CRYBA1 Gene - Crystallin Beta A1
A key structural lens protein gene associated with congenital cataracts
Gene Information Card
| Symbol | CRYBA1 |
|---|---|
| Full Name | crystallin beta A1 |
| Gene Type | protein-coding |
| Chromosomal Location | 17q11.2 |
| NCBI Gene ID | 1410 ncbi.nlm.nih.gov/gene/1410 |
| Ensembl ID | ENSG00000108423 |
| UniProt ID | P05813 |
| OMIM ID | 123610 |
| HGNC ID | 2396 |
| Aliases | CRYB1, CTRCT10, beta-A1-crystallin |
Description
CRYBA1 encodes beta-crystallin A1, a structural protein that is a major component of the vertebrate eye lens. Beta-crystallins form heteromeric aggregates essential for maintaining lens transparency and refractive index. Mutations in CRYBA1 are a known cause of autosomal dominant congenital cataracts, particularly pulverulent or nuclear types.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Congenital cataract (autosomal dominant) | Missense or frameshift mutations disrupt protein folding and aggregation, leading to lens opacification | ClinVar, OMIM #123610 |
| Cataract 10 multiple types | Dominant-negative or loss-of-function variants cause nuclear or lamellar cataracts | OMIM #600881 |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Eye (lens) | High | High |
| Retina | Low | Low |
| Brain | Not detected | Not detected |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| ARPE-19 (retinal pigment epithelium) | 0.1 | Low expression |
| HLE-B3 (human lens epithelial) | High | High expression |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.275G>A (p.Gly92Asp) | Missense | Rare | Dominant-negative; causes congenital cataract |
| c.1A>G (p.Met1Val) | Start loss | Rare | Loss of function; cataract |
| c.323_324insC | Frameshift | Rare | Truncation; cataract |
Mutation functional classification
Loss of Function (LOF)
Start-loss and frameshift mutations reduce protein levels.
Gain of Function (GOF)
Not reported.
Dominant Negative (DN)
Missense mutations (e.g., Gly92Asp) disrupt crystallin aggregation, causing opacity.
View complete mutation data：
Gene Ontology (GO)
| • structural constituent of eye lens | • protein homodimerization activity |
| • identical protein binding |
Pathways
• Lens development
• Crystallin aggregation
Protein Summary
Beta-crystallin A1 is a 198-amino acid protein that forms dimers and higher-order oligomers in the lens. It contains four Greek key motifs and is critical for lens transparency. Post-translational modifications and mutations can lead to aggregation and cataract formation.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| CRYBA1 Knockout HEK293 Cell Line | EDJ-KQ4351 | Human | 1411 | Details Get a Quote |
| CRYBA1 Knockout HeLa Cell Line | EDJ-KQ52988 | Human | 1411 | Details Get a Quote |
| CRYBA1 Knockout A-549 Cell Line | EDJ-KQ61455 | Human | 1411 | Details Get a Quote |
| CRYBA1 Knockout HCT 116 Cell Line | EDJ-KQ69952 | Human | 1411 | Details Get a Quote |
