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Q9NUX5

- POTE1_HUMAN

UniProt

Q9NUX5 - POTE1_HUMAN

Protein

Protection of telomeres protein 1

Gene

POT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. Is a component of the double-stranded telomeric DNA-binding TRF1 complex which is involved in the regulation of telomere length by cis-inhibition of telomerase. Also acts as a single-stranded telomeric DNA-binding protein and thus may act as a downstream effector of the TRF1 complex and may transduce information about telomere maintenance and/or length to the telomere terminus. 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. Binds to two or more telomeric single-stranded 5'-TTAGGG-3' repeats (G-strand) and with high specificity to a minimal telomeric single-stranded 5'-TAGGGTTAG-3' sequence. Binds telomeric single-stranded sequences internally or at proximity of a 3'-end. Its activity is TERT dependent but it does not increase TERT activity by itself. In contrast, the ACD-POT1 heterodimer enhances telomere elongation by increasing telomerase processivity.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei243 – 2431DNA binding

    GO - Molecular functioni

    1. DEAD/H-box RNA helicase binding Source: BHF-UCL
    2. protein binding Source: IntAct
    3. single-stranded telomeric DNA binding Source: UniProtKB
    4. telomerase inhibitor activity Source: BHF-UCL

    GO - Biological processi

    1. DNA duplex unwinding Source: BHF-UCL
    2. negative regulation of telomerase activity Source: BHF-UCL
    3. negative regulation of telomere maintenance via telomerase Source: BHF-UCL
    4. positive regulation of DNA strand elongation Source: BHF-UCL
    5. positive regulation of helicase activity Source: BHF-UCL
    6. positive regulation of telomerase activity Source: BHF-UCL
    7. positive regulation of telomere maintenance via telomerase Source: BHF-UCL
    8. telomere capping Source: BHF-UCL
    9. telomere formation via telomerase Source: BHF-UCL
    10. telomere maintenance Source: Reactome
    11. telomere maintenance via telomerase Source: UniProtKB

    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:
    Protection of telomeres protein 1
    Short name:
    hPot1
    Alternative name(s):
    POT1-like telomere end-binding protein
    Gene namesi
    Name:POT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:17284. POT1.

    Subcellular locationi

    Nucleus 1 Publication. Chromosometelomere 1 Publication
    Note: Colocalizes with telomeric DNA.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti67038. B-cell chronic lymphocytic leukemia.
    PharmGKBiPA134934904.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 634634Protection of telomeres protein 1PRO_0000121728Add
    BLAST

    Proteomic databases

    MaxQBiQ9NUX5.
    PaxDbiQ9NUX5.
    PRIDEiQ9NUX5.

    PTM databases

    PhosphoSiteiQ9NUX5.

    Expressioni

    Tissue specificityi

    Ubiquitous.2 Publications

    Gene expression databases

    ArrayExpressiQ9NUX5.
    BgeeiQ9NUX5.
    CleanExiHS_POT1.
    GenevestigatoriQ9NUX5.

    Organism-specific databases

    HPAiHPA051625.

    Interactioni

    Subunit structurei

    Homodimer or homooligomer. Component of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2, TERF2IP, ACD and POT1. Binds single-stranded telomeric DNA as a monomer By similarity. Component of the telomerase holoenzyme complex at least composed of TERT, DKC1, WRAP53/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). Found in a complex with TERF1, TINF2 and TNKS1. Interacts with TNKS1. Forms heterodimers with ACD. Identified in a complex with ACD and single-stranded telomeric DNA.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACDQ96AP03EBI-752420,EBI-717666
    TERF2Q155543EBI-752420,EBI-706637

    Protein-protein interaction databases

    BioGridi117417. 204 interactions.
    DIPiDIP-29610N.
    IntActiQ9NUX5. 28 interactions.
    MINTiMINT-1466135.
    STRINGi9606.ENSP00000350249.

    Structurei

    Secondary structure

    1
    634
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 163
    Beta strandi19 – 3719
    Beta strandi39 – 5012
    Beta strandi56 – 6510
    Helixi66 – 683
    Beta strandi78 – 8912
    Beta strandi92 – 10615
    Helixi127 – 14317
    Helixi153 – 1553
    Beta strandi161 – 17313
    Beta strandi175 – 18410
    Turni200 – 2023
    Helixi207 – 2137
    Helixi214 – 2163
    Beta strandi217 – 2237
    Helixi226 – 2327
    Beta strandi238 – 25114
    Beta strandi257 – 2659
    Helixi270 – 2723
    Beta strandi274 – 2785
    Helixi283 – 29715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XJVX-ray1.73A6-299[»]
    3KJOX-ray1.80A1-299[»]
    3KJPX-ray1.80A1-299[»]
    ProteinModelPortaliQ9NUX5.
    SMRiQ9NUX5. Positions 6-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NUX5.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni33 – 4816DNA bindingAdd
    BLAST
    Regioni270 – 2734DNA binding

    Sequence similaritiesi

    Belongs to the telombin family.Curated

    Phylogenomic databases

    eggNOGiNOG284004.
    HOGENOMiHOG000015271.
    HOVERGENiHBG053641.
    InParanoidiQ9NUX5.
    KOiK11109.
    OMAiDKTSWIP.
    OrthoDBiEOG7N0C4C.
    PhylomeDBiQ9NUX5.
    TreeFamiTF328398.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR028389. POT1.
    IPR011564. Telomer_end-bd_POT1/Cdc13.
    [Graphical view]
    PANTHERiPTHR14513. PTHR14513. 1 hit.
    PfamiPF02765. POT1. 1 hit.
    [Graphical view]
    SMARTiSM00976. Telo_bind. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 2 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: A number of isoforms are produced.

    Isoform 1 (identifier: Q9NUX5-1) [UniParc]FASTAAdd to Basket

    Also known as: Variant 1

    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

    MSLVPATNYI YTPLNQLKGG TIVNVYGVVK FFKPPYLSKG TDYCSVVTIV    50
    DQTNVKLTCL LFSGNYEALP IIYKNGDIVR FHRLKIQVYK KETQGITSSG 100
    FASLTFEGTL GAPIIPRTSS KYFNFTTEDH KMVEALRVWA STHMSPSWTL 150
    LKLCDVQPMQ YFDLTCQLLG KAEVDGASFL LKVWDGTRTP FPSWRVLIQD 200
    LVLEGDLSHI HRLQNLTIDI LVYDNHVHVA RSLKVGSFLR IYSLHTKLQS 250
    MNSENQTMLS LEFHLHGGTS YGRGIRVLPE SNSDVDQLKK DLESANLTAN 300
    QHSDVICQSE PDDSFPSSGS VSLYEVERCQ QLSATILTDH QYLERTPLCA 350
    ILKQKAPQQY RIRAKLRSYK PRRLFQSVKL HCPKCHLLQE VPHEGDLDII 400
    FQDGATKTPD VKLQNTSLYD SKIWTTKNQK GRKVAVHFVK NNGILPLSNE 450
    CLLLIEGGTL SEICKLSNKF NSVIPVRSGH EDLELLDLSA PFLIQGTIHH 500
    YGCKQCSSLR SIQNLNSLVD KTSWIPSSVA EALGIVPLQY VFVMTFTLDD 550
    GTGVLEAYLM DSDKFFQIPA SEVLMDDDLQ KSVDMIMDMF CPPGIKIDAY 600
    PWLECFIKSY NVTNGTDNQI CYQIFDTTVA EDVI 634
    Length:634
    Mass (Da):71,442
    Last modified:October 1, 2000 - v1
    Checksum:i123A12CABE708C91
    GO
    Isoform 2 (identifier: Q9NUX5-2) [UniParc]FASTAAdd to Basket

    Also known as: Variant 3

    The sequence of this isoform differs from the canonical sequence as follows:
         532-538: ALGIVPL → DVNSVLV
         539-634: Missing.

    Show »
    Length:538
    Mass (Da):60,534
    Checksum:i7D04F3ECC01D448D
    GO

    Sequence cautioni

    The sequence BAB15404.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti410 – 4101D → V in BAA91568. (PubMed:14702039)Curated
    Sequence conflicti412 – 4121K → Q in BAB15404. (PubMed:14702039)Curated
    Sequence conflicti499 – 4991H → D in CAB43281. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti529 – 5291V → M.
    Corresponds to variant rs34973253 [ dbSNP | Ensembl ].
    VAR_034393

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei532 – 5387ALGIVPL → DVNSVLV in isoform 2. CuratedVSP_010846
    Alternative sequencei539 – 63496Missing in isoform 2. CuratedVSP_010847Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY823520 mRNA. Translation: AAW22613.1.
    AK001230 mRNA. Translation: BAA91568.1.
    AK001935 mRNA. Translation: BAA91988.1.
    AK022580 mRNA. Translation: BAB14110.1.
    AK026234 mRNA. Translation: BAB15404.1. Different initiation.
    AC004925 Genomic DNA. Translation: AAD08852.1.
    AC096665 Genomic DNA. No translation available.
    AC110791 Genomic DNA. No translation available.
    CH471070 Genomic DNA. Translation: EAW83616.1.
    BC002923 mRNA. Translation: AAH02923.1.
    AL050120 mRNA. Translation: CAB43281.1.
    CCDSiCCDS5793.1. [Q9NUX5-1]
    PIRiT08766.
    RefSeqiNP_001036059.1. NM_001042594.1.
    NP_056265.2. NM_015450.2. [Q9NUX5-1]
    XP_006715980.1. XM_006715917.1. [Q9NUX5-1]
    UniGeneiHs.31968.

    Genome annotation databases

    EnsembliENST00000357628; ENSP00000350249; ENSG00000128513. [Q9NUX5-1]
    GeneIDi25913.
    KEGGihsa:25913.
    UCSCiuc003vlm.3. human. [Q9NUX5-1]

    Polymorphism databases

    DMDMi50401179.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY823520 mRNA. Translation: AAW22613.1 .
    AK001230 mRNA. Translation: BAA91568.1 .
    AK001935 mRNA. Translation: BAA91988.1 .
    AK022580 mRNA. Translation: BAB14110.1 .
    AK026234 mRNA. Translation: BAB15404.1 . Different initiation.
    AC004925 Genomic DNA. Translation: AAD08852.1 .
    AC096665 Genomic DNA. No translation available.
    AC110791 Genomic DNA. No translation available.
    CH471070 Genomic DNA. Translation: EAW83616.1 .
    BC002923 mRNA. Translation: AAH02923.1 .
    AL050120 mRNA. Translation: CAB43281.1 .
    CCDSi CCDS5793.1. [Q9NUX5-1 ]
    PIRi T08766.
    RefSeqi NP_001036059.1. NM_001042594.1.
    NP_056265.2. NM_015450.2. [Q9NUX5-1 ]
    XP_006715980.1. XM_006715917.1. [Q9NUX5-1 ]
    UniGenei Hs.31968.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XJV X-ray 1.73 A 6-299 [» ]
    3KJO X-ray 1.80 A 1-299 [» ]
    3KJP X-ray 1.80 A 1-299 [» ]
    ProteinModelPortali Q9NUX5.
    SMRi Q9NUX5. Positions 6-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117417. 204 interactions.
    DIPi DIP-29610N.
    IntActi Q9NUX5. 28 interactions.
    MINTi MINT-1466135.
    STRINGi 9606.ENSP00000350249.

    Chemistry

    BindingDBi Q9NUX5.
    ChEMBLi CHEMBL5908.

    PTM databases

    PhosphoSitei Q9NUX5.

    Polymorphism databases

    DMDMi 50401179.

    Proteomic databases

    MaxQBi Q9NUX5.
    PaxDbi Q9NUX5.
    PRIDEi Q9NUX5.

    Protocols and materials databases

    DNASUi 25913.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357628 ; ENSP00000350249 ; ENSG00000128513 . [Q9NUX5-1 ]
    GeneIDi 25913.
    KEGGi hsa:25913.
    UCSCi uc003vlm.3. human. [Q9NUX5-1 ]

    Organism-specific databases

    CTDi 25913.
    GeneCardsi GC07M124462.
    HGNCi HGNC:17284. POT1.
    HPAi HPA051625.
    MIMi 606478. gene.
    neXtProti NX_Q9NUX5.
    Orphaneti 67038. B-cell chronic lymphocytic leukemia.
    PharmGKBi PA134934904.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG284004.
    HOGENOMi HOG000015271.
    HOVERGENi HBG053641.
    InParanoidi Q9NUX5.
    KOi K11109.
    OMAi DKTSWIP.
    OrthoDBi EOG7N0C4C.
    PhylomeDBi Q9NUX5.
    TreeFami TF328398.

    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 Q9NUX5.
    GeneWikii POT1.
    GenomeRNAii 25913.
    NextBioi 47408.
    PROi Q9NUX5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NUX5.
    Bgeei Q9NUX5.
    CleanExi HS_POT1.
    Genevestigatori Q9NUX5.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR028389. POT1.
    IPR011564. Telomer_end-bd_POT1/Cdc13.
    [Graphical view ]
    PANTHERi PTHR14513. PTHR14513. 1 hit.
    Pfami PF02765. POT1. 1 hit.
    [Graphical view ]
    SMARTi SM00976. Telo_bind. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Pot1, the putative telomere end-binding protein in fission yeast and humans."
      Baumann P., Cech T.R.
      Science 292:1171-1175(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SINGLE-STRANDED TELOMERE DNA-BINDING.
      Tissue: Ovary.
    2. "Human Pot1 (protection of telomeres) protein: cytolocalization, gene structure, and alternative splicing."
      Baumann P., Podell E., Cech T.R.
      Mol. Cell. Biol. 22:8079-8087(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, SINGLE-STRANDED TELOMERE DNA-BINDING.
    3. "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 1).
      Tissue: Placenta, Small intestine and Teratocarcinoma.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Skin.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 499-634 (ISOFORM 1).
      Tissue: Uterus.
    8. "Human POT1 facilitates telomere elongation by telomerase."
      Colgin L.M., Baran K., Baumann P., Cech T.R., Reddel R.R.
      Curr. Biol. 13:942-946(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TELOMERE REGULATION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SINGLE-STRANDED TELOMERE DNA-BINDING.
    9. "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: FUNCTION IN TELOMERE REGULATION, IDENTIFICATION IN A COMPLEX WITH TERF1; TINF2 AND TNKS1, INTERACTION WITH TNKS1.
    10. "DNA binding features of human POT1: a nonamer 5'-TAGGGTTAG-3' minimal binding site, sequence specificity, and internal binding to multimeric sites."
      Loayza D., Parsons H., Donigian J., Hoke K., de Lange T.
      J. Biol. Chem. 279:13241-13248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SINGLE-STRANDED TELOMERE DNA-BINDING.
    11. "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.
    12. "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.
    13. "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.
    14. "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.
    15. "The POT1-TPP1 telomere complex is a telomerase processivity factor."
      Wang F., Podell E.R., Zaug A.J., Yang Y., Baciu P., Cech T.R., Lei M.
      Nature 445:506-510(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH ACD AND SINGLE-STRANDED TELOMERIC DNA.
    16. "A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis."
      Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M., Veenstra T.D., Terns M.P., Artandi S.E.
      Science 323:644-648(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
    17. "Functional interaction between telomere protein TPP1 and telomerase."
      Zaug A.J., Podell E.R., Nandakumar J., Cech T.R.
      Genes Dev. 24:613-622(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Structure of human POT1 bound to telomeric single-stranded DNA provides a model for chromosome end-protection."
      Lei M., Podell E.R., Cech T.R.
      Nat. Struct. Mol. Biol. 11:1223-1229(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 6-299 IN COMPLEX WITH SINGLE-STRANDED TELOMERIC DNA.

    Entry informationi

    Entry nameiPOTE1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NUX5
    Secondary accession number(s): O95018
    , Q5MJ36, Q9H662, Q9NW19, Q9UG95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 135 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 7
      Human chromosome 7: 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