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Q15554 (TERF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceEvidence 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.6 Ref.10 Ref.24

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.7 Ref.8 Ref.9 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.21 Ref.24 Ref.29 Ref.30

Subcellular location

Nucleus. Chromosometelomere. Note: Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase. Ref.24

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.30

The HTH domain is an independent structural unit and mediates binding to telomeric DNA. Ref.30

Post-translational modification

Phosphorylated upon DNA damage, most probably by ATM. Phosphorylated TERF2 is not bound to telomeric DNA, and rapidly localizes to damage sites. Ref.11

Methylated by PRMT1 at multiple arginines within the N-terminal Arg-rich region. Methylation may control association with telomeres. Ref.22

Sequence similarities

Contains 1 HTH myb-type DNA-binding domain.

Sequence caution

The sequence AAB81135.1 differs from that shown. Reason: Frameshift at position 36.

The sequence AAB81135.1 differs from that shown. Reason: Contaminating sequence. The N-terminus may be contaminated with vector sequence.

The sequence AAH24890.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentChromosome
Nucleus
Telomere
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   PTMMethylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processage-dependent telomere shortening

Non-traceable author statement PubMed 17395247. Source: BHF-UCL

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular senescence

Non-traceable author statement PubMed 17395247. Source: BHF-UCL

negative regulation of telomere maintenance

Inferred from direct assay PubMed 17055345. Source: UniProtKB

negative regulation of telomere maintenance via semi-conservative replication

Non-traceable author statement PubMed 15007108. Source: BHF-UCL

protection from non-homologous end joining at telomere

Inferred from mutant phenotype PubMed 17499040. Source: BHF-UCL

protein localization to chromosome, telomeric region

Inferred from mutant phenotype PubMed 17499040. Source: BHF-UCL

telomere capping

Inferred from mutant phenotype PubMed 12768206PubMed 15657433. Source: BHF-UCL

telomere maintenance

Inferred from mutant phenotype Ref.24. Source: UniProtKB

telomere maintenance via telomerase

Inferred by curator PubMed 15657433. Source: BHF-UCL

telomere maintenance via telomere shortening

Inferred from mutant phenotype PubMed 11971978. Source: BHF-UCL

telomeric loop formation

Inferred from direct assay PubMed 10338214. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

chromosome, telomeric region

Inferred from direct assay Ref.24. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nuclear telomere cap complex

Inferred from direct assay PubMed 15181449PubMed 16880378. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17055345. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: InterPro

double-stranded telomeric DNA binding

Inferred from sequence or structural similarity Ref.3. Source: BHF-UCL

protein C-terminus binding

Inferred from physical interaction PubMed 12181313. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.3. Source: BHF-UCL

telomeric DNA binding

Inferred from direct assay Ref.24. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15554-3)

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: Q15554-4)

The sequence of this isoform differs from the canonical sequence as follows:
     281-293: MAKKALKSESAAS → VRLGPSPITMVCP
     294-542: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542Telomeric repeat-binding factor 2
PRO_0000197131

Regions

Domain484 – 54158HTH myb-type
DNA binding512 – 53726H-T-H motif Ref.24
Region84 – 287204TRFH dimerization
Motif371 – 3755Nuclear localization signal Potential
Compositional bias55 – 7218Arg-rich (basic)

Amino acid modifications

Modified residue591Asymmetric dimethylarginine; by PRMT1 Ref.22
Modified residue601Omega-N-methylarginine Ref.22
Modified residue2301Phosphothreonine; by ATM Ref.11
Modified residue3651Phosphoserine Ref.12 Ref.16 Ref.19 Ref.23 Ref.25 Ref.27

Natural variations

Alternative sequence281 – 29313MAKKA…ESAAS → VRLGPSPITMVCP in isoform 2.
VSP_003304
Alternative sequence294 – 542249Missing in isoform 2.
VSP_003305
Natural variant4551S → G.
Corresponds to variant rs35874485 [ dbSNP | Ensembl ].
VAR_050196

Secondary structure

.......................................... 542
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 16, 2014. Version 3.
Checksum: 3A278AC6B594C43A

FASTA54259,594
        10         20         30         40         50         60 
MAAGAGTAGP ASGPGVVRDP AASQPRKRPG REGGEGARRS DTMAGGGGSS DGSGRAAGRR 

        70         80         90        100        110        120 
ASRSSGRARR GRHEPGLGGP AERGAGEARL EEAVNRWVLK FYFHEALRAF RGSRYGDFRQ 

       130        140        150        160        170        180 
IRDIMQALLV RPLGKEHTVS RLLRVMQCLS RIEEGENLDC SFDMEAELTP LESAINVLEM 

       190        200        210        220        230        240 
IKTEFTLTEA VVESSRKLVK EAAVIICIKN KEFEKASKIL KKHMSKDPTT QKLRNDLLNI 

       250        260        270        280        290        300 
IREKNLAHPV IQNFSYETFQ QKMLRFLESH LDDAEPYLLT MAKKALKSES AASSTGKEDK 

       310        320        330        340        350        360 
QPAPGPVEKP PREPARQLRN PPTTIGMMTL KAAFKTLSGA QDSEAAFAKL DQKDLVLPTQ 

       370        380        390        400        410        420 
ALPASPALKN KRPRKDENES SAPADGEGGS ELQPKNKRMT ISRLVLEEDS QSTEPSAGLN 

       430        440        450        460        470        480 
SSQEAASAPP SKPTVLNQPL PGEKNPKVPK GKWNSSNGVE EKETWVEEDE LFQVQAAPDE 

       490        500        510        520        530        540 
DSTTNITKKQ KWTVEESEWV KAGVQKYGEG NWAAISKNYP FVNRTAVMIK DRWRTMKRLG 


MN 

« Hide

Isoform 2 [UniParc].

Checksum: F9B31F886F3D3C23
Show »

FASTA29332,298

References

« Hide 'large scale' references
[1]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Adrenal cortex.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-542 (ISOFORM 1).
Tissue: Mammary carcinoma.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 83-542 (ISOFORM 1).
Tissue: Cervix carcinoma.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 480-542 (ISOFORM 1).
Tissue: Cervix carcinoma.
[6]"TRF2 protects human telomeres from end-to-end fusions."
van Steensel B., Smogorzewska A., de Lange T.
Cell 92:401-413(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NBN.
[8]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SHELTERIN COMPLEX.
[9]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SHELTERIN COMPLEX.
[10]"Shelterin: the protein complex that shapes and safeguards human telomeres."
de Lange T.
Genes Dev. 19:2100-2110(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE SHELTERIN COMPLEX.
[11]"DNA damage-induced phosphorylation of the human telomere-associated protein TRF2."
Tanaka H., Mendonca M.S., Bradshaw P.S., Hoelz D.J., Malkas L.H., Meyn M.S., Gilley D.
Proc. Natl. Acad. Sci. U.S.A. 102:15539-15544(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-230 BY ATM.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCLRE1B.
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCLRE1B.
[15]"hSnm1B is a novel telomere-associated protein."
Freibaum B.D., Counter C.M.
J. Biol. Chem. 281:15033-15036(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCLRE1B.
[16]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCLRE1B.
[18]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCLRE1B.
[19]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLX4.
[22]"Arginine methylation regulates telomere length and stability."
Mitchell T.R., Glenfield K., Jeyanthan K., Zhu X.D.
Mol. Cell. Biol. 29:4918-4934(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-59 AND ARG-60 BY PRMT1.
[23]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[24]"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. expand/collapse author list , Wu Y., Biroccio A., Londono-Vallejo A., Giraud-Panis M.J., Gilson E.
Cell 142:230-242(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DCLRE1B, DNA-BINDING.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, 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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[29]"How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a view from high-resolution crystal structures."
Court R., Chapman L., Fairall L., Rhodes D.
EMBO Rep. 6:39-45(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 488-542 IN COMPLEX WITH TELOMERIC DNA, SUBUNIT.
[30]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 84-318 IN COMPLEX WITH TINF2 AND DCLRE1B, DOMAIN TRFH DIMERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC026464 Genomic DNA. No translation available.
BC024890 mRNA. Translation: AAH24890.1. Different initiation.
AF002999 mRNA. Translation: AAB81135.1. Sequence problems.
U95970 mRNA. Translation: AAD00821.1.
X93512 mRNA. Translation: CAA63769.1.
PIRS67923.
RefSeqNP_005643.2. NM_005652.4.
UniGeneHs.63335.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H6PX-ray2.20A/B85-287[»]
1VF9NMR-A480-542[»]
1VFCNMR-A480-542[»]
1W0UX-ray1.80A/B488-542[»]
1XG1NMR-A480-542[»]
3BU8X-ray2.15A/B84-318[»]
3BUAX-ray2.50A/B/C/D84-287[»]
3K6GX-ray1.95D/E/F317-358[»]
3SJMX-ray1.35A/B483-542[»]
4M7CX-ray2.05A/B87-286[»]
ProteinModelPortalQ15554.
SMRQ15554. Positions 43-249, 281-316, 446-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112873. 241 interactions.
DIPDIP-34052N.
IntActQ15554. 19 interactions.
MINTMINT-2831307.
STRING9606.ENSP00000254942.

PTM databases

PhosphoSiteQ15554.

Polymorphism databases

DMDM21542277.

Proteomic databases

PaxDbQ15554.
PRIDEQ15554.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254942; ENSP00000254942; ENSG00000132604. [Q15554-3]
ENST00000603068; ENSP00000474453; ENSG00000132604. [Q15554-1]
GeneID7014.
KEGGhsa:7014.

Organism-specific databases

CTD7014.
GeneCardsGC16M069389.
HGNCHGNC:11729. TERF2.
HPACAB010451.
HPA001907.
HPA002735.
MIM602027. gene.
neXtProtNX_Q15554.
PharmGKBPA36446.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44337.
HOGENOMHOG000154547.
HOVERGENHBG108560.
InParanoidQ15554.
KOK11111.
OMAITKKQKW.
OrthoDBEOG7DFXCF.
PhylomeDBQ15554.
TreeFamTF333209.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressQ15554.
BgeeQ15554.
CleanExHS_TERF2.
GenevestigatorQ15554.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
1.25.40.210. 1 hit.
InterProIPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
IPR017357. Telomere_repeat-bd-1/2.
IPR013867. Telomere_rpt-bd_fac_dimer_dom.
[Graphical view]
PfamPF00249. Myb_DNA-binding. 1 hit.
PF08558. TRF. 1 hit.
[Graphical view]
PIRSFPIRSF038016. Telomere_bd-1_Pin2. 1 hit.
ProDomPD014243. Telomere_repeat-bd_fac_dimer. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00717. SANT. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
SSF63600. SSF63600. 1 hit.
PROSITEPS51294. HTH_MYB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTERF2. human.
EvolutionaryTraceQ15554.
GeneWikiTERF2.
GenomeRNAi7014.
NextBio27401.
PROQ15554.
SOURCESearch...

Entry information

Entry nameTERF2_HUMAN
AccessionPrimary (citable) accession number: Q15554
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: April 16, 2014
Last modified: April 16, 2014
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM