Telomerase reverse transcriptase Recombinant Rabbit Monoclonal Antibody [JF0586]

Function

Telomerase is an RNA-dependent DNA polymerase that catalyzes the addition of telomeric repeat sequences to chromosome ends. In most human somatic cells, telomerase activity is undetectable, and telomeres shorten with successive cell divisions. However, telomerase activity is detectable in immortal cells and in many human tumors. Two candidate mammalian telomerase proteins have been cloned. Human TP1 (for telomerase-associated protein 1), also designated TLP1 in rat (for telomerase protein component 1), is homologous to the Tetrahymena p80 telomerase protein and has been shown to interact with mammalian telomerase RNA. Human TERT (for telomerase reverse transcriptase), also designated hEST2 (for ever shorter telomeres), is homologous to the p123 telomerase protein from Euplotes and to the yeast Est2 protein. Expression of TERT mRNA has been shown to correlate with telomerase activity in various cell lines.

Background References

1. Yang Y et al. MR molecular imaging of tumours using ferritin heavy chain reporter gene expression mediated by the hTERT promoter. Eur Radiol 26:4089-4097 (2016).

2. Patel PL et al. Derepression of hTERT gene expression promotes escape from oncogene-induced cellular senescence. Proc Natl Acad Sci U S A 113:E5024-33 (2016).

Sequence Similarity

Belongs to the reverse transcriptase family. Telomerase subfamily.

Tissue Specificity

Expressed at a high level in thymocyte subpopulations, at an intermediate level in tonsil T-lymphocytes, and at a low to undetectable level in peripheral blood T-lymphocytes.

Post-translational Modification

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.

Subcellular Location

Nucleus, Chromosome, Cytoplasm.

UNIPROT

SwissProt: O14746 Human

Synonyms