Version 5.4
Bos taurus Gene: CRYAB
Summary
InnateDB Gene IDBG-630321.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol CRYAB
Gene Name Alpha-crystallin B chain
Synonyms
Species Bos taurus
Ensembl Gene ENSBTAG00000000434
Encoded Proteins
IDBP-681769
Alpha-crystallin B chain
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
InnateDB Annotation from Orthologs
Summary
PMID 23242137
[Mus musculus] CRYAB is a suppressor of neuroinflammation, and the suppression is mediated by DRD2 in astrocytes.
Entrez Gene
Summary This gene does not have any Entrez summary - the following is the summary from its human ortholog ENSG00000109846:
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. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. [provided by RefSeq, Jul 2008]
Mammalian lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
Gene Information
Type Protein coding
Genomic Location Chromosome 15:22566929-22570256
Strand Reverse strand
Band
Transcripts
ENSBTAT00000000556 ENSBTAP00000000556
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 4 experimentally validated interaction(s) in this database.
They are also associated with 49 interaction(s) predicted by orthology.
Experimentally validated
Total 4 [view]
Protein-Protein 4 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 49 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005212 structural constituent of eye lens
GO:0005515 protein binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0051082 unfolded protein binding
Biological Process
GO:0001666 response to hypoxia
GO:0002088 lens development in camera-type eye
GO:0007021 tubulin complex assembly
GO:0007517 muscle organ development
GO:0010629 negative regulation of gene expression
GO:0010941 regulation of cell death
GO:0032387 negative regulation of intracellular transport
GO:0042542 response to hydrogen peroxide
GO:0043010 camera-type eye development
GO:0043066 negative regulation of apoptotic process
GO:0043154 negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
GO:0051260 protein homooligomerization
GO:0060561 apoptotic process involved in morphogenesis
GO:0071480 cellular response to gamma radiation
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0030018 Z disc
GO:0043292 contractile fiber
GO:0070062 extracellular vesicular exosome
Orthologs
Species
Homo sapiens
Mus musculus
Gene ID
Gene Order
ENSG00000109846
View Gene Order
ENSMUSG00000032060
View Gene Order
Pathway Predictions based on Human Orthology Data
NETPATH
NetPath_9
TNFalpha pathway
REACTOME
KEGG
hsa04141
Protein processing in endoplasmic reticulum pathway
mmu04141
Protein processing in endoplasmic reticulum pathway
INOH
PID NCI
Cross-References
SwissProt P02510
TrEMBL V6F832
UniProt Splice Variant
Entrez Gene 281719
UniGene Bt.88059
RefSeq NM_174290
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL AF029793 BC102745 GJ062397
GenPept AAB95323 AAI02746 DAA22360
RNA Seq Atlas 281719

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca