CRYBB2

Name

crystallin beta B2

Type

protein-coding

Position

25,212,564–25,231,870 (+)

Aliases

CCA2, CRYB2, CRYB2A, CTRCT3, D22S665

Ensembl

ENSG00000244752

RefSeq RNA

NM_000496.3, XM_006724141.4, XM_054325114.1, XM_054325115.1

RefSeq protein

NP_000487.1, XP_006724204.1, XP_054181089.1, XP_054181090.1

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].

via MyGene.info

Gene · Ensembl

crystallin beta B2

Symbol

CRYBB2

Biotype

Protein coding

Organism

Homo sapiens

Location

22:25,212,564-25,231,870

Strand

Forward (+)

Assembly

GRCh38

Wikidata facts

Image

Protein CRYBB2 PDB 1bd7.png

via Wikidata · CC0