Aliases for CRYBB1 Gene
External Ids for CRYBB1 Gene
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains 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 considered 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, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta basic group member, undergoes extensive cleavage at its N-terminal extension during lens maturation. It is also a member of a gene cluster with beta-A4, beta-B2, and beta-B3. [provided by RefSeq, Jul 2008]
GeneCards Summary for CRYBB1 Gene
CRYBB1 (Crystallin, Beta B1) is a Protein Coding gene. Diseases associated with CRYBB1 include cataract 17, multiple types and nuclear cataract. GO annotations related to this gene include structural constituent of eye lens. An important paralog of this gene is CRYGC.
UniProtKB/Swiss-Prot for CRYBB1 Gene
Crystallins are the dominant structural components of the vertebrate eye lens