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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02489: Variant p.Gly98Arg

Alpha-crystallin A chain
Gene: CRYAA
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Variant information Variant position: help 98 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 Glycine (G) to Arginine (R) at position 98 (G98R, p.Gly98Arg). 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 glycine (G) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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; forms inclusion bodies, decreases chaperone activity, decreases protein stability at 45 degrees Celsius and increases protein aggregate formation in response to DTT in vitro. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 98 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 KHFSPEDLTVKVQDDFVEIH G KHNERQDDHGYISREFHRRY 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                         KHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRY

                              KHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRY

Rhesus macaque                KHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRY

Mouse                         KHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRY

Rat                           KHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRY

Pig                           KHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRY

Bovine                        KHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRY

Rabbit                        KHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRY

Sheep                         KHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRY

Cat                           KHFSPEDLTVKVLEDFVEIHGKHNERQDDHGYISREFHRRY

Horse                         KHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRY

Chicken                       KHFSPEDLSVKIIDDFVEIHGKHSERQDDHGYISREFHRRY
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 90 – 90 Deamidated glutamine; partial
Modified residue 99 – 99 N6-acetyllysine
Modified residue 101 – 101 Deamidated asparagine; partial



Literature citations
Identification of a novel, putative cataract-causing allele in CRYAA (G98R) in an Indian family.
Santhiya S.T.; Soker T.; Klopp N.; Illig T.; Prakash M.V.; Selvaraj B.; Gopinath P.M.; Graw J.;
Mol. Vis. 12:768-773(2006)
Cited for: VARIANT CTRCT9 ARG-98; Cataract-causing alphaAG98R mutant shows substrate-dependent chaperone activity.
Murugesan R.; Santhoshkumar P.; Sharma K.K.;
Mol. Vis. 13:2301-2309(2007)
Cited for: CHARACTERIZATION OF VARIANT CTRCT9 ARG-98; FUNCTION; Mutation analysis of 12 genes in Chinese families with congenital cataracts.
Sun W.; Xiao X.; Li S.; Guo X.; Zhang Q.;
Mol. Vis. 17:2197-2206(2011)
Cited for: VARIANTS CTRCT9 ARG-98 AND 117-ARG-TYR-118 DELINS HIS;
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.