CRYBB1

Protein identityUniProt · HPA

UniProt accession

P53674

Gene

CRYBB1

Ensembl

ENSG00000100122

Chromosome

22

Canonical length

252 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 basic group member, undergoes extensive cleavage at its N-terminal extension during lens maturation. It is also a member of a gene cluster with beta-A4, beta-B2, and beta-B3. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

252 residues, UniProt reviewed canonical sequence.

>P53674|CRYBB1
     1  MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR
    61  LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE
   121  YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS
   181  DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE
   241  GSFPVLATEP PK

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against CRYBB1 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)

0.37

Highest tissue expression

9.1 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about CRYBB1.

Disease | AllUniProt

Conditions CRYBB1 is implicated in, by any mechanism.

• Cataract 17, multiple types (CTRCT17) MIM:611544

Disease | GeneticClinVar

14 pathogenic / likely-pathogenic of 126 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Cataract 17 multiple types
• Developmental cataract
• Cataract 17
• Early-onset non-syndromic cataract

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

0.35

DepMap mean gene effect

0.03

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% 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

• structural constituent of eye lens

Protein domainsUniProt · Pfam · InterPro

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

KeywordsUniProt

• Acetylation
• Cataract
• Eye lens protein
• Repeat