Human Gene CRYBA1 (uc002hdw.3) Description and Page Index
  Description: Homo sapiens crystallin, beta A1 (CRYBA1), mRNA.
RefSeq Summary (NM_005208): 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'. [provided by RefSeq, Jul 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: BY794946.2, BC113693.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA2148093, SAMEA2148874 [ECO:0000350] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, expression ##RefSeq-Attributes-END##
Transcript (Including UTRs)
   Position: hg19 chr17:27,573,875-27,581,502 Size: 7,628 Total Exon Count: 6 Strand: +
Coding Region
   Position: hg19 chr17:27,573,882-27,581,367 Size: 7,486 Coding Exon Count: 6 

Page IndexSequence and LinksUniProtKB CommentsGenetic AssociationsMalaCardsCTD
Gene AllelesRNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther Species
GO AnnotationsmRNA DescriptionsOther NamesModel InformationMethods
Data last updated: 2013-06-14

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr17:27,573,875-27,581,502)mRNA (may differ from genome)Protein (215 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
BioGPSCGAPEnsemblEntrez GeneExonPrimerGeneCards
GeneNetworkHGNCHPRDLynxMGIneXtProt
OMIMPubMedStanford SOURCETreefamUniProtKBWikipedia

-  Comments and Description Text from UniProtKB
  ID: CRBA1_HUMAN
DESCRIPTION: RecName: Full=Beta-crystallin A3; Contains: RecName: Full=Beta-crystallin A3, isoform A1, Delta4 form; Contains: RecName: Full=Beta-crystallin A3, isoform A1, Delta7 form; Contains: RecName: Full=Beta-crystallin A3, isoform A1, Delta8 form;
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 (By similarity).
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 several truncated forms. Cleavages do not seem to have adverse effects on solubility.
PTM: S-methylation and glutathionylation occur in normal young lenses and do not seem to be detrimental.
PTM: Isoform A1 initiator methionine is removed. The new N- terminal amino acid is then N-acetylated.
MASS SPECTROMETRY: Mass=25192; Mass_error=3; Method=Electrospray; Range=1-215; Source=PubMed:8999933;
MASS SPECTROMETRY: Mass=25192; Method=Electrospray; Range=1-215; Source=PubMed:15576560;
MASS SPECTROMETRY: Mass=23101; Mass_error=3; Method=Electrospray; Range=19-215; Source=PubMed:8999933;
MASS SPECTROMETRY: Mass=23102; Method=Electrospray; Range=19-215; Source=PubMed:15576560;
MASS SPECTROMETRY: Mass=22646; Method=Electrospray; Range=23-215; Source=PubMed:15576560;
MASS SPECTROMETRY: Mass=22351; Method=Electrospray; Range=26-215; Source=PubMed:15576560;
MASS SPECTROMETRY: Mass=22294; Method=Electrospray; Range=27-215; Source=PubMed:15576560;
DISEASE: Defects in CRYBA1 are the cause of cataract congenital zonular with sutural opacities (CCZS) [MIM:600881]. A form of zonular cataract. Zonular or lamellar cataracts are concentric opacities, broad or narrow, usually consisting of powdery white dots affecting one lamella or zonule of an otherwise clear lens.
SIMILARITY: Belongs to the beta/gamma-crystallin family.
SIMILARITY: Contains 4 beta/gamma crystallin 'Greek key' domains.

-  Genetic Association Studies of Complex Diseases and Disorders
  Genetic Association Database (archive): CRYBA1
CDC HuGE Published Literature: CRYBA1

-  MalaCards Disease Associations
  MalaCards Gene Search: CRYBA1
Diseases sorted by gene-association score: cataract 10, multiple types* (1027), cataract 25* (143), early-onset nuclear cataract* (106), cataract 16, multiple types* (97), cataract (14), posterior polar cataract (12), cataract 9, multiple types (5)
* = Manually curated disease association

-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene

+  Common Gene Haplotype Alleles
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-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 0.11 RPKM in Brain - Cerebellar Hemisphere
Total median expression: 1.53 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
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-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
3' UTR -18.70135-0.139 Picture PostScript Text

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.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR001064 - Beta/gamma_crystallin
IPR011024 - G_crystallin-rel

Pfam Domains:
PF00030 - Beta/Gamma crystallin

SCOP Domains:
49695 - gamma-Crystallin-like

ModBase Predicted Comparative 3D Structure on P05813
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  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.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologGenome BrowserNo orthologNo orthologNo ortholog
Gene Details     
Gene Sorter     
  Ensembl   
  Protein Sequence   
  Alignment   

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0003674 molecular_function
GO:0005212 structural constituent of eye lens
GO:0005515 protein binding

Biological Process:
GO:0001818 negative regulation of cytokine production
GO:0002088 lens development in camera-type eye
GO:0007601 visual perception
GO:0014067 negative regulation of phosphatidylinositol 3-kinase signaling
GO:0032007 negative regulation of TOR signaling
GO:0051898 negative regulation of protein kinase B signaling
GO:0070373 negative regulation of ERK1 and ERK2 cascade
GO:2000210 positive regulation of anoikis

Cellular Component:
GO:0005634 nucleus
GO:0005737 cytoplasm


-  Descriptions from all associated GenBank mRNAs
  JD369535 - Sequence 350559 from Patent EP1572962.
BC113693 - Homo sapiens crystallin, beta A1, mRNA (cDNA clone MGC:142253 IMAGE:8322745), complete cds.
CU686900 - Synthetic construct Homo sapiens gateway clone IMAGE:100022570 5' read CRYBA1 mRNA.
HQ258110 - Synthetic construct Homo sapiens clone IMAGE:100072419 crystallin, beta A1 (CRYBA1) gene, encodes complete protein.
HQ448459 - Synthetic construct Homo sapiens clone IMAGE:100071887; CCSB013867_01 crystallin, beta A1 (CRYBA1) gene, encodes complete protein.
KJ890972 - Synthetic construct Homo sapiens clone ccsbBroadEn_00366 CRYBA1 gene, encodes complete protein.
KR336661 - Homo sapiens isolate PS truncated beta-crystallin A3 (CRYBA1) mRNA, complete cds.
BC069537 - Homo sapiens crystallin, beta A1, mRNA (cDNA clone MGC:97015 IMAGE:7262224), complete cds.
KX119959 - Homo sapiens isolate MR67-CRYBA1A3-TV truncated beta crystallin A3/A1 chain (CRYBA1) mRNA, complete cds.
KM230602 - Homo sapiens beta crystallin A3 chain transcript CN (CRYBA1) mRNA, partial cds.
KM230603 - Homo sapiens beta crystallin A3 chain transcript LAM (CRYBA1) mRNA, partial cds.
KM230604 - Homo sapiens beta crystallin A3 chain transcript PS (CRYBA1) mRNA, partial cds.
KR336660 - Homo sapiens isolate CC beta-crystallin A3 (CRYBA1) mRNA, partial cds.
KM230605 - Homo sapiens beta crystallin A3 chain transcript TC (CRYBA1) mRNA, partial cds.
U59058 - Human beta-A3/A1 crystallin (CYRBA3/A1) mRNA, partial cds.
JD266096 - Sequence 247120 from Patent EP1572962.

-  Other Names for This Gene
  Alternate Gene Symbols: CRBA1_HUMAN, CRYB1, NM_005208, NP_005199, P05813, Q13633, Q14CM9
UCSC ID: uc002hdw.3
RefSeq Accession: NM_005208
Protein: P05813 (aka CRBA1_HUMAN or CRBA_HUMAN)
CCDS: CCDS11249.1

-  Gene Model Information
 
category: coding nonsense-mediated-decay: no RNA accession: NM_005208.4
exon count: 6CDS single in 3' UTR: no RNA size: 806
ORF size: 648CDS single in intron: no Alignment % ID: 100.00
txCdsPredict score: 1496.00frame shift in genome: no % Coverage: 98.01
has start codon: yes stop codon in genome: no # of Alignments: 1
has end codon: yes retained intron: no # AT/AC introns 0
selenocysteine: no end bleed into intron: 0# strange splices: 0
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-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.