Description: Homo sapiens crystallin, beta B1 (CRYBB1), mRNA. RefSeq Summary (NM_001887): 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 basic group member, undergoes extensive cleavage at its N-terminal extension during lens maturation. It is also a member of a gene cluster with beta-A4, beta-B2, and beta-B3. [provided by RefSeq, Jul 2008]. Transcript (Including UTRs) Position: hg19 chr22:26,995,362-27,013,991 Size: 18,630 Total Exon Count: 6 Strand: - Coding Region Position: hg19 chr22:26,995,454-27,012,283 Size: 16,830 Coding Exon Count: 5
ID:CRBB1_HUMAN DESCRIPTION: RecName: Full=Beta-crystallin B1; AltName: Full=Beta-B1 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. 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 truncated forms, leading to impaired oligomerization and protein insolubilization. MASS SPECTROMETRY: Mass=27941; Mass_error=6; Method=Electrospray; Range=2-252; Source=PubMed:8626774; DISEASE: Defects in CRYBB1 are the cause of cataract congenital nuclear autosomal recessive type 3 (CATCN3) [MIM:611544]. A congenital cataract affecting the central nucleus of the eye. Nuclear cataracts are often not highly visually significant. The density of the opacities varies greatly from fine dots to a dense, white and chalk-like, central cataract. The condition is usually bilateral. Nuclear cataracts are often combined with opacified cortical fibers encircling the nuclear opacity, which are referred to as cortical riders. DISEASE: Defects in CRYBB1 are a cause of cataract-microcornea syndrome (CAMIS) [MIM:116150]. An ocular disorder characterized by the association of congenital cataract and microcornea without any other systemic anomaly or dysmorphism. Clinical findings include a corneal diameter inferior to 10 mm in both meridians in an otherwise normal eye, and an inherited cataract, which is most often bilateral posterior polar with opacification in the lens periphery. The cataract progresses to form a total cataract after visual maturity has been achieved, requiring cataract extraction in the first to third decade of life. Microcornea-cataract syndrome can be associated with other rare ocular manifestations, including myopia, iris coloboma, sclerocornea and Peters anomaly. Transmission is in most cases autosomal dominant, but cases of autosomal recessive transmission have recently been described. 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 P53674
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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
