CRYBA1 crystallin beta A1 [Homo sapiens (human)] - Gene

Summary

Official Symbol: CRYBA1provided by HGNC
Official Full Name: crystallin beta A1provided by HGNC
Primary source: HGNC:HGNC:2394
See related: Ensembl:ENSG00000108255 MIM:123610; AllianceGenome:HGNC:2394
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: CRYB1; CTRCT10
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. 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]
Expression: Low expression observed in reference dataset See more
Orthologs: mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 17q11.2

Exon count:: 6

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	17	NC_000017.11 (29246859..29254494)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	17	NC_060941.1 (30189627..30197262)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	17	NC_000017.10 (27573877..27581512)

Chromosome 17 - NC_000017.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Cataract-causing G91del mutant destabilised betaA3 heteromers formation linking with structural stability and cellular viability.
Title: Cataract-causing G91del mutant destabilised βA3 heteromers formation linking with structural stability and cellular viability.
A novel missense mutation of CRYBA1 in a northern Chinese family with inherited coronary cataract with blue punctate opacities.
Title: A novel missense mutation of CRYBA1 in a northern Chinese family with inherited coronary cataract with blue punctate opacities.
Pathogenic mechanism of congenital cataract caused by the CRYBA1/A3-G91del variant and related intervention strategies.
Title: Pathogenic mechanism of congenital cataract caused by the CRYBA1/A3-G91del variant and related intervention strategies.
CRYBA1 showed lower expression in cataract lenses than in control lenses. The deleted form (p.G91del) of CRYBA1 showed lower expression and was more aggregate to the cell membrane than the wild-type CRYBA1.
Title: The identification and characterization of the p.G91 deletion in CRYBA1 in a Chinese family with congenital cataracts.
This study investigated the mechanism of cataracts caused by a c.215 + 1G > A splice mutation in CRYBA1. The mutant beta A3/A1 crystallin causes toxicity and degeneration of differentiating lens cells. The mutant beta A3/A1 crystallin acts by inducing the unfolded protein response culminating in apoptosis.
Title: Human βA3/A1-crystallin splicing mutation causes cataracts by activating the unfolded protein response and inducing apoptosis in differentiating lens fiber cells.
A recurrent DeltaG91CRYBA1/A3 mutation occurs independently in 6.4% of the Chinese families with autosomal dominant nuclear cataracts and most likely represents a mutational hot spot, which underscores the relations between nonprogressive nuclear cataract and CRYBA1/A3.
Title: Mutation Analysis of Families with Autosomal Dominant Congenital Cataract: A Recurrent Mutation in the CRYBA1/A3 Gene Causing Congenital Nuclear Cataract.
We identified a de novo in-frame 3-bp deletion in the proband with an autosomal dominant congenital cataract, but not in her parents, in an Iranian family. This mutation has occurred de novo on a paternal gamete during spermatogenesis. The in-silico results predicted the interaction of CRYBA1 protein with the other CRY as well as proteins responsible for eye cell signaling.
Title: Identification of a De Novo 3bp Deletion in CRYBA1/A3 Gene in Autosomal Dominant Congenital Cataract.
The findings suggest that impaired endolysosomal signaling in ocular astrocytes can cause PFV disease, by adversely affecting the vascular remodeling processes essential to ocular development, including regression of the fetal vasculature. [review]
Title: βA3/A1-crystallin and persistent fetal vasculature (PFV) disease of the eye.
association between a frameshift mutation in exon 6 of CRYBA1/A3 and congenital cataracts
Title: Congenital cataracts due to a novel 2‑bp deletion in CRYBA1/A3.
Data indicate that alpha-crystallin B chain and beta-crystallin A3-cyrstallins dissociate to the monomers upon racemization of d-aspartic acids (Asp).
Title: Alpha B- and βA3-crystallins containing d-aspartic acids exist in a monomeric state.

Submit: New GeneRIF Correction See all GeneRIFs (31)

Phenotypes

Go to the top of the page Help

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

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Cataract 10 multiple types MedGen: C1833229 OMIM: 600881 GeneReviews: Not available	Compare labs

Copy number response

Description
Copy number response Haploinsufficency No evidence available (Last evaluated 2013-06-06) ClinGen Genome Curation Page Triplosensitivity No evidence available (Last evaluated 2013-06-06) ClinGen Genome Curation Page

Variation

Go to the top of the page Help

See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Markers

GDB:180957 (e-PCR)
- UniSTS:155144

NoName (e-PCR)
- UniSTS:483100

NoName (e-PCR)
- UniSTS:481859

RH79897 (e-PCR)
- UniSTS:85206

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables molecular_function	ND No biological Data available more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables structural constituent of eye lens	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in lens development in camera-type eye	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of ERK1 and ERK2 cascade	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of TOR signaling	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of cytokine production	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction	IEA Inferred from Electronic Annotation more info
involved_in phagocytosis	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of anoikis	IEA Inferred from Electronic Annotation more info
involved_in regulation of autophagy	IEA Inferred from Electronic Annotation more info
involved_in visual perception	IBA Inferred from Biological aspect of Ancestor more info
involved_in visual perception	NAS Non-traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	ISS Inferred from Sequence or Structural Similarity more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info

General protein information

Go to the top of the page Help

Preferred Names: beta-crystallin A3

Names: beta crystallin A3 chain transcript CN; beta crystallin A3 chain transcript LAM; beta crystallin A3 chain transcript PS; beta crystallin A3 chain transcript TC; crystallin beta A3/A1; crystallin, beta A3; eye lens structural protein

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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.