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Q27ID4

- TERT_BOVIN

UniProt

Q27ID4 - TERT_BOVIN

Protein

Telomerase reverse transcriptase

Gene

TERT

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 2 (02 May 2006)
      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 bindingi705 – 7051Magnesium; 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. RNA binding Source: InterPro
    4. telomeric template RNA reverse transcriptase activity Source: InterPro

    Keywords - Molecular functioni

    Nucleotidyltransferase, Ribonucleoprotein, RNA-directed DNA polymerase, Transferase

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Telomerase reverse transcriptase (EC:2.7.7.49)
    Alternative name(s):
    Telomerase catalytic subunit
    Gene namesi
    Name:TERT
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    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-700. 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: UniProtKB-SubCell
    3. nucleolus Source: UniProtKB-SubCell
    4. PML body Source: UniProtKB-SubCell
    5. ribonucleoprotein complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus, Telomere

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11251125Telomerase reverse transcriptasePRO_0000245166Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei231 – 2311Phosphoserine; by PKB/AKT1By similarity
    Modified residuei450 – 4501Phosphoserine; by DYRK2By similarity
    Modified residuei700 – 7001Phosphotyrosine; by SRC-type Tyr-kinasesBy similarity

    Post-translational modificationi

    Phosphorylation at Tyr-700 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-231 by the AKT pathway promotes nuclear location. Phosphorylation at the G2/M phase at Ser-450 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-450 by DYRK2. Ubiquitinated leads to proteasomal degradation By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ27ID4.

    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

    Structurei

    3D structure databases

    ProteinModelPortaliQ27ID4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini598 – 928331Reverse transcriptasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 234234RNA-interacting domain 1By similarityAdd
    BLAST
    Regioni58 – 199142GQ motifBy similarityAdd
    BLAST
    Regioni137 – 1415Required for regulating specificity for telomeric DNA and for processivity for primer elongationBy similarity
    Regioni235 – 31278LinkerBy similarityAdd
    BLAST
    Regioni290 – 531242Required for oligomerizationBy similarityAdd
    BLAST
    Regioni313 – 543231RNA-interacting domain 2By similarityAdd
    BLAST
    Regioni364 – 514151QFP motifBy similarityAdd
    BLAST
    Regioni385 – 40521CP motifBy similarityAdd
    BLAST
    Regioni907 – 92115Required for oligomerizationBy similarityAdd
    BLAST
    Regioni923 – 9275Primer grip sequenceBy similarity
    Regioni929 – 1125197CTEBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi226 – 24419Bipartite nuclear localization signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi180 – 1856Poly-Ala

    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.
    HOGENOMiHOG000148780.
    HOVERGENiHBG000460.
    InParanoidiQ27ID4.
    KOiK11126.

    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.

    Q27ID4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRAPRCRAV RALLRASYRQ VLPLAAFVRR LRPQGHRLVR RGDPAAFRAL     50
    VAQCLVCVPW DAQPPPAAPS FRQVSCLKEL VARVVQRLCE RGARNVLAFG 100
    FTLLAGARGG PPVAFTTSVR SYLPNTVTDT LRGSGAWGLL LHRVGDDVLT 150
    HLLSRCALYL LVPPTCAYQV CGPPLYDLRA AAAAARRPTR QVGGTRAGFG 200
    LPRPASSNGG HGEAEGLLEA RAQGARRRRS SARGRLPPAK RPRRGLEPGR 250
    DLEGQVARSP PRVVTPTRDA AEAKSRKGDV PGPCRLFPGG ERGVGSASWR 300
    LSPSEGEPGA GACAETKRFL YCSGGGEQLR RSFLLCSLPP SLAGARTLVE 350
    TIFLDSKPGP PGAPRRPRRL PARYWQMRPL FRKLLGNHAR SPYGALLRAH 400
    CPLPASAPRA GPDHQKCPGV GGCPSERPAA APEGEANSGR LVQLLRQHSS 450
    PWQVYGLLRA CLRRLVPAGL WGSRHNERRF LRNVKKLLSL GKHGRLSQQE 500
    LTWKMKVQDC AWLRASPGAR CVPAAEHRQR EAVLGRFLHW LMGAYVVELL 550
    RSFFYVTETT FQKNRLFFFR KRIWSQLQRL GVRQHLDRVR LRELSEAEVR 600
    QHQEARPALL TSRLRFVPKP GGLRPIVNVG CVEGAPAPPR DKKVQHLSSR 650
    VKTLFAVLNY ERARRPGLLG ASVLGMDDIH RAWRAFVLPL RARGPAPPLY 700
    FVKVDVVGAY DALPQDKLAE VIANVLQPQE NTYCVRHCAM VRTARGRMRK 750
    SFKRHVSTFS DFQPYLRQLV EHLQAMGSLR DAVVIEQSCS LNEPGSSLFN 800
    LFLHLVRSHV IRIGGRSYIQ CQGIPQGSIL STLLCSFCYG DMENKLFPGV 850
    QQDGVLLRLV DDFLLVTPHL TRARDFLRTL VRGVPEYGCQ VNLRKTVVNF 900
    PVEPGALGGA APLQLPAHCL FPWCGLLLDT RTLEVHGDHS SYARTSIRAS 950
    LTFTQGFKPG RNMRRKLLAV LQLKCHGLFL DLQVNSLQTV FTNVYKIFLL 1000
    QAYRFHACVL QLPFSQPVRS SPAFFLQVIA DTASRGYALL KARNAGASLG 1050
    ARGAAGLFPS EAAQWLCLHA FLLKLARHRV TYSRLLGALR TARARLHRQL 1100
    PGPTRAALEA AADPALTADF KTILD 1125
    Length:1,125
    Mass (Da):124,447
    Last modified:May 2, 2006 - v2
    Checksum:i717F437B50BB747B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ399842 Genomic DNA. Translation: ABD61652.2.
    RefSeqiNP_001039707.1. NM_001046242.1.
    UniGeneiBt.60929.

    Genome annotation databases

    GeneIDi518884.
    KEGGibta:518884.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ399842 Genomic DNA. Translation: ABD61652.2 .
    RefSeqi NP_001039707.1. NM_001046242.1.
    UniGenei Bt.60929.

    3D structure databases

    ProteinModelPortali Q27ID4.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q27ID4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 518884.
    KEGGi bta:518884.

    Organism-specific databases

    CTDi 7015.

    Phylogenomic databases

    eggNOGi NOG276584.
    HOGENOMi HOG000148780.
    HOVERGENi HBG000460.
    InParanoidi Q27ID4.
    KOi K11126.

    Miscellaneous databases

    NextBioi 20872758.

    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. "Cloning and expression of the reverse transcriptase component of Bos taurus telomerase."
      Zhao D., Du Z., Li N.
      Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiTERT_BOVIN
    AccessioniPrimary (citable) accession number: Q27ID4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: May 2, 2006
    Last modified: October 1, 2014
    This is version 57 of the entry and version 2 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