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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].
LIM domains are protein structural domains, composed of two contiguous zinc fingers, separated by a two-amino acid residue hydrophobic linker. [1] The domain name is an acronym of the three genes in which it was first identified (LIN-11, Isl-1 and MEC-3). [2] LIM is a protein interaction domain that is involved in binding to many structurally ...
53861 Ensembl ENSG00000132485 ENSMUSG00000028180 UniProt O95218 Q9R020 RefSeq (mRNA) NM_005455 NM_203350 NM_017381 NM_001355381 NM_001355386 RefSeq (protein) NP_005446 NP_976225 NP_059077 NP_001342310 NP_001342315 Location (UCSC) Chr 1: 71.06 – 71.08 Mb Chr 3: 157.24 – 157.25 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Zinc finger Ran-binding domain-containing protein 2 is a ...
The protein encoded by this gene is an adaptor protein which contains five LIM domains, or double zinc fingers. The protein is likely involved in integrin signaling through its LIM domain-mediated interaction with integrin-linked kinase, found in focal adhesion plaques. It is also thought to act as a bridge linking integrin-linked kinase to NCK ...
Zinc finger is a small structural motif of protein that allows protein binding to DNA or RNA molecule that is characterized by the coordination of one or more zinc ions (Zn 2+) in order to stabilize the fold. Ikaros displays crucial functions in the hematopoietic system and is a known regulator of immune cells development, mainly in early B ...
The FYVE domain is composed of two small beta hairpins (or zinc knuckles) followed by an alpha helix. [5] The FYVE finger binds two zinc ions. The FYVE finger has eight potential zinc coordinating cysteine positions and is characterized by having basic amino acids around the cysteines.
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.