Aliases for CRYAB Gene
External Ids for CRYAB Gene
Previous HGNC Symbols for CRYAB Gene
Previous GeneCards Identifiers for CRYAB Gene
Mammalian lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
GeneCards Summary for CRYAB Gene
CRYAB (Crystallin Alpha B) is a Protein Coding gene. Diseases associated with CRYAB include Myopathy, Myofibrillar, 2 and Cataract 16, Multiple Types. Among its related pathways are Protein processing in endoplasmic reticulum and Longevity regulating pathway - multiple species. GO annotations related to this gene include protein homodimerization activity and microtubule binding. An important paralog of this gene is LOC102724652.
UniProtKB/Swiss-Prot for CRYAB Gene
May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.