Non-annotated gene. Preliminary data : if you are an author who wish to write a full paper/card on this gene, contribute in submission tool
Other Information
Locus ID:
NCBI: 1427
MIM: 123730
HGNC: 2417
Ensembl: ENSG00000213139
Variants:
dbSNP: 1427
ClinVar: 1427
TCGA: ENSG00000213139
COSMIC: CRYGS
RNA/Proteins
| Gene ID | Transcript ID | Uniprot |
|---|---|---|
| ENSG00000213139 | ENST00000307944 | P22914 |
| ENSG00000213139 | ENST00000307944 | A0A140CTX8 |
| ENSG00000213139 | ENST00000392499 | P22914 |
| ENSG00000213139 | ENST00000392499 | A0A140CTX8 |
Expression (GTEx)
Protein levels (Protein atlas)
References
| Pubmed ID | Year | Title | Citations |
|---|---|---|---|
| 37586630 | 2023 | The 18th amino acid glycine plays an essential role in maintaining the structural stabilities of γS-crystallin linking with congenital cataract. | 0 |
| 37762633 | 2023 | Human γS-Crystallin Mutation F10_Y11delinsLN in the First Greek Key Pair Destabilizes and Impairs Tight Packing Causing Cortical Lamellar Cataract. | 0 |
| 37586630 | 2023 | The 18th amino acid glycine plays an essential role in maintaining the structural stabilities of γS-crystallin linking with congenital cataract. | 0 |
| 37762633 | 2023 | Human γS-Crystallin Mutation F10_Y11delinsLN in the First Greek Key Pair Destabilizes and Impairs Tight Packing Causing Cortical Lamellar Cataract. | 0 |
| 35021623 | 2022 | Human γS-Crystallin Resists Unfolding Despite Extensive Chemical Modification from Exposure to Ionizing Radiation. | 0 |
| 35021623 | 2022 | Human γS-Crystallin Resists Unfolding Despite Extensive Chemical Modification from Exposure to Ionizing Radiation. | 0 |
| 33454329 | 2021 | A novel F30S mutation in γS-crystallin causes autosomal dominant congenital nuclear cataract by increasing susceptibility to stresses. | 3 |
| 33454329 | 2021 | A novel F30S mutation in γS-crystallin causes autosomal dominant congenital nuclear cataract by increasing susceptibility to stresses. | 3 |
| 31812542 | 2020 | Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein. | 5 |
| 32234236 | 2020 | The cataract-related S39C variant increases γS-crystallin sensitivity to environmental stress by destroying the intermolecular disulfide cross-links. | 4 |
| 32307080 | 2020 | ATP antagonizes the crowding-induced destabilization of the human eye-lens protein γS-crystallin. | 7 |
| 32697405 | 2020 | Cumulative deamidations of the major lens protein γS-crystallin increase its aggregation during unfolding and oxidation. | 20 |
| 32753316 | 2020 | Cataract-causing G18V eliminates the antagonization by ATP against the crowding-induced destabilization of human γS-crystallin. | 2 |
| 33004175 | 2020 | ATP differentially antagonizes the crowding-induced destabilization of human γS-crystallin and its four cataract-causing mutants. | 6 |
| 31812542 | 2020 | Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein. | 5 |
Citation
Dessen P
CRYGS (crystallin gamma S)
Atlas Genet Cytogenet Oncol Haematol. 2018-11-01
Online version: http://atlasgeneticsoncology.org/gene/57635/crygs-(crystallin-gamma-s)
