Disease:Crystallins do not turn over as the lens ages , providing ample opportunity for post-translational modifications or oxidations. These modifications may change crystallin solubility properties and favor senile cataract. ,Disease:Defects in CRYAB are the cause of alpha-B crystallinopathy [MIM:608810]. Alpha-B crystallinopathy is a an autosomal dominant form of desmin-related myopathy (DRM) that results in weakness of the proximal and distal limb muscle (including neck , velopharynx , and trunk muscles) , signs of cardiomyopathy and cataract. Patients with progressive myopathy characterized by myofibrillar degeneration that commences at the Z-disk , have been described. Mutations truncate the essential C-terminal domain of the protein required for the chaperone function. ,Disease:Seen as Rosenthal fiber protein in the brain tissue of patients with Alexander disease. ,Function:May contribute to the transparency and refractive index of the lens. ,mass spectrometry: PubMed:10930324 ,mass spectrometry: PubMed:8175657 ,mass spectrometry:With 1 phosphate group PubMed:10930324 ,mass spectrometry:With 1 phosphate group PubMed:8175657 ,mass spectrometry:With 2 phosphate groups PubMed:8175657 ,similarity:Belongs to the small heat shock protein (HSP20) family. ,subunit:Aggregates with homologous proteins , including CRYAA and the small heat shock protein HSPB1 , to form large heteromeric complexes. Interacts with HSPBAP1 and TTN/titin. ,tissue specificity:Lens as well as other tissues. ,
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