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Q9NYB0

- TE2IP_HUMAN

UniProt

Q9NYB0 - TE2IP_HUMAN

Protein

Telomeric repeat-binding factor 2-interacting protein 1

Gene

TERF2IP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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.2 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: UniProtKB
    3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    4. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    5. protection from non-homologous end joining at telomere Source: BHF-UCL
    6. protein localization to chromosome, telomeric region Source: BHF-UCL
    7. regulation of double-strand break repair via homologous recombination Source: UniProtKB
    8. regulation of transcription, DNA-templated Source: UniProtKB
    9. telomere maintenance Source: BHF-UCL
    10. telomere maintenance via telomerase Source: ProtInc
    11. telomere maintenance via telomere lengthening Source: UniProtKB
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    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-interacting protein 1
    Short name:
    TERF2-interacting telomeric protein 1
    Short name:
    TRF2-interacting telomeric protein 1
    Alternative name(s):
    Dopamine receptor-interacting protein 5
    Repressor/activator protein 1 homolog
    Short name:
    RAP1 homolog
    Short name:
    hRap1
    Gene namesi
    Name:TERF2IP
    Synonyms:DRIP5, RAP1
    ORF Names:PP8000
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:19246. TERF2IP.

    Subcellular locationi

    Nucleus. Cytoplasm By similarity. 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 By similarity.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus, Telomere

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134976325.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 399398Telomeric repeat-binding factor 2-interacting protein 1PRO_0000197126Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei36 – 361Phosphoserine2 Publications
    Modified residuei154 – 1541Phosphoserine3 Publications
    Modified residuei156 – 1561Phosphoserine1 Publication
    Modified residuei203 – 2031Phosphoserine5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NYB0.
    PaxDbiQ9NYB0.
    PeptideAtlasiQ9NYB0.
    PRIDEiQ9NYB0.

    PTM databases

    PhosphoSiteiQ9NYB0.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed.

    Gene expression databases

    ArrayExpressiQ9NYB0.
    BgeeiQ9NYB0.
    CleanExiHS_TERF2IP.
    GenevestigatoriQ9NYB0.

    Organism-specific databases

    HPAiCAB018660.
    CAB018749.
    HPA006719.

    Interactioni

    Subunit structurei

    Associates with the I-kappa-B-kinase (IKK) core complex, composed of CHUK, IKBKB and IKBKG By similarity. Homodimer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with TERF2; the interaction is direct. Does not interact with TERF1. Interacts with SLX4/BTBD12.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SLX4Q8IY924EBI-750109,EBI-2370740
    TERF2Q155547EBI-750109,EBI-706637
    TINF2Q9BSI4-33EBI-750109,EBI-717418

    Protein-protein interaction databases

    BioGridi119942. 143 interactions.
    DIPiDIP-34868N.
    IntActiQ9NYB0. 17 interactions.
    MINTiMINT-1454139.
    STRINGi9606.ENSP00000300086.

    Structurei

    Secondary structure

    1
    399
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi138 – 15013
    Turni155 – 1595
    Helixi162 – 1698
    Beta strandi172 – 1743
    Helixi178 – 18710
    Helixi308 – 32417
    Helixi329 – 33810
    Turni339 – 3413
    Helixi343 – 35210
    Helixi364 – 3707
    Helixi375 – 38511
    Helixi387 – 39711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FEXNMR-A132-190[»]
    3K6GX-ray1.95A/B/C303-399[»]
    ProteinModelPortaliQ9NYB0.
    SMRiQ9NYB0. Positions 132-190, 306-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NYB0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini78 – 10124BRCTAdd
    BLAST
    Domaini128 – 18861Myb-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi383 – 39917Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi214 – 30491Asp/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.
    HOGENOMiHOG000120115.
    HOVERGENiHBG054209.
    InParanoidiQ9NYB0.
    KOiK11113.
    OMAiSISFYVR.
    OrthoDBiEOG7KDFBG.
    PhylomeDBiQ9NYB0.
    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.

    Q9NYB0-1 [UniParc]FASTAAdd to Basket

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    MAEAMDLGKD PNGPTHSSTL FVRDDGSSMS FYVRPSPAKR RLSTLILHGG    50
    GTVCRVQEPG AVLLAQPGEA LAEASGDFIS TQYILDCVER NERLELEAYR 100
    LGPASAADTG SEAKPGALAE GAAEPEPQRH AGRIAFTDAD DVAILTYVKE 150
    NARSPSSVTG NALWKAMEKS SLTQHSWQSL KDRYLKHLRG QEHKYLLGDA 200
    PVSPSSQKLK RKAEEDPEAA DSGEPQNKRT PDLPEEEYVK EEIQENEEAV 250
    KKMLVEATRE FEEVVVDESP PDFEIHITMC DDDPPTPEED SETQPDEEEE 300
    EEEEKVSQPE VGAAIKIIRQ LMEKFNLDLS TVTQAFLKNS GELEATSAFL 350
    ASGQRADGYP IWSRQDDIDL QKDDEDTREA LVKKFGAQNV ARRIEFRKK 399
    Length:399
    Mass (Da):44,260
    Last modified:October 1, 2000 - v1
    Checksum:iEAA615777F9D3D3D
    GO

    Sequence cautioni

    The sequence AAL55783.1 differs from that shown. Reason: Frameshift at position 151.
    The sequence BAG60996.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA91317.1 differs from that shown. Reason: Erroneous termination at position 299. Translated as Glu.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831Y → H in BAA91317. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti324 – 3241K → E.
    Corresponds to variant rs4888444 [ dbSNP | Ensembl ].
    VAR_050195

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF262988 mRNA. Translation: AAF72711.1.
    AF250393 mRNA. Translation: AAQ14259.1.
    AF289599 mRNA. Translation: AAL55783.1. Frameshift.
    AK000669 mRNA. Translation: BAA91317.1. Sequence problems.
    AK298880 mRNA. Translation: BAG60996.1. Different initiation.
    AC025287 Genomic DNA. No translation available.
    CH471114 Genomic DNA. Translation: EAW95616.1.
    CH471114 Genomic DNA. Translation: EAW95618.1.
    BC004465 mRNA. Translation: AAH04465.1.
    BC005841 mRNA. Translation: AAH05841.1.
    BC022428 mRNA. Translation: AAH22428.1.
    BC078171 mRNA. Translation: AAH78171.1.
    CCDSiCCDS32491.1.
    RefSeqiNP_061848.2. NM_018975.3.
    UniGeneiHs.301419.

    Genome annotation databases

    EnsembliENST00000300086; ENSP00000300086; ENSG00000166848.
    GeneIDi54386.
    KEGGihsa:54386.
    UCSCiuc002fet.2. human.

    Polymorphism databases

    DMDMi21542267.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF262988 mRNA. Translation: AAF72711.1 .
    AF250393 mRNA. Translation: AAQ14259.1 .
    AF289599 mRNA. Translation: AAL55783.1 . Frameshift.
    AK000669 mRNA. Translation: BAA91317.1 . Sequence problems.
    AK298880 mRNA. Translation: BAG60996.1 . Different initiation.
    AC025287 Genomic DNA. No translation available.
    CH471114 Genomic DNA. Translation: EAW95616.1 .
    CH471114 Genomic DNA. Translation: EAW95618.1 .
    BC004465 mRNA. Translation: AAH04465.1 .
    BC005841 mRNA. Translation: AAH05841.1 .
    BC022428 mRNA. Translation: AAH22428.1 .
    BC078171 mRNA. Translation: AAH78171.1 .
    CCDSi CCDS32491.1.
    RefSeqi NP_061848.2. NM_018975.3.
    UniGenei Hs.301419.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FEX NMR - A 132-190 [» ]
    3K6G X-ray 1.95 A/B/C 303-399 [» ]
    ProteinModelPortali Q9NYB0.
    SMRi Q9NYB0. Positions 132-190, 306-398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119942. 143 interactions.
    DIPi DIP-34868N.
    IntActi Q9NYB0. 17 interactions.
    MINTi MINT-1454139.
    STRINGi 9606.ENSP00000300086.

    PTM databases

    PhosphoSitei Q9NYB0.

    Polymorphism databases

    DMDMi 21542267.

    Proteomic databases

    MaxQBi Q9NYB0.
    PaxDbi Q9NYB0.
    PeptideAtlasi Q9NYB0.
    PRIDEi Q9NYB0.

    Protocols and materials databases

    DNASUi 54386.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300086 ; ENSP00000300086 ; ENSG00000166848 .
    GeneIDi 54386.
    KEGGi hsa:54386.
    UCSCi uc002fet.2. human.

    Organism-specific databases

    CTDi 54386.
    GeneCardsi GC16P075681.
    HGNCi HGNC:19246. TERF2IP.
    HPAi CAB018660.
    CAB018749.
    HPA006719.
    MIMi 605061. gene.
    neXtProti NX_Q9NYB0.
    PharmGKBi PA134976325.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39788.
    HOGENOMi HOG000120115.
    HOVERGENi HBG054209.
    InParanoidi Q9NYB0.
    KOi K11113.
    OMAi SISFYVR.
    OrthoDBi EOG7KDFBG.
    PhylomeDBi Q9NYB0.
    TreeFami TF332348.

    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 TERF2IP. human.
    EvolutionaryTracei Q9NYB0.
    GeneWikii TERF2IP.
    GenomeRNAii 54386.
    NextBioi 56609.
    PROi Q9NYB0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NYB0.
    Bgeei Q9NYB0.
    CleanExi HS_TERF2IP.
    Genevestigatori Q9NYB0.

    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. "Identification of human RAP1: implications for telomere evolution."
      Li B., Oestreich S., de Lange T.
      Cell 101:471-483(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cervix carcinoma.
    2. "Cloning and characterization of DRIP5, a new protein that specifically interacts with the D1 dopamine receptor."
      Lafuente M.J., Nasir J.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Ileal mucosa and Teratocarcinoma.
    5. "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].
    6. 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].
      Tissue: Colon, Lung and Skin.
    8. "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.
    9. "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.
    10. "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.
    11. "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.
    12. "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-156 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-154 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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].
    16. "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.
    17. "Human RAP1 inhibits non-homologous end joining at telomeres."
      Sarthy J., Bae N.S., Scrafford J., Baumann P.
      EMBO J. 28:3390-3399(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "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-154 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "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-36; SER-154 AND SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "NMR structure of the hRap1 Myb motif reveals a canonical three-helix bundle lacking the positive surface charge typical of Myb DNA-binding domains."
      Hanaoka S., Nagadoi A., Yoshimura S., Aimoto S., Li B., de Lange T., Nishimura Y.
      J. Mol. Biol. 312:167-175(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 132-190.

    Entry informationi

    Entry nameiTE2IP_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYB0
    Secondary accession number(s): B4DQN4
    , Q4W4Y2, Q8WYZ3, Q9NWR2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 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

    Miscellaneous

    Shares a bidirectional promoter with KARS.1 Publication

    Caution

    Was reported to participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair in the absence of TERF2 (PubMed:19763083). However, this probably does not corresponds to its primary function and experiments in mouse showed that it is dispensible for such process and is required for repressiion of homology-directed repair (HDR).1 Publication

    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