Human Gene CRYBA1 (uc002hdw.3) Description and Page Index
Description: Homo sapiens crystallin, beta A1 (CRYBA1), mRNA. RefSeq Summary (NM_005208): 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, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mRNA, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alternate translation initiation site. Deletion of exons 3 and 4 causes the autosomal dominant disease 'zonular cataract with sutural opacities'. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BY794946.2, BC113693.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA2148093, SAMEA2148874 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END## Transcript (Including UTRs) Position: hg19 chr17:27,573,875-27,581,502 Size: 7,628 Total Exon Count: 6 Strand: + Coding Region Position: hg19 chr17:27,573,882-27,581,367 Size: 7,486 Coding Exon Count: 6
ID:CRBA1_HUMAN DESCRIPTION: RecName: Full=Beta-crystallin A3; Contains: RecName: Full=Beta-crystallin A3, isoform A1, Delta4 form; Contains: RecName: Full=Beta-crystallin A3, isoform A1, Delta7 form; Contains: RecName: Full=Beta-crystallin A3, isoform A1, Delta8 form; 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. PTM: Specific cleavages in the N-terminal arm occur during lens maturation and give rise to several truncated forms. Cleavages do not seem to have adverse effects on solubility. PTM: S-methylation and glutathionylation occur in normal young lenses and do not seem to be detrimental. PTM: Isoform A1 initiator methionine is removed. The new N- terminal amino acid is then N-acetylated. MASS SPECTROMETRY: Mass=25192; Mass_error=3; Method=Electrospray; Range=1-215; Source=PubMed:8999933; MASS SPECTROMETRY: Mass=25192; Method=Electrospray; Range=1-215; Source=PubMed:15576560; MASS SPECTROMETRY: Mass=23101; Mass_error=3; Method=Electrospray; Range=19-215; Source=PubMed:8999933; MASS SPECTROMETRY: Mass=23102; Method=Electrospray; Range=19-215; Source=PubMed:15576560; MASS SPECTROMETRY: Mass=22646; Method=Electrospray; Range=23-215; Source=PubMed:15576560; MASS SPECTROMETRY: Mass=22351; Method=Electrospray; Range=26-215; Source=PubMed:15576560; MASS SPECTROMETRY: Mass=22294; Method=Electrospray; Range=27-215; Source=PubMed:15576560; DISEASE: Defects in CRYBA1 are the cause of cataract congenital zonular with sutural opacities (CCZS) [MIM:600881]. A form of zonular cataract. Zonular or lamellar cataracts are concentric opacities, broad or narrow, usually consisting of powdery white dots affecting one lamella or zonule of an otherwise clear lens. SIMILARITY: Belongs to the beta/gamma-crystallin family. SIMILARITY: Contains 4 beta/gamma crystallin 'Greek key' domains.
Genetic Association Studies of Complex Diseases and Disorders
Genetic Association Database (archive): CRYBA1 CDC HuGE Published Literature: CRYBA1
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 P05813
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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.
Biological Process: GO:0001818 negative regulation of cytokine production GO:0002088 lens development in camera-type eye GO:0007601 visual perception GO:0014067 negative regulation of phosphatidylinositol 3-kinase signaling GO:0032007 negative regulation of TOR signaling GO:0051898 negative regulation of protein kinase B signaling GO:0070373 negative regulation of ERK1 and ERK2 cascade GO:2000210 positive regulation of anoikis