Q15554 (TERF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Telomeric repeat-binding factor 2

Alternative name(s):
TTAGGG repeat-binding factor 2
Telomeric DNA-binding protein

Gene names

Name:	TERF2
Synonyms:	TRBF2, TRF2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length. Ref.5 Ref.10 Ref.26
Subunit structure	Homodimer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP/RAP1, ACD and POT1. Interacts with TERF2IP. Interacts with NBN. Interacts with SLX4/BTBD12. Interacts with DCLRE1B/Apollo and TERF2IP/RAP1; the interaction is direct. Ref.6 Ref.12 Ref.13 Ref.14 Ref.18 Ref.19 Ref.23 Ref.26 Ref.29
Subcellular location	Nucleus. Chromosome › telomere. Note: Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase. Ref.26
Tissue specificity	Ubiquitous. Highly expressed in spleen, thymus, prostate, uterus, testis, small intestine, colon and peripheral blood leukocytes.
Domain	The TRFH dimerization region mediates the interaction with DCLRE1B/Apollo but not TINF2. Ref.29
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.11 Ref.15 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.24
Sequence similarities	Contains 1 HTH myb-type DNA-binding domain.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Chromosome Nucleus Telomere
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	age-dependent telomere shortening Non-traceable author statement. Source: BHF-UCL cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cellular senescence Non-traceable author statement. Source: BHF-UCL negative regulation of telomere maintenance via semi-conservative replication Non-traceable author statement. Source: BHF-UCL protection from non-homologous end joining at telomere Inferred from mutant phenotype. Source: BHF-UCL protein localization to chromosome, telomeric region Inferred from mutant phenotype. Source: BHF-UCL regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro telomere maintenance via telomerase Inferred by curator. Source: BHF-UCL telomeric loop formation Inferred from direct assay. Source: BHF-UCL
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA nuclear telomere cap complex Inferred from direct assay. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome
Molecular function	double-stranded telomeric DNA binding Inferred from sequence or structural similarity Ref.1. Source: BHF-UCL protein C-terminus binding Inferred from physical interaction. Source: UniProtKB protein homodimerization activity Inferred from physical interaction Ref.1. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BLM	P54132	8	EBI-706637,EBI-621372
DCLRE1B	Q9H816	6	EBI-706637,EBI-3508943
POT1	Q9NUX5	3	EBI-706637,EBI-752420
SLX4	Q8IY92	5	EBI-706637,EBI-2370740
TERF2IP	Q9NYB0	5	EBI-706637,EBI-750109
TINF2	Q9BSI4-3	4	EBI-706637,EBI-717418
WRN	Q14191	8	EBI-706637,EBI-368417

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15554-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q15554-2)

The sequence of this isoform differs from the canonical sequence as follows:
     239-251: MAKKALKSESAAS → VRLGPSPITMVCP
     252-500: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 500

500

Telomeric repeat-binding factor 2

PRO_0000197131

Regions

Domain

442 – 499

58

HTH myb-type

DNA binding

470 – 495

26

H-T-H motif Ref.26

Region

42 – 245

204

TRFH dimerization

Motif

329 – 333

5

Nuclear localization signal Potential

Compositional bias

13 – 30

18

Arg-rich (basic)

Amino acid modifications

Modified residue

169

1

N6-acetyllysine Ref.25

Modified residue

323

1

Phosphoserine Ref.9 Ref.11 Ref.15 Ref.17 Ref.20 Ref.21 Ref.22 Ref.24

Modified residue

368

1

Phosphoserine Ref.16

Modified residue

380

1

Phosphoserine Ref.16

Natural variations

Alternative sequence

239 – 251

13

MAKKA…ESAAS → VRLGPSPITMVCP in isoform 2.

VSP_003304

Alternative sequence

252 – 500

249

Missing in isoform 2.

VSP_003305

Natural variant

413

1

S → G.
Corresponds to variant rs35874485 [ dbSNP | Ensembl ].

VAR_050196

Secondary structure

1

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500

Helix Strand Turn

Details...

Helix

44 – 69

26

Helix

73 – 86

14

Helix

98 – 111

14

Turn

112 – 114

3

Helix

128 – 142

15

Helix

147 – 167

21

Helix

171 – 181

11

Helix

193 – 201

9

Turn

202 – 204

3

Helix

214 – 227

14

Helix

235 – 244

10

Turn

440 – 443

4

Helix

452 – 465

14

Helix

470 – 476

7

Helix

484 – 496

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 2. Checksum: 733DCA413BCFBFEE	FASTA	500	55,551
	10 20 30 40 50 60 MAGGGGSSDG SGRAAGRRAS RSSGRARRGR HEPGLGGPAE RGAGEARLEE AVNRWVLKFY 70 80 90 100 110 120 FHEALRAFRG SRYGDFRQIR DIMQALLVRP LGKEHTVSRL LRVMQCLSRI EEGENLDCSF 130 140 150 160 170 180 DMEAELTPLE SAINVLEMIK TEFTLTEAVV ESSRKLVKEA AVIICIKNKE FEKASKILKK 190 200 210 220 230 240 HMSKDPTTQK LRNDLLNIIR EKNLAHPVIQ NFSYETFQQK MLRFLESHLD DAEPYLLTMA 250 260 270 280 290 300 KKALKSESAA SSTGKEDKQP APGPVEKPPR EPARQLRNPP TTIGMMTLKA AFKTLSGAQD 310 320 330 340 350 360 SEAAFAKLDQ KDLVLPTQAL PASPALKNKR PRKDENESSA PADGEGGSEL QPKNKRMTIS 370 380 390 400 410 420 RLVLEEDSQS TEPSAGLNSS QEAASAPPSK PTVLNQPLPG EKNPKVPKGK WNSSNGVEEK 430 440 450 460 470 480 ETWVEEDELF QVQAAPDEDS TTNITKKQKW TVEESEWVKA GVQKYGEGNW AAISKNYPFV 490 500 NRTAVMIKDR WRTMKRLGMN
	Isoform 2 [UniParc]. Checksum: 13EBD6CF07690DA5	FASTA	251	28,256
	10 20 30 40 50 60 MAGGGGSSDG SGRAAGRRAS RSSGRARRGR HEPGLGGPAE RGAGEARLEE AVNRWVLKFY 70 80 90 100 110 120 FHEALRAFRG SRYGDFRQIR DIMQALLVRP LGKEHTVSRL LRVMQCLSRI EEGENLDCSF 130 140 150 160 170 180 DMEAELTPLE SAINVLEMIK TEFTLTEAVV ESSRKLVKEA AVIICIKNKE FEKASKILKK 190 200 210 220 230 240 HMSKDPTTQK LRNDLLNIIR EKNLAHPVIQ NFSYETFQQK MLRFLESHLD DAEPYLLTVR 250 LGPSPITMVC P

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2." Broccoli D., Smogorzewska A., Chong L., de Lange T. Nat. Genet. 17:231-235(1997) [PubMed: 9326950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Mammary carcinoma.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Adrenal cortex.
[3]	"Telomeric localization of TRF2, a novel human telobox protein." Bilaud T., Brun C., Ancelin K., Koering C.E., Larouche T., Gilson E. Nat. Genet. 17:236-239(1997) [PubMed: 9326951] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-500 (ISOFORM 1). Tissue: Cervix carcinoma.
[4]	"The telobox, a Myb-related telomeric DNA binding motif found in proteins from yeast, plants and human." Bilaud T., Koering C.E., Binet-Brasselet E., Ancelin K., Pollice A., Gasser S.M., Gilson E. Nucleic Acids Res. 24:1294-1303(1996) [PubMed: 8614633] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 438-500 (ISOFORM 1). Tissue: Cervix carcinoma.
[5]	"TRF2 protects human telomeres from end-to-end fusions." van Steensel B., Smogorzewska A., de Lange T. Cell 92:401-413(1998) [PubMed: 9476899] [Abstract] Cited for: FUNCTION.
[6]	"Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres." Zhu X.-D., Kuester B., Mann M., Petrini J.H.J., de Lange T. Nat. Genet. 25:347-352(2000) [PubMed: 10888888] [Abstract] Cited for: INTERACTION WITH NBN.
[7]	"TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on telomeres." Ye J.Z.-S., Donigian J.R., van Overbeek M., Loayza D., Luo Y., Krutchinsky A.N., Chait B.T., de Lange T. J. Biol. Chem. 279:47264-47271(2004) [PubMed: 15316005] [Abstract] Cited for: IDENTIFICATION IN THE SHELTERIN COMPLEX.
[8]	"Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins." Liu D., O'Connor M.S., Qin J., Songyang Z. J. Biol. Chem. 279:51338-51342(2004) [PubMed: 15383534] [Abstract] Cited for: IDENTIFICATION IN THE SHELTERIN COMPLEX.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Shelterin: the protein complex that shapes and safeguards human telomeres." de Lange T. Genes Dev. 19:2100-2110(2005) [PubMed: 16166375] [Abstract] Cited for: FUNCTION OF THE SHELTERIN COMPLEX.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Apollo, an Artemis-related nuclease, interacts with TRF2 and protects human telomeres in S phase." van Overbeek M., de Lange T. Curr. Biol. 16:1295-1302(2006) [PubMed: 16730176] [Abstract] Cited for: INTERACTION WITH DCLRE1B.
[13]	"The Apollo 5' exonuclease functions together with TRF2 to protect telomeres from DNA repair." Lenain C., Bauwens S., Amiard S., Brunori M., Giraud-Panis M.J., Gilson E. Curr. Biol. 16:1303-1310(2006) [PubMed: 16730175] [Abstract] Cited for: INTERACTION WITH DCLRE1B.
[14]	"hSnm1B is a novel telomere-associated protein." Freibaum B.D., Counter C.M. J. Biol. Chem. 281:15033-15036(2006) [PubMed: 16606622] [Abstract] Cited for: INTERACTION WITH DCLRE1B.
[15]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368 AND SER-380, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Endogenous hSNM1B/Apollo interacts with TRF2 and stimulates ATM in response to ionizing radiation." Demuth I., Bradshaw P.S., Lindner A., Anders M., Heinrich S., Kallenbach J., Schmelz K., Digweed M., Meyn M.S., Concannon P. DNA Repair 7:1192-1201(2008) [PubMed: 18468965] [Abstract] Cited for: INTERACTION WITH DCLRE1B.
[19]	"The protein hSnm1B is stabilized when bound to the telomere-binding protein TRF2." Freibaum B.D., Counter C.M. J. Biol. Chem. 283:23671-23676(2008) [PubMed: 18593705] [Abstract] Cited for: INTERACTION WITH DCLRE1B.
[20]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[23]	"Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair." Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., Elledge S.J., Harper J.W. Cell 138:63-77(2009) [PubMed: 19596235] [Abstract] Cited for: INTERACTION WITH SLX4.
[24]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169, MASS SPECTROMETRY.
[26]	"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 M.J., Gilson E. Cell 142:230-242(2010) [PubMed: 20655466] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DCLRE1B, DNA-BINDING.
[27]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2." Fairall L., Chapman L., Moss H., de Lange T., Rhodes D. Mol. Cell 8:351-361(2001) [PubMed: 11545737] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[29]	"A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins." Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P., de Lange T., Lei M. Science 319:1092-1096(2008) [PubMed: 18202258] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 42-276 IN COMPLEX WITH TINF2 AND DCLRE1B, DOMAIN TRFH DIMERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF002999 mRNA. Translation: AAB81135.1.
BC024890 mRNA. Translation: AAH24890.1.
U95970 mRNA. Translation: AAD00821.1.
X93512 mRNA. Translation: CAA63769.1.

IPI

IPI00024214.
IPI00216552.

PIR

S67923.

RefSeq

NP_005643.1. NM_005652.3.

UniGene

Hs.63335.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H6P	X-ray	2.20	A/B	43-245	[»]
1VF9	NMR	-	A	438-500	[»]
1VFC	NMR	-	A	438-500	[»]
1W0U	X-ray	1.80	A/B	446-500	[»]
1XG1	NMR	-	A	438-500	[»]
3BU8	X-ray	2.15	A/B	42-276	[»]
3BUA	X-ray	2.50	A/B/C/D	42-245	[»]
3K6G	X-ray	1.95	D/E/F	275-316	[»]

ProteinModelPortal

Q15554.

SMR

Q15554. Positions 43-249, 281-316, 438-500.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34052N.

IntAct

Q15554. 11 interactions.

MINT

MINT-2831307.

STRING

Q15554.

PTM databases

PhosphoSite

Q15554.

Polymorphism databases

DMDM

21542277.

Proteomic databases

PRIDE

Q15554.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000254942; ENSP00000254942; ENSG00000132604.

GeneID

7014.

KEGG

hsa:7014.

UCSC

uc002exd.1. human.
uc002exe.2. human.

Organism-specific databases

CTD

7014.

GeneCards

GC16M069389.

H-InvDB

HIX0013184.

HGNC

HGNC:11729. TERF2.

HPA

CAB010451.
HPA001907.
HPA002735.

MIM

602027. gene.

neXtProt

NX_Q15554.

PharmGKB

PA36446.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16406.

GeneTree

ENSGT00530000063796.

HOGENOM

HBG283423.

HOVERGEN

HBG108560.

InParanoid

Q15554.

OMA

PARQLRN.

OrthoDB

EOG4TB4CV.

PhylomeDB

Q15554.

Enzyme and pathway databases

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Reactome

REACT_111183. Meiosis.
REACT_22172. Chromosome Maintenance.

Gene expression databases

ArrayExpress

Q15554.

Bgee

Q15554.

CleanEx

HS_TERF2.

Genevestigator

Q15554.

GermOnline

ENSG00000132604. Homo sapiens.

Family and domain databases

InterPro

IPR009057. Homeodomain-like.
IPR012287. Homeodomain-rel.
IPR014778. Myb_DNA-bd.
IPR001005. SANT_DNA-bd.
IPR017357. Telomere_repeat-bd-1/2.
IPR013867. Telomere_rpt-bd_fac_dimer_dom.
IPR017930. Tscrpt_reg_HTH_Myb-type.
[Graphical view]

Gene3D

G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.
G3DSA:1.25.40.210. Telomere_repeat-bd_fac_dimer. 1 hit.

KO

K11111.

Pfam

PF00249. Myb_DNA-binding. 1 hit.
PF08558. TRF. 1 hit.
[Graphical view]

PIRSF

PIRSF038016. Telomere_bd-1_Pin2. 1 hit.

ProDom

PD014243. Telomere_repeat-bd_fac_dimer. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00717. SANT. 1 hit.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 1 hit.
SSF63600. Telo_rept_bnd_D. 1 hit.

PROSITE

PS51294. HTH_MYB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

27401.

SOURCE

Search...

Entry information

Entry name

TERF2_HUMAN

Accession

Primary (citable) accession number: Q15554

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.