CRYAB crystallin, alpha B [Homo sapiens] - Gene

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Summary

Official Symbol: CRYABprovided by HGNC
Official Full Name: crystallin, alpha Bprovided by HGNC
Primary source: HGNC:2389
See related: Ensembl:ENSG00000109846; HPRD:00428; MIM:123590; Vega:OTTHUMG00000166885
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: CRYA2; CTPP2; HSPB5
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]

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Genomic context

Location :: 11q22.3-q23.1

Sequence :: Chromosome: 11; NC_000011.9 (111779350..111782473, complement)

See CRYAB in Epigenomics, MapViewer

Chromosome 11 - NC_000011.9 Genomic Context describing neighboring genes

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Genomic regions, transcripts, and products

Genomic Sequence

Go to nucleotideGraphics FASTA GenBank

Go to reference sequence details

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Bibliography

GeneRIFs: Gene References Into Functions What's a GeneRIF?

A novel CRYAB mutation, D109H, associated with posterior polar cataract, myofibrillar myopathy and cardiomyopathy in a two-generation family with five affected individuals.
Title: A novel CRYAB mutation resulting in multisystemic disease.
The data suggest that all three sequences (beta3-strand, beta8-strand and C-terminal residues 155-165) of alphaB-crystallin contribute to its interaction with desmin filaments.
Title: Multiple sites in αB-crystallin modulate its interactions with desmin filaments assembled in vitro.
analysis of molecular architecture of the eye lens chaperone alphaB-crystallin elucidated by a triple hybrid approach
Title: Multiple molecular architectures of the eye lens chaperone αB-crystallin elucidated by a triple hybrid approach.
Structural and mechanistic implications of metal binding in the small heat-shock protein alphaB-crystallin.
Title: Structural and mechanistic implications of metal binding in the small heat-shock protein αB-crystallin.
Results provide the first evidence that the G allele of CRYAB C-802G is correlated with oral cancer risk and this polymorphism may be a useful marker for oral cancer recurrence and survival prediction for clinical reference.
Title: Association of alpha B-crystallin genotypes with oral cancer susceptibility, survival, and recurrence in Taiwan.
Our results provide evidence that the G allele of CRYAB C-802G is correlated with breast cancer risk and this polymorphism may be a useful marker for early detection of breast cancer in clinical practice.
Title: Association of Alpha B-Crystallin (CRYAB) genotypes with breast cancer susceptibility in Taiwan.
Novel mutations in the crystalline genes have been identified in Chinese families with congenital cataracts.
Title: Mutation analysis of 12 genes in Chinese families with congenital cataracts.
Alpha-B-crystallin may be used as an adjunct marker in the diagnosis of metaplastic carcinoma.
Title: Increased alpha-B-crystallin expression in mammary metaplastic carcinomas.
strong down-regulation of MCK activity contributes to F-actin instability and induces post-translational modification of alphaB-crystallin and desmin
Title: Muscle creatine kinase deficiency triggers both actin depolymerization and desmin disorganization by advanced glycation end products in dilated cardiomyopathy.
These findings indicate a novel function for BAG3 in inhibiting protein aggregation caused by the genetic mutation of CRYAB responsible for human myofibrillar myopathy.
Title: BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicity.

Submit: New GeneRIF Correction See all (136)

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Phenotypes

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Myopathy, myofibrillar, alpha-B crystallin-related

MIM: 608810

Myopathy, myofibrillar, fatal infantile hypertrophy, alpha-B crystallin-related

MIM: 613869

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Products	Interactant	Other Gene	Source	Pubs	Description
NP_001876.1		BAX	BIND	PubMed	HalphaB-crystallin interacts with Bax.
NP_001876.1	NP_001182.1	BCL2L1	BIND	PubMed	HalphaB-crystallin interacts with Bcl-Xs.
P02511	P05067	APP	HPRD	PubMed
P02511	Q07817	BCL2L1	HPRD	PubMed
P02511	Q13873	BMPR2	HPRD	PubMed
P02511	P02489	CRYAA	HPRD	PubMed
P02511	P02511	CRYAB	HPRD	PubMed
P02511	P43320	CRYBB2	HPRD	PubMed
P02511	P07315	CRYGC	HPRD	PubMed
P02511	O75390	CS	HPRD	PubMed
P02511	P11171	EPB41	HPRD	PubMed
P02511	P04792	HSPB1	HPRD	PubMed
P02511	P25788	PSMA3	HPRD	PubMed
P02511	Q8WZ42	TTN	HPRD	PubMed
BioGRID:107800	BioGRID:108791	ADAM2	BioGRID	PubMed	Affinity Capture-Western
BioGRID:107800	BioGRID:107127	BMPR2	BioGRID	PubMed	Affinity Capture-MS
BioGRID:107800	BioGRID:107067	CCND1	BioGRID	PubMed	Biochemical Activity; Reconstituted Complex
BioGRID:107800	BioGRID:107799	CRYAA	BioGRID	PubMed	Affinity Capture-Western; Two-hybrid
BioGRID:107800	BioGRID:107800	CRYAB	BioGRID	PubMed	Two-hybrid
BioGRID:107800	BioGRID:107805	CRYBB2	BioGRID	PubMed	Affinity Capture-Western; Two-hybrid
BioGRID:107800	BioGRID:107810	CRYGC	BioGRID	PubMed	Affinity Capture-Western; Two-hybrid
BioGRID:107800	BioGRID:107818	CS	BioGRID	PubMed	Reconstituted Complex
BioGRID:107800	BioGRID:109315	HDAC1	BioGRID	PubMed	Affinity Capture-Western
BioGRID:107800	BioGRID:109547	HSPB1	BioGRID	PubMed	Affinity Capture-Western; Co-purification; Reconstituted Complex; Two-hybrid
BioGRID:107800	BioGRID:109548	HSPB2	BioGRID	PubMed	Two-hybrid
BioGRID:107800	BioGRID:111657	PSMA3	BioGRID	PubMed	Affinity Capture-Western; Co-fractionation; Two-hybrid
BioGRID:107800	BioGRID:111683	PSMD4	BioGRID	PubMed	Affinity Capture-MS
BioGRID:107800	BioGRID:113164	UBC	BioGRID	PubMed	Affinity Capture-MS

Function	Evidence Code	Pubs
protein binding	IPI Inferred from Physical Interaction more info	PubMed
protein homodimerization activity	IPI Inferred from Physical Interaction more info	PubMed
structural constituent of eye lens	IEA Inferred from Electronic Annotation more info
unfolded protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
anti-apoptosis	IDA Inferred from Direct Assay more info	PubMed
muscle contraction	TAS Traceable Author Statement more info	PubMed
negative regulation of intracellular transport	IDA Inferred from Direct Assay more info	PubMed
protein folding	NAS Non-traceable Author Statement more info	PubMed
protein homooligomerization	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
cytoplasm	IDA Inferred from Direct Assay more info	PubMed
nucleus	IDA Inferred from Direct Assay more info	PubMed

General protein information

Preferred Names: alpha-crystallin B chain

Names: alpha-crystallin B chain; heat shock protein beta-5; rosenthal fiber component; heat-shock 20 kD like-protein; renal carcinoma antigen NY-REN-27

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NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_009824.1 RefSeqGene

Range

5001..8124

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001885.1 → NP_001876.1 alpha-crystallin B chain

Status: REVIEWED

Source sequence(s)

S45630

Consensus CDS

CCDS8351.1

UniProtKB/Swiss-Prot

P02511

Related

ENSP00000436051, OTTHUMP00000234278, ENST00000526180, OTTHUMT00000391654

Conserved Domains (3) summary

COG0071
Location:40 – 161
Blast Score: 124

IbpA; Molecular chaperone (small heat shock protein) [Posttranslational modification, protein turnover, chaperones]

cd06498
Location:67 – 150
Blast Score: 409

ACD_alphaB-crystallin_HspB5; Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaB-crystallin (HspB5, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers ...

pfam00525
Location:1 – 59
Blast Score: 242

Crystallin; Alpha crystallin A chain, N terminal

RefSeqs of Annotated Genomes: Build 37.3

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh37.p5 Primary Assembly

Genomic

NC_000011.9 Reference GRCh37.p5 Primary Assembly

Range

111779350..111782473, complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

AC_000143.1 Alternate HuRef

Range

107703256..107706379, complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

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Related Sequences

Nucleotide		Protein
Heading	Accession and Version	Protein
genomic	AP000907.6 (10242..13365)	None
genomic	CH471065.1	EAW67162.1
		EAW67163.1
		EAW67164.1
		EAW67165.1
		EAW67166.1
		EAW67167.1
genomic	EF444955.1	ACA05949.1
genomic	M28638.1	AAA52104.1
mRNA	AF007162.1	AAC19161.1
mRNA	AK295498.1	BAG58418.1
mRNA	AK314029.1	BAG36739.1
mRNA	BC007008.1	AAH07008.1
mRNA	BT006770.1	AAP35416.1
mRNA	FJ876064.1	ACP18852.1
mRNA	M24906.1	AAA60267.1
mRNA	S45630.1	AAB23453.1
other-genetic	AM392549.1	CAL37427.1
other-genetic	AM393027.1	CAL37905.1
other-genetic	DQ892517.2	ABM83443.1
other-genetic	DQ895729.2	ABM86655.1