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Q673L6

- TERT_RAT

UniProt

Q673L6 - TERT_RAT

Protein

Telomerase reverse transcriptase

Gene

Tert

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis By similarity.By similarity

    Catalytic activityi

    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei169 – 1691Required for optimal binding of telomeric ssDNA and incorporation of nucleotides at the second position of the templateBy similarity
    Metal bindingi702 – 7021Magnesium; catalyticPROSITE-ProRule annotation
    Sitei860 – 8601Required for nucleotide incorporation and primer extension rateBy similarity
    Metal bindingi861 – 8611Magnesium; catalyticPROSITE-ProRule annotation
    Metal bindingi862 – 8621Magnesium; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. telomeric RNA binding Source: Ensembl
    4. telomeric template RNA reverse transcriptase activity Source: RGD

    GO - Biological processi

    1. DNA strand elongation Source: Ensembl
    2. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    3. replicative senescence Source: Ensembl
    4. telomere formation via telomerase Source: Ensembl
    5. telomere maintenance via telomerase Source: Ensembl

    Keywords - Molecular functioni

    Nucleotidyltransferase, Ribonucleoprotein, RNA-directed DNA polymerase, Transferase

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_225711. Telomere Extension By Telomerase.
    REACT_226234. formation of the beta-catenin:TCF transactivating complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Telomerase reverse transcriptase (EC:2.7.7.49)
    Alternative name(s):
    Telomerase catalytic subunit
    Gene namesi
    Name:TertImported
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi70494. Tert.

    Subcellular locationi

    Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity. Nucleus Curated. Chromosometelomere. Cytoplasm By similarity. NucleusPML body By similarity
    Note: Shuttling between nuclear and cytoplasm depends on cell cycle, phosphorylation states, transformation and DNA damage. Diffuse localization in the nucleoplasm. Enriched in nucleoli of certain cell types. Translocated to the cytoplasm via nuclear pores in a CRM1/RAN-dependent manner involving oxidative stress-mediated phosphorylation at Tyr-697. Dephosphorylation at this site by SHP2 retains TERT in the nucleus. Translocated to the nucleus by phosphorylation by AKT By similarity.By similarity

    GO - Cellular componenti

    1. chromosome, telomeric region Source: UniProtKB-SubCell
    2. cytoplasm Source: RGD
    3. nucleolus Source: UniProtKB-SubCell
    4. nucleus Source: RGD
    5. PML body Source: UniProtKB-SubCell
    6. telomerase holoenzyme complex Source: Ensembl

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus, Telomere

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11251125Telomerase reverse transcriptasePRO_0000245165Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei447 – 4471Phosphoserine; by DYRK2By similarity
    Modified residuei697 – 6971Phosphotyrosine; by SRC-type Tyr-kinasesBy similarity

    Post-translational modificationi

    Phosphorylation at Tyr-697 under oxidative stress leads to translocation of TERT to the cytoplasm and reduces its antiapoptotic activity. Dephosphorylated by SHP2/PTPN11 leading to nuclear retention. Phosphorylation at the G2/M phase at Ser-447 by DYRK2 promotes ubiquitination by the EDVP complex and degradation By similarity.By similarity
    Ubiquitinated by the EDVP complex, a E3 ligase complex following phosphorylation at Ser-447 by DYRK2. Ubiquitinated leads to proteasomal degradation By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ673L6.
    PRIDEiQ673L6.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 expressed in thymus, liver, spleen, lung, kidney and testis. High level of inactive isoform 3 in adult hippocampus, low level in heart, cortex and cerebellum.2 Publications

    Developmental stagei

    High activity in cortex at embryonic stage 16 and postnatal day 2. Low activity in cortex from postnatal day 5.1 Publication

    Inductioni

    Down-regulated by TGFbeta in fibroblasts. This inhibition is mediated by SMAD3.1 Publication

    Gene expression databases

    GenevestigatoriQ673L6.

    Interactioni

    Subunit structurei

    Homodimer; dimerization is required to produce a functional complex. Oligomer; can form oligomers in the absence of the telomerase RNA template component (TERC). Catalytic subunit of the telomerase holoenzyme complex composed minimally of TERT and TERC. The telomerase complex is composed of TERT, DKC1, WDR79/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). The molecular chaperone HSP90/P23 complex is required for correct assembly and stabilization of the active telomerase. Interacts directly with HSP90A and PTGES3. Interacts with HSPA1A; the interaction occurs in the absence of TERC and dissociates once the complex has formed. Interacts with RAN; the interaction promotes nuclear export of TERT. Interacts with XPO1. Interacts with PTPN11; the interaction retains TERT in the nucleus. Interacts with NCL (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains); the interaction is important for nucleolar localization of TERT. Interacts with SMARCA4 (via the bromodomain); the interaction regulates Wnt-mediated signaling By similarity. Interacts with MCRS1 (isoform MCRS2); the interaction inhibits in vitro telomerase activity. Interacts with PIF1; the interaction has no effect on the elongation activity of TERT. Interacts with PML; the interaction recruits TERT to PML bodies and inhibits telomerase activity By similarity. Interacts with GNL3L By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000022683.

    Structurei

    3D structure databases

    ProteinModelPortaliQ673L6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini595 – 928334Reverse transcriptasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 239239RNA-interacting domain 1By similarityAdd
    BLAST
    Regioni58 – 205148GQ motifBy similarityAdd
    BLAST
    Regioni137 – 1415Required for regulating specificity for telomeric DNA and for processivity for primer elongationBy similarity
    Regioni240 – 32889LinkerBy similarityAdd
    BLAST
    Regioni306 – 528223Required for oligomerizationBy similarityAdd
    BLAST
    Regioni329 – 540212RNA-interacting domain 2By similarityAdd
    BLAST
    Regioni381 – 511131QFP motifBy similarityAdd
    BLAST
    Regioni402 – 42221CP motifBy similarityAdd
    BLAST
    Regioni907 – 92115Required for oligomerizationBy similarityAdd
    BLAST
    Regioni923 – 9275Primer grip sequenceBy similarity
    Regioni929 – 1125197CTEBy similarityAdd
    BLAST

    Domaini

    The primer grip sequence in the RT domain is required for telomerase activity and for stable association with short telomeric primers.By similarity
    The RNA-interacting domain 1 (RD1)/N-terminal extension (NTE) is required for interaction with the pseudoknot-template domain of each of TERC dimers. It contains anchor sites that bind primer nucleotides upstream of the RNA-DNA hybrid and is thus an essential determinant of repeat addition processivity By similarity.By similarity
    The RNA-interacting domain 2 (RD2) is essential for both interaction with the CR4-CR5 domain of TERC and for DNA sythesis.By similarity

    Sequence similaritiesi

    Belongs to the reverse transcriptase family. Telomerase subfamily.Sequence Analysis
    Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG276584.
    GeneTreeiENSGT00390000018531.
    HOGENOMiHOG000148780.
    HOVERGENiHBG000460.
    InParanoidiQ673L6.
    KOiK11126.
    OMAiRACFYAT.
    OrthoDBiEOG744TB3.
    PhylomeDBiQ673L6.
    TreeFamiTF329048.

    Family and domain databases

    InterProiIPR000477. RT_dom.
    IPR021891. Telomerase_RBD.
    IPR003545. Telomerase_RT.
    [Graphical view]
    PfamiPF00078. RVT_1. 1 hit.
    PF12009. Telomerase_RBD. 1 hit.
    [Graphical view]
    PRINTSiPR01365. TELOMERASERT.
    SMARTiSM00975. Telomerase_RBD. 1 hit.
    [Graphical view]
    PROSITEiPS50878. RT_POL. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q673L6-1) [UniParc]FASTAAdd to Basket

    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

    MPRAPRCPAV RSLLRSRYRE VWPLATFVRR LGLEGSRLVQ PGDPKVFRTL     50
    VAQCLVCVPW GSQPPPADLS FHQVSSLKEL VSRVVQKLCE RGERNVLAFG 100
    FALLNGARGG PPMAFTTSVH SYLPNSVTES LCVSGAWMLL LSRVGDDLLV 150
    YLLSHCALYL LVPPSCAYQV CGSPLYQICA TTDTWSSVPA GYRPTRPVGG 200
    NFTNLGSAHQ IKNSGHQEAP KPQALPSRGT KRLLSLTSTN VPSAKKARFE 250
    PALRVDKGPH RQVVPTPSGK TWAPSPAASP KVPPAAKNLS LKGKASDPSL 300
    SGSVCCKHKP SSSSLLSSPP QDAEKLRPFT ETRHFLYSRG GGQEELNPSF 350
    LLNSLPPSLT GARRLVEIIF LGSRPRTSGP FCRTRRLPRR YWQMRPLFQQ 400
    LLMNHAKCQY VRFLRSHCRF RTANQRVPDA MDTSPSHLTS LLRLHSSPWQ 450
    VYGFLRACLR ELVPAGLWGT RHNERRFLKN VKKFISLGKY AKLSLQELMW 500
    RVKVEDCHWL RSSPEKDTVP AAEHRLRERI LAMFLFWLMD TYVVQLLRSF 550
    FYITETTFQK NRLFFYRKSV WSKLQSIGIR QQLERVQLRE LSQEEVKHHQ 600
    DTWLAMPICR LRFIPKLNGL RPIVNMSYGM DTRAFGKKKQ TQCFTQSLKT 650
    LFSVLNYERT KHPNLMGASV LGTSDSYRIW RTFVLRVRAL DQTPRMYFVK 700
    ADVTGAYDAI PQDKLVEIVA NIIRRSESMY CIRQYAVVQK DSQGQVHKSF 750
    RRQVSTLSDL QPYMGQFTKH LQDSDASALR NSVVIEQSIS MNETGSSLLH 800
    FFLRFVRHSV VKIDGRFYVQ CQGIPQGSSL STLLCSLCFG DMENKLFAEV 850
    QQDGLLLRFV DDFLLVTPHL AHAKAFLSTL VHGVPEYGCM INLQKTVVNF 900
    PVETGALGGA APHQLPAHCL FPWCGLLLDT RTLEVFCDYS GYGRTSIKMS 950
    LTFQGVSRAG KTMRYKLLSV LRLKCHGLFL DLQVNSLQTV CINIYKIFLL 1000
    QAYRFHACVI RLPFGQHVRK NHAFFLGIIS NLASCCYAIL KVKNPGVSLR 1050
    AKGAPGSFPP EATRWLCYQA FLLKLAAHSV TYKCLLGPLR TAQKQLCRKL 1100
    PEATMTLLKT AADPALSTDF QTILD 1125
    Length:1,125
    Mass (Da):126,934
    Last modified:October 11, 2004 - v1
    Checksum:iB8B2A11C914372DF
    GO
    Isoform 21 Publication (identifier: Q673L6-2) [UniParc]FASTAAdd to Basket

    Also known as: a1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         641-646: Missing.

    Show »
    Length:1,119
    Mass (Da):126,225
    Checksum:i4CABB74D64E3F972
    GO
    Isoform 31 Publication (identifier: Q673L6-3) [UniParc]FASTAAdd to Basket

    Also known as: b1 Publication

    , c1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         515-615: EKDTVPAAEH...MPICRLRFIP → ACTSFWDSPS...VPEEPPFLLP
         616-1125: Missing.

    Note: Inactive form.

    Show »
    Length:615
    Mass (Da):68,614
    Checksum:i2892840D86620B63
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti521 – 5211A → V in DAA01427. (PubMed:15057822)Curated
    Sequence conflicti528 – 5281E → V in DAA01427. (PubMed:15057822)Curated
    Sequence conflicti550 – 5512FF → LL in DAA01427. (PubMed:15057822)Curated
    Sequence conflicti583 – 5831L → P in DAA01427. (PubMed:15057822)Curated
    Sequence conflicti630 – 6301M → L in DAA01427. (PubMed:15057822)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei515 – 615101EKDTV…LRFIP → ACTSFWDSPSPSQVSFIFIT AGKPSFPWIRRPLRYLETHR VELTHPAWQEGHCPCRRAPS EGEDPCHVPVLANGHICGTA AEVILLHHRDHVPEEPPFLL P in isoform 3. 1 PublicationVSP_052081Add
    BLAST
    Alternative sequencei616 – 1125510Missing in isoform 3. 1 PublicationVSP_052082Add
    BLAST
    Alternative sequencei641 – 6466Missing in isoform 2. 1 PublicationVSP_052083

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY539717 mRNA. Translation: AAT09124.1.
    AY539718 mRNA. Translation: AAT09125.1.
    AY539719 mRNA. Translation: AAT09126.1.
    AY539720 mRNA. Translation: AAT09127.1.
    AC123569 Genomic DNA. No translation available.
    DQ021473 Genomic DNA. Translation: AAY40300.1.
    AJ440965 mRNA. Translation: CAD29524.1.
    AJ440966 Genomic DNA. Translation: CAD29525.2.
    BK000660 mRNA. Translation: DAA01427.1.
    RefSeqiNP_445875.1. NM_053423.1. [Q673L6-1]
    UniGeneiRn.48802.

    Genome annotation databases

    EnsembliENSRNOT00000022683; ENSRNOP00000022683; ENSRNOG00000025327. [Q673L6-1]
    ENSRNOT00000034937; ENSRNOP00000033885; ENSRNOG00000025327. [Q673L6-3]
    GeneIDi301965.
    KEGGirno:301965.
    UCSCiRGD:70494. rat. [Q673L6-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY539717 mRNA. Translation: AAT09124.1 .
    AY539718 mRNA. Translation: AAT09125.1 .
    AY539719 mRNA. Translation: AAT09126.1 .
    AY539720 mRNA. Translation: AAT09127.1 .
    AC123569 Genomic DNA. No translation available.
    DQ021473 Genomic DNA. Translation: AAY40300.1 .
    AJ440965 mRNA. Translation: CAD29524.1 .
    AJ440966 Genomic DNA. Translation: CAD29525.2 .
    BK000660 mRNA. Translation: DAA01427.1 .
    RefSeqi NP_445875.1. NM_053423.1. [Q673L6-1 ]
    UniGenei Rn.48802.

    3D structure databases

    ProteinModelPortali Q673L6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000022683.

    Proteomic databases

    PaxDbi Q673L6.
    PRIDEi Q673L6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000022683 ; ENSRNOP00000022683 ; ENSRNOG00000025327 . [Q673L6-1 ]
    ENSRNOT00000034937 ; ENSRNOP00000033885 ; ENSRNOG00000025327 . [Q673L6-3 ]
    GeneIDi 301965.
    KEGGi rno:301965.
    UCSCi RGD:70494. rat. [Q673L6-1 ]

    Organism-specific databases

    CTDi 7015.
    RGDi 70494. Tert.

    Phylogenomic databases

    eggNOGi NOG276584.
    GeneTreei ENSGT00390000018531.
    HOGENOMi HOG000148780.
    HOVERGENi HBG000460.
    InParanoidi Q673L6.
    KOi K11126.
    OMAi RACFYAT.
    OrthoDBi EOG744TB3.
    PhylomeDBi Q673L6.
    TreeFami TF329048.

    Enzyme and pathway databases

    Reactomei REACT_225711. Telomere Extension By Telomerase.
    REACT_226234. formation of the beta-catenin:TCF transactivating complex.

    Miscellaneous databases

    NextBioi 649227.
    PROi Q673L6.

    Gene expression databases

    Genevestigatori Q673L6.

    Family and domain databases

    InterProi IPR000477. RT_dom.
    IPR021891. Telomerase_RBD.
    IPR003545. Telomerase_RT.
    [Graphical view ]
    Pfami PF00078. RVT_1. 1 hit.
    PF12009. Telomerase_RBD. 1 hit.
    [Graphical view ]
    PRINTSi PR01365. TELOMERASERT.
    SMARTi SM00975. Telomerase_RBD. 1 hit.
    [Graphical view ]
    PROSITEi PS50878. RT_POL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Predominant expression of rTERTb, an inactive TERT variant, in the adult rat brain."
      Kaneko R., Esumi S., Yagi T., Hirabayashi T.
      Protein Pept. Lett. 13:59-65(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: Brown NorwayImported.
    2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway1 Publication.
    3. "Role of Smad3 in the regulation of rat telomerase reverse transcriptase by TGFbeta."
      Hu B., Tack D.C., Liu T., Wu Z., Ullenbruch M.R., Phan S.H.
      Oncogene 25:1030-1041(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58, INDUCTION.
    4. "Detection and quantification of transcripts for the catalytic subunit TERT and the RNA component of telomerase in rat tissue."
      Holzmann K., Berger W., Mejri D., Cerni C., Sasgary S.
      Anal. Biochem. 317:120-123(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 46-161, TISSUE SPECIFICITY.
      Strain: FischerImported.
    5. "The identification and characterization of rat telomerase catalytic subunit rTERT mRNA from rat genomic sequence."
      Kim M.H., Choi C.
      Chonnam Med. J. 41:1-13(2005)
      Cited for: IDENTIFICATION.
      Strain: Brown Norway.

    Entry informationi

    Entry nameiTERT_RAT
    AccessioniPrimary (citable) accession number: Q673L6
    Secondary accession number(s): Q1LZ57
    , Q4U0V7, Q673L3, Q673L5, Q80SU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 80 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3