alpha-crystallin A chain; heat shock protein beta-4; HspB4 (CRYAA, CRYA1, HSPB4)
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Function
- may contribute to the transparency & refractive index of the lens
- deamidation of Asn-101 in lens occurs mostly during the first 30 years of age
- deamidation of Asn-101 ~5% during the next 40 years resulting in a maximum of ~50% deamidation during a lifetime
- phosphorylation on Ser-122 seems to be developmentally regulated
- absent in the first months of life
- appears during the first 12 years of human lifetime
- relative amount of phosphorylated form does not change over the lifetime
- absent in the first months of life
Structure
- O-glycosylated; contains N-acetylglucosamine side chains
- belongs to the small heat shock protein (HSP20) family
Compartment
- cytoplasm, nucleus
- translocates to the nucleus during heat shock & resides in nuclear speckles
Pathology
- defects in CRYAA are a cause of autosomal dominant cataracts