Human Gene CRYGS (ENST00000392499.6) from GENCODE V44
Description: Crystallins are the dominant structural components of the vertebrate eye lens. (from UniProt P22914) RefSeq Summary (NM_017541): 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]. Gencode Transcript: ENST00000392499.6 Gencode Gene: ENSG00000213139.8 Transcript (Including UTRs) Position: hg38 chr3:186,538,441-186,546,702 Size: 8,262 Total Exon Count: 4 Strand: - Coding Region Position: hg38 chr3:186,538,696-186,544,326 Size: 5,631 Coding Exon Count: 3
ID:CRBS_HUMAN DESCRIPTION: RecName: Full=Beta-crystallin S; AltName: Full=Gamma-S-crystallin; AltName: Full=Gamma-crystallin S; FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. SUBUNIT: Monomer. DOMAIN: Has a two-domain beta-structure, folded into four very similar Greek key motifs. MASS SPECTROMETRY: Mass=20918; Mass_error=0.3; Method=Electrospray; Range=2-178; Source=PubMed:8999933; SIMILARITY: Belongs to the beta/gamma-crystallin family. SIMILARITY: Contains 4 beta/gamma crystallin 'Greek key' domains.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P22914
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
