Human Gene CRYBA2 (ENST00000392096.6) from GENCODE V44
Description: Homo sapiens crystallin beta A2 (CRYBA2), transcript variant 3, mRNA. (from RefSeq NM_057094) RefSeq Summary (NM_057094): Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain 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 defined 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 but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported. [provided by RefSeq, Jul 2008]. Gencode Transcript: ENST00000392096.6 Gencode Gene: ENSG00000163499.12 Transcript (Including UTRs) Position: hg38 chr2:218,990,189-218,993,421 Size: 3,233 Total Exon Count: 5 Strand: - Coding Region Position: hg38 chr2:218,990,252-218,993,176 Size: 2,925 Coding Exon Count: 4
ID:CRBA2_HUMAN DESCRIPTION: RecName: Full=Beta-crystallin A2; AltName: Full=Beta-A2 crystallin; FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SUBUNIT: Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms (By similarity). DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. SIMILARITY: Belongs to the beta/gamma-crystallin family. SIMILARITY: Contains 4 beta/gamma crystallin 'Greek key' domains.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P53672
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
Sequence and Links to Tools and Databases 
Microarray Expression Data 
