Zinc Finger Protein 738 (ZNF738)
ZNF738 May be involved in transcriptional regulation.Contains 1 KRAB domain. Despite its name, it does not contain a canonical C2H2-type zinc-finger.
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. They occur in nature as the part of transcription factors conferring DNA sequence specificity as the DNA-binding domain. They have also found use in protein engineering due to their modularity and have prospects as components of tools for use in therapeutic gene modulation and zinc finger nucleases. Zinc finger protein consists of anti-parallel hairpin motif. It consists of 2 beta strands, one alpha helix and a hairpin structure.
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. They occur in nature as the part of transcription factors conferring DNA sequence specificity as the DNA-binding domain. They have also found use in protein engineering due to their modularity and have prospects as components of tools for use in therapeutic gene modulation and zinc finger nucleases. Zinc finger protein consists of anti-parallel hairpin motif. It consists of 2 beta strands, one alpha helix and a hairpin structure.
Organism species: Homo sapiens (Human)
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