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Q91VL8

- TE2IP_MOUSE

UniProt

Q91VL8 - TE2IP_MOUSE

Protein

Telomeric repeat-binding factor 2-interacting protein 1

Gene

Terf2ip

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes.3 Publications

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of DNA recombination at telomere Source: UniProtKB
    2. negative regulation of telomere maintenance Source: Ensembl
    3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    4. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    5. protein localization to chromosome, telomeric region Source: Ensembl
    6. regulation of double-strand break repair via homologous recombination Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB
    8. telomere maintenance via telomere lengthening Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_188819. DNA Damage/Telomere Stress Induced Senescence.
    REACT_198626. Meiotic synapsis.
    REACT_226125. Packaging Of Telomere Ends.
    REACT_75800. Meiotic Synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Telomeric repeat-binding factor 2-interacting protein 1
    Short name:
    TERF2-interacting telomeric protein 1
    Short name:
    TRF2-interacting telomeric protein 1
    Alternative name(s):
    Repressor/activator protein 1 homolog
    Short name:
    RAP1 homolog
    Gene namesi
    Name:Terf2ip
    Synonyms:Rap1
    ORF Names:MNCb-0448, MNCb-0628
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1929871. Terf2ip.

    Subcellular locationi

    Nucleus. Cytoplasm. Chromosome. Chromosometelomere
    Note: Associates with chromosomes, both at telomeres and in extratelomeric sites. Also exists as a cytoplasmic form, where it associates with the IKK complex.

    GO - Cellular componenti

    1. chromosome, telomeric region Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. Mre11 complex Source: Ensembl
    4. nuclear chromosome, telomeric region Source: MGI
    5. nuclear telomere cap complex Source: Ensembl
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus, Telomere

    Pathology & Biotechi

    Disruption phenotypei

    Mice are viable and fertile. No major telomere dysfunction such as telomere fusions are observed. An increased telomere fragility and recombination due to defects in HDR are however present. Mice with conditional deletion in stratified epithelia display shorter telomeres and developed skin hyperpigmentation in adulthood.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 393392Telomeric repeat-binding factor 2-interacting protein 1PRO_0000197127Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei36 – 361PhosphoserineBy similarity
    Modified residuei151 – 1511PhosphoserineBy similarity
    Modified residuei153 – 1531PhosphoserineBy similarity
    Modified residuei200 – 2001PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ91VL8.
    PaxDbiQ91VL8.
    PRIDEiQ91VL8.

    PTM databases

    PhosphoSiteiQ91VL8.

    Expressioni

    Gene expression databases

    BgeeiQ91VL8.
    GenevestigatoriQ91VL8.

    Interactioni

    Subunit structurei

    Homodimer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Binds to TERF2 (but not TERF1) with its C-terminus. Interacts with SLX4/BTBD12 By similarity. Interacts with TERF2; the interaction is direct. Does not interact with TERF1. Associates with the I-kappa-B-kinase (IKK) core complex, composed of CHUK, IKBKB and IKBKG.By similarity2 Publications

    Protein-protein interaction databases

    IntActiQ91VL8. 2 interactions.
    MINTiMINT-4137361.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91VL8.
    SMRiQ91VL8. Positions 129-187, 300-392.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini78 – 10124BRCTAdd
    BLAST
    Domaini125 – 18561Myb-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi377 – 39317Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi232 – 29766Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the RAP1 family.Curated
    Contains 1 BRCT domain.Curated
    Contains 1 Myb-like domain.Curated

    Phylogenomic databases

    eggNOGiNOG39788.
    GeneTreeiENSGT00390000005351.
    HOGENOMiHOG000120115.
    HOVERGENiHBG054209.
    InParanoidiQ8C2Y1.
    KOiK11113.
    OMAiSISFYVR.
    OrthoDBiEOG7KDFBG.
    PhylomeDBiQ91VL8.
    TreeFamiTF332348.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    InterProiIPR009057. Homeodomain-like.
    IPR021661. Rap1_C.
    IPR015010. Rap1_Myb_dom.
    [Graphical view]
    PfamiPF08914. Myb_DNA-bind_2. 1 hit.
    PF11626. Rap1_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q91VL8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEAMDLGKD PNGPTHSSTL FVREDGSAMS FYVRPSSAKR RLSTLILHGG    50
    GTVCRVQEPG AVLLAQPGEA LAEASGDFIS TQYILDCVDR NEKLDLEAYR 100
    LGLTEQASDP KPGASTEGST EPEPQPLTGR IAYTDAEDVA ILTYVKENAR 150
    SPSSVTGNAL WKAMEKSSLT QHSWQSLKDR YLKHLRGQEH KYLLGNAPVS 200
    PSSQKLKRKA EQDPEAADSG EPQNKRAPDL PEEECVKGEI KENGEADNKL 250
    FEEAAPEFGE AVVDESPDFE IHITMCDGDP PTPEEDSETQ PDEEEEEPKV 300
    STQEVGTAIK VIRQLMEKFN LDLSTVTQAL LKNSGELEAT SSFLESGRRP 350
    DGYPIWCRQD DLDLQKDDDD TKNALVKKFG AQNVARRIEF RKK 393
    Length:393
    Mass (Da):43,353
    Last modified:December 1, 2001 - v1
    Checksum:i7A15CFD83733BE2D
    GO

    Sequence cautioni

    The sequence BAA95043.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti281 – 2866PTPEED → HTHTQS in BAA95042. 1 PublicationCurated
    Sequence conflicti281 – 2866PTPEED → HTHTQS in BAA95043. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK041613 mRNA. Translation: BAC31005.1.
    AK051818 mRNA. Translation: BAC34781.1.
    AK081557 mRNA. Translation: BAC38258.1.
    AK087729 mRNA. Translation: BAC39985.1.
    AK084563 mRNA. Translation: BAC39217.1.
    AK148508 mRNA. Translation: BAE28592.1.
    AK148537 mRNA. Translation: BAE28607.1.
    AK161452 mRNA. Translation: BAE36404.1.
    AK165074 mRNA. Translation: BAE38026.1.
    AC114648 Genomic DNA. No translation available.
    BC012270 mRNA. Translation: AAH12270.1.
    BC017641 mRNA. Translation: AAH17641.1.
    AB041557 mRNA. Translation: BAA95042.1.
    AB041559 mRNA. Translation: BAA95043.1. Different initiation.
    CCDSiCCDS52678.1.
    RefSeqiNP_065609.2. NM_020584.2.
    UniGeneiMm.213064.

    Genome annotation databases

    EnsembliENSMUST00000052138; ENSMUSP00000052170; ENSMUSG00000033430.
    GeneIDi57321.
    KEGGimmu:57321.
    UCSCiuc012gla.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK041613 mRNA. Translation: BAC31005.1 .
    AK051818 mRNA. Translation: BAC34781.1 .
    AK081557 mRNA. Translation: BAC38258.1 .
    AK087729 mRNA. Translation: BAC39985.1 .
    AK084563 mRNA. Translation: BAC39217.1 .
    AK148508 mRNA. Translation: BAE28592.1 .
    AK148537 mRNA. Translation: BAE28607.1 .
    AK161452 mRNA. Translation: BAE36404.1 .
    AK165074 mRNA. Translation: BAE38026.1 .
    AC114648 Genomic DNA. No translation available.
    BC012270 mRNA. Translation: AAH12270.1 .
    BC017641 mRNA. Translation: AAH17641.1 .
    AB041557 mRNA. Translation: BAA95042.1 .
    AB041559 mRNA. Translation: BAA95043.1 . Different initiation.
    CCDSi CCDS52678.1.
    RefSeqi NP_065609.2. NM_020584.2.
    UniGenei Mm.213064.

    3D structure databases

    ProteinModelPortali Q91VL8.
    SMRi Q91VL8. Positions 129-187, 300-392.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q91VL8. 2 interactions.
    MINTi MINT-4137361.

    PTM databases

    PhosphoSitei Q91VL8.

    Proteomic databases

    MaxQBi Q91VL8.
    PaxDbi Q91VL8.
    PRIDEi Q91VL8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000052138 ; ENSMUSP00000052170 ; ENSMUSG00000033430 .
    GeneIDi 57321.
    KEGGi mmu:57321.
    UCSCi uc012gla.1. mouse.

    Organism-specific databases

    CTDi 54386.
    MGIi MGI:1929871. Terf2ip.

    Phylogenomic databases

    eggNOGi NOG39788.
    GeneTreei ENSGT00390000005351.
    HOGENOMi HOG000120115.
    HOVERGENi HBG054209.
    InParanoidi Q8C2Y1.
    KOi K11113.
    OMAi SISFYVR.
    OrthoDBi EOG7KDFBG.
    PhylomeDBi Q91VL8.
    TreeFami TF332348.

    Enzyme and pathway databases

    Reactomei REACT_188819. DNA Damage/Telomere Stress Induced Senescence.
    REACT_198626. Meiotic synapsis.
    REACT_226125. Packaging Of Telomere Ends.
    REACT_75800. Meiotic Synapsis.

    Miscellaneous databases

    ChiTaRSi TERF2IP. mouse.
    NextBioi 313686.
    PROi Q91VL8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q91VL8.
    Genevestigatori Q91VL8.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    InterProi IPR009057. Homeodomain-like.
    IPR021661. Rap1_C.
    IPR015010. Rap1_Myb_dom.
    [Graphical view ]
    Pfami PF08914. Myb_DNA-bind_2. 1 hit.
    PF11626. Rap1_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Eye, Head, Heart, Ovary, Oviduct, Pancreas, Testis and Thymus.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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].
      Tissue: Mammary tumor.
    4. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
      Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-286.
      Strain: C57BL/6.
      Tissue: Brain.
    5. "The telomeric protein Rap1 is conserved in vertebrates and is expressed from a bidirectional promoter positioned between the Rap1 and KARS genes."
      Tan M., Wei C., Price C.M.
      Gene 323:1-10(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIDIRECTIONAL PROMOTER WITH KARS.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Mammalian Rap1 controls telomere function and gene expression through binding to telomeric and extratelomeric sites."
      Martinez P., Thanasoula M., Carlos A.R., Gomez-Lopez G., Tejera A.M., Schoeftner S., Dominguez O., Pisano D.G., Tarsounas M., Blasco M.A.
      Nat. Cell Biol. 12:768-780(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    9. Cited for: FUNCTION IN NF-KAPPA-B PATHWAY, SUBCELLULAR LOCATION, INTERACTION WITH TERF2; CHUK; IKBKB AND IKBKG.
    10. "Loss of Rap1 induces telomere recombination in the absence of NHEJ or a DNA damage signal."
      Sfeir A., Kabir S., van Overbeek M., Celli G.B., de Lange T.
      Science 327:1657-1661(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH TERF2.

    Entry informationi

    Entry nameiTE2IP_MOUSE
    AccessioniPrimary (citable) accession number: Q91VL8
    Secondary accession number(s): D3YWE8
    , Q543F4, Q8C2Y1, Q9JJE8, Q9JJE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Shares a bidirectional promoter with KARS (PubMed:14659874). This shared promoter with an essential gene complicated the task when generating knockout mice; the problem was overcome by generating conditional knockout strategies (PubMed:20339076 and PubMed:20622869;).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3