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Q9BSI4

- TINF2_HUMAN

UniProt

Q9BSI4 - TINF2_HUMAN

Protein

TERF1-interacting nuclear factor 2

Gene

TINF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG 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. Plays a role in shelterin complex assembly. Isoform 1 may have additional role in tethering telomeres to the nuclear matrix.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. telomeric DNA binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of epithelial cell proliferation Source: BHF-UCL
    2. negative regulation of protein ADP-ribosylation Source: BHF-UCL
    3. negative regulation of telomere maintenance via telomerase Source: BHF-UCL
    4. positive regulation of telomere maintenance Source: BHF-UCL
    5. protein localization to chromosome Source: BHF-UCL
    6. protein localization to chromosome, telomeric region Source: BHF-UCL
    7. telomere assembly Source: BHF-UCL
    8. telomere maintenance Source: Reactome
    9. telomere maintenance via telomere lengthening Source: BHF-UCL

    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:
    TERF1-interacting nuclear factor 2
    Alternative name(s):
    TRF1-interacting nuclear protein 2
    Gene namesi
    Name:TINF2
    Synonyms:TIN2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:11824. TINF2.

    Subcellular locationi

    Nucleus 1 Publication. Chromosometelomere 1 Publication
    Note: Associated with telomeres.
    Isoform 1 : Nucleus matrix 1 Publication

    GO - Cellular componenti

    1. chromosome, telomeric region Source: BHF-UCL
    2. nuclear matrix Source: UniProtKB-SubCell
    3. nuclear telomere cap complex Source: BHF-UCL
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA
    6. perinucleolar chromocenter Source: BHF-UCL

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    Pathology & Biotechi

    Involvement in diseasei

    Dyskeratosis congenita, autosomal dominant, 3 (DKCA3) [MIM:613990]: A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti280 – 2801K → E in DKCA3. 1 Publication
    VAR_043914
    Natural varianti282 – 2821R → H in DKCA3 and DKCA5. 1 Publication
    VAR_043915
    Natural varianti282 – 2821R → S in DKCA3. 1 Publication
    VAR_043916
    Dyskeratosis congenita, autosomal dominant, 5 (DKCA5) [MIM:268130]: A disease characterized by bone marrow hypoplasia, nail dystrophy, fine sparse hair, fine reticulate skin pigmentation, oral leukoplakia, bilateral exudative retinopathy, cerebellar hypoplasia, and growth retardation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti282 – 2821R → H in DKCA3 and DKCA5. 1 Publication
    VAR_043915

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi258 – 2581F → A: Abolishes interaction with TERF1. 1 Publication
    Mutagenesisi262 – 2621P → A: Does not effect interaction with TERF1. 1 Publication

    Keywords - Diseasei

    Disease mutation, Dyskeratosis congenita

    Organism-specific databases

    MIMi268130. phenotype.
    613990. phenotype.
    Orphaneti1775. Dyskeratosis congenita.
    3322. Hoyeraal-Hreidarsson syndrome.
    3088. Retinopathy - anemia- central nervous system anomalies.
    PharmGKBiPA36530.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 451450TERF1-interacting nuclear factor 2PRO_0000072541Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei295 – 2951Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BSI4.
    PaxDbiQ9BSI4.
    PRIDEiQ9BSI4.

    PTM databases

    PhosphoSiteiQ9BSI4.

    Expressioni

    Tissue specificityi

    Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

    Gene expression databases

    ArrayExpressiQ9BSI4.
    BgeeiQ9BSI4.
    CleanExiHS_TINF2.
    GenevestigatoriQ9BSI4.

    Organism-specific databases

    HPAiHPA059061.

    Interactioni

    Subunit structurei

    Monomer. Found in a complex with POT1; TERF1 and TNKS1. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with TERF1, TERF2 and ACD.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACDQ96AP05EBI-717418,EBI-717666
    TERF2Q155544EBI-717418,EBI-706637
    TERF2IPQ9NYB03EBI-717418,EBI-750109

    Protein-protein interaction databases

    BioGridi117660. 93 interactions.
    DIPiDIP-29413N.
    IntActiQ9BSI4. 10 interactions.
    MINTiMINT-221357.
    STRINGi9606.ENSP00000267415.

    Structurei

    Secondary structure

    1
    451
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi263 – 2653

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BQOX-ray2.00B257-276[»]
    3BU8X-ray2.15C/D258-275[»]
    ProteinModelPortaliQ9BSI4.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BSI4.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi256 – 27823TBMAdd
    BLAST
    Motifi262 – 2687Nuclear localization signalSequence Analysis

    Domaini

    The TBM domain mediates interaction with TERF1.1 Publication

    Phylogenomic databases

    eggNOGiNOG43106.
    HOGENOMiHOG000247003.
    HOVERGENiHBG057120.
    InParanoidiQ9BSI4.
    KOiK11112.
    OMAiGRPWAQV.
    PhylomeDBiQ9BSI4.
    TreeFamiTF334731.

    Family and domain databases

    InterProiIPR029400. TINF2_N.
    [Graphical view]
    PfamiPF14973. TINF2_N. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q9BSI4-1) [UniParc]FASTAAdd to Basket

    Also known as: TIN2L

    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

    MATPLVAGPA ALRFAAAASW QVVRGRCVEH FPRVLEFLRS LRAVAPGLVR    50
    YRHHERLCMG LKAKVVVELI LQGRPWAQVL KALNHHFPES GPIVRDPKAT 100
    KQDLRKILEA QETFYQQVKQ LSEAPVDLAS KLQELEQEYG EPFLAAMEKL 150
    LFEYLCQLEK ALPTPQAQQL QDVLSWMQPG VSITSSLAWR QYGVDMGWLL 200
    PECSVTDSVN LAEPMEQNPP QQQRLALHNP LPKAKPGTHL PQGPSSRTHP 250
    EPLAGRHFNL APLGRRRVQS QWASTRGGHK ERPTVMLFPF RNLGSPTQVI 300
    SKPESKEEHA IYTADLAMGT RAASTGKSKS PCQTLGGRAL KENPVDLPAT 350
    EQKENCLDCY MDPLRLSLLP PRARKPVCPP SLCSSVITIG DLVLDSDEEE 400
    NGQGEGKESL ENYQKTKFDT LIPTLCEYLP PSGHGAIPVS SCDCRDSSRP 450
    L 451
    Length:451
    Mass (Da):50,023
    Last modified:June 1, 2001 - v1
    Checksum:iE5A7FD11CE523979
    GO
    Isoform 2 (identifier: Q9BSI4-2) [UniParc]FASTAAdd to Basket

    Also known as: TIN2S

    The sequence of this isoform differs from the canonical sequence as follows:
         355-451: Missing.

    Show »
    Length:354
    Mass (Da):39,444
    Checksum:i903B69D7B6A15C01
    GO
    Isoform 3 (identifier: Q9BSI4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         134-137: ELEQ → VRLV
         138-451: Missing.

    Show »
    Length:137
    Mass (Da):15,434
    Checksum:i3BA7286B15EAC870
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441V → I in BAB14440. (PubMed:14702039)Curated
    Sequence conflicti67 – 671Missing in BAB14440. (PubMed:14702039)Curated
    Sequence conflicti302 – 3021K → N in AAF18439. (PubMed:10581025)Curated
    Sequence conflicti323 – 33210ASTGKSKSPC → PSNGKYKGPY in AAF18439. (PubMed:10581025)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431A → T.
    Corresponds to variant rs35653076 [ dbSNP | Ensembl ].
    VAR_051423
    Natural varianti237 – 2371G → D.
    Corresponds to variant rs17102313 [ dbSNP | Ensembl ].
    VAR_051424
    Natural varianti241 – 2411P → S.
    Corresponds to variant rs17102311 [ dbSNP | Ensembl ].
    VAR_051425
    Natural varianti280 – 2801K → E in DKCA3. 1 Publication
    VAR_043914
    Natural varianti282 – 2821R → H in DKCA3 and DKCA5. 1 Publication
    VAR_043915
    Natural varianti282 – 2821R → S in DKCA3. 1 Publication
    VAR_043916

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei134 – 1374ELEQ → VRLV in isoform 3. 1 PublicationVSP_003987
    Alternative sequencei138 – 451314Missing in isoform 3. 1 PublicationVSP_003988Add
    BLAST
    Alternative sequencei355 – 45197Missing in isoform 2. 1 PublicationVSP_003989Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF195512 mRNA. Translation: AAF18439.1.
    AK023166 mRNA. Translation: BAB14440.1.
    BC005030 mRNA. Translation: AAH05030.1.
    BC019343 mRNA. Translation: AAH19343.1.
    EU851975 mRNA. Translation: ACF17559.1.
    CCDSiCCDS41936.1. [Q9BSI4-1]
    CCDS41937.1. [Q9BSI4-2]
    RefSeqiNP_001092744.1. NM_001099274.1. [Q9BSI4-1]
    NP_036593.2. NM_012461.2. [Q9BSI4-2]
    UniGeneiHs.496191.

    Genome annotation databases

    EnsembliENST00000267415; ENSP00000267415; ENSG00000092330. [Q9BSI4-1]
    ENST00000399423; ENSP00000382350; ENSG00000092330. [Q9BSI4-2]
    GeneIDi26277.
    KEGGihsa:26277.
    UCSCiuc001woa.4. human. [Q9BSI4-1]

    Polymorphism databases

    DMDMi21542262.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF195512 mRNA. Translation: AAF18439.1 .
    AK023166 mRNA. Translation: BAB14440.1 .
    BC005030 mRNA. Translation: AAH05030.1 .
    BC019343 mRNA. Translation: AAH19343.1 .
    EU851975 mRNA. Translation: ACF17559.1 .
    CCDSi CCDS41936.1. [Q9BSI4-1 ]
    CCDS41937.1. [Q9BSI4-2 ]
    RefSeqi NP_001092744.1. NM_001099274.1. [Q9BSI4-1 ]
    NP_036593.2. NM_012461.2. [Q9BSI4-2 ]
    UniGenei Hs.496191.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BQO X-ray 2.00 B 257-276 [» ]
    3BU8 X-ray 2.15 C/D 258-275 [» ]
    ProteinModelPortali Q9BSI4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117660. 93 interactions.
    DIPi DIP-29413N.
    IntActi Q9BSI4. 10 interactions.
    MINTi MINT-221357.
    STRINGi 9606.ENSP00000267415.

    PTM databases

    PhosphoSitei Q9BSI4.

    Polymorphism databases

    DMDMi 21542262.

    Proteomic databases

    MaxQBi Q9BSI4.
    PaxDbi Q9BSI4.
    PRIDEi Q9BSI4.

    Protocols and materials databases

    DNASUi 26277.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267415 ; ENSP00000267415 ; ENSG00000092330 . [Q9BSI4-1 ]
    ENST00000399423 ; ENSP00000382350 ; ENSG00000092330 . [Q9BSI4-2 ]
    GeneIDi 26277.
    KEGGi hsa:26277.
    UCSCi uc001woa.4. human. [Q9BSI4-1 ]

    Organism-specific databases

    CTDi 26277.
    GeneCardsi GC14M024708.
    GeneReviewsi TINF2.
    HGNCi HGNC:11824. TINF2.
    HPAi HPA059061.
    MIMi 268130. phenotype.
    604319. gene.
    613990. phenotype.
    neXtProti NX_Q9BSI4.
    Orphaneti 1775. Dyskeratosis congenita.
    3322. Hoyeraal-Hreidarsson syndrome.
    3088. Retinopathy - anemia- central nervous system anomalies.
    PharmGKBi PA36530.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43106.
    HOGENOMi HOG000247003.
    HOVERGENi HBG057120.
    InParanoidi Q9BSI4.
    KOi K11112.
    OMAi GRPWAQV.
    PhylomeDBi Q9BSI4.
    TreeFami TF334731.

    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

    EvolutionaryTracei Q9BSI4.
    GeneWikii TINF2.
    GenomeRNAii 26277.
    NextBioi 35470863.
    PROi Q9BSI4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BSI4.
    Bgeei Q9BSI4.
    CleanExi HS_TINF2.
    Genevestigatori Q9BSI4.

    Family and domain databases

    InterProi IPR029400. TINF2_N.
    [Graphical view ]
    Pfami PF14973. TINF2_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "TIN2, a new regulator of telomere length in human cells."
      Kim S.-H., Kaminker P., Campisi J.
      Nat. Genet. 23:405-412(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Fibroblast.
    2. "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] (ISOFORM 3).
      Tissue: Teratocarcinoma.
    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] (ISOFORM 1).
      Tissue: Placenta and Uterus.
    4. "A novel form of telomere-associated TIN2 localizes to the nuclear matrix."
      Kaminker P.G., Kim S.-H., Desprez P.Y., Campisi J.
      Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 163-451 (ISOFORM 1).
    5. "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; TERF1 AND TNKS1.
    6. "POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex."
      Ye J.Z.-S., Hockemeyer D., Krutchinsky A.N., Loayza D., Hooper S.M., Chait B.T., de Lange T.
      Genes Dev. 18:1649-1654(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACD.
    7. "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.
    8. "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.
    9. "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.
    10. "A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly."
      O'Connor M.S., Safari A., Xin H., Liu D., Songyang Z.
      Proc. Natl. Acad. Sci. U.S.A. 103:11874-11879(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SHELTERIN COMPLEX ASSEMBLY.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "The long and short of it: a new isoform of TIN2 in the nuclear matrix."
      Smith S.
      Cell Cycle 8:797-798(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION.
    13. "A novel form of the telomere-associated protein TIN2 localizes to the nuclear matrix."
      Kaminker P.G., Kim S.H., Desprez P.Y., Campisi J.
      Cell Cycle 8:931-939(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1).
    14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    17. "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 258-275 IN COMPLEX WITH TERF1 OR TERF2, DOMAIN TBM, MUTAGENESIS OF PHE-258 AND PRO-262.
    18. "TINF2, a component of the shelterin telomere protection complex, is mutated in dyskeratosis congenita."
      Savage S.A., Giri N., Baerlocher G.M., Orr N., Lansdorp P.M., Alter B.P.
      Am. J. Hum. Genet. 82:501-509(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DKCA3 GLU-280; HIS-282 AND SER-282, VARIANT DKCA5 HIS-282.

    Entry informationi

    Entry nameiTINF2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BSI4
    Secondary accession number(s): B3W5Q7, Q9H904, Q9UHC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 124 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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

    External Data

    Dasty 3