CRYGS, crystallin gamma S

CRYGS, crystallin gamma S

• 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. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. This gene encodes a protein initially considered to be a beta-crystallin but the encoded protein is monomeric and has greater sequence similarity to other gamma-crystallins. This gene encodes the most significant gamma-crystallin in adult eye lens tissue. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation. [provided by RefSeq, Jul 2008]

• Gene Synonyms (gamma-crystallin S, beta-crystallin S, crystallin, gamma 8, CRYG8, CTRCT20,)
• NCBI Gene ID: 1427
• Species: Homo sapiens (Human)
• UNIPROT ID#>>P22914
  UNIPROT ID#>>A0A140CTX8
• View the NCBI Database for this Gene »

Gene products are often involved in multiple pathways and networks within a living cell. Learn more about other interacting partners.

crystallin gamma S interacts with:

• C-terminal Src kinase
  protection of telomeres 1
  TERF1 interacting nuclear factor 2
  TERF2 interacting protein

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