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Q15554

- TERF2_HUMAN

UniProt

Q15554 - TERF2_HUMAN

Protein

Telomeric repeat-binding factor 2

Gene

TERF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 3 (16 Apr 2014)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi512 – 53726H-T-H motifPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: InterPro
    2. double-stranded telomeric DNA binding Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. protein C-terminus binding Source: UniProtKB
    5. protein homodimerization activity Source: BHF-UCL
    6. telomeric DNA binding Source: UniProtKB

    GO - Biological processi

    1. age-dependent telomere shortening Source: BHF-UCL
    2. cell cycle Source: UniProtKB-KW
    3. cellular senescence Source: BHF-UCL
    4. in utero embryonic development Source: Ensembl
    5. negative regulation of telomere maintenance Source: UniProtKB
    6. negative regulation of telomere maintenance via semi-conservative replication Source: BHF-UCL
    7. positive regulation of telomere maintenance Source: Ensembl
    8. protection from non-homologous end joining at telomere Source: BHF-UCL
    9. protein localization to chromosome, telomeric region Source: BHF-UCL
    10. telomere capping Source: BHF-UCL
    11. telomere maintenance Source: UniProtKB
    12. telomere maintenance via telomerase Source: BHF-UCL
    13. telomere maintenance via telomere shortening Source: BHF-UCL
    14. telomeric loop formation Source: BHF-UCL

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_75792. Meiotic synapsis.
    REACT_7963. Packaging Of Telomere Ends.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Telomeric repeat-binding factor 2
    Alternative name(s):
    TTAGGG repeat-binding factor 2
    Telomeric DNA-binding protein
    Gene namesi
    Name:TERF2
    Synonyms:TRBF2, TRF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:11729. TERF2.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation. Chromosometelomere 1 Publication
    Note: Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase.

    GO - Cellular componenti

    1. chromosome, telomeric region Source: UniProtKB
    2. cytoplasm Source: HPA
    3. Golgi apparatus Source: HPA
    4. male germ cell nucleus Source: Ensembl
    5. nuclear telomere cap complex Source: BHF-UCL
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36446.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 542542Telomeric repeat-binding factor 2PRO_0000197131Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591Asymmetric dimethylarginine; by PRMT11 Publication
    Modified residuei60 – 601Omega-N-methylarginine1 Publication
    Modified residuei230 – 2301Phosphothreonine; by ATM1 Publication
    Modified residuei365 – 3651Phosphoserine6 Publications

    Post-translational modificationi

    Phosphorylated upon DNA damage, most probably by ATM. Phosphorylated TERF2 is not bound to telomeric DNA, and rapidly localizes to damage sites.7 Publications
    Methylated by PRMT1 at multiple arginines within the N-terminal Arg-rich region. Methylation may control association with telomeres.1 Publication

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15554.
    PaxDbiQ15554.
    PRIDEiQ15554.

    PTM databases

    PhosphoSiteiQ15554.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in spleen, thymus, prostate, uterus, testis, small intestine, colon and peripheral blood leukocytes.

    Gene expression databases

    ArrayExpressiQ15554.
    BgeeiQ15554.
    CleanExiHS_TERF2.
    GenevestigatoriQ15554.

    Organism-specific databases

    HPAiCAB010451.
    HPA001907.
    HPA002735.

    Interactioni

    Subunit structurei

    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.12 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BLMP541328EBI-706637,EBI-621372
    DCLRE1BQ9H8166EBI-706637,EBI-3508943
    EBNA1P032113EBI-706637,EBI-996522From a different organism.
    ORC1Q134152EBI-706637,EBI-374847
    ORC2Q134163EBI-706637,EBI-374957
    POT1Q9NUX53EBI-706637,EBI-752420
    SLX4Q8IY925EBI-706637,EBI-2370740
    TERF2IPQ9NYB07EBI-706637,EBI-750109
    TINF2Q9BSI4-34EBI-706637,EBI-717418
    WRNQ141918EBI-706637,EBI-368417

    Protein-protein interaction databases

    BioGridi112873. 245 interactions.
    DIPiDIP-34052N.
    IntActiQ15554. 19 interactions.
    MINTiMINT-2831307.
    STRINGi9606.ENSP00000254942.

    Structurei

    Secondary structure

    1
    542
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni87 – 893
    Helixi90 – 11122
    Helixi115 – 12814
    Helixi137 – 15317
    Turni154 – 1563
    Beta strandi163 – 1653
    Helixi170 – 18415
    Helixi189 – 20921
    Helixi213 – 22311
    Helixi228 – 2303
    Helixi231 – 24313
    Turni244 – 2463
    Helixi249 – 2524
    Helixi256 – 26813
    Helixi277 – 2859
    Turni286 – 2883
    Helixi327 – 33812
    Helixi343 – 35210
    Turni482 – 4854
    Beta strandi487 – 4893
    Helixi494 – 50714
    Helixi512 – 5187
    Helixi526 – 53813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ15554.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15554.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini484 – 54158HTH myb-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni84 – 287204TRFH dimerizationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi371 – 3755Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi55 – 7218Arg-rich (basic)Add
    BLAST

    Domaini

    The TRFH dimerization region mediates the interaction with DCLRE1B/Apollo but not TINF2.1 Publication
    The HTH domain is an independent structural unit and mediates binding to telomeric DNA.1 Publication

    Sequence similaritiesi

    Contains 1 HTH myb-type DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG44337.
    HOGENOMiHOG000154547.
    HOVERGENiHBG108560.
    InParanoidiQ15554.
    KOiK11111.
    OMAiITKKQKW.
    OrthoDBiEOG7DFXCF.
    TreeFamiTF333209.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    1.25.40.210. 1 hit.
    InterProiIPR009057. Homeodomain-like.
    IPR017930. Myb_dom.
    IPR001005. SANT/Myb.
    IPR017357. Telomere_repeat-bd-1/2.
    IPR013867. Telomere_rpt-bd_fac_dimer_dom.
    [Graphical view]
    PfamiPF00249. Myb_DNA-binding. 1 hit.
    PF08558. TRF. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038016. Telomere_bd-1_Pin2. 1 hit.
    ProDomiPD014243. Telomere_repeat-bd_fac_dimer. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00717. SANT. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.
    SSF63600. SSF63600. 1 hit.
    PROSITEiPS51294. HTH_MYB. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15554-3) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAAGAGTAGP ASGPGVVRDP AASQPRKRPG REGGEGARRS DTMAGGGGSS    50
    DGSGRAAGRR ASRSSGRARR GRHEPGLGGP AERGAGEARL EEAVNRWVLK 100
    FYFHEALRAF RGSRYGDFRQ IRDIMQALLV RPLGKEHTVS RLLRVMQCLS 150
    RIEEGENLDC SFDMEAELTP LESAINVLEM IKTEFTLTEA VVESSRKLVK 200
    EAAVIICIKN KEFEKASKIL KKHMSKDPTT QKLRNDLLNI IREKNLAHPV 250
    IQNFSYETFQ QKMLRFLESH LDDAEPYLLT MAKKALKSES AASSTGKEDK 300
    QPAPGPVEKP PREPARQLRN PPTTIGMMTL KAAFKTLSGA QDSEAAFAKL 350
    DQKDLVLPTQ ALPASPALKN KRPRKDENES SAPADGEGGS ELQPKNKRMT 400
    ISRLVLEEDS QSTEPSAGLN SSQEAASAPP SKPTVLNQPL PGEKNPKVPK 450
    GKWNSSNGVE EKETWVEEDE LFQVQAAPDE DSTTNITKKQ KWTVEESEWV 500
    KAGVQKYGEG NWAAISKNYP FVNRTAVMIK DRWRTMKRLG MN 542
    Length:542
    Mass (Da):59,594
    Last modified:April 16, 2014 - v3
    Checksum:i3A278AC6B594C43A
    GO
    Isoform 2 (identifier: Q15554-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         281-293: MAKKALKSESAAS → VRLGPSPITMVCP
         294-542: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:293
    Mass (Da):32,298
    Checksum:iF9B31F886F3D3C23
    GO

    Sequence cautioni

    The sequence AAB81135.1 differs from that shown. Reason: Contaminating sequence. The N-terminus may be contaminated with vector sequence.
    The sequence AAB81135.1 differs from that shown. Reason: Frameshift at position 36.
    The sequence AAH24890.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti455 – 4551S → G.
    Corresponds to variant rs35874485 [ dbSNP | Ensembl ].
    VAR_050196

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei281 – 29313MAKKA…ESAAS → VRLGPSPITMVCP in isoform 2. 1 PublicationVSP_003304Add
    BLAST
    Alternative sequencei294 – 542249Missing in isoform 2. 1 PublicationVSP_003305Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS10879.2. [Q15554-3]
    PIRiS67923.
    RefSeqiNP_005643.2. NM_005652.4. [Q15554-3]
    UniGeneiHs.63335.

    Genome annotation databases

    EnsembliENST00000254942; ENSP00000254942; ENSG00000132604. [Q15554-3]
    ENST00000567296; ENSP00000454955; ENSG00000132604. [Q15554-4]
    GeneIDi7014.
    KEGGihsa:7014.
    UCSCiuc002exd.4. human. [Q15554-3]

    Polymorphism databases

    DMDMi21542277.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS10879.2. [Q15554-3 ]
    PIRi S67923.
    RefSeqi NP_005643.2. NM_005652.4. [Q15554-3 ]
    UniGenei Hs.63335.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H6P X-ray 2.20 A/B 85-287 [» ]
    1VF9 NMR - A 480-542 [» ]
    1VFC NMR - A 480-542 [» ]
    1W0U X-ray 1.80 A/B 488-542 [» ]
    1XG1 NMR - A 480-542 [» ]
    3BU8 X-ray 2.15 A/B 84-318 [» ]
    3BUA X-ray 2.50 A/B/C/D 84-287 [» ]
    3K6G X-ray 1.95 D/E/F 317-358 [» ]
    3SJM X-ray 1.35 A/B 483-542 [» ]
    4M7C X-ray 2.05 A/B 87-286 [» ]
    ProteinModelPortali Q15554.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112873. 245 interactions.
    DIPi DIP-34052N.
    IntActi Q15554. 19 interactions.
    MINTi MINT-2831307.
    STRINGi 9606.ENSP00000254942.

    PTM databases

    PhosphoSitei Q15554.

    Polymorphism databases

    DMDMi 21542277.

    Proteomic databases

    MaxQBi Q15554.
    PaxDbi Q15554.
    PRIDEi Q15554.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254942 ; ENSP00000254942 ; ENSG00000132604 . [Q15554-3 ]
    ENST00000567296 ; ENSP00000454955 ; ENSG00000132604 . [Q15554-4 ]
    GeneIDi 7014.
    KEGGi hsa:7014.
    UCSCi uc002exd.4. human. [Q15554-3 ]

    Organism-specific databases

    CTDi 7014.
    GeneCardsi GC16M069389.
    HGNCi HGNC:11729. TERF2.
    HPAi CAB010451.
    HPA001907.
    HPA002735.
    MIMi 602027. gene.
    neXtProti NX_Q15554.
    PharmGKBi PA36446.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44337.
    HOGENOMi HOG000154547.
    HOVERGENi HBG108560.
    InParanoidi Q15554.
    KOi K11111.
    OMAi ITKKQKW.
    OrthoDBi EOG7DFXCF.
    TreeFami TF333209.

    Enzyme and pathway databases

    Reactomei REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_75792. Meiotic synapsis.
    REACT_7963. Packaging Of Telomere Ends.

    Miscellaneous databases

    ChiTaRSi TERF2. human.
    EvolutionaryTracei Q15554.
    GeneWikii TERF2.
    GenomeRNAii 7014.
    NextBioi 27401.
    PROi Q15554.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15554.
    Bgeei Q15554.
    CleanExi HS_TERF2.
    Genevestigatori Q15554.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    1.25.40.210. 1 hit.
    InterProi IPR009057. Homeodomain-like.
    IPR017930. Myb_dom.
    IPR001005. SANT/Myb.
    IPR017357. Telomere_repeat-bd-1/2.
    IPR013867. Telomere_rpt-bd_fac_dimer_dom.
    [Graphical view ]
    Pfami PF00249. Myb_DNA-binding. 1 hit.
    PF08558. TRF. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038016. Telomere_bd-1_Pin2. 1 hit.
    ProDomi PD014243. Telomere_repeat-bd_fac_dimer. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00717. SANT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    SSF63600. SSF63600. 1 hit.
    PROSITEi PS51294. HTH_MYB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiTERF2_HUMAN
    AccessioniPrimary (citable) accession number: Q15554
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2002
    Last sequence update: April 16, 2014
    Last modified: October 1, 2014
    This is version 155 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3