CRYBA1
You don't need to be Editor-In-Chief to add or edit content to WikiDoc. You can begin to add to or edit text on this WikiDoc page by clicking on the edit button at the top of this page. Next enter or edit the information that you would like to appear here. Once you are done editing, scroll down and click the Save page button at the bottom of the page.
| Crystallin, beta A1
| |||||||||||
| Identifiers | |||||||||||
| Symbol(s) | CRYBA1; CRYB1 | ||||||||||
| External IDs | OMIM: 123610 MGI: 88518 Homologene: 3815 | ||||||||||
| |||||||||||
| RNA expression pattern | |||||||||||
| Orthologs | |||||||||||
| Human | Mouse | ||||||||||
| Entrez | 1411 | 12957 | |||||||||
| Ensembl | ENSG00000108255 | ENSMUSG00000000724 | |||||||||
| Uniprot | P05813 | Q8BNB5 | |||||||||
| Refseq | NM_005208 (mRNA) NP_005199 (protein) | NM_009965 (mRNA) NP_034095 (protein) | |||||||||
| Location | Chr 17: 24.6 - 24.61 Mb | Chr 11: 77.53 - 77.54 Mb | |||||||||
| Pubmed search | [1] | [2] | |||||||||
Crystallin, beta A1, also known as CRYBA1, is a human gene.[1]
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'.[1]
References
Further reading
- Hulsebos TJ, Bijlsma EK, Geurts van Kessel AH, et al. (1991). "Direct assignment of the human beta B2 and beta B3 crystallin genes to 22q11.2----q12: markers for neurofibromatosis 2.". Cytogenet. Cell Genet. 56 (3-4): 171-5. PMID 2055112.
- Hogg D, Tsui LC, Gorin M, Breitman ML (1986). "Characterization of the human beta-crystallin gene Hu beta A3/A1 reveals ancestral relationships among the beta gamma-crystallin superfamily.". J. Biol. Chem. 261 (26): 12420-7. PMID 3745196.
- Sparkes RS, Mohandas T, Heinzmann C, et al. (1986). "Assignment of a human beta-crystallin gene to 17cen-q23.". Hum. Genet. 74 (2): 133-6. PMID 3770741.
- Basti S, Hejtmancik JF, Padma T, et al. (1996). "Autosomal dominant zonular cataract with sutural opacities in a four-generation family.". Am. J. Ophthalmol. 121 (2): 162-8. PMID 8623885.
- Werten PJ, Carver JA, Jaenicke R, de Jong WW (1997). "The elusive role of the N-terminal extension of beta A3- and beta A1-crystallin.". Protein Eng. 9 (11): 1021-8. PMID 8961355.
- Lampi KJ, Ma Z, Shih M, et al. (1997). "Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens.". J. Biol. Chem. 272 (4): 2268-75. PMID 8999933.
- Kannabiran C, Rogan PK, Olmos L, et al. (1998). "Autosomal dominant zonular cataract with sutural opacities is associated with a splice mutation in the betaA3/A1-crystallin gene.". Mol. Vis. 4: 21. PMID 9788845.
- Srivastava OP, Srivastava K (1999). "Characterization of a sodium deoxycholate-activatable proteinase activity associated with betaA3/A1-crystallin of human lenses.". Biochim. Biophys. Acta 1434 (2): 331-46. PMID 10525151.
- Graw J, Jung M, Löster J, et al. (2000). "Mutation in the betaA3/A1-crystallin encoding gene Cryba1 causes a dominant cataract in the mouse.". Genomics 62 (1): 67-73. doi:10.1006/geno.1999.5974. PMID 10585769.
- Vanita , Sarhadi V, Reis A, et al. (2001). "A unique form of autosomal dominant cataract explained by gene conversion between beta-crystallin B2 and its pseudogene.". J. Med. Genet. 38 (6): 392-6. PMID 11424921.
- MacCoss MJ, McDonald WH, Saraf A, et al. (2002). "Shotgun identification of protein modifications from protein complexes and lens tissue.". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 7900-5. doi:10.1073/pnas.122231399. PMID 12060738.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
- Qi Y, Jia H, Huang S, et al. (2004). "A deletion mutation in the betaA1/A3 crystallin gene ( CRYBA1/A3) is associated with autosomal dominant congenital nuclear cataract in a Chinese family.". Hum. Genet. 114 (2): 192-7. doi:10.1007/s00439-003-1049-7. PMID 14598164.
- Reddy MA, Bateman OA, Chakarova C, et al. (2004). "Characterization of the G91del CRYBA1/3-crystallin protein: a cause of human inherited cataract.". Hum. Mol. Genet. 13 (9): 945-53. doi:10.1093/hmg/ddh110. PMID 15016766.
- Ferrini W, Schorderet DF, Othenin-Girard P, et al. (2004). "CRYBA3/A1 gene mutation associated with suture-sparing autosomal dominant congenital nuclear cataract: a novel phenotype.". Invest. Ophthalmol. Vis. Sci. 45 (5): 1436-41. PMID 15111599.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
- Lapko VN, Cerny RL, Smith DL, Smith JB (2005). "Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation.". Protein Sci. 14 (1): 45-54. doi:10.1110/ps.04738505. PMID 15576560.
- Takata T, Oxford JT, Brandon TR, Lampi KJ (2007). "Deamidation alters the structure and decreases the stability of human lens betaA3-crystallin.". Biochemistry 46 (30): 8861-71. doi:10.1021/bi700487q. PMID 17616172.
- Lu S, Zhao C, Jiao H, et al. (2007). "Two Chinese families with pulverulent congenital cataracts and deltaG91 CRYBA1 mutations.". Mol. Vis. 13: 1154-60. PMID 17653060.
 | This protein-related article is a stub. You can help WikiDoc by expanding it. |
Acknowledgement and Attribution Regarding Sources of Content
Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .
