Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02489: Variant p.Arg116Cys

Alpha-crystallin A chain
Gene: CRYAA
Feedback?
Variant information Variant position: help 116 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Arginine (R) to Cysteine (C) at position 116 (R116C, p.Arg116Cys). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (R) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In CTRCT9; zonular central nuclear cataract; reduced chaperone-like activity and increased membrane-binding capacity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 116 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 173 The length of the canonical sequence.
Location on the sequence: help IHGKHNERQDDHGYISREFH R RYRLPSNVDQSALSCSLSAD The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         IHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSAD

                              IHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSAD

Rhesus macaque                IHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSAD

Mouse                         IHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSAD

Rat                           IHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSAD

Pig                           IHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSAD

Bovine                        IHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSAD

Rabbit                        IHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSAD

Sheep                         IHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSAD

Cat                           IHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSAD

Horse                         IHGKHNERQDDHGYISREFHRRYRLPSNVDQTALSCSVSAD

Chicken                       IHGKHSERQDDHGYISREFHRRYRLPANVDQSAITCSLSSD
Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 1 – 173 Alpha-crystallin A chain
Chain 1 – 172 Alpha-crystallin A(1-172)
Chain 1 – 168 Alpha-crystallin A(1-168)
Chain 1 – 162 Alpha-crystallin A(1-162)
Domain 52 – 164 sHSP
Binding site 100 – 100
Binding site 102 – 102
Binding site 107 – 107
Modified residue 99 – 99 N6-acetyllysine
Modified residue 101 – 101 Deamidated asparagine; partial
Modified residue 122 – 122 Phosphoserine
Modified residue 123 – 123 Deamidated asparagine; partial
Mutagenesis 123 – 123 N -> D. Impairs chaperone activity.



Literature citations
Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA.
Litt M.; Kramer P.; la Morticella D.M.; Murphey W.; Lovrien E.W.; Weleber R.G.;
Hum. Mol. Genet. 7:471-474(1998)
Cited for: VARIANT CTRCT9 CYS-116; Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts.
Cobb B.A.; Petrash J.M.;
Biochemistry 39:15791-15798(2000)
Cited for: CHARACTERIZATION OF VARIANT CTRCT9 CYS-116; A novel fan-shaped cataract-microcornea syndrome caused by a mutation of CRYAA in an Indian family.
Vanita V.; Singh J.R.; Hejtmancik J.F.; Nuernberg P.; Hennies H.C.; Singh D.; Sperling K.;
Mol. Vis. 12:518-522(2006)
Cited for: VARIANT CTRCT9 CYS-116; New phenotype associated with an Arg116Cys mutation in the CRYAA gene: nuclear cataract, iris coloboma, and microphthalmia.
Beby F.; Commeaux C.; Bozon M.; Denis P.; Edery P.; Morle L.;
Arch. Ophthalmol. 125:213-216(2007)
Cited for: VARIANT CTRCT9 CYS-116; Autosomal dominant congenital nuclear cataracts caused by a CRYAA gene mutation.
Li F.F.; Yang M.; Ma X.; Zhang Q.; Zhang M.; Wang S.Z.; Zhu S.Q.;
Curr. Eye Res. 35:492-498(2010)
Cited for: VARIANT CTRCT9 CYS-116; Mutation screening of crystallin genes in Chinese families with congenital cataracts.
Zhuang J.; Cao Z.; Zhu Y.; Liu L.; Tong Y.; Chen X.; Wang Y.; Lu C.; Ma X.; Yang J.;
Mol. Vis. 25:427-437(2019)
Cited for: VARIANTS CTRCT9 LEU-12; TRP-21 AND CYS-116;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.