CRYBB2

Crystallin, beta B2, also known as CRYBB2, is a human gene.cite web | title = Entrez Gene: CRYBB2 crystallin, beta B2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1415| accessdate = ]

PBB_Summary
section_title =
summary_text = 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-B3. A chain-terminating mutation was found to cause type 2 cerulean cataracts.cite web | title = Entrez Gene: CRYBB2 crystallin, beta B2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1415| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Datiles MB, Schumer DJ, Zigler JS, "et al." |title=Two-dimensional gel electrophoretic analysis of human lens proteins. |journal=Curr. Eye Res. |volume=11 |issue= 7 |pages= 669–77 |year= 1992 |pmid= 1521468 |doi=
*cite journal | author=Hulsebos TJ, Bijlsma EK, Geurts van Kessel AH, "et al." |title=Direct assignment of the human beta B2 and beta B3 crystallin genes to 22q11.2----q12: markers for neurofibromatosis 2. |journal=Cytogenet. Cell Genet. |volume=56 |issue= 3-4 |pages= 171–5 |year= 1991 |pmid= 2055112 |doi=
*cite journal | author=Aarts HJ, Den Dunnen JT, Lubsen NH, Schoenmakers JG |title=Linkage between the beta B2 and beta B3 crystallin genes in man and rat: a remnant of an ancient beta-crystallin gene cluster. |journal=Gene |volume=59 |issue= 1 |pages= 127–35 |year= 1988 |pmid= 3436525 |doi=
*cite journal | author=Miesbauer LR, Zhou X, Yang Z, "et al." |title=Post-translational modifications of water-soluble human lens crystallins from young adults. |journal=J. Biol. Chem. |volume=269 |issue= 17 |pages= 12494–502 |year= 1994 |pmid= 8175657 |doi=
*cite journal | author=Chambers C, Russell P |title=Sequence of the human lens beta B2-crystallin-encoding cDNA. |journal=Gene |volume=133 |issue= 2 |pages= 295–9 |year= 1993 |pmid= 8224918 |doi=
*cite journal | author=Miesbauer LR, Smith JB, Smith DL |title=Amino acid sequence of human lens beta B2-crystallin. |journal=Protein Sci. |volume=2 |issue= 2 |pages= 290–1 |year= 1993 |pmid= 8443605 |doi=
*cite journal | author=Kramer P, Yount J, Mitchell T, "et al." |title=A second gene for cerulean cataracts maps to the beta crystallin region on chromosome 22. |journal=Genomics |volume=35 |issue= 3 |pages= 539–42 |year= 1996 |pmid= 8812489 |doi= 10.1006/geno.1996.0395
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Lampi KJ, Ma Z, Shih M, "et al." |title=Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2268–75 |year= 1997 |pmid= 8999933 |doi=
*cite journal | author=Litt M, Carrero-Valenzuela R, LaMorticella DM, "et al." |title=Autosomal dominant cerulean cataract is associated with a chain termination mutation in the human beta-crystallin gene CRYBB2. |journal=Hum. Mol. Genet. |volume=6 |issue= 5 |pages= 665–8 |year= 1997 |pmid= 9158139 |doi=
*cite journal | author=Dunham I, Shimizu N, Roe BA, "et al." |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489–95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031
*cite journal | author=Gill D, Klose R, Munier FL, "et al." |title=Genetic heterogeneity of the Coppock-like cataract: a mutation in CRYBB2 on chromosome 22q11.2. |journal=Invest. Ophthalmol. Vis. Sci. |volume=41 |issue= 1 |pages= 159–65 |year= 2000 |pmid= 10634616 |doi=
*cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, "et al." |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491–6 |year= 2000 |pmid= 10737800 |doi=
*cite journal | author=Hanson SR, Hasan A, Smith DL, Smith JB |title=The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage. |journal=Exp. Eye Res. |volume=71 |issue= 2 |pages= 195–207 |year= 2000 |pmid= 10930324 |doi= 10.1006/exer.2000.0868
*cite journal | author=Vanita , Sarhadi V, Reis A, "et al." |title=A unique form of autosomal dominant cataract explained by gene conversion between beta-crystallin B2 and its pseudogene. |journal=J. Med. Genet. |volume=38 |issue= 6 |pages= 392–6 |year= 2001 |pmid= 11424921 |doi=
*cite journal | author=Fu L, Liang JJ |title=Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay. |journal=J. Biol. Chem. |volume=277 |issue= 6 |pages= 4255–60 |year= 2002 |pmid= 11700327 |doi= 10.1074/jbc.M110027200
*cite journal | author=MacCoss MJ, McDonald WH, Saraf A, "et al." |title=Shotgun identification of protein modifications from protein complexes and lens tissue. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 12 |pages= 7900–5 |year= 2002 |pmid= 12060738 |doi= 10.1073/pnas.122231399
*cite journal | author=Fu L, Liang JJ |title=Unfolding of human lens recombinant betaB2- and gammaC-crystallins. |journal=J. Struct. Biol. |volume=139 |issue= 3 |pages= 191–8 |year= 2003 |pmid= 12457849 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Srivastava OP, Srivastava K |title=BetaB2-crystallin undergoes extensive truncation during aging in human lenses. |journal=Biochem. Biophys. Res. Commun. |volume=301 |issue= 1 |pages= 44–9 |year= 2003 |pmid= 12535638 |doi=

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