Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O70372

- TERT_MOUSE

UniProt

O70372 - TERT_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Telomerase reverse transcriptase

Gene

Tert

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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. telomerase activity Source: MGI
  4. telomeric RNA binding Source: Ensembl
  5. telomeric template RNA reverse transcriptase activity Source: InterPro

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_216539. 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:Tert
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1202709. Tert.

Subcellular locationi

Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity. Nucleus. 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: UniProtKB-KW
  3. PML body Source: Ensembl
  4. 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 – 11221122Telomerase reverse transcriptasePRO_0000054926Add
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 by the AKT pathway promotes nuclear location. 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

PaxDbiO70372.
PRIDEiO70372.

PTM databases

PhosphoSiteiO70372.

Expressioni

Tissue specificityi

High activity in intestine, liver and testis, moderate in lung, very low in muscle, heart and brain.3 Publications

Developmental stagei

Highest levels in midgestational stages, E9.5 to E15.5.1 Publication

Gene expression databases

BgeeiO70372.
CleanExiMM_TERT.
ExpressionAtlasiO70372. baseline and differential.
GenevestigatoriO70372.

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 similarity3 Publications

Protein-protein interaction databases

BioGridi204118. 1 interaction.
DIPiDIP-60451N.

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 – 1122194CTEBy 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

Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG276584.
GeneTreeiENSGT00390000018531.
HOGENOMiHOG000148780.
HOVERGENiHBG000460.
InParanoidiO70372.
KOiK11126.
OMAiRACFYAT.
OrthoDBiEOG744TB3.
PhylomeDBiO70372.
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]

Sequencei

Sequence statusi: Complete.

O70372-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTRAPRCPAV RSLLRSRYRE VWPLATFVRR LGPEGRRLVQ PGDPKIYRTL
60 70 80 90 100
VAQCLVCMHW GSQPPPADLS FHQVSSLKEL VARVVQRLCE RNERNVLAFG
110 120 130 140 150
FELLNEARGG PPMAFTSSVR SYLPNTVIET LRVSGAWMLL LSRVGDDLLV
160 170 180 190 200
YLLAHCALYL LVPPSCAYQV CGSPLYQICA TTDIWPSVSA SYRPTRPVGR
210 220 230 240 250
NFTNLRFLQQ IKSSSRQEAP KPLALPSRGT KRHLSLTSTS VPSAKKARCY
260 270 280 290 300
PVPRVEEGPH RQVLPTPSGK SWVPSPARSP EVPTAEKDLS SKGKVSDLSL
310 320 330 340 350
SGSVCCKHKP SSTSLLSPPR QNAFQLRPFI ETRHFLYSRG DGQERLNPSF
360 370 380 390 400
LLSNLQPNLT GARRLVEIIF LGSRPRTSGP LCRTHRLSRR YWQMRPLFQQ
410 420 430 440 450
LLVNHAECQY VRLLRSHCRF RTANQQVTDA LNTSPPHLMD LLRLHSSPWQ
460 470 480 490 500
VYGFLRACLC KVVSASLWGT RHNERRFFKN LKKFISLGKY GKLSLQELMW
510 520 530 540 550
KMKVEDCHWL RSSPGKDRVP AAEHRLRERI LATFLFWLMD TYVVQLLRSF
560 570 580 590 600
FYITESTFQK NRLFFYRKSV WSKLQSIGVR QHLERVRLRE LSQEEVRHHQ
610 620 630 640 650
DTWLAMPICR LRFIPKPNGL RPIVNMSYSM GTRALGRRKQ AQHFTQRLKT
660 670 680 690 700
LFSMLNYERT KHPHLMGSSV LGMNDIYRTW RAFVLRVRAL DQTPRMYFVK
710 720 730 740 750
ADVTGAYDAI PQGKLVEVVA NMIRHSESTY CIRQYAVVRR DSQGQVHKSF
760 770 780 790 800
RRQVTTLSDL QPYMGQFLKH LQDSDASALR NSVVIEQSIS MNESSSSLFD
810 820 830 840 850
FFLHFLRHSV VKIGDRCYTQ CQGIPQGSSL STLLCSLCFG DMENKLFAEV
860 870 880 890 900
QRDGLLLRFV DDFLLVTPHL DQAKTFLSTL VHGVPEYGCM INLQKTVVNF
910 920 930 940 950
PVEPGTLGGA APYQLPAHCL FPWCGLLLDT QTLEVFCDYS GYAQTSIKTS
960 970 980 990 1000
LTFQSVFKAG KTMRNKLLSV LRLKCHGLFL DLQVNSLQTV CINIYKIFLL
1010 1020 1030 1040 1050
QAYRFHACVI QLPFDQRVRK NLTFFLGIIS SQASCCYAIL KVKNPGMTLK
1060 1070 1080 1090 1100
ASGSFPPEAA HWLCYQAFLL KLAAHSVIYK CLLGPLRTAQ KLLCRKLPEA
1110 1120
TMTILKAAAD PALSTDFQTI LD
Length:1,122
Mass (Da):127,978
Last modified:August 1, 1998 - v1
Checksum:iF85266905DD6558C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti553 – 5531I → V in AAB84200. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF051911 mRNA. Translation: AAC09323.1.
AF073311 mRNA. Translation: AAC34821.1.
AF247818 mRNA. Translation: AAF62177.1.
AF029235 mRNA. Translation: AAB84200.1.
CCDSiCCDS26633.1.
RefSeqiNP_033380.1. NM_009354.1.
UniGeneiMm.10109.

Genome annotation databases

EnsembliENSMUST00000022104; ENSMUSP00000022104; ENSMUSG00000021611.
GeneIDi21752.
KEGGimmu:21752.
UCSCiuc007rdq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF051911 mRNA. Translation: AAC09323.1 .
AF073311 mRNA. Translation: AAC34821.1 .
AF247818 mRNA. Translation: AAF62177.1 .
AF029235 mRNA. Translation: AAB84200.1 .
CCDSi CCDS26633.1.
RefSeqi NP_033380.1. NM_009354.1.
UniGenei Mm.10109.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204118. 1 interaction.
DIPi DIP-60451N.

PTM databases

PhosphoSitei O70372.

Proteomic databases

PaxDbi O70372.
PRIDEi O70372.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022104 ; ENSMUSP00000022104 ; ENSMUSG00000021611 .
GeneIDi 21752.
KEGGi mmu:21752.
UCSCi uc007rdq.1. mouse.

Organism-specific databases

CTDi 7015.
MGIi MGI:1202709. Tert.

Phylogenomic databases

eggNOGi NOG276584.
GeneTreei ENSGT00390000018531.
HOGENOMi HOG000148780.
HOVERGENi HBG000460.
InParanoidi O70372.
KOi K11126.
OMAi RACFYAT.
OrthoDBi EOG744TB3.
PhylomeDBi O70372.
TreeFami TF329048.

Enzyme and pathway databases

Reactomei REACT_216539. formation of the beta-catenin:TCF transactivating complex.

Miscellaneous databases

NextBioi 301049.
PROi O70372.
SOURCEi Search...

Gene expression databases

Bgeei O70372.
CleanExi MM_TERT.
ExpressionAtlasi O70372. baseline and differential.
Genevestigatori O70372.

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. "Expression of mouse telomerase reverse transcriptase during development, differentiation and proliferation."
    Greenberg R.A., Allsopp R.C., Chin L., Morin G.B., DePinho R.A.
    Oncogene 16:1723-1730(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, TISSUE SPECIFICITY.
  2. "Expression of mouse telomerase catalytic subunit in embryos and adult tissues."
    Martin-Rivera L., Herrera E., Albar J.P., Blasco M.A.
    Proc. Natl. Acad. Sci. U.S.A. 95:10471-10476(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "Cloning of rat telomerase catalytic subunit functional domains, reconstitution of telomerase activity and enzymatic profile of pig and chicken tissues."
    Wong S.C., Ong L.L., Er C.P., Gao S., Yu H., So J.B.
    Life Sci. 73:2749-2760(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 548-1122, TISSUE SPECIFICITY.
  4. "Partial sequence of Mus musculus telomerase catalytic subunit homolog."
    Drissi R., Cleveland J.L.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 550-616.
  5. "Murine Pif1 interacts with telomerase and is dispensable for telomere function in vivo."
    Snow B.E., Mateyak M., Paderova J., Wakeham A., Iorio C., Zakian V., Squire J., Harrington L.
    Mol. Cell. Biol. 27:1017-1026(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIF1, FUNCTION.
  6. "GNL3L stabilizes the TRF1 complex and promotes mitotic transition."
    Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.
    J. Cell Biol. 185:827-839(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GNL3L.
  7. Cited for: INTERACTION WITH SMARCA4, FUNCTION.

Entry informationi

Entry nameiTERT_MOUSE
AccessioniPrimary (citable) accession number: O70372
Secondary accession number(s): O35432, Q9JK99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: October 29, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to originate from rat.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3