Aliases for CRYBA2 Gene
External Ids for CRYBA2 Gene
Previous GeneCards Identifiers for CRYBA2 Gene
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also defined as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported. [provided by RefSeq, Jul 2008]
GeneCards Summary for CRYBA2 Gene
CRYBA2 (Crystallin Beta A2) is a Protein Coding gene. Diseases associated with CRYBA2 include Cataract 42 and Early-Onset Anterior Polar Cataract. GO annotations related to this gene include protein homodimerization activity and structural constituent of eye lens. An important paralog of this gene is CRYGC.
UniProtKB/Swiss-Prot for CRYBA2 Gene
Crystallins are the dominant structural components of the vertebrate eye lens.