CRYBB1

Name

crystallin beta B1

Type

protein-coding

Position

26,599,277–26,619,630 (−)

Aliases

CATCN3, CTRCT17

Ensembl

ENSG00000100122

RefSeq RNA

NM_001887.4, XM_011529899.4, XM_054325113.1

RefSeq protein

NP_001878.1, XP_011528201.1, XP_054181088.1

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, 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].

via MyGene.info

Gene · Ensembl

crystallin beta B1

Symbol

CRYBB1

Biotype

Protein coding

Organism

Homo sapiens

Location

22:26,599,277-26,619,630

Strand

Reverse (−)

Assembly

GRCh38

Wikidata facts

Image

Protein CRYBB1 PDB 1oki.png

via Wikidata · CC0