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Description for Protein CRYAB

crystallin, alpha B
15 total interacting proteins; 10 platelet interacting proteins
Icon Book Platelet Evidence (proteome studies/others : 0/0)
(Not detected in platelets)
Summary:
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. 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 (sHSP also known as the 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. 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. [provided by RefSeq] (PubMed Links)
Domains and Motifs:
None Available
Gene Ontology:
Gene Ontology Annotations
KEGG - Enzyme ID(s):
None Available
KEGG - Orthology:
K09542
KEGG - Pathway(s):
None Available
Nomenclature / Alternative Names:
Crystallin, alpha 2; CRYA2; Rosenthal fiber component; Heat shock 20 kD like protein
Approved Symbol:
CRYAB
(De-) Phosphorylations:
Total (de-) phosphorylation sites: 7
Human (de-) phosphorylation sites: 7; No platelet phosphorylation sites
Phosphorylation Targets:
Total phosphorylation targets: 0
Human phosphorylation targets: 0;Predicted platelet targets: 0
Protein Characteristics:
Isoform-specific Information
Icon DrugsAssociated Drugs (DrugBank Accession):

None Available

Associated Genetic Diseases:

  • Alpha-B crystallinopathy(Pd);
  • Alpha-B crystallinopathy with cataract(Pd);
  • Cataract, posterior polar, 2(Pd)
    		• Predicted Transmembrane Domains:
  • Isoform 1 : 0
    • Additional Identifiers:

    HPRD: 00428 Entrez Gene ID: 1410 OMIM ID: 123590 Swissprot Accession: P02511;