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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02489: Variant p.Arg49Cys

Alpha-crystallin A chain
Gene: CRYAA
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Variant information Variant position: help 49 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 49 (R49C, p.Arg49Cys). 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. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 49 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 EGLFEYDLLPFLSSTISPYY R QSLFRTVLDSGISEVRSDRD 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                         EGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISE-----------------------VRSDRD

                              EGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISE------

Rhesus macaque                EGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISE------

Mouse                         EGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISELMTHMW

Rat                           EGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISELMTHMW

Pig                           EGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGVSE------

Bovine                        EGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISE------

Rabbit                        EGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISE------

Sheep                         EGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISE------

Cat                           EGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISE------

Horse                         EGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISE------

Chicken                       EGLLEYDLLPLFSSTISPYYRQSLFRSVLESGISE------
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)
Region 1 – 63 Required for complex formation with BFSP1 and BFSP2; during homooligomerization, mediates the association of 2 dimers to form a tetramer
Site 34 – 34 Susceptible to oxidation
Modified residue 45 – 45 Phosphoserine
Modified residue 50 – 50 Deamidated glutamine; partial



Literature citations
Cell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21q.
Mackay D.S.; Andley U.P.; Shiels A.;
Eur. J. Hum. Genet. 11:784-793(2003)
Cited for: VARIANT CTRCT9 CYS-49; SUBCELLULAR LOCATION; Comprehensive mutational screening in a cohort of Danish families with hereditary congenital cataract.
Hansen L.; Mikkelsen A.; Nuernberg P.; Nuernberg G.; Anjum I.; Eiberg H.; Rosenberg T.;
Invest. Ophthalmol. Vis. Sci. 50:3291-3303(2009)
Cited for: VARIANTS CTRCT9 TRP-21 AND CYS-49; The genetic landscape of crystallins in congenital cataract.
Berry V.; Ionides A.; Pontikos N.; Georgiou M.; Yu J.; Ocaka L.A.; Moore A.T.; Quinlan R.A.; Michaelides M.;
Orphanet J. Rare Dis. 15:333-333(2020)
Cited for: VARIANT CTRCT9 CYS-49;
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.