CRYBB2

Protein identityUniProt · HPA

UniProt accession

P43320

Gene

CRYBB2

Ensembl

ENSG00000244752

Chromosome

22

Canonical length

205 aa

Protein class

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

Subcellular location

Nucleoplasm

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 basic group member, is part of a gene cluster with beta-A4, beta-B1, and beta-B3. A chain-terminating mutation was found to cause type 2 cerulean cataracts. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

205 residues, UniProt reviewed canonical sequence.

>P43320|CRYBB2
     1  MASDHQTQAG KPQSLNPKII IFEQENFQGH SHELNGPCPN LKETGVEKAG SVLVQAGPWV
    61  GYEQANCKGE QFVFEKGEYP RWDSWTSSRR TDSLSSLRPI KVDSQEHKII LYENPNFTGK
   121  KMEIIDDDVP SFHAHGYQEK VSSVRVQSGT WVGYQYPGYR GLQYLLEKGD YKDSSDFGAP
   181  HPQVQSVRRI RDMQWHQRGA FHPSN

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against CRYBB2 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

2.2 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about CRYBB2.

Disease | AllUniProt

Conditions CRYBB2 is implicated in, by any mechanism.

• Cataract 3, multiple types (CTRCT3) MIM:601547

Disease | GeneticClinVar

15 pathogenic / likely-pathogenic of 142 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Cataract 3 multiple types
• Developmental cataract
• CRYBB2-related disorder

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)

0.57

gnomAD pLI

0.39

gnomAD missense Z

1.07

DepMap mean gene effect

0.05

DepMap dependency class

none

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
• visual perception

Molecular functions

• identical protein binding
• structural constituent of eye lens
• structural molecule activity

Protein domainsUniProt · Pfam · InterPro

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

KeywordsUniProt

• Acetylation
• Cataract
• Eye lens protein
• Repeat
• Sensory transduction
• Vision

InteractionsUniProt · HPA

Protein binding partners of CRYBB2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• CRYAA
• CRYAB
• CRYGC