CRYGS crystallin gamma S [Homo sapiens (human)] - Gene

Summary

Official Symbol: CRYGSprovided by HGNC
Official Full Name: crystallin gamma Sprovided by HGNC
Primary source: HGNC:HGNC:2417
See related: Ensembl:ENSG00000213139 MIM:123730; AllianceGenome:HGNC:2417
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: CRYG8; CTRCT20
Summary: 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]
Expression: Ubiquitous expression in spleen (RPKM 1.8), skin (RPKM 1.8) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 3q27.3

Exon count:: 3

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	3	NC_000003.12 (186538443..186544380, complement)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	3	NC_060927.1 (189354165..189360102, complement)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	3	NC_000003.11 (186256232..186262169, complement)

Chromosome 3 - NC_000003.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Human gammaS-Crystallin Mutation F10_Y11delinsLN in the First Greek Key Pair Destabilizes and Impairs Tight Packing Causing Cortical Lamellar Cataract.
Title: Human γS-Crystallin Mutation F10_Y11delinsLN in the First Greek Key Pair Destabilizes and Impairs Tight Packing Causing Cortical Lamellar Cataract.
The 18th amino acid glycine plays an essential role in maintaining the structural stabilities of gammaS-crystallin linking with congenital cataract.
Title: The 18th amino acid glycine plays an essential role in maintaining the structural stabilities of γS-crystallin linking with congenital cataract.
Human gammaS-Crystallin Resists Unfolding Despite Extensive Chemical Modification from Exposure to Ionizing Radiation.
Title: Human γS-Crystallin Resists Unfolding Despite Extensive Chemical Modification from Exposure to Ionizing Radiation.
A novel F30S mutation in gammaS-crystallin causes autosomal dominant congenital nuclear cataract by increasing susceptibility to stresses.
Title: A novel F30S mutation in γS-crystallin causes autosomal dominant congenital nuclear cataract by increasing susceptibility to stresses.
The cataract-related S39C variant increases gammaS-crystallin sensitivity to environmental stress by destroying the intermolecular disulfide cross-links.
Title: The cataract-related S39C variant increases γS-crystallin sensitivity to environmental stress by destroying the intermolecular disulfide cross-links.
ATP differentially antagonizes the crowding-induced destabilization of human gammaS-crystallin and its four cataract-causing mutants.
Title: ATP differentially antagonizes the crowding-induced destabilization of human γS-crystallin and its four cataract-causing mutants.
Cataract-causing G18V eliminates the antagonization by ATP against the crowding-induced destabilization of human gammaS-crystallin.
Title: Cataract-causing G18V eliminates the antagonization by ATP against the crowding-induced destabilization of human γS-crystallin.
Cumulative deamidations of the major lens protein gammaS-crystallin increase its aggregation during unfolding and oxidation.
Title: Cumulative deamidations of the major lens protein γS-crystallin increase its aggregation during unfolding and oxidation.
ATP antagonizes the crowding-induced destabilization of the human eye-lens protein gammaS-crystallin.
Title: ATP antagonizes the crowding-induced destabilization of the human eye-lens protein γS-crystallin.
Kinetic Stability of Long-Lived Human Lens gamma-Crystallins and Their Isolated Double Greek Key Domains.
Title: Kinetic Stability of Long-Lived Human Lens γ-Crystallins and Their Isolated Double Greek Key Domains.

Submit: New GeneRIF Correction See all GeneRIFs (39)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Cataract 20 multiple types MedGen: C0524524 OMIM: 116100 GeneReviews: Not available	Compare labs

EBI GWAS Catalog

Description
A genome-wide association study of behavioral disinhibition. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
integrase	gag-pol	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	PubMed

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

STS-L36869 (e-PCR)
- UniSTS:49744

D11S3114 (e-PCR)
- UniSTS:152207

RH68614 (e-PCR)
- UniSTS:966

NoName (e-PCR)
- UniSTS:481525

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables structural constituent of eye lens	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in lens development in camera-type eye	IBA Inferred from Biological aspect of Ancestor more info
involved_in morphogenesis of an epithelium	IEA Inferred from Electronic Annotation more info
involved_in visual perception	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: gamma-crystallin S

Names: beta-crystallin S; crystallin, gamma 8

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.