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. Zinc finger matrin-type protein 4 (ZMAT4) is a 229 amino acid protein that contains four matrin-type zinc fingers. The matrin-type zinc finger, which is very similar in structure to the classical DNA-binding C2H2 zinc finger, was first identified in the protein matrin-3. It has also been identified in several spliceosome RNA-binding proteins, suggesting a role in pre-mRNA binding. ZMAT4 is localized to the nucleus, and two isoforms of this protein exist as a result of alternative splicing events.
A synthesized peptide derived from human ZMIZ1.
A synthesized peptide derived from human ZMPSTE24.
A synthesized peptide derived from human ZMYM1.
A synthesized peptide derived from human ZMYM3.
This gene encodes a protein containing a MYND-type zinc finger domain that likely functions in assembly of the dynein motor. Mutations in this gene can cause primary ciliary dyskinesia. This gene is also considered a tumor suppressor gene and is often mutated, deleted, or hypermethylated and silenced in cancer cells. Alternative splicing results in multiple transcript variants.
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