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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02511: Variant p.Arg120Gly

Alpha-crystallin B chain
Gene: CRYAB
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Variant information Variant position: help 120 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 Glycine (G) at position 120 (R120G, p.Arg120Gly). 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 glycine (G) 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 MFM2; decreased interactions with wild-type CRYAA and CRYAB but increased interactions with wild-type CRYBB2 and CRYGC; cytoplasmic aggregation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 120 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 175 The length of the canonical sequence.
Location on the sequence: help VHGKHEERQDEHGFISREFH R KYRIPADVDPLTITSSLSSD 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                         VHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSD

Mouse                         VHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSD

Rat                           VHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSD

Pig                           VHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSD

Bovine                        VHGKHEERQDEHGFISREFHRKYRIPADVDPLAITSSLSSD

Rabbit                        VHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSD

Sheep                         VHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSD

Chicken                       IHGKHEERQDEHGFIAREFSRKYRIPADVDPLTITSSLSLD
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 – 175 Alpha-crystallin B chain
Domain 56 – 164 sHSP
Binding site 104 – 104
Binding site 106 – 106
Binding site 111 – 111
Binding site 119 – 119
Beta strand 112 – 123



Literature citations
The novel alphaB-crystallin (CRYAB) mutation p.D109G causes restrictive cardiomyopathy.
Brodehl A.; Gaertner-Rommel A.; Klauke B.; Grewe S.A.; Schirmer I.; Peterschroeder A.; Faber L.; Vorgerd M.; Gummert J.; Anselmetti D.; Schulz U.; Paluszkiewicz L.; Milting H.;
Hum. Mutat. 38:947-952(2017)
Cited for: SUBCELLULAR LOCATION; TISSUE SPECIFICITY; INVOLVEMENT IN RESTRICTIVE CARDIOMYOPATHY; VARIANT GLY-109; CHARACTERIZATION OF VARIANT GLY-109 AND GLY-120; A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy.
Vicart P.; Caron A.; Guicheney P.; Li Z.; Prevost M.-C.; Faure A.; Chateau D.; Chapon F.; Tome F.; Dupret J.-M.; Paulin D.; Fardeau M.;
Nat. Genet. 20:92-95(1998)
Cited for: VARIANT MFM2 GLY-120; Alteration of protein-protein interactions of congenital cataract crystallin mutants.
Fu L.; Liang J.J.-N.;
Invest. Ophthalmol. Vis. Sci. 44:1155-1159(2003)
Cited for: CHARACTERIZATION OF VARIANTS MFM2 GLY-120;
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.