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Tbio Beta-crystallin S

Crystallins are the dominant structural components of the vertebrate eye lens.

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]

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Property Summary

NCBI Gene PubMed Count 35
PubMed Score 605.09
PubTator Score 48.42

Knowledge Summary

Patent

No data available

TINX Plot

  Disease Sources (5)

Disease Target Count P-value
subependymal giant cell astrocytoma 2287 0.0273952492793592
Disease Target Count Z-score Confidence
Cataract 104 4.961 2.5
Disease Target Count Z-score Confidence
Blindness 84 3.642 1.8
Microphthalmia 79 3.277 1.6
Disease Target Count
cataract 20 multiple types 1

Expression

  Differential Expression (1)

Disease log2 FC p
subependymal giant cell astrocytoma 4.044 0.027

Synonym

Accession P22914 B2RAF8
Symbols CRYG8
CTRCT20

Gene

CRYGS

PDB

1HA4   2M3T   2M3U  

  Ortholog (8)

Species Source
Chimp OMA EggNOG
Mouse OMA EggNOG Inparanoid
Rat OMA EggNOG Inparanoid
Cow OMA EggNOG Inparanoid
Opossum OMA EggNOG Inparanoid
Platypus OMA EggNOG Inparanoid
Chicken OMA EggNOG Inparanoid
Anole lizard OMA EggNOG Inparanoid

 GO Function (1)

 GO Process (2)

 Compartment GO Term (7)

 OMIM Term (1)

 MGI Term (1)

 HCA RNA Cell Line (56)

See all...

Pathway (1)

 UniProt Keyword (9)

Gene RIF (19)

PMID Text
26158710 The data suggest that enhanced attractive protein-protein interactions, arising from the deamidation of HGS, promote protein aggregation, thereby leading to increased light scattering and opacity over time.
24328668 novel mutation (G57W) in CRYGS in this Chinese family is associated with autosomal dominant pulverulent cataract.
24287181 The effects of the V41M mutation on the structural changes of gamma S-crystallin were studied.
23761725 The cataract-associated mutant D26G of human gammaS-crystallin is remarkably close to the wild type molecule in structural features, with only a microenvironmental change in the packing around the mutation site.
23284690 replacement of valine in position 42 by the longer and bulkier methionine in human gammaS-crystallin perturbs the compact beta-sheet core packing topology in the N-terminal domain of the molecule
22995907 age-dependent cleavage of gammaS-crystallin generates a peptide that binds to cell membranes
22858140 A crystallin variant, derived from the C-terminal domain of the eye lens protein human gammaS-crystallin, interacts with the integrase C-terminal domain and inhibits integrase substrate affinity
22593035 The degree of deamidation for Gln92 and Gln170 was found to increase from birth to teen-age years and then to remain constant for four decades.
21866213 Novel mutations in the crystalline genes have been identified in Chinese families with congenital cataracts.
21447408 The presence of significant amounts of small peptides derived from gammaS- and betaB1-crystallins in the water-insoluble fraction of the lens indicates that these interact tightly with cytoskeletal or membrane components.
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AA Sequence 

MSKTGTKITFYEDKNFQGRRYDCDCDCADFHTYLSRCNSIKVEGGTWAVYERPNFAGYMYILPQGEYPEY      1 - 70
QRWMGLNDRLSSCRAVHLPSGGQYKIQIFEKGDFSGQMYETTEDCPSIMEQFHMREIHSCKVLEGVWIFY     71 - 140
ELPNYRGRQYLLDKKEYRKPIDWGAASPAVQSFRRIVE                                    141 - 178
//

Text Mined References (36)

PMID Year Title
26158710 2015 Deamidation of Human ?S-Crystallin Increases Attractive Protein Interactions: Implications for Cataract.
24328668 2015 A G57W Mutation of CRYGS Associated with Autosomal Dominant Pulverulent Cataracts in a Chinese Family.
24287181 2014 The cataract-associated V41M mutant of human ?S-crystallin shows specific structural changes that directly enhance local surface hydrophobicity.
23942779 2013 A genome-wide association study of behavioral disinhibition.
23761725 2013 Structural analysis of the mutant protein D26G of human ?S-crystallin, associated with Coppock cataract.
23284690 2012 The mutation V42M distorts the compact packing of the human gamma-S-crystallin molecule, resulting in congenital cataract.
22995907 2012 Degradation of an old human protein: age-dependent cleavage of ?S-crystallin generates a peptide that binds to cell membranes.
22593035 2012 Age-dependent deamidation of glutamine residues in human ?S crystallin: deamidation and unstructured regions.
21866213 2011 Mutation analysis of 12 genes in Chinese families with congenital cataracts.
21447408 2011 Truncation, cross-linking and interaction of crystallins and intermediate filament proteins in the aging human lens.
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