CRYAB

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. 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 2019]

Description

Crystallin alpha B

Tissue specificity

Tissue enhanced (heart muscle, skeletal muscle, tongue)

Subcell location

Plasma membrane, Cytosol

Predicted location

Intracellular, Membrane

Protein family

Cancer-related genes
Disease related genes
Human disease related genes
Mapped to neXtProt
Mapped to UniProt SWISS-PROT
Predicted intracellular proteins
Predicted membrane proteins
Protein evidence (Ezkurdia et al 2014)
Protein evidence (Kim et al 2014)

Chromosome

11 (111908564 - 111923722)

Ensembl ID

ENSG00000109846  (ver. 103.38)

Orthologs

Mouse Cryab: ENSMUSG00000032060

UniProt

P02511

neXtProt

NX_P02511

Human splice variants
Mouse splice variants

Protein structure