Telomerase reverse transcriptase (Protein name
), TERT_HUMAN from NCBI database.
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Gene name:
TERT(EST2;TCS1;TRT);
Protein name:
Telomerase reverse transcriptase;
Alternative:
Telomerase catalytic subunit;HEST2;Telomerase-associated protein 2(TP2);
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
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.
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.
Subcellular Location:
Nucleus
nucleolus
Nucleus
nucleoplasm
Nucleus
Chromosome
telomere
Cytoplasm
Nucleus
PML body
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.
"Sequence of a BAC carrying the entire hTERT gene." Londono-Vallejo J.A.
Submitted (2001-10) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]
7.
NIEHS SNPs program
Submitted (2005-10) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANTS TYR-412 AND THR-1062
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Cited for: FUNCTION IN TELOMERASE ACTIVITY;TISSUE SPECIFICITY;ASSOCIATION WITH TEP1;MUTAGENESIS OF ASP-712; ASP-868 AND ASP-869
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Cited for: RECONSTITUTION OF THE TELOMERASE COMPLEX;MUTAGENESIS OF ASP-712; ASP-868 AND ASP-869
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Cited for: PHOSPHORYLATION AT TYR-707;SUBCELLULAR LOCATION;INTERACTION WITH RAN AND XP01;MUTAGENESIS OF TYR-707
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Cited for: FUNCTIONAL DOMAINS;MUTAGENESIS OF TRP-547 AND ASP-868
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Cited for: FUNCTION;MUTAGENESIS OF ARG-631; ASP-712 AND ASP-868
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Cited for: FUNCTION;DNA-BINDING;MUTAGENESIS OF 137-TRP--LEU-141; ASP-712 AND 930-TRP--LEU-934
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Cited for: INTERACTION WITH PTPN11;PHOSPHORYLATION AT TYR-707;SUBCELLULAR LOCATION;MUTAGENESIS OF TYR-707
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Cited for: FUNCTION;SUBCELLULAR LOCATION;INTERACTION WITH PML
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Cited for: IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX
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Cited for: PHOSPHORYLATION AT SER-227;SUBCELLULAR LOCATION;NUCLEAR LOCALIZATION SIGNAL
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Cited for: PHOSPHORYLATION AT SER-457;UBIQUITINATION;MUTAGENESIS OF SER-457
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Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 461-469 IN COMPLEX WITH CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX (MHC)
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Cited for: VARIANT AA SUSCEPTIBILITY THR-202;VARIANTS DKCA2 TRP-979 AND LEU-1127;CHARACTERIZATION OF VARIANT AA SUSCEPTIBILTY THR-202;CHARACTERIZATION OF VARIANTS DKCA2 TRP-979 AND LEU-1127
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Cited for: VARIANTS PFBMFT1 THR-202; TYR-412; MET-694; CYS-772 AND MET-1090;VARIANTS THR-279; GLU-441 DEL AND THR-1062
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Cited for: VARIANT DKCA2 ASN-902;CHARACTERIZATION OF VARIANT DKCA2 ASN-902
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Cited for: VARIANTS AA SUSCEPTIBILITY ASP-682 AND MET-726;CHARACTERIZATION OF MET-726
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Cited for: VARIANT AA SUSCEPTIBILITY ASN-570;CHARACTERIZATION OF VARIANTS ASN-570; ASP-682; ARG-721; MET-726; ASN-902; TRP-979 AND LEU-1127
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Cited for: VARIANTS DKCB4 CYS-811 AND TRP-901;CHARACTERIZATION OF VARIANTS DKCB4 CYS-811 AND TRP-901
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Cited for: VARIANTS IDIOPATHIC PULMONARY FIBROSIS SUSCEPTIBILITY GLN-55 AND MET-1110;CHARACTERIZATION OF VARIANTS GLN-55 AND MET-1110
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Cited for: VARIANTS DKCB4 TYR-412 AND SER-704;CHARACTERIZATION OF VARIANTS DKCB4 TYR-412 AND SER-704
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Cited for: VARIANTS ALA-65; MET-299; LYS-522 AND THR-1062;VARIANTS AA SUSCEPTIBILITY THR-202; TYR-412; GLU-441 DEL; ASN-570; GLN-631; MET-694 AND LEU-785
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Cited for: VARIANTS ALA-65; MET-299; TYR-412; GLU-441 DEL; LYS-522 AND THR-1062
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Cited for: VARIANTS PFBMFT1 MET-170; THR-716; PHE-841; ARG-902 AND PHE-1025;CHARACTERIZATION OF VARIANTS PFBMFT1 MET-170; THR-716; PHE-841 AND PHE-1025
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Cited for: VARIANTS PFBMFT1 ILE-791 AND MET-867;CHARACTERIZATION OF VARIANTS PFBMFT1 ILE-791 AND MET-867