CRYA1 Contributes 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. Belongs to the small heat shock protein (HSP20) family. Expressed in eye lens. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Heat shock protein
Cellular Component:  cytoplasm; nucleus
Molecular Function:  metal ion binding; protein binding; structural constituent of eye lens; unfolded protein binding
Biological Process:  actin filament organization; apoptotic process involved in morphogenesis; embryonic camera-type eye morphogenesis; lens fiber cell morphogenesis; microtubule-based process; mitochondrion organization; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; negative regulation of gene expression; positive regulation of cell growth; positive regulation of protein phosphorylation; response to hydrogen peroxide; response to hypoxia; response to UV-A; tubulin complex assembly
Reference #:  P02470 (UniProtKB)
Alt. Names/Synonyms: alpha crystallin A chain; Alpha-crystallin A chain; CRAA; CRYA1; CRYAA; crystallin, alpha A; crystallin, alphaA
Gene Symbols: CRYAA
Molecular weight: 19,790 Da
Basal Isoelectric point: 5.78  Predict pI for various phosphorylation states
Select Structure to View Below

CRYA1

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene  |  Ensembl Protein