Zinc Finger Protein 610 (ZNF610)
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Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. A zinc finger protein is a DNA-binding protein domain consisting of zinc fingers ranging from two in the Drosophila regulator ADR1, the more common three in mammalian Sp1 up to nine in TFIIIA. Zinc finger protein 610 () is a 462 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZNF610 contains nine C2H2-type zinc fingers and one KRAB domain through which it is thought to be involved in DNA-binding and transcriptional regulation. Two isoforms of ZNF610 exist as a result of alternative splicing events.
Organism species: Homo sapiens (Human)
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