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- CRYBB3 abstract "Beta-crystallin B3 is a protein that in humans is encoded by the CRYBB3 gene.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, is part of a gene cluster with beta-A4, beta-B1, and beta-B2.".
- CRYBB3 entrezgene "1417".
- CRYBB3 wikiPageID "15183315".
- CRYBB3 wikiPageLength "6754".
- CRYBB3 wikiPageOutDegree "2".
- CRYBB3 wikiPageRevisionID "673175057".
- CRYBB3 wikiPageWikiLink Gene.
- CRYBB3 wikiPageWikiLink Protein.
- CRYBB3 wikiPageWikiLinkText "CRYBB3".
- CRYBB3 requireManualInspection "no".
- CRYBB3 summaryText "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 . 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, is part of a gene cluster with beta-A4, beta-B1, and beta-B2.".
- CRYBB3 updateCitations "yes".
- CRYBB3 updatePage "yes".
- CRYBB3 updateProteinBox "yes".
- CRYBB3 updateSummary "yes".
- CRYBB3 wikiPageUsesTemplate Template:Cite_journal.
- CRYBB3 wikiPageUsesTemplate Template:Eye_proteins.
- CRYBB3 wikiPageUsesTemplate Template:Gene-22-stub.
- CRYBB3 wikiPageUsesTemplate Template:PBB.
- CRYBB3 wikiPageUsesTemplate Template:PBB_Controls.
- CRYBB3 wikiPageUsesTemplate Template:PBB_Further_reading.
- CRYBB3 wikiPageUsesTemplate Template:PBB_Summary.
- CRYBB3 wikiPageUsesTemplate Template:Refbegin.
- CRYBB3 wikiPageUsesTemplate Template:Refend.
- CRYBB3 wikiPageUsesTemplate Template:Reflist.
- CRYBB3 hypernym Protein.
- CRYBB3 type Biomolecule.
- CRYBB3 type Protein.
- CRYBB3 type Thing.
- CRYBB3 type Q206229.
- CRYBB3 type Q8054.
- CRYBB3 comment "Beta-crystallin B3 is a protein that in humans is encoded by the CRYBB3 gene.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.".
- CRYBB3 label "CRYBB3".
- CRYBB3 sameAs Q17910229.
- CRYBB3 sameAs m.03hl5bh.
- CRYBB3 sameAs Q17910229.
- CRYBB3 wasDerivedFrom CRYBB3?oldid=673175057.
- CRYBB3 isPrimaryTopicOf CRYBB3.