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Q673L6

- TERT_RAT

UniProt

Q673L6 - TERT_RAT

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Protein

Telomerase reverse transcriptase

Gene

Tert

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

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
Complete GO annotation...

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-KW
  2. cytoplasm Source: RGD
  3. nucleus Source: RGD
  4. PML body Source: Ensembl
  5. telomerase holoenzyme complex Source: Ensembl
Complete GO annotation...

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

        10         20         30         40         50
MPRAPRCPAV RSLLRSRYRE VWPLATFVRR LGLEGSRLVQ PGDPKVFRTL
60 70 80 90 100
VAQCLVCVPW GSQPPPADLS FHQVSSLKEL VSRVVQKLCE RGERNVLAFG
110 120 130 140 150
FALLNGARGG PPMAFTTSVH SYLPNSVTES LCVSGAWMLL LSRVGDDLLV
160 170 180 190 200
YLLSHCALYL LVPPSCAYQV CGSPLYQICA TTDTWSSVPA GYRPTRPVGG
210 220 230 240 250
NFTNLGSAHQ IKNSGHQEAP KPQALPSRGT KRLLSLTSTN VPSAKKARFE
260 270 280 290 300
PALRVDKGPH RQVVPTPSGK TWAPSPAASP KVPPAAKNLS LKGKASDPSL
310 320 330 340 350
SGSVCCKHKP SSSSLLSSPP QDAEKLRPFT ETRHFLYSRG GGQEELNPSF
360 370 380 390 400
LLNSLPPSLT GARRLVEIIF LGSRPRTSGP FCRTRRLPRR YWQMRPLFQQ
410 420 430 440 450
LLMNHAKCQY VRFLRSHCRF RTANQRVPDA MDTSPSHLTS LLRLHSSPWQ
460 470 480 490 500
VYGFLRACLR ELVPAGLWGT RHNERRFLKN VKKFISLGKY AKLSLQELMW
510 520 530 540 550
RVKVEDCHWL RSSPEKDTVP AAEHRLRERI LAMFLFWLMD TYVVQLLRSF
560 570 580 590 600
FYITETTFQK NRLFFYRKSV WSKLQSIGIR QQLERVQLRE LSQEEVKHHQ
610 620 630 640 650
DTWLAMPICR LRFIPKLNGL RPIVNMSYGM DTRAFGKKKQ TQCFTQSLKT
660 670 680 690 700
LFSVLNYERT KHPNLMGASV LGTSDSYRIW RTFVLRVRAL DQTPRMYFVK
710 720 730 740 750
ADVTGAYDAI PQDKLVEIVA NIIRRSESMY CIRQYAVVQK DSQGQVHKSF
760 770 780 790 800
RRQVSTLSDL QPYMGQFTKH LQDSDASALR NSVVIEQSIS MNETGSSLLH
810 820 830 840 850
FFLRFVRHSV VKIDGRFYVQ CQGIPQGSSL STLLCSLCFG DMENKLFAEV
860 870 880 890 900
QQDGLLLRFV DDFLLVTPHL AHAKAFLSTL VHGVPEYGCM INLQKTVVNF
910 920 930 940 950
PVETGALGGA APHQLPAHCL FPWCGLLLDT RTLEVFCDYS GYGRTSIKMS
960 970 980 990 1000
LTFQGVSRAG KTMRYKLLSV LRLKCHGLFL DLQVNSLQTV CINIYKIFLL
1010 1020 1030 1040 1050
QAYRFHACVI RLPFGQHVRK NHAFFLGIIS NLASCCYAIL KVKNPGVSLR
1060 1070 1080 1090 1100
AKGAPGSFPP EATRWLCYQA FLLKLAAHSV TYKCLLGPLR TAQKQLCRKL
1110 1120
PEATMTLLKT AADPALSTDF QTILD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

Chemistry

ChEMBLi CHEMBL3108654.

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

« Hide 'large scale' publications
  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 29, 2014
This is version 81 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