease activity	PMID:15200954^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	regulates_activity_of:(UniProtKB:Q14191)	Seeded From UniProt	complete
involved_in	GO:1905839	negative regulation of telomeric D-loop disassembly	PMID:15200954^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1904357	negative regulation of telomere maintenance via telomere lengthening	PMID:24012755^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000781	chromosome, telomeric region	PMID:20479256^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:20479256^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9H816	F		Seeded From UniProt	complete
involved_in	GO:0032208	negative regulation of telomere maintenance via recombination	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O35144	P		Seeded From UniProt	complete
enables	GO:0042162	telomeric DNA binding	PMID:19854130^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0032210	regulation of telomere maintenance via telomerase	PMID:19864690^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0098505	G-rich strand telomeric DNA binding	PMID:17694070^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0032208	negative regulation of telomere maintenance via recombination	PMID:15507207^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1904430	negative regulation of t-circle formation	PMID:15507207^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0032208)	Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:15109494^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070187	shelterin complex	PMID:21852327^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070187	shelterin complex	PMID:15383534^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:19135898^[15]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0032211	negative regulation of telomere maintenance via telomerase	PMID:17055345^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061820	telomeric D-loop disassembly	PMID:22039056^[17]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:O94761	P	occurs_at:(GO:0000781)	Seeded From UniProt	complete
involved_in	GO:0032210	regulation of telomere maintenance via telomerase	PMID:23685356^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
contributes_to	GO:0003720	telomerase activity	PMID:23685356^[18]	ECO:0000314	direct assay evidence used in manual assertion		F	part_of:(GO:0007004)	Seeded From UniProt	complete
part_of	GO:0070187	shelterin complex	PMID:23685356^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:23685356^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042162	telomeric DNA binding	PMID:23685356^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	PMID:24270157^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031848	protection from non-homologous end joining at telomere	PMID:24095731^[20]	ECO:0000353	physical interaction evidence used in manual assertion	ComplexPortal:CPX-1993	P		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:24095731^[20]	ECO:0000353	physical interaction evidence used in manual assertion	ComplexPortal:CPX-1993	F	occurs_at:(GO:0000781)	Seeded From UniProt	complete
enables	GO:0003691	double-stranded telomeric DNA binding	PMID:21852327^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1904354	negative regulation of telomere capping	PMID:24270157^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	PMID:11927518^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0002544) has_regulation_target:(UniProtKB:P05362)	Seeded From UniProt	complete
involved_in	GO:2000773	negative regulation of cellular senescence	PMID:11927518^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0002544)	Seeded From UniProt	complete
involved_in	GO:1903770	negative regulation of beta-galactosidase activity	PMID:11927518^[21]	ECO:0000314	direct assay evidence used in manual assertion		P	occurs_in:(CL:0002544) happens_during:(GO:0090398) occurs_in:(GO:0005737)	Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:11927518^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0002544) has_regulation_target:(UniProtKB:P29474)	Seeded From UniProt	complete
involved_in	GO:0051000	positive regulation of nitric-oxide synthase activity	PMID:11927518^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0002544)	Seeded From UniProt	complete
involved_in	GO:0032204	regulation of telomere maintenance	PMID:22536324^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016233	telomere capping	PMID:17395247^[22]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016233	telomere capping	PMID:14690602^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:14690602^[23]	ECO:0000353	physical interaction evidence used in manual assertion	ComplexPortal:CPX-478	F		Seeded From UniProt	complete
involved_in	GO:0031848	protection from non-homologous end joining at telomere	PMID:14690602^[23]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090398	cellular senescence	PMID:17395247^[22]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070198	protein localization to chromosome, telomeric region	PMID:17499040^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:9326950^[25]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q15554	F		Seeded From UniProt	complete
involved_in	GO:0032214	negative regulation of telomere maintenance via semi-conservative replication	PMID:15007108^[26]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031848	protection from non-homologous end joining at telomere	PMID:17499040^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031627	telomeric loop formation	PMID:10338214^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0030870	Mre11 complex	PMID:10888888^[28]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016233	telomere capping	PMID:12768206^[29]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016233	telomere capping	PMID:15657433^[30]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032211	negative regulation of telomere maintenance via telomerase	PMID:11971978^[31]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032211	negative regulation of telomere maintenance via telomerase	PMID:15657433^[30]	ECO:0000305	curator inference used in manual assertion	GO:0016233	P		Seeded From UniProt	complete
enables	GO:0003691	double-stranded telomeric DNA binding	PMID:9326950^[25]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O35144	F		Seeded From UniProt	complete
involved_in	GO:1903824	negative regulation of telomere single strand break repair	PMID:17395247^[22]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000783	nuclear telomere cap complex	PMID:15181449^[32]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000783	nuclear telomere cap complex	PMID:16880378^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000781	chromosome, telomeric region	PMID:12768206^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042162	telomeric DNA binding	PMID:20655466^[34]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0032205	negative regulation of telomere maintenance	PMID:17055345^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:12181313^[35]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q14191	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17055345^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000781	chromosome, telomeric region	PMID:20655466^[34]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	PMID:20655466^[34]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1905839	negative regulation of telomeric D-loop disassembly	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002929876 UniProtKB:Q15554	P		Seeded From UniProt	complete
enables	GO:0098505	G-rich strand telomeric DNA binding	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002929876 UniProtKB:Q15554	F		Seeded From UniProt	complete
involved_in	GO:0070198	protein localization to chromosome, telomeric region	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002929876 UniProtKB:Q15554	P		Seeded From UniProt	complete
part_of	GO:0070187	shelterin complex	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002929876 UniProtKB:Q15554	C		Seeded From UniProt	complete
involved_in	GO:0032210	regulation of telomere maintenance via telomerase	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002929876 UniProtKB:Q15554	P		Seeded From UniProt	complete
involved_in	GO:0032204	regulation of telomere maintenance	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1195972 PANTHER:PTN002929876 UniProtKB:Q15554	P		Seeded From UniProt	complete
involved_in	GO:0031848	protection from non-homologous end joining at telomere	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1195972 PANTHER:PTN002929876 UniProtKB:Q15554	P		Seeded From UniProt	complete
involved_in	GO:0031627	telomeric loop formation	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1195972 PANTHER:PTN002929876 UniProtKB:Q15554	P		Seeded From UniProt	complete
contributes_to	GO:0003720	telomerase activity	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002929876 UniProtKB:Q15554	F		Seeded From UniProt	complete
enables	GO:0003691	double-stranded telomeric DNA binding	PMID:21873635^[36]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1195972 PANTHER:PTN002929876 UniProtKB:Q15554	F		Seeded From UniProt	complete
part_of	GO:0016604	nuclear body	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006278	RNA-dependent DNA biosynthetic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003720	P		Seeded From UniProt	complete
involved_in	GO:0006278	RNA-dependent DNA biosynthetic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003720	P		Seeded From UniProt	complete
involved_in	GO:0006357	regulation of transcription by RNA polymerase II	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0000981	P		Seeded From UniProt	complete
part_of	GO:1904115	axon cytoplasm	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0099087	C		Seeded From UniProt	complete
involved_in	GO:0099087	anterograde axonal transport of messenger ribonucleoprotein complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:D3ZJF7 ensembl:ENSRNOP00000027695	P		Seeded From UniProt	complete
involved_in	GO:0000723	telomere maintenance	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017357 InterPro:IPR030657	P		Seeded From UniProt	complete
part_of	GO:0000784	nuclear chromosome, telomeric region	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017357 InterPro:IPR030657	C		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR009057	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR017357 InterPro:IPR030657	C		Seeded From UniProt	complete
involved_in	GO:0031848	protection from non-homologous end joining at telomere	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR030657	P		Seeded From UniProt	complete
enables	GO:0042162	telomeric DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013867 InterPro:IPR017357 InterPro:IPR030657	F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013867	F		Seeded From UniProt	complete
part_of	GO:0070187	shelterin complex	PMID:18202258^[37]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016233	telomere capping	PMID:24095731^[20] Reactome:R-HSA-181450 Reactome:R-HSA-176700	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1904430	negative regulation of t-circle formation	PMID:19581589^[38]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042162	telomeric DNA binding	PMID:9476899^[39]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-3785711 Reactome:R-HSA-181450 Reactome:R-HSA-176700	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F		Seeded From UniProt	complete
part_of	GO:0005694	chromosome	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0158	C		Seeded From UniProt	complete
part_of	GO:0000781	chromosome, telomeric region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0779 UniProtKB-SubCell:SL-0276	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Galati, A et al. (2012) TRF2 controls telomeric nucleosome organization in a cell cycle phase-dependent manner. PLoS ONE 7 e34386 PubMed GONUTS page
↑ Kaur, P et al. (2016) Enhanced electrostatic force microscopy reveals higher-order DNA looping mediated by the telomeric protein TRF2. Sci Rep 6 20513 PubMed GONUTS page
↑ Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page
↑ ^4.0 ^4.1 Wan, B et al. (2013) SLX4 assembles a telomere maintenance toolkit by bridging multiple endonucleases with telomeres. Cell Rep 4 861-9 PubMed GONUTS page
↑ Wu, Y et al. (2008) Human XPF controls TRF2 and telomere length maintenance through distinctive mechanisms. Mech. Ageing Dev. 129 602-10 PubMed GONUTS page
↑ ^6.0 ^6.1 Opresko, PL et al. (2004) The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2. Mol. Cell 14 763-74 PubMed GONUTS page
↑ ^7.0 ^7.1 Touzot, F et al. (2010) Function of Apollo (SNM1B) at telomere highlighted by a splice variant identified in a patient with Hoyeraal-Hreidarsson syndrome. Proc. Natl. Acad. Sci. U.S.A. 107 10097-102 PubMed GONUTS page
↑ Miyake, Y et al. (2009) RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of the Pot1 pathway. Mol. Cell 36 193-206 PubMed GONUTS page
↑ Takai, KK et al. (2010) In vivo stoichiometry of shelterin components. J. Biol. Chem. 285 1457-67 PubMed GONUTS page
↑ Wu, Y et al. (2007) MRE11-RAD50-NBS1 and ATM function as co-mediators of TRF1 in telomere length control. Nat. Struct. Mol. Biol. 14 832-40 PubMed GONUTS page
↑ ^11.0 ^11.1 Wang, RC et al. (2004) Homologous recombination generates T-loop-sized deletions at human telomeres. Cell 119 355-68 PubMed GONUTS page
↑ Tarsounas, M et al. (2004) Telomere maintenance requires the RAD51D recombination/repair protein. Cell 117 337-47 PubMed GONUTS page
↑ ^13.0 ^13.1 Choi, KH et al. (2011) Characterization of the DNA binding specificity of Shelterin complexes. Nucleic Acids Res. 39 9206-23 PubMed GONUTS page
↑ Liu, D et al. (2004) Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins. J. Biol. Chem. 279 51338-42 PubMed GONUTS page
↑ Déjardin, J & Kingston, RE (2009) Purification of proteins associated with specific genomic Loci. Cell 136 175-86 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Wu, Y et al. (2007) XPF with mutations in its conserved nuclease domain is defective in DNA repair but functions in TRF2-mediated telomere shortening. DNA Repair (Amst.) 6 157-66 PubMed GONUTS page
↑ Ghosh, AK et al. (2012) RECQL4, the protein mutated in Rothmund-Thomson syndrome, functions in telomere maintenance. J. Biol. Chem. 287 196-209 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 ^18.4 Kappei, D et al. (2013) HOT1 is a mammalian direct telomere repeat-binding protein contributing to telomerase recruitment. EMBO J. 32 1681-701 PubMed GONUTS page
↑ ^19.0 ^19.1 Grolimund, L et al. (2013) A quantitative telomeric chromatin isolation protocol identifies different telomeric states. Nat Commun 4 2848 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 Ribes-Zamora, A et al. (2013) TRF2 interaction with Ku heterotetramerization interface gives insight into c-NHEJ prevention at human telomeres. Cell Rep 5 194-206 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 ^21.3 ^21.4 Minamino, T et al. (2002) Endothelial cell senescence in human atherosclerosis: role of telomere in endothelial dysfunction. Circulation 105 1541-4 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 Richter, T et al. (2007) TRF2 overexpression diminishes repair of telomeric single-strand breaks and accelerates telomere shortening in human fibroblasts. Mech. Ageing Dev. 128 340-5 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 Zhu, XD et al. (2003) ERCC1/XPF removes the 3' overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes. Mol. Cell 12 1489-98 PubMed GONUTS page
↑ ^24.0 ^24.1 Bae, NS & Baumann, P (2007) A RAP1/TRF2 complex inhibits nonhomologous end-joining at human telomeric DNA ends. Mol. Cell 26 323-34 PubMed GONUTS page
↑ ^25.0 ^25.1 Broccoli, D et al. (1997) Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2. Nat. Genet. 17 231-5 PubMed GONUTS page
↑ Ohki, R & Ishikawa, F (2004) Telomere-bound TRF1 and TRF2 stall the replication fork at telomeric repeats. Nucleic Acids Res. 32 1627-37 PubMed GONUTS page
↑ Griffith, JD et al. (1999) Mammalian telomeres end in a large duplex loop. Cell 97 503-14 PubMed GONUTS page
↑ Zhu, XD et al. (2000) Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres. Nat. Genet. 25 347-52 PubMed GONUTS page
↑ ^29.0 ^29.1 Loayza, D & De Lange, T (2003) POT1 as a terminal transducer of TRF1 telomere length control. Nature 423 1013-8 PubMed GONUTS page
↑ ^30.0 ^30.1 Yang, Q et al. (2005) POT1 and TRF2 cooperate to maintain telomeric integrity. Mol. Cell. Biol. 25 1070-80 PubMed GONUTS page
↑ Ancelin, K 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 3474-87 PubMed GONUTS page
↑ Liu, D et al. (2004) PTOP interacts with POT1 and regulates its localization to telomeres. Nat. Cell Biol. 6 673-80 PubMed GONUTS page
↑ O'Connor, MS et al. (2006) A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly. Proc. Natl. Acad. Sci. U.S.A. 103 11874-9 PubMed GONUTS page
↑ ^34.0 ^34.1 ^34.2 Ye, J et al. (2010) TRF2 and apollo cooperate with topoisomerase 2alpha to protect human telomeres from replicative damage. Cell 142 230-42 PubMed GONUTS page
↑ Opresko, PL et al. (2002) Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases. J. Biol. Chem. 277 41110-9 PubMed GONUTS page
↑ ^36.0 ^36.1 ^36.2 ^36.3 ^36.4 ^36.5 ^36.6 ^36.7 ^36.8 ^36.9 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Chen, Y et al. (2008) A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins. Science 319 1092-6 PubMed GONUTS page
↑ Wang, Y et al. (2009) Ku86 represses lethal telomere deletion events in human somatic cells. Proc. Natl. Acad. Sci. U.S.A. 106 12430-5 PubMed GONUTS page
↑ van Steensel, B et al. (1998) TRF2 protects human telomeres from end-to-end fusions. Cell 92 401-13 PubMed GONUTS page

[PMID:22536324-1] 1.0 ^1.1 Galati, A et al. (2012) TRF2 controls telomeric nucleosome organization in a cell cycle phase-dependent manner. PLoS ONE 7 e34386 PubMed GONUTS page

[PMID:26856421-2] Kaur, P et al. (2016) Enhanced electrostatic force microscopy reveals higher-order DNA looping mediated by the telomeric protein TRF2. Sci Rep 6 20513 PubMed GONUTS page

[PMID:19274049-3] Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page

[PMID:24012755-4] 4.0 ^4.1 Wan, B et al. (2013) SLX4 assembles a telomere maintenance toolkit by bridging multiple endonucleases with telomeres. Cell Rep 4 861-9 PubMed GONUTS page

[PMID:18812185-5] Wu, Y et al. (2008) Human XPF controls TRF2 and telomere length maintenance through distinctive mechanisms. Mech. Ageing Dev. 129 602-10 PubMed GONUTS page

[PMID:15200954-6] 6.0 ^6.1 Opresko, PL et al. (2004) The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D loops in a manner regulated by TRF1 and TRF2. Mol. Cell 14 763-74 PubMed GONUTS page

[PMID:20479256-7] 7.0 ^7.1 Touzot, F et al. (2010) Function of Apollo (SNM1B) at telomere highlighted by a splice variant identified in a patient with Hoyeraal-Hreidarsson syndrome. Proc. Natl. Acad. Sci. U.S.A. 107 10097-102 PubMed GONUTS page

[PMID:19854130-8] Miyake, Y et al. (2009) RPA-like mammalian Ctc1-Stn1-Ten1 complex binds to single-stranded DNA and protects telomeres independently of the Pot1 pathway. Mol. Cell 36 193-206 PubMed GONUTS page

[PMID:19864690-9] Takai, KK et al. (2010) In vivo stoichiometry of shelterin components. J. Biol. Chem. 285 1457-67 PubMed GONUTS page

[PMID:17694070-10] Wu, Y et al. (2007) MRE11-RAD50-NBS1 and ATM function as co-mediators of TRF1 in telomere length control. Nat. Struct. Mol. Biol. 14 832-40 PubMed GONUTS page

[PMID:15507207-11] 11.0 ^11.1 Wang, RC et al. (2004) Homologous recombination generates T-loop-sized deletions at human telomeres. Cell 119 355-68 PubMed GONUTS page

[PMID:15109494-12] Tarsounas, M et al. (2004) Telomere maintenance requires the RAD51D recombination/repair protein. Cell 117 337-47 PubMed GONUTS page

[PMID:21852327-13] 13.0 ^13.1 Choi, KH et al. (2011) Characterization of the DNA binding specificity of Shelterin complexes. Nucleic Acids Res. 39 9206-23 PubMed GONUTS page

[PMID:15383534-14] Liu, D et al. (2004) Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins. J. Biol. Chem. 279 51338-42 PubMed GONUTS page

[PMID:19135898-15] Déjardin, J & Kingston, RE (2009) Purification of proteins associated with specific genomic Loci. Cell 136 175-86 PubMed GONUTS page

[PMID:17055345-16] 16.0 ^16.1 ^16.2 Wu, Y et al. (2007) XPF with mutations in its conserved nuclease domain is defective in DNA repair but functions in TRF2-mediated telomere shortening. DNA Repair (Amst.) 6 157-66 PubMed GONUTS page

[PMID:22039056-17] Ghosh, AK et al. (2012) RECQL4, the protein mutated in Rothmund-Thomson syndrome, functions in telomere maintenance. J. Biol. Chem. 287 196-209 PubMed GONUTS page

[PMID:23685356-18] 18.0 ^18.1 ^18.2 ^18.3 ^18.4 Kappei, D et al. (2013) HOT1 is a mammalian direct telomere repeat-binding protein contributing to telomerase recruitment. EMBO J. 32 1681-701 PubMed GONUTS page

[PMID:24270157-19] 19.0 ^19.1 Grolimund, L et al. (2013) A quantitative telomeric chromatin isolation protocol identifies different telomeric states. Nat Commun 4 2848 PubMed GONUTS page

[PMID:24095731-20] 20.0 ^20.1 ^20.2 Ribes-Zamora, A et al. (2013) TRF2 interaction with Ku heterotetramerization interface gives insight into c-NHEJ prevention at human telomeres. Cell Rep 5 194-206 PubMed GONUTS page

[PMID:11927518-21] 21.0 ^21.1 ^21.2 ^21.3 ^21.4 Minamino, T et al. (2002) Endothelial cell senescence in human atherosclerosis: role of telomere in endothelial dysfunction. Circulation 105 1541-4 PubMed GONUTS page

[PMID:17395247-22] 22.0 ^22.1 ^22.2 Richter, T et al. (2007) TRF2 overexpression diminishes repair of telomeric single-strand breaks and accelerates telomere shortening in human fibroblasts. Mech. Ageing Dev. 128 340-5 PubMed GONUTS page

[PMID:14690602-23] 23.0 ^23.1 ^23.2 Zhu, XD et al. (2003) ERCC1/XPF removes the 3' overhang from uncapped telomeres and represses formation of telomeric DNA-containing double minute chromosomes. Mol. Cell 12 1489-98 PubMed GONUTS page

[PMID:17499040-24] 24.0 ^24.1 Bae, NS & Baumann, P (2007) A RAP1/TRF2 complex inhibits nonhomologous end-joining at human telomeric DNA ends. Mol. Cell 26 323-34 PubMed GONUTS page

[PMID:9326950-25] 25.0 ^25.1 Broccoli, D et al. (1997) Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2. Nat. Genet. 17 231-5 PubMed GONUTS page

[PMID:15007108-26] Ohki, R & Ishikawa, F (2004) Telomere-bound TRF1 and TRF2 stall the replication fork at telomeric repeats. Nucleic Acids Res. 32 1627-37 PubMed GONUTS page

[PMID:10338214-27] Griffith, JD et al. (1999) Mammalian telomeres end in a large duplex loop. Cell 97 503-14 PubMed GONUTS page

[PMID:10888888-28] Zhu, XD et al. (2000) Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres. Nat. Genet. 25 347-52 PubMed GONUTS page

[PMID:12768206-29] 29.0 ^29.1 Loayza, D & De Lange, T (2003) POT1 as a terminal transducer of TRF1 telomere length control. Nature 423 1013-8 PubMed GONUTS page

[PMID:15657433-30] 30.0 ^30.1 Yang, Q et al. (2005) POT1 and TRF2 cooperate to maintain telomeric integrity. Mol. Cell. Biol. 25 1070-80 PubMed GONUTS page

[PMID:11971978-31] Ancelin, K 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 3474-87 PubMed GONUTS page

[PMID:15181449-32] Liu, D et al. (2004) PTOP interacts with POT1 and regulates its localization to telomeres. Nat. Cell Biol. 6 673-80 PubMed GONUTS page

[PMID:16880378-33] O'Connor, MS et al. (2006) A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly. Proc. Natl. Acad. Sci. U.S.A. 103 11874-9 PubMed GONUTS page

[PMID:20655466-34] 34.0 ^34.1 ^34.2 Ye, J et al. (2010) TRF2 and apollo cooperate with topoisomerase 2alpha to protect human telomeres from replicative damage. Cell 142 230-42 PubMed GONUTS page

[PMID:12181313-35] Opresko, PL et al. (2002) Telomere-binding protein TRF2 binds to and stimulates the Werner and Bloom syndrome helicases. J. Biol. Chem. 277 41110-9 PubMed GONUTS page

[PMID:21873635-36] 36.0 ^36.1 ^36.2 ^36.3 ^36.4 ^36.5 ^36.6 ^36.7 ^36.8 ^36.9 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:18202258-37] Chen, Y et al. (2008) A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins. Science 319 1092-6 PubMed GONUTS page

[PMID:19581589-38] Wang, Y et al. (2009) Ku86 represses lethal telomere deletion events in human somatic cells. Proc. Natl. Acad. Sci. U.S.A. 106 12430-5 PubMed GONUTS page

[PMID:9476899-39] van Steensel, B et al. (1998) TRF2 protects human telomeres from end-to-end fusions. Cell 92 401-13 PubMed GONUTS page

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