CRYBB2: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
WikiBot (talk | contribs)
Bots, Bureaucrats, bureaucrats, interwiki, nocaptcha, Administrators
57,550 edits
m Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}})
 
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Beta-crystallin B2''' is a [[protein]] that in humans is encoded by the ''CRYBB2'' [[gene]].<ref name="pmid9158139">{{cite journal | vauthors = Litt M, Carrero-Valenzuela R, LaMorticella DM, Schultz DW, Mitchell TN, Kramer P, Maumenee IH | 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 |date=Jul 1997 | pmid = 9158139 | pmc =  | doi =10.1093/hmg/6.5.665  }}</ref><ref name="pmid8224918">{{cite journal | vauthors = Chambers C, Russell P | title = Sequence of the human lens beta B2-crystallin-encoding cDNA | journal = Gene | volume = 133 | issue = 2 | pages = 295–9 |date=Dec 1993 | pmid = 8224918 | pmc =  | doi =10.1016/0378-1119(93)90655-M  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CRYBB2 crystallin, beta B2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1415| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_CRYBB2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bd7.
| PDB = {{PDB2|1bd7}}, {{PDB2|1blb}}, {{PDB2|1e7n}}, {{PDB2|1ytq}}, {{PDB2|2bb2}}
| Name = Crystallin, beta B2
| HGNCid = 2398
| Symbol = CRYBB2
| AltSymbols =; CCA2; CRYB2; CRYB2A; D22S665
| OMIM = 123620
| ECnumber = 
| Homologene = 420
| MGIid = 88519
| GeneAtlas_image1 = PBB_GE_CRYBB2_206777_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CRYBB2_206778_at_tn.png
| Function = {{GNF_GO|id=GO:0005212 |text = structural constituent of eye lens}}
| Component =
| Process = {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1415
    | Hs_Ensembl = ENSG00000100058
    | Hs_RefseqProtein = NP_000487
    | Hs_RefseqmRNA = NM_000496
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 22
    | Hs_GenLoc_start = 23947385
    | Hs_GenLoc_end = 23957822
    | Hs_Uniprot = P43320
    | Mm_EntrezGene = 12961
    | Mm_Ensembl = ENSMUSG00000042240
    | Mm_RefseqmRNA = NM_007773
    | Mm_RefseqProtein = NP_031799
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 113298561
    | Mm_GenLoc_end = 113309963
    | Mm_Uniprot = Q0VGT6
  }}
}}
'''Crystallin, beta B2''', also known as '''CRYBB2''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Crystallin]]s 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-terminal]] 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 [[heterodimer]]s 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.<ref name="entrez" />
{{PBB_Summary
 
| section_title =
==Interactions==
| 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.<ref name="entrez">{{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 = }}</ref>
CRYBB2 has been shown to [[Protein-protein interaction|interact]] with [[Hsp27]],<ref name="pmid11700327">{{cite journal | vauthors = 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 |date=February 2002 | pmid = 11700327 | doi = 10.1074/jbc.M110027200 }}</ref> [[CRYGC]],<ref name=pmid11700327/> [[CRYAA]]<ref name=pmid11700327/> and [[CRYAB]].<ref name=pmid11700327/>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|CRYBB2}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | vauthors=Datiles MB, Schumer DJ, Zigler JS |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=10.3109/02713689209000740 |display-authors=etal}}
| citations =
*{{cite journal  | vauthors=Hulsebos TJ, Bijlsma EK, Geurts van Kessel AH |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=10.1159/000133080 |display-authors=etal}}
*{{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  | vauthors=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=10.1016/0378-1119(87)90273-3 }}
*{{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  | vauthors=Miesbauer LR, Zhou X, Yang Z |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=  |display-authors=etal}}
*{{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  | vauthors=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=10.1002/pro.5560020217  | pmc=2142348 }}
*{{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  | vauthors=Kramer P, Yount J, Mitchell T |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 |display-authors=etal}}
*{{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  | vauthors=Lampi KJ, Ma Z, Shih M |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=10.1074/jbc.272.4.2268 |display-authors=etal}}
*{{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  | vauthors=Gill D, Klose R, Munier FL |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=  |display-authors=etal}}
*{{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  | vauthors=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=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=Vanita, Sarhadi V | author2=Reis A |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=10.1136/jmg.38.6.392 | pmc=1734905  |display-authors=etal}}
*{{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  | vauthors=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=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  | vauthors=MacCoss MJ, McDonald WH, Saraf A |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 | pmc=122992 |display-authors=etal}}
*{{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  | vauthors=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=10.1016/S1047-8477(02)00545-2 }}
*{{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  | vauthors=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=10.1016/S0006-291X(02)02975-3  }}
*{{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  | vauthors=MacDonald JT, Purkiss AG, Smith MA |title=Unfolding crystallins: The destabilizing role of a β-hairpin cysteine in BetaB2-crystallin by simulation and experiment |journal=[[Protein Science]] |volume=14 |issue= 5 |pages= 1282–1292 |year= 2005 |pmid= 15840832  | pmc=2253261 |doi=10.1110/ps.041227805 |display-authors=etal}}
*{{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=  }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=1415}}
{{Eye proteins}}


{{gene-22-stub}}
{{gene-22-stub}}
{{WikiDoc Sources}}

Latest revision as of 10:04, 30 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Beta-crystallin B2 is a protein that in humans is encoded by the CRYBB2 gene.[1][2][3]

Function

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-terminal 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.[3]

Interactions

CRYBB2 has been shown to interact with Hsp27,[4] CRYGC,[4] CRYAA[4] and CRYAB.[4]

References

  1. ↑ Litt M, Carrero-Valenzuela R, LaMorticella DM, Schultz DW, Mitchell TN, Kramer P, Maumenee IH (Jul 1997). "Autosomal dominant cerulean cataract is associated with a chain termination mutation in the human beta-crystallin gene CRYBB2". Hum Mol Genet. 6 (5): 665–8. doi:10.1093/hmg/6.5.665. PMID 9158139.
  2. ↑ Chambers C, Russell P (Dec 1993). "Sequence of the human lens beta B2-crystallin-encoding cDNA". Gene. 133 (2): 295–9. doi:10.1016/0378-1119(93)90655-M. PMID 8224918.
  3. ↑ 3.0 3.1 "Entrez Gene: CRYBB2 crystallin, beta B2".
  4. ↑ 4.0 4.1 4.2 4.3 Fu L, Liang JJ (February 2002). "Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay". J. Biol. Chem. 277 (6): 4255–60. doi:10.1074/jbc.M110027200. PMID 11700327.

External links

Further reading


Retrieved from "https://www.wikidoc.org/index.php?title=CRYBB2&oldid=1419968"