Version 5.4
Homo sapiens Gene: CRYAB
Summary
InnateDB Gene IDBG-71081.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol CRYAB
Gene Name crystallin, alpha B
Synonyms CMD1II; CRYA2; CTPP2; CTRCT16; HEL-S-101; HSPB5; MFM2
Species Homo sapiens
Ensembl Gene ENSG00000109846
Encoded Proteins
IDBP-71083
crystallin, alpha B
IDBP-589858
crystallin, alpha B
IDBP-587441
crystallin, alpha B
IDBP-599692
crystallin, alpha B
IDBP-586735
crystallin, alpha B
IDBP-590543
crystallin, alpha B
IDBP-595809
crystallin, alpha B
IDBP-600855
crystallin, alpha B
IDBP-592699
crystallin, alpha B
IDBP-600393
crystallin, alpha B
IDBP-596071
crystallin, alpha B
IDBP-594242
crystallin, alpha B
IDBP-586566
crystallin, alpha B
IDBP-595810
crystallin, alpha B
IDBP-601920
crystallin, alpha B
IDBP-807004
crystallin, alpha B
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 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 11:111908565-111923722
Strand Reverse strand
Band q23.1
Transcripts
ENST00000227251 ENSP00000227251
ENST00000526180 ENSP00000436051
ENST00000524660 ENSP00000432454
ENST00000533280 ENSP00000435046
ENST00000525823 ENSP00000435411
ENST00000533475 ENSP00000433560
ENST00000527950 ENSP00000437149
ENST00000531198 ENSP00000434247
ENST00000528961 ENSP00000435960
ENST00000527899 ENSP00000436089
ENST00000526167 ENSP00000434793
ENST00000529647 ENSP00000431754
ENST00000533971 ENSP00000434269
ENST00000528628 ENSP00000432182
ENST00000533879 ENSP00000435931
ENST00000616970 ENSP00000483554
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 98 experimentally validated interaction(s) in this database.
They are also associated with 12 interaction(s) predicted by orthology.
Experimentally validated
Total 98 [view]
Protein-Protein 98 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 12 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005212 structural constituent of eye lens
GO:0005515 protein binding
GO:0008017 microtubule binding
GO:0008092 cytoskeletal 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:0006457 protein folding
GO:0006936 muscle contraction
GO:0007021 tubulin complex assembly
GO:0007517 muscle organ development
GO:0007568 aging
GO:0010629 negative regulation of gene expression
GO:0010941 regulation of cell death
GO:0030308 negative regulation of cell growth
GO:0031109 microtubule polymerization or depolymerization
GO:0032355 response to estradiol
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:0051403 stress-activated MAPK cascade
GO:0060561 apoptotic process involved in morphogenesis
GO:0071480 cellular response to gamma radiation
GO:2000378 negative regulation of reactive oxygen species metabolic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005794 Golgi apparatus
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0015630 microtubule cytoskeleton
GO:0030018 Z disc
GO:0031674 I band
GO:0032432 actin filament bundle
GO:0043292 contractile fiber
GO:0070062 extracellular vesicular exosome
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000032060
View Gene Order
ENSBTAG00000000434
Not yet available
Pathways
NETPATH
NetPath_9
TNFalpha pathway
REACTOME
KEGG
hsa04141
Protein processing in endoplasmic reticulum pathway
INOH
PID NCI
Cross-References
SwissProt
TrEMBL E9PJL7 E9PNH7 E9PR44 E9PRS4 E9PS12
UniProt Splice Variant
Entrez Gene 1410
UniGene
RefSeq NM_001289807 NM_001289808 NM_001885
HUGO HGNC:2389
OMIM 123590
CCDS CCDS8351
HPRD 00428
IMGT
EMBL AP000907
GenPept
RNA Seq Atlas 1410

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