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This method classifies zinc finger proteins into "fold groups" based on the overall shape of the protein backbone in the folded domain. The most common "fold groups" of zinc fingers are the Cys 2 His 2-like (the "classic zinc finger"), treble clef, and zinc ribbon. [19] The following table [19] shows the different structures and their key features:
The encoded protein has five LIM domains, each domain forming two zinc fingers, which permit interactions which regulate cell shape and migration. A pseudogene of this gene is located on chromosome 4. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2011].
Two GATA zinc fingers are found in GATA-family transcription factors. However, there are several proteins that only contain a single copy of the domain. It is also worth noting that many GATA-type Znfs (such as those found in the proteins GATAD2B and MTA1) have not been experimentally demonstrated to be DNA-binding domains. Furthermore, several ...
52915 Ensembl ENSG00000122515 ENSMUSG00000041164 UniProt Q8NF64 Q8CIE2 RefSeq (mRNA) NM_001300959 NM_031449 NM_174929 NM_001005867 NM_028601 RefSeq (protein) NP_001287888 NP_113637 NP_777589 NP_001005867 NP_082877 Location (UCSC) Chr 7: 44.75 – 44.77 Mb Chr 11: 6.39 – 6.41 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Zinc finger MIZ domain-containing protein 2 is a protein ...
ZNF821 protein contains two C2H2 Zinc Finger motifs (spanning amino acids 120-140 and 152–172, respectively) and an STPR (one-score-and-three-amino acid peptide repeat) domain (spanning amino acids 223–314) containing a bipartite nuclear localization signal.
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.
The protein encoded by this gene belongs to the C2H2-type zinc-finger protein family. The exact function of this gene is not known, however, zinc-finger proteins are known to interact with DNA and function as transcription regulators. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Fpg is a monomer composed of 2 domains connected by a flexible hinge. [2] The two DNA-binding motifs (a zinc finger and the helix-two-turns-helix motifs) suggest that the oxidized base is flipped out from double-stranded DNA in the binding mode and excised by a catalytic mechanism similar to that of bifunctional base excision repair enzymes. [2]