Mouse Anti-TERT Recombinant Antibody (CBFYE-1667) (CBMAB-E2336-FY)

Telomerase Reverse Transcriptase

Telomerase is a ribonucleoprotein polymerase that maintains telomere ends by addition of the telomere repeat TTAGGG. The enzyme consists of a protein component with reverse transcriptase activity, encoded by this gene, and an RNA component which serves as a template for the telomere repeat. Telomerase expression plays a role in cellular senescence, as it is normally repressed in postnatal somatic cells resulting in progressive shortening of telomeres. Deregulation of telomerase expression in somatic cells may be involved in oncogenesis. Studies in mouse suggest that telomerase also participates in chromosomal repair, since de novo synthesis of telomere repeats may occur at double-stranded breaks. Alternatively spliced variants encoding different isoforms of telomerase reverse transcriptase have been identified; the full-length sequence of some variants has not been determined. Alternative splicing at this locus is thought to be one mechanism of regulation of telomerase activity.

Telomerase Reverse Transcriptase; Telomerase-Associated Protein 2; Telomerase Catalytic Subunit; EC 2.7.7.49; HEST2; TCS1; EST2; TP2

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.

Biological Process cellular response to hypoxiaSource:BHF-UCL1 Publication
Biological Process DNA biosynthetic processSource:BHF-UCL2 Publications
Biological Process DNA strand elongationSource:BHF-UCL1 Publication
Biological Process establishment of protein localization to telomereSource:BHF-UCL1 Publication
Biological Process mitochondrion organizationSource:BHF-UCL1 Publication
Biological Process negative regulation of cellular senescenceSource:BHF-UCL1 Publication
Biological Process negative regulation of endothelial cell apoptotic processSource:Ensembl
Biological Process negative regulation of extrinsic apoptotic signaling pathway in absence of ligandSource:BHF-UCL1 Publication
Biological Process negative regulation of gene expressionSource:BHF-UCL1 Publication
Biological Process negative regulation of miRNA maturationSource:ARUK-UCL1 Publication
Biological Process negative regulation of neuron apoptotic processSource:Ensembl
Biological Process negative regulation of siRNA productionSource:BHF-UCL1 Publication
Biological Process positive regulation of angiogenesisSource:Ensembl
Biological Process positive regulation of G1/S transition of mitotic cell cycleSource:Ensembl
Biological Process positive regulation of glucose importSource:Ensembl
Biological Process positive regulation of hair cycleSource:BHF-UCL
Biological Process positive regulation of miRNA transcriptionSource:BHF-UCL1 Publication
Biological Process positive regulation of nitric-oxide synthase activitySource:BHF-UCL1 Publication
Biological Process positive regulation of protein bindingSource:BHF-UCL1 Publication
Biological Process positive regulation of protein localization to nucleolusSource:BHF-UCL1 Publication
Biological Process positive regulation of stem cell proliferationSource:BHF-UCL
Biological Process positive regulation of transdifferentiationSource:Ensembl
Biological Process positive regulation of vascular associated smooth muscle cell migrationSource:Ensembl
Biological Process positive regulation of vascular associated smooth muscle cell proliferationSource:Ensembl
Biological Process positive regulation of Wnt signaling pathwaySource:BHF-UCL1 Publication
Biological Process regulation of protein stabilitySource:BHF-UCL2 Publications
Biological Process replicative senescenceSource:BHF-UCL1 Publication
Biological Process response to cadmium ionSource:Ensembl
Biological Process RNA-templated DNA biosynthetic processSource:BHF-UCL1 Publication
Biological Process RNA-templated transcriptionSource:BHF-UCL1 Publication
Biological Process siRNA processingSource:BHF-UCL1 Publication
Biological Process siRNA transcriptionSource:BHF-UCL1 Publication
Biological Process telomere maintenanceSource:UniProtKB1 Publication
Biological Process telomere maintenance via telomeraseSource:UniProtKB1 Publication

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.

Aplastic anemia (AA):
A form of anemia in which the bone marrow fails to produce adequate numbers of peripheral blood elements. It is characterized by peripheral pancytopenia and marrow hypoplasia.
Dyskeratosis congenita, autosomal dominant, 2 (DKCA2):
A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.
Pulmonary fibrosis, and/or bone marrow failure, telomere-related, 1 (PFBMFT1):
An autosomal dominant disease associated with shortened telomeres. Pulmonary fibrosis is the most common manifestation. Other manifestations include aplastic anemia due to bone marrow failure, hepatic fibrosis, and increased cancer risk, particularly myelodysplastic syndrome and acute myeloid leukemia. Phenotype, age at onset, and severity are determined by telomere length.
Dyskeratosis congenita, autosomal recessive, 4 (DKCB4):
A severe form of dyskeratosis congenita, a rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.
Melanoma, cutaneous malignant 9 (CMM9):
A malignant neoplasm of melanocytes, arising de novo or from a pre-existing benign nevus, which occurs most often in the skin but may also involve other sites.

Phosphorylation at Tyr-707 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-227 by the AKT pathway promotes nuclear location. Phosphorylation at the G2/M phase at Ser-457 by DYRK2 promotes ubiquitination by the EDVP complex and degradation.
Ubiquitinated by the EDVP complex, a E3 ligase complex following phosphorylation at Ser-457 by DYRK2. Ubiquitinated leads to proteasomal degradation.
(Microbial infection) In case of infection by HIV-1, the EDVP complex is hijacked by HIV-1 via interaction between HIV-1 Vpr and DCAF1/VPRBP, leading to ubiquitination and degradation.