CRYBA1

Protein identityUniProt · HPA

UniProt accession

P05813

Gene

CRYBA1

Ensembl

ENSG00000108255

Chromosome

17

Canonical length

215 aa

Protein class

Disease related genes, Human disease related genes, Plasma proteins, Predicted intracellular proteins

OverviewNCBI Gene

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]

Canonical amino-acid sequenceUniProt

215 residues, UniProt reviewed canonical sequence.

>P05813|CRYBA1
     1  METQAEQQEL ETLPTTKMAQ TNPTPGSLGP WKITIYDQEN FQGKRMEFTS SCPNVSERSF
    61  DNVRSLKVES GAWIGYEHTS FCGQQFILER GEYPRWDAWS GSNAYHIERL MSFRPICSAN
   121  HKESKMTIFE KENFIGRQWE ISDDYPSLQA MGWFNNEVGS MKIQSGAWVC YQYPGYRGYQ
   181  YILECDHHGG DYKHWREWGS HAQTSQIQSI RRIQQ

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against CRYBA1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Unknown

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.29

Highest tissue expression

0.2 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about CRYBA1.

Disease | AllUniProt

Conditions CRYBA1 is implicated in, by any mechanism.

• Cataract 10, multiple types (CTRCT10) MIM:600881

Disease | GeneticClinVar

16 pathogenic / likely-pathogenic of 94 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Cataract 10 multiple types
• CRYBA1-related disorder
• Inborn genetic diseases

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

1

gnomAD pLI

0

gnomAD missense Z

0.63

DepMap mean gene effect

-0.18

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• lens development in camera-type eye
• negative regulation of cytokine production
• negative regulation of ERK1 and ERK2 cascade
• negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
• negative regulation of TOR signaling
• phagocytosis
• positive regulation of anoikis
• regulation of autophagy
• visual perception

Molecular functions

• structural constituent of eye lens

Protein domainsUniProt · Pfam · InterPro

• Beta/gamma crystallin
• Gamma-crystallin-like
• Beta/Gamma-Crystallin
• Beta/Gamma crystallin

KeywordsUniProt

• Acetylation
• Alternative initiation
• Cataract
• Eye lens protein
• Glutathionylation
• Methylation
• Oxidation
• Repeat

InteractionsUniProt · HPA

Protein binding partners of CRYBA1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• SLC36A4
• CRYAB