CRYBA4
Gene Information
- Official Symbol: CRYBA4
- Official Name: crystallin beta A4
- Aliases and Previous Symbols: N/A
- Entrez ID: 1413
- UniProt: P53673
- Interactions: BioGRID
- PubMed articles: Open PubMed
- OMIM: Open OMIM
Function Summary
- Entrez 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. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta acidic group member, is part of a gene cluster with beta-B1, beta-B2, and beta-B3. [provided by RefSeq, Jul 2008].
- UniProt Summary: Crystallins are the dominant structural components of the vertebrate eye lens.
CRISPR Data
Essentiality in NALM6
- Essentiality Rank: 6647
- Expression level (log2 read counts): -5.6
CRYBA4 Expression in NALM6 Cells: -5.6
