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Q27ID4

- TERT_BOVIN

UniProt

Q27ID4 - TERT_BOVIN

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Protein

Telomerase reverse transcriptase

Gene
TERT
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

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.

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

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 template By similarity
Metal bindingi705 – 7051Magnesium; catalytic By similarity
Sitei860 – 8601Required for nucleotide incorporation and primer extension rate By similarity
Metal bindingi861 – 8611Magnesium; catalytic By similarity
Metal bindingi862 – 8621Magnesium; catalytic By similarity

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
Complete GO annotation...

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.

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
Complete GO annotation...

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/AKT1 By similarity
Modified residuei450 – 4501Phosphoserine; by DYRK2 By similarity
Modified residuei700 – 7001Phosphotyrosine; by SRC-type Tyr-kinases By 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.
Ubiquitinated by the EDVP complex, a E3 ligase complex following phosphorylation at Ser-450 by DYRK2. Ubiquitinated leads to proteasomal degradation 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.

Structurei

3D structure databases

ProteinModelPortaliQ27ID4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini598 – 928331Reverse transcriptaseAdd
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi226 – 24419Bipartite nuclear localization signal By 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.
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

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

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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: March 19, 2014
This is version 56 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

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