CRYBB1

Identifiers Symbols CRYBB1; CATCN3 External IDs OMIM: 600929 MGI: 104992 HomoloGene: 1423 GeneCards: CRYBB1 Gene

Gene Ontology
Molecular function structural constituent of eye lens
Biological process visual perception
Sources: Amigo / QuickGO
RNA expression pattern More reference expression data Orthologs Species Human Mouse Entrez 1414 12960 Ensembl ENSG00000100122 ENSMUSG00000029343 UniProt P53674 Q9WVJ5 RefSeq (mRNA) NM_001887 NM_023695 RefSeq (protein) NP_001878 NP_076184 Location (UCSC) Chr 22:
27 – 27.01 Mb Chr 5:
112.26 – 112.27 Mb PubMed search

Beta-crystallin B1 is a protein that in humans is encoded by the 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.