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P54274

- TERF1_HUMAN

UniProt

P54274 - TERF1_HUMAN

Protein

Telomeric repeat-binding factor 1

Gene

TERF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. 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.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi403 – 42826H-T-H motifPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: InterPro
    2. DNA binding Source: UniProtKB
    3. DNA binding, bending Source: BHF-UCL
    4. double-stranded telomeric DNA binding Source: UniProtKB
    5. microtubule binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein heterodimerization activity Source: UniProtKB
    8. protein homodimerization activity Source: UniProtKB
    9. telomeric DNA binding Source: UniProtKB

    GO - Biological processi

    1. age-dependent telomere shortening Source: UniProtKB
    2. G2/M transition of mitotic cell cycle Source: UniProtKB
    3. mitotic nuclear division Source: UniProtKB-KW
    4. mitotic spindle assembly checkpoint Source: UniProtKB
    5. negative regulation of DNA replication Source: BHF-UCL
    6. negative regulation of telomerase activity Source: BHF-UCL
    7. negative regulation of telomere maintenance via semi-conservative replication Source: BHF-UCL
    8. negative regulation of telomere maintenance via telomerase Source: BHF-UCL
    9. positive regulation of apoptotic process Source: UniProtKB
    10. positive regulation of microtubule polymerization Source: UniProtKB
    11. positive regulation of mitosis Source: UniProtKB
    12. positive regulation of mitotic cell cycle Source: UniProtKB
    13. protein homooligomerization Source: UniProtKB
    14. response to drug Source: Ensembl
    15. telomere maintenance Source: Reactome
    16. telomere maintenance via telomerase Source: UniProtKB
    17. telomere maintenance via telomere shortening Source: BHF-UCL

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    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 1
    Alternative name(s):
    NIMA-interacting protein 2
    TTAGGG repeat-binding factor 1
    Telomeric protein Pin2/TRF1
    Gene namesi
    Name:TERF1
    Synonyms:PIN2, TRBF1, TRF, TRF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:11728. TERF1.

    Subcellular locationi

    Nucleus. Cytoplasmcytoskeletonspindle. Chromosometelomere
    Note: Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle.

    GO - Cellular componenti

    1. chromosome, telomeric region Source: BHF-UCL
    2. cytoplasm Source: UniProtKB-KW
    3. nuclear telomere cap complex Source: BHF-UCL
    4. nucleolus Source: HPA
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProtKB
    7. spindle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Cytoskeleton, Nucleus, Telomere

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi74 – 741A → D: Abolishes dimerization and telomere binding; when associated with P-75. 1 Publication
    Mutagenesisi75 – 751A → P: Abolishes dimerization and telomere binding; when associated with D-74. 1 Publication
    Mutagenesisi77 – 771W → P: Abolishes telomere binding. 1 Publication
    Mutagenesisi81 – 811F → P: Abolishes telomere binding. 1 Publication
    Mutagenesisi90 – 901F → P: Diminishes telomere binding.
    Mutagenesisi115 – 1151L → R: Loss of interaction with FBXO4. 1 Publication
    Mutagenesisi120 – 1201L → R: Loss of interaction with FBXO4. 1 Publication
    Mutagenesisi219 – 2191S → A: Loss of phosphorylation; induction of mitotic entry and apoptosis and increased radiation hypersensitivity of ataxia-telangiectasia cells. 1 Publication
    Mutagenesisi219 – 2191S → D or E: Fails to induce apoptosis and decreases radiation hypersensitivity of ataxia-telangiectasia cells (phospho-mimicking mutants). 1 Publication

    Organism-specific databases

    PharmGKBiPA36445.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 439438Telomeric repeat-binding factor 1PRO_0000197129Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei11 – 111Phosphoserine2 Publications
    Modified residuei219 – 2191Phosphoserine; by ATM1 Publication

    Post-translational modificationi

    Phosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage.3 Publications
    ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind to telomeric DNA.
    Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-protein ligase complex, leading to its degradation by the proteasome.2 Publications

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP54274.
    PaxDbiP54274.
    PRIDEiP54274.

    PTM databases

    PhosphoSiteiP54274.

    Expressioni

    Tissue specificityi

    Highly expressed and ubiquitous. Isoform Pin2 predominates.

    Inductioni

    Expression is tightly regulated during the cell cycle; levels are low in G1 and S phase and increase during G2 phase and mitosis.

    Gene expression databases

    ArrayExpressiP54274.
    BgeeiP54274.
    CleanExiHS_TERF1.
    GenevestigatoriP54274.

    Organism-specific databases

    HPAiHPA048379.

    Interactioni

    Subunit structurei

    Homodimer; can contain both isoforms. Found in a complex with POT1; TINF2 and TNKS1. Interacts with ATM, TINF2, TNKS1, TNKS2, PINX1, NEK2 and MAPRE1. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with RLIM (via N-terminus). Interacts with FBXO4. Interaction with TINF2 protects against interaction with FBXO4 and subsequent polyubiquitination and proteasomal degradation. Interacts with GNL3L; this interaction promotes homodimerization. Interacts with TIN2. Interacts with RTEL1. Interactions with GNL3L and TIN2 are mutually exclusive. Interacts with CCDC79/TERB1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATMQ133155EBI-711018,EBI-495465
    BLMP541323EBI-710997,EBI-621372
    FBXO4Q9UKT5-13EBI-711018,EBI-960421
    MAPRE1Q156912EBI-710997,EBI-1004115
    STAG1Q8WVM74EBI-710997,EBI-1175097
    TNKS2Q9H2K22EBI-710997,EBI-4398527

    Protein-protein interaction databases

    BioGridi112872. 300 interactions.
    DIPiDIP-29412N.
    IntActiP54274. 31 interactions.
    MINTiMINT-221323.
    STRINGi9606.ENSP00000276603.

    Structurei

    Secondary structure

    1
    439
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi63 – 9230
    Helixi95 – 11016
    Beta strandi113 – 1153
    Helixi117 – 13317
    Turni134 – 1363
    Beta strandi143 – 1453
    Helixi150 – 1589
    Helixi167 – 18620
    Helixi190 – 20011
    Beta strandi203 – 2053
    Helixi211 – 2199
    Helixi226 – 2305
    Helixi233 – 25119
    Beta strandi252 – 2543
    Helixi255 – 26511
    Beta strandi377 – 3793
    Helixi385 – 39814
    Helixi403 – 4097
    Helixi417 – 42812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BA5NMR-A378-430[»]
    1H6OX-ray2.90A62-265[»]
    1ITYNMR-A371-439[»]
    1IV6NMR-A371-439[»]
    1W0TX-ray2.00A/B379-431[»]
    3BQOX-ray2.00A58-268[»]
    3L82X-ray2.40A58-268[»]
    ProteinModelPortaliP54274.
    SMRiP54274. Positions 64-266, 373-439.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54274.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini375 – 43258HTH myb-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni58 – 268211TRFH dimerizationAdd
    BLAST
    Regioni265 – 378114Interaction with RLIMAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi337 – 35620Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 7170Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi55 – 628Poly-Glu

    Domaini

    The acidic N-terminal domain binds to the ankyrin repeats of TNKS1 and TNKS2. The C-terminal domain binds microtubules.1 Publication
    The TRFH dimerization region mediates the interaction with 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

    eggNOGiNOG72230.
    HOGENOMiHOG000132847.
    HOVERGENiHBG054097.
    InParanoidiP54274.
    KOiK11110.
    OMAiYQLRTVY.
    OrthoDBiEOG7DFXCF.
    PhylomeDBiP54274.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P54274-1) [UniParc]FASTAAdd to Basket

    Also known as: TRF1

    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

    MAEDVSSAAP SPRGCADGRD ADPTEEQMAE TERNDEEQFE CQELLECQVQ    50
    VGAPEEEEEE EEDAGLVAEA EAVAAGWMLD FLCLSLCRAF RDGRSEDFRR 100
    TRNSAEAIIH GLSSLTACQL RTIYICQFLT RIAAGKTLDA QFENDERITP 150
    LESALMIWGS IEKEHDKLHE EIQNLIKIQA IAVCMENGNF KEAEEVFERI 200
    FGDPNSHMPF KSKLLMIISQ KDTFHSFFQH FSYNHMMEKI KSYVNYVLSE 250
    KSSTFLMKAA AKVVESKRTR TITSQDKPSG NDVEMETEAN LDTRKSVSDK 300
    QSAVTESSEG TVSLLRSHKN LFLSKLQHGT QQQDLNKKER RVGTPQSTKK 350
    KKESRRATES RIPVSKSQPV TPEKHRARKR QAWLWEEDKN LRSGVRKYGE 400
    GNWSKILLHY KFNNRTSVML KDRWRTMKKL KLISSDSED 439
    Length:439
    Mass (Da):50,246
    Last modified:September 23, 2008 - v3
    Checksum:iAB548E7D3124A211
    GO
    Isoform 2 (identifier: P54274-2) [UniParc]FASTAAdd to Basket

    Also known as: Pin2

    The sequence of this isoform differs from the canonical sequence as follows:
         296-315: Missing.

    Show »
    Length:419
    Mass (Da):48,239
    Checksum:i4C261E58E09C2AF9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141G → R in AAB54036. (PubMed:7502076)Curated
    Sequence conflicti14 – 141G → R in AAB17975. (PubMed:9326950)Curated
    Sequence conflicti14 – 141G → R in AAB81137. (PubMed:9326950)Curated
    Sequence conflicti14 – 141G → R in AAB53363. (PubMed:9391075)Curated
    Sequence conflicti338 – 3381K → E in CAA63768. (PubMed:8614633)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei296 – 31520Missing in isoform 2. 3 PublicationsVSP_003303Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40705 mRNA. Translation: AAB54036.1.
    AF003001 mRNA. Translation: AAB81137.1.
    AH003684 Genomic DNA. Translation: AAB17975.1.
    U74382 mRNA. Translation: AAB53363.1.
    EU088287 Genomic DNA. Translation: ABV02580.1.
    AC022893 Genomic DNA. No translation available.
    BC029378 mRNA. Translation: AAH29378.1.
    X93511 mRNA. Translation: CAA63768.1.
    CCDSiCCDS6210.1. [P54274-2]
    CCDS6211.1. [P54274-1]
    PIRiA57573.
    RefSeqiNP_003209.2. NM_003218.3. [P54274-2]
    NP_059523.2. NM_017489.2. [P54274-1]
    UniGeneiHs.442707.

    Genome annotation databases

    EnsembliENST00000276602; ENSP00000276602; ENSG00000147601. [P54274-2]
    ENST00000276603; ENSP00000276603; ENSG00000147601. [P54274-1]
    GeneIDi7013.
    KEGGihsa:7013.
    UCSCiuc003xzd.2. human. [P54274-1]
    uc003xze.2. human. [P54274-2]

    Polymorphism databases

    DMDMi206729904.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40705 mRNA. Translation: AAB54036.1 .
    AF003001 mRNA. Translation: AAB81137.1 .
    AH003684 Genomic DNA. Translation: AAB17975.1 .
    U74382 mRNA. Translation: AAB53363.1 .
    EU088287 Genomic DNA. Translation: ABV02580.1 .
    AC022893 Genomic DNA. No translation available.
    BC029378 mRNA. Translation: AAH29378.1 .
    X93511 mRNA. Translation: CAA63768.1 .
    CCDSi CCDS6210.1. [P54274-2 ]
    CCDS6211.1. [P54274-1 ]
    PIRi A57573.
    RefSeqi NP_003209.2. NM_003218.3. [P54274-2 ]
    NP_059523.2. NM_017489.2. [P54274-1 ]
    UniGenei Hs.442707.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BA5 NMR - A 378-430 [» ]
    1H6O X-ray 2.90 A 62-265 [» ]
    1ITY NMR - A 371-439 [» ]
    1IV6 NMR - A 371-439 [» ]
    1W0T X-ray 2.00 A/B 379-431 [» ]
    3BQO X-ray 2.00 A 58-268 [» ]
    3L82 X-ray 2.40 A 58-268 [» ]
    ProteinModelPortali P54274.
    SMRi P54274. Positions 64-266, 373-439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112872. 300 interactions.
    DIPi DIP-29412N.
    IntActi P54274. 31 interactions.
    MINTi MINT-221323.
    STRINGi 9606.ENSP00000276603.

    PTM databases

    PhosphoSitei P54274.

    Polymorphism databases

    DMDMi 206729904.

    Proteomic databases

    MaxQBi P54274.
    PaxDbi P54274.
    PRIDEi P54274.

    Protocols and materials databases

    DNASUi 7013.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000276602 ; ENSP00000276602 ; ENSG00000147601 . [P54274-2 ]
    ENST00000276603 ; ENSP00000276603 ; ENSG00000147601 . [P54274-1 ]
    GeneIDi 7013.
    KEGGi hsa:7013.
    UCSCi uc003xzd.2. human. [P54274-1 ]
    uc003xze.2. human. [P54274-2 ]

    Organism-specific databases

    CTDi 7013.
    GeneCardsi GC08P073921.
    H-InvDB HIX0007582.
    HGNCi HGNC:11728. TERF1.
    HPAi HPA048379.
    MIMi 600951. gene.
    neXtProti NX_P54274.
    PharmGKBi PA36445.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG72230.
    HOGENOMi HOG000132847.
    HOVERGENi HBG054097.
    InParanoidi P54274.
    KOi K11110.
    OMAi YQLRTVY.
    OrthoDBi EOG7DFXCF.
    PhylomeDBi P54274.
    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 TERF1. human.
    EvolutionaryTracei P54274.
    GeneWikii TERF1.
    GenomeRNAii 7013.
    NextBioi 27395.
    PROi P54274.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54274.
    Bgeei P54274.
    CleanExi HS_TERF1.
    Genevestigatori P54274.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Cervix carcinoma.
    2. de Lange T.
      Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 14.
    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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-138 (ISOFORM1/2).
    4. "Characterization and cell cycle regulation of the related human telomeric proteins Pin2 and TRF1 suggest a role in mitosis."
      Shen M., Haggblom C., Vogt M., Hunter T., Lu K.P.
      Proc. Natl. Acad. Sci. U.S.A. 94:13618-13623(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Cervix carcinoma.
    5. NIEHS SNPs program
      Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Liver.
    8. "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 329-439 (ISOFORMS 1/2).
      Tissue: Cervix carcinoma.
    9. "Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks."
      Kishi S., Zhou X.Z., Ziv Y., Khoo C., Hill D.E., Shiloh Y., Lu K.P.
      J. Biol. Chem. 276:29282-29291(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-219, PHOSPHORYLATION AT SER-219, INTERACTION WITH ATM.
    10. "Involvement of the telomeric protein Pin2/TRF1 in the regulation of the mitotic spindle."
      Nakamura M., Zhen Zhou X., Kishi S., Ping Lu K.
      FEBS Lett. 514:193-198(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAPRE1 AND WITH THE MITOTIC SPINDLE.
    11. "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres."
      Cook B.D., Dynek J.N., Chang W., Shostak G., Smith S.
      Mol. Cell. Biol. 22:332-342(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ADP-RIBOSYLATION.
    12. "POT1 as a terminal transducer of TRF1 telomere length control."
      Loayza D., De Lange T.
      Nature 423:1013-1018(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH POT1; TINF2 AND TNKS1.
    13. "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.
    14. "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.
    15. "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.
    16. "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-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    19. "Ubiquitin ligase RLIM modulates telomere length homeostasis through a proteolysis of TRF1."
      Her Y.R., Chung I.K.
      J. Biol. Chem. 284:8557-8566(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RLIM, SUBCELLULAR LOCATION, UBIQUITINATION.
    20. "GNL3L stabilizes the TRF1 complex and promotes mitotic transition."
      Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.
      J. Cell Biol. 185:827-839(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    21. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: INTERACTION WITH RTEL1.
    23. "Solution structure of the DNA-binding domain of human telomeric protein, hTRF1."
      Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y.
      Structure 6:1057-1065(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 378-430.
    24. "Solution structure of a telomeric DNA complex of human TRF1."
      Nishikawa T., Okamura H., Nagadoi A., Koenig P., Rhodes D., Nishimura Y.
      Structure 9:1237-1251(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 371-439.
    25. "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 (2.9 ANGSTROMS) OF 48-268, MUTAGENESIS OF ALA-74; ALA-75; TRP-77 AND PHE-81.
    26. "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 (2.0 ANGSTROMS) OF 379-431 IN COMPLEX WITH TELOMERIC DNA, SUBUNIT.
    27. "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 (2.0 ANGSTROMS) OF 58-268 IN COMPLEX WITH TINF2, INTERACTION WITH TINF2 AND PINX1, DOMAIN TRFH DIMERIZATION, SUBUNIT.
    28. "Structural basis of selective ubiquitination of TRF1 by SCFFbx4."
      Zeng Z., Wang W., Yang Y., Chen Y., Yang X., Diehl J.A., Liu X., Lei M.
      Dev. Cell 18:214-225(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 58-268 IN COMPLEX WITH FBXO4, MUTAGENESIS OF LEU-115 AND LEU-120, INTERACTION WITH TINF2, SUBUNIT, UBIQUITINATION.

    Entry informationi

    Entry nameiTERF1_HUMAN
    AccessioniPrimary (citable) accession number: P54274
    Secondary accession number(s): A7XP29
    , Q15553, Q8NHT6, Q93029
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 167 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3