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Cartoon representation of the protein Zif268 (blue) containing three zinc fingers in complex with DNA (orange). The coordinating amino acid residues and zinc ions (green) are highlighted. A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn 2+) which stabilizes the
This gene is a member of the Krueppel C2H2-type zinc-finger protein family and encodes a zinc finger transcription factor that contains nine Kruppel-type zinc finger domains at the carboxyl terminus. This protein is located in the nucleus, is involved in cell cycle progression, and interacts with a histone deacetylase.
Zinc finger FYVE domain-containing protein 9 or SARA (SMAD anchor for receptor activation) is a protein that in humans is encoded by the ZFYVE9 gene. [5] SARA contains a double zinc finger (FYVE domain). SARA is an anchoring protein involved in TGF beta signaling.
The BTB/POZ domain (BTB for BR-C, ttk and bab [2] or POZ for Pox virus and Zinc finger [3]) is a structural domain found in proteins across the domain Eukarya. [4] Given its prevalence in eukaryotes and its absence in Archaea and bacteria, it likely arose after the origin of eukaryotes. [5]
The KRAB domain had initially been identified in 1988 as a periodic array of leucine residues separated by six amino acids 5’ to the zinc finger region of KOX1/ZNF10 [7] coined heptad repeat of leucines (also known as a leucine zipper). [8] Later, this domain was named in association with the C2H2-Zinc finger proteins Krüppel associated box ...
Zinc finger and BTB domain-containing protein 32 is a protein that in humans is encoded by the 1960 bp ZBTB32 gene.The 52 kDa protein (487 aa) is a transcriptional repressor and the gene is expressed in T and B cells upon activation, but also significantly in testis cells.
In molecular biology, a RING (short for Really Interesting New Gene) finger domain is a protein structural domain of zinc finger type which contains a C 3 HC 4 amino acid motif which binds two zinc cations (seven cysteines and one histidine arranged non-consecutively).
In molecular biology the B-box-type zinc finger domain is a short protein domain of around 40 amino acid residues in length. B-box zinc fingers can be divided into two groups, where types 1 and 2 B-box domains differ in their consensus sequence and in the spacing of the 7-8 zinc-binding residues.
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