Target intelligence / Profile preview

Zinc finger and BTB domain-containing protein 10 (ZBTB10)

Target
ZBTB10
Molecular classification
Transcription factor, Zinc finger protein, BTB (Broad-complex, Tramtrack and Bric-à-brac) domain-containing protein
01

Overview

Zinc finger and BTB domain-containing protein 10 (ZBTB10) is a nuclear transcription factor characterized by a combination of C2H2-type zinc finger DNA binding domains and a BTB/POZ oligomerization motif. ZBTB10 directly binds to telomeric and telomeric variant DNA repeats, particularly displaying high affinity for the telomeric variant repeat sequence TTGGGG via its tandem zinc finger domains. Functionally, ZBTB10 participates in negative regulation of gene expression by RNA polymerase II and is involved in chromatin organization, with documented interactions with cellular complexes such as GTF2H (involved in transcription and nucleotide excision repair) and PTW/PP1 (regulation of chromatin structure and cell cycle), as well as the shelterin subunits TRF2 and RAP1 that are important for telomere protection and maintenance. ZBTB10 does not appear to be essential for baseline telomere maintenance in human cells but may contribute to telomeric DNA processing, variant repeat binding, and DNA-damage response, which have potential implications in tumor biology and genome instability. There are currently no drugs directly targeting ZBTB10, nor established clinical biomarkers or safety concerns directly connected to this protein.

Other names
Zinc finger protein RINZFRINZFFLJ12752RINZFCZinc finger protein RIN ZF
02

Biological functions

DNA binding, including telomeric repeat and variant repeat bindingNegative regulation of transcription by RNA polymerase IIRegulation of chromatin structure and cell cycle progressionInteraction with DNA repair proteins and chromatin-associated complexesPotential involvement in RNA processing
03

Disease associations

Cancer (noted in some studies due to roles in telomere regulation and interaction with DNA damage response proteins)Other (the role in disease is not fully established, but interaction with DNA repair proteins and telomere-binding suggests potential implications in genomic instability and carcinogenesis)

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