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Telomerase reverse transcriptase (EC 2.7.7.49) (HEST2) (Telomerase catalytic subunit) (Telomerase-associated protein 2) (TP2)

 TERT_HUMAN              Reviewed;        1132 AA.
O14746; O14783; Q2XS35; Q8N6C3; Q8NG38; Q8NG46;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 171.
RecName: Full=Telomerase reverse transcriptase;
EC=2.7.7.49;
AltName: Full=HEST2;
AltName: Full=Telomerase catalytic subunit;
AltName: Full=Telomerase-associated protein 2;
Short=TP2;
Name=TERT; Synonyms=EST2, TCS1, TRT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9288757; DOI=10.1016/S0092-8674(00)80538-3;
Meyerson M., Counter C.M., Eaton E.N., Ellisen L.W., Steiner P.,
Caddle S.D., Ziaugra L., Beijersbergen R.L., Davidoff M.J., Liu Q.,
Bacchetti S., Haber D.A., Weinberg R.A.;
"hEST2, the putative human telomerase catalytic subunit gene, is up-
regulated in tumor cells and during immortalization.";
Cell 90:785-795(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Embryonic kidney;
PubMed=9252327; DOI=10.1126/science.277.5328.955;
Nakamura T.M., Morin G.B., Chapman K.B., Weinrich S.L., Andrews W.H.,
Lingner J., Harley C.B., Cech T.R.;
"Telomerase catalytic subunit homologs from fission yeast and human.";
Science 277:955-959(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10333526; DOI=10.1016/S0378-1119(99)00108-0;
Wick M., Zubov D., Hagen G.;
"Genomic organization and promoter characterization of the gene
encoding the human telomerase reverse transcriptase (hTERT).";
Gene 232:97-106(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=12869302; DOI=10.1016/S1476-5586(03)80051-9;
Hisatomi H., Ohyashiki K., Ohyashiki J.H., Nagao K., Kanamaru T.,
Hirata H., Hibi N., Tsukada Y.;
"Expression profile of a gamma-deletion variant of the human
telomerase reverse transcriptase gene.";
Neoplasia 5:193-197(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
TISSUE=Stomach cancer;
PubMed=14654914;
Nagao K., Katsumata K., Aizawa Y., Saito N., Hirata H., Sasaki H.,
Yamamoto S., Hikiji K., Koiwa T., Hisatomi H.;
"Differential alternative splicing expressions of telomerase reverse
transcriptase in gastrointestinal cell lines.";
Oncol. Rep. 11:127-131(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Londono-Vallejo J.A.;
"Sequence of a BAC carrying the entire hTERT gene.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-412 AND THR-1062.
NIEHS SNPs program;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=8676067; DOI=10.1084/jem.183.6.2471;
Weng N.P., Levine B.L., June C.H., Hodes R.J.;
"Regulated expression of telomerase activity in human T lymphocyte
development and activation.";
J. Exp. Med. 183:2471-2479(1996).
[11]
FUNCTION IN TELOMERASE ACTIVITY, TISSUE SPECIFICITY, ASSOCIATION WITH
TEP1, AND MUTAGENESIS OF ASP-712; ASP-868 AND ASP-869.
PubMed=9389643; DOI=10.1101/gad.11.23.3109;
Harrington L., Zhou W., McPhail T., Oulton R., Yeung D.S., Mar V.,
Bass M.B., Robinson M.O.;
"Human telomerase contains evolutionarily conserved catalytic and
structural subunits.";
Genes Dev. 11:3109-3115(1997).
[12]
RECONSTITUTION OF THE TELOMERASE COMPLEX, AND MUTAGENESIS OF ASP-712;
ASP-868 AND ASP-869.
PubMed=9443919; DOI=10.1016/S0960-9822(98)70067-3;
Beattie T.L., Zhou W., Robinson M.O., Harrington L.;
"Reconstitution of human telomerase activity in vitro.";
Curr. Biol. 8:177-180(1998).
[13]
ASSOCIATION WITH TEP1.
PubMed=11029039; DOI=10.1091/mbc.11.10.3329;
Beattie T.L., Zhou W., Robinson M.O., Harrington L.;
"Polymerization defects within human telomerase are distinct from
telomerase RNA and TEP1 binding.";
Mol. Biol. Cell 11:3329-3340(2000).
[14]
INTERACTION WITH HSPA1A; HSP90A AND PTGES3.
PubMed=11274138; DOI=10.1074/jbc.C100055200;
Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.;
"Stable association of hsp90 and p23, but Not hsp70, with active human
telomerase.";
J. Biol. Chem. 276:15571-15574(2001).
[15]
PHOSPHORYLATION AT TYR-707, SUBCELLULAR LOCATION, INTERACTION WITH RAN
AND XP01, AND MUTAGENESIS OF TYR-707.
PubMed=12808100; DOI=10.1128/MCB.23.13.4598-4610.2003;
Haendeler J., Hoffmann J., Brandes R.P., Zeiher A.M., Dimmeler S.;
"Hydrogen peroxide triggers nuclear export of telomerase reverse
transcriptase via Src kinase family-dependent phosphorylation of
tyrosine 707.";
Mol. Cell. Biol. 23:4598-4610(2003).
[16]
INTERACTION WITH MCRS1.
PubMed=15044100; DOI=10.1016/j.bbrc.2004.02.166;
Song H., Li Y., Chen G., Xing Z., Zhao J., Yokoyama K.K., Li T.,
Zhao M.;
"Human MCRS2, a cell-cycle-dependent protein, associates with
LPTS/PinX1 and reduces the telomere length.";
Biochem. Biophys. Res. Commun. 316:1116-1123(2004).
[17]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=14963003; DOI=10.1161/01.RES.0000121104.05977.F3;
Haendeler J., Hoffmann J., Diehl J.F., Vasa M., Spyridopoulos I.,
Zeiher A.M., Dimmeler S.;
"Antioxidants inhibit nuclear export of telomerase reverse
transcriptase and delay replicative senescence of endothelial cells.";
Circ. Res. 94:768-775(2004).
[18]
SUBCELLULAR LOCATION.
PubMed=15138842; DOI=10.1007/s00418-004-0645-5;
Yan P., Benhattar J., Seelentag W., Stehle J.C., Bosman F.T.;
"Immunohistochemical localization of hTERT protein in human tissues.";
Histochem. Cell Biol. 121:391-397(2004).
[19]
INTERACTION WITH NCL, AND SUBCELLULAR LOCATION.
PubMed=15371412; DOI=10.1074/jbc.M407643200;
Khurts S., Masutomi K., Delgermaa L., Arai K., Oishi N., Mizuno H.,
Hayashi N., Hahn W.C., Murakami S.;
"Nucleolin interacts with telomerase.";
J. Biol. Chem. 279:51508-51515(2004).
[20]
FUNCTIONAL DOMAINS, AND MUTAGENESIS OF TRP-547 AND ASP-868.
PubMed=15082768; DOI=10.1128/MCB.24.9.3720-3733.2004;
Moriarty T.J., Marie-Egyptienne D.T., Autexier C.;
"Functional organization of repeat addition processivity and DNA
synthesis determinants in the human telomerase multimer.";
Mol. Cell. Biol. 24:3720-3733(2004).
[21]
INTERACTION WITH MKRN1, AND UBIQUITINATION.
PubMed=15805468; DOI=10.1101/gad.1289405;
Kim J.H., Park S.-M., Kang M.R., Oh S.-Y., Lee T.H., Muller M.T.,
Chung I.K.;
"Ubiquitin ligase MKRN1 modulates telomere length homeostasis through
a proteolysis of hTERT.";
Genes Dev. 19:776-781(2005).
[22]
FUNCTION, AND MUTAGENESIS OF ASP-868.
PubMed=15857955; DOI=10.1091/mbc.E05-02-0148;
Moriarty T.J., Ward R.J., Taboski M.A., Autexier C.;
"An anchor site-type defect in human telomerase that disrupts telomere
length maintenance and cellular immortalization.";
Mol. Biol. Cell 16:3152-3161(2005).
[23]
FUNCTION, AND MUTAGENESIS OF ARG-631; ASP-712 AND ASP-868.
PubMed=17026956; DOI=10.1016/j.bbrc.2006.09.125;
Rahman R., Mo L., Cui W.;
"Telomerase with mutated catalytic motifs has dominant negative
effects on telomerase activity and inhibits cell growth.";
Biochem. Biophys. Res. Commun. 350:796-802(2006).
[24]
PHOSPHORYLATION, AND FUNCTION.
PubMed=17548608; DOI=10.4049/jimmunol.178.12.7710;
Plunkett F.J., Franzese O., Finney H.M., Fletcher J.M.,
Belaramani L.L., Salmon M., Dokal I., Webster D., Lawson A.D.,
Akbar A.N.;
"The loss of telomerase activity in highly differentiated CD8+CD28-
CD27- T cells is associated with decreased Akt (Ser473)
phosphorylation.";
J. Immunol. 178:7710-7719(2007).
[25]
INTERACTION WITH NAT10.
PubMed=18082603; DOI=10.1016/j.molcel.2007.09.023;
Fu D., Collins K.;
"Purification of human telomerase complexes identifies factors
involved in telomerase biogenesis and telomere length regulation.";
Mol. Cell 28:773-785(2007).
[26]
FUNCTION, DNA-BINDING, AND MUTAGENESIS OF 137-TRP--LEU-141; ASP-712
AND 930-TRP--LEU-934.
PubMed=17296728; DOI=10.1128/MCB.02368-06;
Wyatt H.D., Lobb D.A., Beattie T.L.;
"Characterization of physical and functional anchor site interactions
in human telomerase.";
Mol. Cell. Biol. 27:3226-3240(2007).
[27]
FUNCTION, AND MUTAGENESIS OF LEU-866 AND VAL-867.
PubMed=17264120; DOI=10.1093/nar/gkm002;
Drosopoulos W.C., Prasad V.R.;
"The active site residue Valine 867 in human telomerase reverse
transcriptase influences nucleotide incorporation and fidelity.";
Nucleic Acids Res. 35:1155-1168(2007).
[28]
INTERACTION WITH PTPN11, PHOSPHORYLATION AT TYR-707, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF TYR-707.
PubMed=18829466; DOI=10.1074/jbc.M805138200;
Jakob S., Schroeder P., Lukosz M., Buchner N., Spyridopoulos I.,
Altschmied J., Haendeler J.;
"Nuclear protein tyrosine phosphatase Shp-2 is one important negative
regulator of nuclear export of telomerase reverse transcriptase.";
J. Biol. Chem. 283:33155-33161(2008).
[29]
PHOSPHORYLATION, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19188162; DOI=10.1158/1078-0432.CCR-08-0792;
Ram R., Uziel O., Eldan O., Fenig E., Beery E., Lichtenberg S.,
Nordenberg Y., Lahav M.;
"Ionizing radiation up-regulates telomerase activity in cancer cell
lines by post-translational mechanism via ras/phosphatidylinositol 3-
kinase/Akt pathway.";
Clin. Cancer Res. 15:914-923(2009).
[30]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML.
PubMed=19567472; DOI=10.1242/jcs.048066;
Oh W., Ghim J., Lee E.W., Yang M.R., Kim E.T., Ahn J.H., Song J.;
"PML-IV functions as a negative regulator of telomerase by interacting
with TERT.";
J. Cell Sci. 122:2613-2622(2009).
[31]
INTERACTION WITH SMARCA4, AND FUNCTION.
PubMed=19571879; DOI=10.1038/nature08137;
Park J.I., Venteicher A.S., Hong J.Y., Choi J., Jun S., Shkreli M.,
Chang W., Meng Z., Cheung P., Ji H., McLaughlin M., Veenstra T.D.,
Nusse R., McCrea P.D., Artandi S.E.;
"Telomerase modulates Wnt signalling by association with target gene
chromatin.";
Nature 460:66-72(2009).
[32]
FUNCTION, DNA-BINDING, AND MUTAGENESIS OF GLN-169.
PubMed=19777057; DOI=10.1371/journal.pone.0007176;
Wyatt H.D., Tsang A.R., Lobb D.A., Beattie T.L.;
"Human telomerase reverse transcriptase (hTERT) Q169 is essential for
telomerase function in vitro and in vivo.";
PLoS ONE 4:E7176-E7176(2009).
[33]
IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
PubMed=19179534; DOI=10.1126/science.1165357;
Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M.,
Veenstra T.D., Terns M.P., Artandi S.E.;
"A human telomerase holoenzyme protein required for Cajal body
localization and telomere synthesis.";
Science 323:644-648(2009).
[34]
SUBCELLULAR LOCATION, AND INTERACTION WITH NVL.
PubMed=22226966; DOI=10.1016/j.bbrc.2011.12.101;
Her J., Chung I.K.;
"The AAA-ATPase NVL2 is a telomerase component essential for
holoenzyme assembly.";
Biochem. Biophys. Res. Commun. 417:1086-1092(2012).
[35]
PHOSPHORYLATION AT SER-227, SUBCELLULAR LOCATION, AND NUCLEAR
LOCALIZATION SIGNAL.
PubMed=22366458; DOI=10.1242/jcs.099267;
Chung J., Khadka P., Chung I.K.;
"Nuclear import of hTERT requires a bipartite nuclear localization
signal and Akt-mediated phosphorylation.";
J. Cell Sci. 125:2684-2697(2012).
[36]
PHOSPHORYLATION AT SER-457, UBIQUITINATION, AND MUTAGENESIS OF
SER-457.
PubMed=23362280; DOI=10.1074/jbc.M112.416792;
Jung H.Y., Wang X., Jun S., Park J.I.;
"Dyrk2-associated EDD-DDB1-VprBP E3 ligase inhibits telomerase by TERT
degradation.";
J. Biol. Chem. 288:7252-7262(2013).
[37]
UBIQUITINATION.
PubMed=23612978; DOI=10.1074/jbc.M112.416735;
Wang X., Singh S., Jung H.Y., Yang G., Jun S., Sastry K.J., Park J.I.;
"HIV-1 Vpr protein inhibits telomerase activity via the EDD-DDB1-VPRBP
E3 ligase complex.";
J. Biol. Chem. 288:15474-15480(2013).
[38]
INVOLVEMENT IN CMM9.
PubMed=23348503; DOI=10.1126/science.1230062;
Horn S., Figl A., Rachakonda P.S., Fischer C., Sucker A., Gast A.,
Kadel S., Moll I., Nagore E., Hemminki K., Schadendorf D., Kumar R.;
"TERT promoter mutations in familial and sporadic melanoma.";
Science 339:959-961(2013).
[39]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 461-469 IN COMPLEX WITH CLASS
I MAJOR HISTOCOMPATIBILITY COMPLEX (MHC).
PubMed=16323248; DOI=10.1002/eji.200535424;
Cole D.K., Rizkallah P.J., Gao F., Watson N.I., Boulter J.M.,
Bell J.I., Sami M., Gao G.F., Jakobsen B.K.;
"Crystal structure of HLA-A*2402 complexed with a telomerase
peptide.";
Eur. J. Immunol. 36:170-179(2006).
[40]
VARIANT AA THR-202, VARIANTS DKCA2 TRP-979 AND LEU-1127,
CHARACTERIZATION OF VARIANT AA THR-202, AND CHARACTERIZATION OF
VARIANTS DKCA2 TRP-979 AND LEU-1127.
PubMed=15885610; DOI=10.1016/j.bcmd.2004.12.008;
Vulliamy T.J., Walne A., Baskaradas A., Mason P.J., Marrone A.,
Dokal I.;
"Mutations in the reverse transcriptase component of telomerase (TERT)
in patients with bone marrow failure.";
Blood Cells Mol. Dis. 34:257-263(2005).
[41]
VARIANTS PFBMFT1 THR-202; TYR-412; MET-694; CYS-772 AND MET-1090, AND
VARIANTS THR-279; GLU-441 DEL AND THR-1062.
PubMed=15814878; DOI=10.1056/NEJMoa042980;
Yamaguchi H., Calado R.T., Ly H., Kajigaya S., Baerlocher G.M.,
Chanock S.J., Lansdorp P.M., Young N.S.;
"Mutations in TERT, the gene for telomerase reverse transcriptase, in
aplastic anemia.";
N. Engl. J. Med. 352:1413-1424(2005).
[42]
VARIANT DKCA2 ASN-902, AND CHARACTERIZATION OF VARIANT DKCA2 ASN-902.
PubMed=16247010; DOI=10.1073/pnas.0508124102;
Armanios M., Chen J.-L., Chang Y.-P.C., Brodsky R.A., Hawkins A.,
Griffin C.A., Eshleman J.R., Cohen A.R., Chakravarti A., Hamosh A.,
Greider C.W.;
"Haploinsufficiency of telomerase reverse transcriptase leads to
anticipation in autosomal dominant dyskeratosis congenita.";
Proc. Natl. Acad. Sci. U.S.A. 102:15960-15964(2005).
[43]
INVOLVEMENT IN CAD SUSCEPTIBILITY.
PubMed=16890917; DOI=10.1016/j.bbrc.2006.07.103;
Matsubara Y., Murata M., Watanabe K., Saito I., Miyaki K., Omae K.,
Ishikawa M., Matsushita K., Iwanaga S., Ogawa S., Ikeda Y.;
"Coronary artery disease and a functional polymorphism of hTERT.";
Biochem. Biophys. Res. Commun. 348:669-672(2006).
[44]
VARIANT DKCB4 ARG-721.
PubMed=16332973; DOI=10.1182/blood-2005-07-2622;
Vulliamy T.J., Marrone A., Knight S.W., Walne A., Mason P.J.,
Dokal I.;
"Mutations in dyskeratosis congenita: their impact on telomere length
and the diversity of clinical presentation.";
Blood 107:2680-2685(2006).
[45]
VARIANTS AA ASP-682 AND MET-726, AND CHARACTERIZATION OF VARIANT AA
MET-726.
PubMed=16627250;
Liang J., Yagasaki H., Kamachi Y., Hama A., Matsumoto K., Kato K.,
Kudo K., Kojima S.;
"Mutations in telomerase catalytic protein in Japanese children with
aplastic anemia.";
Haematologica 91:656-658(2006).
[46]
VARIANT AA ASN-570, AND CHARACTERIZATION OF VARIANTS ASN-570; ASP-682;
ARG-721; MET-726; ASN-902; TRP-979 AND LEU-1127.
PubMed=16990594; DOI=10.1182/blood-2006-07-035089;
Xin Z.T., Beauchamp A.D., Calado R.T., Bradford J.W., Regal J.A.,
Shenoy A., Liang Y., Lansdorp P.M., Young N.S., Ly H.;
"Functional characterization of natural telomerase mutations found in
patients with hematologic disorders.";
Blood 109:524-532(2007).
[47]
VARIANTS DKCB4 CYS-811 AND TRP-901, AND CHARACTERIZATION OF VARIANTS
DKCB4 CYS-811 AND TRP-901.
PubMed=17785587; DOI=10.1182/blood-2006-12-062851;
Marrone A., Walne A., Tamary H., Masunari Y., Kirwan M., Beswick R.,
Vulliamy T., Dokal I.;
"Telomerase reverse-transcriptase homozygous mutations in autosomal
recessive dyskeratosis congenita and Hoyeraal-Hreidarsson syndrome.";
Blood 110:4198-4205(2007).
[48]
VARIANTS IDIOPATHIC PULMONARY FIBROSIS SUSCEPTIBILITY GLN-55 AND
MET-1110, AND CHARACTERIZATION OF VARIANTS GLN-55 AND MET-1110.
PubMed=17392301; DOI=10.1056/NEJMoa066157;
Armanios M.Y., Chen J.J., Cogan J.D., Alder J.K., Ingersoll R.G.,
Markin C., Lawson W.E., Xie M., Vulto I., Phillips J.A.,
Lansdorp P.M., Greider C.W., Loyd J.E.;
"Telomerase mutations in families with idiopathic pulmonary
fibrosis.";
N. Engl. J. Med. 356:1317-1326(2007).
[49]
VARIANT PFBMFT1 HIS-865.
PubMed=17460043; DOI=10.1073/pnas.0701009104;
Tsakiri K.D., Cronkhite J.T., Kuan P.J., Xing C., Raghu G.,
Weissler J.C., Rosenblatt R.L., Shay J.W., Garcia C.K.;
"Adult-onset pulmonary fibrosis caused by mutations in telomerase.";
Proc. Natl. Acad. Sci. U.S.A. 104:7552-7557(2007).
[50]
VARIANTS DKCB4 TYR-412 AND SER-704, AND CHARACTERIZATION OF VARIANTS
DKCB4 TYR-412 AND SER-704.
PubMed=18042801; DOI=10.1182/blood-2007-10-120907;
Du H.Y., Pumbo E., Manley P., Field J.J., Bayliss S.J., Wilson D.B.,
Mason P.J., Bessler M.;
"Complex inheritance pattern of dyskeratosis congenita in two families
with 2 different mutations in the telomerase reverse transcriptase
gene.";
Blood 111:1128-1130(2008).
[51]
VARIANTS ALA-65; MET-299; LYS-522 AND THR-1062, AND VARIANTS AA
THR-202; TYR-412; GLU-441 DEL; ASN-570; GLN-631; MET-694 AND LEU-785.
PubMed=19760749; DOI=10.1002/humu.21115;
Kirwan M., Vulliamy T., Marrone A., Walne A.J., Beswick R.,
Hillmen P., Kelly R., Stewart A., Bowen D., Schonland S.O.,
Whittle A.M., McVerry A., Gilleece M., Dokal I.;
"Defining the pathogenic role of telomerase mutations in
myelodysplastic syndrome and acute myeloid leukemia.";
Hum. Mutat. 30:1567-1573(2009).
[52]
VARIANTS ALA-65; MET-299; TYR-412; GLU-441 DEL; LYS-522 AND THR-1062.
PubMed=19147845; DOI=10.1073/pnas.0807057106;
Calado R.T., Regal J.A., Hills M., Yewdell W.T., Dalmazzo L.F.,
Zago M.A., Lansdorp P.M., Hogge D., Chanock S.J., Estey E.H.,
Falcao R.P., Young N.S.;
"Constitutional hypomorphic telomerase mutations in patients with
acute myeloid leukemia.";
Proc. Natl. Acad. Sci. U.S.A. 106:1187-1192(2009).
[53]
VARIANTS PFBMFT1 MET-170; THR-716; PHE-841; ARG-902 AND PHE-1025, AND
CHARACTERIZATION OF VARIANTS PFBMFT1 MET-170; THR-716; PHE-841 AND
PHE-1025.
PubMed=21436073; DOI=10.1182/blood-2010-11-322149;
Parry E.M., Alder J.K., Qi X., Chen J.J., Armanios M.;
"Syndrome complex of bone marrow failure and pulmonary fibrosis
predicts germline defects in telomerase.";
Blood 117:5607-5611(2011).
[54]
VARIANTS PFBMFT1 ILE-791 AND MET-867, AND CHARACTERIZATION OF VARIANTS
PFBMFT1 ILE-791 AND MET-867.
PubMed=21483807; DOI=10.1371/journal.pgen.1001352;
Alder J.K., Cogan J.D., Brown A.F., Anderson C.J., Lawson W.E.,
Lansdorp P.M., Phillips J.A. III, Loyd J.E., Chen J.J., Armanios M.;
"Ancestral mutation in telomerase causes defects in repeat addition
processivity and manifests as familial pulmonary fibrosis.";
PLoS Genet. 7:E1001352-E1001352(2011).
[55]
VARIANT PFBMFT1 LEU-923.
PubMed=22512499; DOI=10.1056/NEJMc1200999;
Gansner J.M., Rosas I.O., Ebert B.L.;
"Pulmonary fibrosis, bone marrow failure, and telomerase mutation.";
N. Engl. J. Med. 366:1551-1553(2012).
-!- FUNCTION: 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. {ECO:0000269|PubMed:14963003,
ECO:0000269|PubMed:15082768, ECO:0000269|PubMed:15857955,
ECO:0000269|PubMed:17026956, ECO:0000269|PubMed:17264120,
ECO:0000269|PubMed:17296728, ECO:0000269|PubMed:17548608,
ECO:0000269|PubMed:19188162, ECO:0000269|PubMed:19567472,
ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:19777057,
ECO:0000269|PubMed:9389643}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- SUBUNIT: 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.
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. Interacts with GNL3L (By similarity).
Interacts with isoform 1 and isoform 2 of NVL (PubMed:22226966).
{ECO:0000250|UniProtKB:O70372, ECO:0000269|PubMed:22226966}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1772203, EBI-1772203;
P35222:CTNNB1; NbExp=2; IntAct=EBI-1772203, EBI-491549;
P03126:E6 (xeno); NbExp=7; IntAct=EBI-1772203, EBI-1177242;
Q9BVP2:GNL3; NbExp=3; IntAct=EBI-1772203, EBI-641642;
P29590-5:PML; NbExp=7; IntAct=EBI-1772203, EBI-304008;
Q9Y265:RUVBL1; NbExp=11; IntAct=EBI-1772203, EBI-353675;
P51532:SMARCA4; NbExp=8; IntAct=EBI-1772203, EBI-302489;
O14773-1:TPP1; NbExp=2; IntAct=EBI-1772203, EBI-15619703;
Q92900:UPF1; NbExp=3; IntAct=EBI-1772203, EBI-373471;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:22226966}. Nucleus, nucleoplasm. Nucleus.
Chromosome, telomere. Cytoplasm. Nucleus, PML body. 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-707. Dephosphorylation at this site by SHP2
retains TERT in the nucleus. Translocated to the nucleus by
phosphorylation by AKT.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O14746-1; Sequence=Displayed;
Name=2;
IsoId=O14746-2; Sequence=VSP_019587, VSP_019588;
Name=3;
IsoId=O14746-3; Sequence=VSP_021727;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay. No
experimental confirmation available.;
Name=4;
IsoId=O14746-4; Sequence=VSP_053369, VSP_019587, VSP_019588;
-!- TISSUE SPECIFICITY: Expressed at a high level in thymocyte
subpopulations, at an intermediate level in tonsil T-lymphocytes,
and at a low to undetectable level in peripheral blood T-
lymphocytes. {ECO:0000269|PubMed:8676067,
ECO:0000269|PubMed:9389643}.
-!- INDUCTION: Activated by cytotoxic events and down-regulated during
aging. In peripheral T-lymphocytes, induced By CD3 and by
PMA/ionomycin. Inhibited by herbimycin B.
{ECO:0000269|PubMed:8676067}.
-!- DOMAIN: The primer grip sequence in the RT domain is required for
telomerase activity and for stable association with short
telomeric primers.
-!- DOMAIN: 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.
-!- DOMAIN: The RNA-interacting domain 2 (RD2) is essential for both
interaction with the CR4-CR5 domain of TERC and for DNA synthesis.
-!- PTM: Phosphorylation at Tyr-707 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 Ser-227 by the AKT pathway
promotes nuclear location. Phosphorylation at the G2/M phase at
Ser-457 by DYRK2 promotes ubiquitination by the EDVP complex and
degradation. {ECO:0000269|PubMed:12808100,
ECO:0000269|PubMed:18829466, ECO:0000269|PubMed:22366458,
ECO:0000269|PubMed:23362280}.
-!- PTM: Ubiquitinated by the EDVP complex, a E3 ligase complex
following phosphorylation at Ser-457 by DYRK2. Ubiquitinated leads
to proteasomal degradation. In case of infection by HIV-1, the
EDVP complex is hijacked by HIV-1 via interaction between HIV-1
Vpr and DCAF1/VPRBP, leading to ubiquitination and degradation.
{ECO:0000269|PubMed:23362280}.
-!- DISEASE: Note=Activation of telomerase has been implicated in cell
immortalization and cancer cell pathogenesis.
-!- DISEASE: Aplastic anemia (AA) [MIM:609135]: A form of anemia in
which the bone marrow fails to produce adequate numbers of
peripheral blood elements. It is characterized by peripheral
pancytopenia and marrow hypoplasia. {ECO:0000269|PubMed:15885610,
ECO:0000269|PubMed:16627250, ECO:0000269|PubMed:16990594,
ECO:0000269|PubMed:19760749}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Note=Genetic variations in TERT are associated with
coronary artery disease (CAD).
-!- DISEASE: Dyskeratosis congenita, autosomal dominant, 2 (DKCA2)
[MIM:613989]: 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. {ECO:0000269|PubMed:15885610,
ECO:0000269|PubMed:16247010}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Pulmonary fibrosis, and/or bone marrow failure, telomere-
related, 1 (PFBMFT1) [MIM:614742]: A disease associated with
shortened telomeres. Pulmonary fibrosis is the most common
manifestation. Other manifestations include aplastic anemia due to
bone marrow failure, hepatic fibrosis, and increased cancer risk,
particularly myelodysplastic syndrome and acute myeloid leukemia.
Phenotype, age at onset, and severity are determined by telomere
length. {ECO:0000269|PubMed:15814878, ECO:0000269|PubMed:17460043,
ECO:0000269|PubMed:21436073, ECO:0000269|PubMed:21483807,
ECO:0000269|PubMed:22512499}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Dyskeratosis congenita, autosomal recessive, 4 (DKCB4)
[MIM:613989]: A severe form of dyskeratosis congenita, 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.
{ECO:0000269|PubMed:16332973, ECO:0000269|PubMed:17785587,
ECO:0000269|PubMed:18042801}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Pulmonary fibrosis, idiopathic (IPF) [MIM:178500]: A lung
disease characterized by shortness of breath, radiographically
evident diffuse pulmonary infiltrates, and varying degrees of
inflammation and fibrosis on biopsy. In some cases, the disorder
can be rapidly progressive and characterized by sequential acute
lung injury with subsequent scarring and end-stage lung disease.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Melanoma, cutaneous malignant 9 (CMM9) [MIM:615134]: A
malignant neoplasm of melanocytes, arising de novo or from a pre-
existing benign nevus, which occurs most often in the skin but
also may involve other sites. {ECO:0000269|PubMed:23348503}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the reverse transcriptase family.
Telomerase subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tert/";
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EMBL; AF018167; AAC51724.1; -; mRNA.
EMBL; AF015950; AAC51672.1; -; mRNA.
EMBL; AF128894; AAD30037.1; -; Genomic_DNA.
EMBL; AF128893; AAD30037.1; JOINED; Genomic_DNA.
EMBL; AB085628; BAC11010.1; -; mRNA.
EMBL; AB086379; BAC11014.1; -; mRNA.
EMBL; AB086950; BAC11015.1; -; mRNA.
EMBL; AY007685; AAG23289.1; -; Genomic_DNA.
EMBL; DQ264729; ABB72674.1; -; Genomic_DNA.
EMBL; AC114291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471102; EAX08167.1; -; Genomic_DNA.
CCDS; CCDS3861.2; -. [O14746-1]
CCDS; CCDS54831.1; -. [O14746-3]
PIR; T03844; T03844.
RefSeq; NP_001180305.1; NM_001193376.1. [O14746-3]
RefSeq; NP_937983.2; NM_198253.2. [O14746-1]
UniGene; Hs.492203; -.
PDB; 2BCK; X-ray; 2.80 A; C/F=461-469.
PDB; 4B18; X-ray; 2.52 A; B=222-240.
PDB; 4MNQ; X-ray; 2.74 A; C=540-548.
PDB; 5MEN; X-ray; 2.81 A; C=540-548.
PDB; 5MEO; X-ray; 1.77 A; C=540-548.
PDB; 5MEP; X-ray; 2.71 A; C/F=540-548.
PDB; 5MEQ; X-ray; 2.27 A; C=540-546.
PDB; 5MER; X-ray; 1.88 A; C/F=540-546.
PDB; 5UGW; X-ray; 2.31 A; A=961-1132.
PDBsum; 2BCK; -.
PDBsum; 4B18; -.
PDBsum; 4MNQ; -.
PDBsum; 5MEN; -.
PDBsum; 5MEO; -.
PDBsum; 5MEP; -.
PDBsum; 5MEQ; -.
PDBsum; 5MER; -.
PDBsum; 5UGW; -.
ProteinModelPortal; O14746; -.
SMR; O14746; -.
BioGrid; 112874; 67.
CORUM; O14746; -.
DIP; DIP-40646N; -.
ELM; O14746; -.
IntAct; O14746; 23.
MINT; MINT-133963; -.
STRING; 9606.ENSP00000309572; -.
BindingDB; O14746; -.
ChEMBL; CHEMBL2916; -.
DrugBank; DB05036; Grn163l.
DrugBank; DB04937; GV1001.
DrugBank; DB00495; Zidovudine.
iPTMnet; O14746; -.
PhosphoSitePlus; O14746; -.
BioMuta; TERT; -.
EPD; O14746; -.
PaxDb; O14746; -.
PeptideAtlas; O14746; -.
PRIDE; O14746; -.
DNASU; 7015; -.
Ensembl; ENST00000310581; ENSP00000309572; ENSG00000164362. [O14746-1]
Ensembl; ENST00000334602; ENSP00000334346; ENSG00000164362. [O14746-3]
Ensembl; ENST00000460137; ENSP00000425003; ENSG00000164362. [O14746-4]
Ensembl; ENST00000508104; ENSP00000426042; ENSG00000164362. [O14746-2]
GeneID; 7015; -.
KEGG; hsa:7015; -.
UCSC; uc003jcb.2; human. [O14746-1]
CTD; 7015; -.
DisGeNET; 7015; -.
EuPathDB; HostDB:ENSG00000164362.18; -.
GeneCards; TERT; -.
GeneReviews; TERT; -.
HGNC; HGNC:11730; TERT.
HPA; HPA054641; -.
HPA; HPA065897; -.
MalaCards; TERT; -.
MIM; 178500; phenotype.
MIM; 187270; gene+phenotype.
MIM; 609135; phenotype.
MIM; 613989; phenotype.
MIM; 614742; phenotype.
MIM; 615134; phenotype.
neXtProt; NX_O14746; -.
OpenTargets; ENSG00000164362; -.
Orphanet; 1775; Dyskeratosis congenita.
Orphanet; 618; Familial melanoma.
Orphanet; 3322; Hoyeraal-Hreidarsson syndrome.
Orphanet; 88; Idiopathic aplastic anemia.
Orphanet; 2032; Idiopathic pulmonary fibrosis.
PharmGKB; PA36447; -.
eggNOG; KOG1005; Eukaryota.
eggNOG; ENOG410XQJH; LUCA.
GeneTree; ENSGT00390000018531; -.
HOGENOM; HOG000148780; -.
HOVERGEN; HBG000460; -.
InParanoid; O14746; -.
KO; K11126; -.
OMA; QCQGIPQ; -.
OrthoDB; EOG091G04DO; -.
PhylomeDB; O14746; -.
TreeFam; TF329048; -.
Reactome; R-HSA-171319; Telomere Extension By Telomerase.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
SIGNOR; O14746; -.
EvolutionaryTrace; O14746; -.
GeneWiki; Telomerase_reverse_transcriptase; -.
GenomeRNAi; 7015; -.
PRO; PR:O14746; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000164362; -.
CleanEx; HS_TERT; -.
Genevisible; O14746; HS.
GO; GO:0000781; C:chromosome, telomeric region; IC:UniProtKB.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0000783; C:nuclear telomere cap complex; IC:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0031379; C:RNA-directed RNA polymerase complex; IPI:BHF-UCL.
GO; GO:0000333; C:telomerase catalytic core complex; IDA:BHF-UCL.
GO; GO:0005697; C:telomerase holoenzyme complex; IDA:UniProtKB.
GO; GO:1990572; C:TERT-RMRP complex; IDA:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016779; F:nucleotidyltransferase activity; IDA:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0047485; F:protein N-terminus binding; IPI:BHF-UCL.
GO; GO:0003723; F:RNA binding; IPI:BHF-UCL.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IDA:BHF-UCL.
GO; GO:0003720; F:telomerase activity; IDA:UniProtKB.
GO; GO:0070034; F:telomerase RNA binding; IDA:BHF-UCL.
GO; GO:0003721; F:telomerase RNA reverse transcriptase activity; IDA:BHF-UCL.
GO; GO:0042162; F:telomeric DNA binding; TAS:ProtInc.
GO; GO:0001223; F:transcription coactivator binding; IPI:BHF-UCL.
GO; GO:0000049; F:tRNA binding; IDA:BHF-UCL.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
GO; GO:0071897; P:DNA biosynthetic process; IDA:BHF-UCL.
GO; GO:0022616; P:DNA strand elongation; IDA:BHF-UCL.
GO; GO:0070200; P:establishment of protein localization to telomere; IDA:BHF-UCL.
GO; GO:0007005; P:mitochondrion organization; IDA:BHF-UCL.
GO; GO:2000773; P:negative regulation of cellular senescence; IDA:BHF-UCL.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
GO; GO:0060253; P:negative regulation of glial cell proliferation; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:1903704; P:negative regulation of production of siRNA involved in RNA interference; IDA:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
GO; GO:0042635; P:positive regulation of hair cycle; ISS:BHF-UCL.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IDA:BHF-UCL.
GO; GO:2000648; P:positive regulation of stem cell proliferation; ISS:BHF-UCL.
GO; GO:1903620; P:positive regulation of transdifferentiation; IEA:Ensembl.
GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IEA:Ensembl.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IGI:BHF-UCL.
GO; GO:0030422; P:production of siRNA involved in RNA interference; IDA:BHF-UCL.
GO; GO:0031647; P:regulation of protein stability; IDA:BHF-UCL.
GO; GO:0090399; P:replicative senescence; IMP:BHF-UCL.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0032774; P:RNA biosynthetic process; IDA:BHF-UCL.
GO; GO:0006278; P:RNA-dependent DNA biosynthetic process; IDA:BHF-UCL.
GO; GO:0000723; P:telomere maintenance; TAS:UniProtKB.
GO; GO:0007004; P:telomere maintenance via telomerase; IDA:BHF-UCL.
GO; GO:0001172; P:transcription, RNA-templated; IDA:BHF-UCL.
InterPro; IPR000477; RT_dom.
InterPro; IPR021891; Telomerase_RBD.
InterPro; IPR003545; Telomerase_RT.
PANTHER; PTHR12066; PTHR12066; 1.
Pfam; PF00078; RVT_1; 1.
Pfam; PF12009; Telomerase_RBD; 1.
PRINTS; PR01365; TELOMERASERT.
SMART; SM00975; Telomerase_RBD; 1.
PROSITE; PS50878; RT_POL; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosome; Complete proteome;
Cytoplasm; Disease mutation; DNA-binding; Dyskeratosis congenita;
Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Ribonucleoprotein;
RNA-directed DNA polymerase; Telomere; Transferase; Ubl conjugation.
CHAIN 1 1132 Telomerase reverse transcriptase.
/FTId=PRO_0000054925.
DOMAIN 605 935 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
REGION 1 230 RNA-interacting domain 1.
REGION 58 197 GQ motif.
REGION 137 141 Required for regulating specificity for
telomeric DNA and for processivity for
primer elongation.
REGION 231 324 Linker.
REGION 301 538 Required for oligomerization.
REGION 325 550 RNA-interacting domain 2.
REGION 376 521 QFP motif.
REGION 397 417 CP motif.
REGION 914 928 Required for oligomerization.
REGION 930 934 Primer grip sequence.
REGION 936 1132 CTE.
MOTIF 222 240 Bipartite nuclear localization signal.
MOTIF 328 333 TFLY; involved in RNA binding.
{ECO:0000250|UniProtKB:Q4KTA7}.
METAL 712 712 Magnesium; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 868 868 Magnesium; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 869 869 Magnesium; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
SITE 169 169 Required for optimal binding of telomeric
ssDNA and incorporation of nucleotides at
the second position of the template.
SITE 867 867 Required for nucleotide incorporation and
primer extension rate.
MOD_RES 227 227 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:22366458}.
MOD_RES 457 457 Phosphoserine; by DYRK2.
{ECO:0000269|PubMed:23362280}.
MOD_RES 707 707 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000269|PubMed:12808100,
ECO:0000269|PubMed:18829466}.
VAR_SEQ 711 722 Missing (in isoform 4).
{ECO:0000303|PubMed:14654914}.
/FTId=VSP_053369.
VAR_SEQ 764 807 STLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSG
LFD -> LRPVPGDPAGLHPLHAALQPVLRRHGEQAVCGDS
AGRAAPAFGG (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:12869302,
ECO:0000303|PubMed:14654914}.
/FTId=VSP_019587.
VAR_SEQ 808 1132 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:12869302,
ECO:0000303|PubMed:14654914}.
/FTId=VSP_019588.
VAR_SEQ 885 947 Missing (in isoform 3).
{ECO:0000303|PubMed:14654914}.
/FTId=VSP_021727.
VARIANT 55 55 L -> Q (in idiopathic pulmonary fibrosis
susceptibility; impaired telomerase
activity; dbSNP:rs387907247).
{ECO:0000269|PubMed:17392301}.
/FTId=VAR_062535.
VARIANT 65 65 P -> A (associated with acute myeloid
leukemia; dbSNP:rs544215765).
{ECO:0000269|PubMed:19147845,
ECO:0000269|PubMed:19760749}.
/FTId=VAR_062780.
VARIANT 170 170 V -> M (in PFBMFT1; the mutant protein is
demonstrated to cause decreased
telomerase activity; dbSNP:rs387907248).
{ECO:0000269|PubMed:21436073}.
/FTId=VAR_068792.
VARIANT 202 202 A -> T (in PFBMFT1 and AA; severe and
moderate; associated with disease
susceptibility; shorter telomeres;
dbSNP:rs121918661).
{ECO:0000269|PubMed:15814878,
ECO:0000269|PubMed:15885610,
ECO:0000269|PubMed:19760749}.
/FTId=VAR_036863.
VARIANT 279 279 A -> T (in dbSNP:rs61748181).
{ECO:0000269|PubMed:15814878}.
/FTId=VAR_036864.
VARIANT 299 299 V -> M (associated with acute myeloid
leukemia; dbSNP:rs756624928).
{ECO:0000269|PubMed:19147845,
ECO:0000269|PubMed:19760749}.
/FTId=VAR_062781.
VARIANT 412 412 H -> Y (in PFBMFT1, AA and DKCB4; severe
and moderate; associated with
susceptibility to acute myelogenous
leukemia; the mutant protein has 36%
residual activity; dbSNP:rs34094720).
{ECO:0000269|PubMed:15814878,
ECO:0000269|PubMed:18042801,
ECO:0000269|PubMed:19147845,
ECO:0000269|PubMed:19760749,
ECO:0000269|Ref.7}.
/FTId=VAR_025149.
VARIANT 441 441 Missing (in AA; associated with
susceptibility to acute myeloid
leukemia). {ECO:0000269|PubMed:15814878,
ECO:0000269|PubMed:19147845,
ECO:0000269|PubMed:19760749}.
/FTId=VAR_036865.
VARIANT 522 522 R -> K (associated with acute myeloid
leukemia). {ECO:0000269|PubMed:19147845,
ECO:0000269|PubMed:19760749}.
/FTId=VAR_062782.
VARIANT 570 570 K -> N (in AA; abolishes telomerase
catalytic activity but no effect on
binding to TERC).
{ECO:0000269|PubMed:16990594,
ECO:0000269|PubMed:19760749}.
/FTId=VAR_062536.
VARIANT 631 631 R -> Q (in AA; dbSNP:rs199422294).
{ECO:0000269|PubMed:19760749}.
/FTId=VAR_062783.
VARIANT 682 682 G -> D (in AA; non-severe; abolishes
telomerase catalytic activity but little
effect on binding to TERC;
dbSNP:rs199422295).
{ECO:0000269|PubMed:16627250,
ECO:0000269|PubMed:16990594}.
/FTId=VAR_062537.
VARIANT 694 694 V -> M (in PFBMFT1 and AA; moderate;
dbSNP:rs121918662).
{ECO:0000269|PubMed:15814878,
ECO:0000269|PubMed:19760749}.
/FTId=VAR_036866.
VARIANT 704 704 P -> S (in DKCB4; the mutant protein has
13% residual activity;
dbSNP:rs199422297).
{ECO:0000269|PubMed:18042801}.
/FTId=VAR_068793.
VARIANT 716 716 A -> T (in PFBMFT1; the mutant protein is
demonstrated to cause severely
compromised telomerase activity;
dbSNP:rs387907249).
{ECO:0000269|PubMed:21436073}.
/FTId=VAR_068794.
VARIANT 721 721 P -> R (in DKCB4; no effect on telomerase
catalytic activity and little effect on
binding to TERC; dbSNP:rs199422299).
{ECO:0000269|PubMed:16332973,
ECO:0000269|PubMed:16990594}.
/FTId=VAR_062538.
VARIANT 726 726 T -> M (in AA; very severe; no effect on
telomerase catalytic activity but
shortened telomeres; dbSNP:rs149566858).
{ECO:0000269|PubMed:16627250,
ECO:0000269|PubMed:16990594}.
/FTId=VAR_062539.
VARIANT 772 772 Y -> C (in PFBMFT1; moderate;
dbSNP:rs121918663).
{ECO:0000269|PubMed:15814878}.
/FTId=VAR_036867.
VARIANT 785 785 P -> L (in AA).
{ECO:0000269|PubMed:19760749}.
/FTId=VAR_062784.
VARIANT 791 791 V -> I (in PFBMFT1; associated with Met-
867 in cis on the same allele; the double
mutant shows severe defects in telomere
repeat addition processivity;
dbSNP:rs141425941).
{ECO:0000269|PubMed:21483807}.
/FTId=VAR_068795.
VARIANT 811 811 R -> C (in DKCB4; 50% reduction in
telomerase activity; dbSNP:rs199422301).
{ECO:0000269|PubMed:17785587}.
/FTId=VAR_062540.
VARIANT 841 841 L -> F (in PFBMFT1).
{ECO:0000269|PubMed:21436073}.
/FTId=VAR_068796.
VARIANT 865 865 R -> H (in PFBMFT1; dbSNP:rs121918666).
{ECO:0000269|PubMed:17460043}.
/FTId=VAR_036868.
VARIANT 867 867 V -> M (in PFBMFT1; associated with Ile-
791 in cis on the same allele; the double
mutant shows severe defects in telomere
repeat addition processivity; this
mutation causes most if not all of the
functional defects; dbSNP:rs201159197).
{ECO:0000269|PubMed:21483807}.
/FTId=VAR_068797.
VARIANT 901 901 R -> W (in DKCB4; severe phenotype
overlapping with Hoyeraal-Hreidarsson
syndrome; very short telomeres and
greatly reduced telomerase activity;
dbSNP:rs199422304).
{ECO:0000269|PubMed:17785587}.
/FTId=VAR_062541.
VARIANT 902 902 K -> N (in DKCA2; abolishes telomerase
catalytic activity but no effect on
binding to TERC; dbSNP:rs121918665).
{ECO:0000269|PubMed:16247010,
ECO:0000269|PubMed:16990594}.
/FTId=VAR_036869.
VARIANT 902 902 K -> R (in PFBMFT1; dbSNP:rs387907250).
{ECO:0000269|PubMed:21436073}.
/FTId=VAR_068798.
VARIANT 923 923 P -> L (in PFBMFT1; dbSNP:rs387907251).
{ECO:0000269|PubMed:22512499}.
/FTId=VAR_068799.
VARIANT 948 948 S -> R (in dbSNP:rs34062885).
/FTId=VAR_053726.
VARIANT 979 979 R -> W (in DKCA2; shortened telomeres but
no effect on telomerase catalytic
activity nor on binding to TERC;
dbSNP:rs199422305).
{ECO:0000269|PubMed:15885610,
ECO:0000269|PubMed:16990594}.
/FTId=VAR_062542.
VARIANT 1025 1025 V -> F (in PFBMFT1).
{ECO:0000269|PubMed:21436073}.
/FTId=VAR_068800.
VARIANT 1062 1062 A -> T (increased incidence in sporadic
acute myeloid leukemia;
dbSNP:rs35719940).
{ECO:0000269|PubMed:15814878,
ECO:0000269|PubMed:19147845,
ECO:0000269|PubMed:19760749,
ECO:0000269|Ref.7}.
/FTId=VAR_025150.
VARIANT 1090 1090 V -> M (in PFBMFT1; severe;
dbSNP:rs121918664).
{ECO:0000269|PubMed:15814878}.
/FTId=VAR_036870.
VARIANT 1110 1110 T -> M (in idiopathic pulmonary fibrosis
susceptibility; impaired telomerase
activity; dbSNP:rs199422306).
{ECO:0000269|PubMed:17392301}.
/FTId=VAR_062543.
VARIANT 1127 1127 F -> L (in DKCA2; severe; shortened
telomeres but no effect on telomerase
catalytic activity nor on binding to
TERC). {ECO:0000269|PubMed:15885610,
ECO:0000269|PubMed:16990594}.
/FTId=VAR_062544.
MUTAGEN 137 141 WGLLL->AAAAA: Reduced catalytic activity
and repeat addition processivity.
Complete loss of catalytic activity but
no loss of binding to telomeric primers;
when associated with 930-A--A-934.
{ECO:0000269|PubMed:17296728}.
MUTAGEN 169 169 Q->A: About 80% loss of enzymatic
activity. Greatly reduced incorporation
of second nucleotide. Altered strength of
binding to ssDNA. Little effect on repeat
addition processivity, nor on TR
interaction nor on protein levels.
{ECO:0000269|PubMed:19777057}.
MUTAGEN 169 169 Q->N: About 85% loss of enzymatic
activity. Greatly reduced incorporation
of second nucleotide. Altered strength of
binding to ssDNA. No effect on protein
levels nor on TR interaction.
{ECO:0000269|PubMed:19777057}.
MUTAGEN 169 169 Q->T: About 90% loss of enzymatic
activity. Greatly reduced incorporation
of second nucleotide. Altered strength of
binding to ssDNA. No effect on protein
levels nor on TR interaction.
{ECO:0000269|PubMed:19777057}.
MUTAGEN 457 457 S->A: Abolishes phosphorylation by DYRK2.
{ECO:0000269|PubMed:23362280}.
MUTAGEN 547 547 W->A: Defective in high-affinity TERC
interactions.
{ECO:0000269|PubMed:15082768}.
MUTAGEN 631 631 R->A: Abolishes telomerase catalytic
activity. {ECO:0000269|PubMed:17026956}.
MUTAGEN 707 707 Y->F: Abolishes oxidative stress-induced
phosphorylation and RAN binding. Impaired
nuclear export and enhanced antiapoptotic
activity against ROS-dependent apoptosis
induction. Impaired interaction with
PTPN11. No dephosphorylation by PTPN11.
{ECO:0000269|PubMed:12808100,
ECO:0000269|PubMed:18829466}.
MUTAGEN 712 712 D->A: Loss of telomerase activity. In the
absence of TR, no loss of binding to
telomeric primers.
{ECO:0000269|PubMed:17026956,
ECO:0000269|PubMed:17296728,
ECO:0000269|PubMed:9389643,
ECO:0000269|PubMed:9443919}.
MUTAGEN 866 866 L->Y: Moderate reduction in telomerase
activity, no change in repeat extension
rate nor on nucleotide incorporation
fidelity. Little further reduction in
activity but 13.5-fold increase in
nucleotide incorporation fidelity; when
associated with M-867.
{ECO:0000269|PubMed:17264120}.
MUTAGEN 867 867 V->A: About 75% reduction in telomerase
activity, about 80% reduction in repeat
reduction rate and 3.9-fold increase in
nucleotide incorporation fidelity.
{ECO:0000269|PubMed:17264120}.
MUTAGEN 867 867 V->M: About 75% reduction in telomerase
activity, about 50% reduction in repeat
extension rate and 5.2-fold increase in
nucleotide incorporation fidelity. Little
further reduction in activity and 13.5-
fold increase in nucleotide incorporation
fidelity; when associated with Y-866.
{ECO:0000269|PubMed:17264120}.
MUTAGEN 867 867 V->T: Severe reduction in telomerase
activity, about 50% reduction in repeat
extension rate and 2.2-fold increase in
nucleotide incorporation fidelity. No
further reduction in activity but 2.8-
fold increase in nucleotide incorporation
fidelity; when associated with Y-866.
{ECO:0000269|PubMed:17264120}.
MUTAGEN 868 869 DD->AA: Loss of telomerase activity.
MUTAGEN 868 868 D->A: Loss of telomerase activity.
{ECO:0000269|PubMed:15082768,
ECO:0000269|PubMed:15857955,
ECO:0000269|PubMed:17026956,
ECO:0000269|PubMed:9389643,
ECO:0000269|PubMed:9443919}.
MUTAGEN 869 869 D->A: Loss of telomerase activity.
{ECO:0000269|PubMed:9389643,
ECO:0000269|PubMed:9443919}.
MUTAGEN 930 934 WCGLL->AAAAA: Completely abolishes
telomerase-mediated primer extension and
reduced binding to short telomeric
primers. Complete loss of catalytic
activity but no further loss of binding
to telomeric primers; when associated
with 137-A--A-141.
{ECO:0000269|PubMed:17296728}.
CONFLICT 516 516 D -> G (in Ref. 1; AAC51724).
{ECO:0000305}.
HELIX 966 983 {ECO:0000244|PDB:5UGW}.
HELIX 984 986 {ECO:0000244|PDB:5UGW}.
TURN 989 991 {ECO:0000244|PDB:5UGW}.
HELIX 994 1017 {ECO:0000244|PDB:5UGW}.
HELIX 1025 1027 {ECO:0000244|PDB:5UGW}.
HELIX 1029 1050 {ECO:0000244|PDB:5UGW}.
TURN 1051 1053 {ECO:0000244|PDB:5UGW}.
HELIX 1067 1082 {ECO:0000244|PDB:5UGW}.
HELIX 1083 1085 {ECO:0000244|PDB:5UGW}.
HELIX 1086 1104 {ECO:0000244|PDB:5UGW}.
HELIX 1111 1118 {ECO:0000244|PDB:5UGW}.
SEQUENCE 1132 AA; 126997 MW; 94E35469C4CA33A0 CRC64;
MPRAPRCRAV RSLLRSHYRE VLPLATFVRR LGPQGWRLVQ RGDPAAFRAL VAQCLVCVPW
DARPPPAAPS FRQVSCLKEL VARVLQRLCE RGAKNVLAFG FALLDGARGG PPEAFTTSVR
SYLPNTVTDA LRGSGAWGLL LRRVGDDVLV HLLARCALFV LVAPSCAYQV CGPPLYQLGA
ATQARPPPHA SGPRRRLGCE RAWNHSVREA GVPLGLPAPG ARRRGGSASR SLPLPKRPRR
GAAPEPERTP VGQGSWAHPG RTRGPSDRGF CVVSPARPAE EATSLEGALS GTRHSHPSVG
RQHHAGPPST SRPPRPWDTP CPPVYAETKH FLYSSGDKEQ LRPSFLLSSL RPSLTGARRL
VETIFLGSRP WMPGTPRRLP RLPQRYWQMR PLFLELLGNH AQCPYGVLLK THCPLRAAVT
PAAGVCAREK PQGSVAAPEE EDTDPRRLVQ LLRQHSSPWQ VYGFVRACLR RLVPPGLWGS
RHNERRFLRN TKKFISLGKH AKLSLQELTW KMSVRDCAWL RRSPGVGCVP AAEHRLREEI
LAKFLHWLMS VYVVELLRSF FYVTETTFQK NRLFFYRKSV WSKLQSIGIR QHLKRVQLRE
LSEAEVRQHR EARPALLTSR LRFIPKPDGL RPIVNMDYVV GARTFRREKR AERLTSRVKA
LFSVLNYERA RRPGLLGASV LGLDDIHRAW RTFVLRVRAQ DPPPELYFVK VDVTGAYDTI
PQDRLTEVIA SIIKPQNTYC VRRYAVVQKA AHGHVRKAFK SHVSTLTDLQ PYMRQFVAHL
QETSPLRDAV VIEQSSSLNE ASSGLFDVFL RFMCHHAVRI RGKSYVQCQG IPQGSILSTL
LCSLCYGDME NKLFAGIRRD GLLLRLVDDF LLVTPHLTHA KTFLRTLVRG VPEYGCVVNL
RKTVVNFPVE DEALGGTAFV QMPAHGLFPW CGLLLDTRTL EVQSDYSSYA RTSIRASLTF
NRGFKAGRNM RRKLFGVLRL KCHSLFLDLQ VNSLQTVCTN IYKILLLQAY RFHACVLQLP
FHQQVWKNPT FFLRVISDTA SLCYSILKAK NAGMSLGAKG AAGPLPSEAV QWLCHQAFLL
KLTRHRVTYV PLLGSLRTAQ TQLSRKLPGT TLTALEAAAN PALPSDFKTI LD


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