Summary

Name POT1
Full Name Protection of telomeres protein 1
Synonyms hPot1, POT1-like telomere end-binding protein
Primary ID Q9NUX5
Links - -
Type protein
Relations 5
Function Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. Is a component of the double-stranded telomeric DNA-binding TRF1 complex which is involved in the regulation of telomere length by cis-inhibition of telomerase. Also acts as a single-stranded telomeric DNA-binding protein and thus may act as a downstream effector of the TRF1 complex and may transduce information about telomere maintenance and/or length to the telomere terminus. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Binds to two or more telomeric single-stranded 5'-TTAGGG-3' repeats (G-strand) and with high specificity to a minimal telomeric single-stranded 5'-TAGGGTTAG-3' sequence. Binds telomeric single-stranded sequences internally or at proximity of a 3'-end. Its activity is TERT dependent but it does not increase TERT activity by itself. In contrast, the ACD-POT1 heterodimer enhances telomere elongation by increasing telomerase processivity.

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Relations

Regulator Mechanism target score ℹ
+ POT1down-regulates activity img/direct_inhibition.png binding RPA3 0.264
Publications: 1
+ POT1down-regulates activity img/direct_inhibition.png binding RPA2 0.407
Publications: 1
+ POT1up-regulates img/direct-activation.png binding TERT 0.674
Publications: 1 Organism: Homo Sapiens
+ POT1down-regulates activity img/direct_inhibition.png binding RPA1 0.295
Publications: 1
+ POT1form complex img/form-complex.png binding POT1/ACD 0.883
Publications: 1 Organism: Homo Sapiens