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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02489: Variant p.Leu139Pro

Alpha-crystallin A chain
Gene: CRYAA
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Variant information Variant position: help 139 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 Leucine (L) to Proline (P) at position 139 (L139P, p.Leu139Pro). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. 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; results in protein aggregation in the cytoplasm. Any additional useful information about the variant.


Sequence information Variant position: help 139 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 RLPSNVDQSALSCSLSADGM L TFCGPKIQTGLDATHAERAI 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                         RLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAI

                              RLPSNVDQSALSCSLSADGMLTFSGPKVPSGVDAGHSERAI

Rhesus macaque                RLPSNVDQSALSCSLSADGMLTFSGPKIQTGLDATH-ERAI

Mouse                         RLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAI

Rat                           RLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAI

Pig                           RLPSNVDQSALSCSLSADGMLTFSGPKVPSGVDAGHSERAI

Bovine                        RLPSNVDQSALSCSLSADGMLTFSGPKIPSGVDAGHSERAI

Rabbit                        RLPSNVDQSALSCSLSADGMLTFSGPKVQSGLDAGHSERAI

Sheep                         RLPSNVDQSALSCSLSADGMLTFSGPKVPSGVDAGHSERAI

Cat                           RLPSNVDQSALSCSLSADGMLTFSGPKVPSGVDAGHSERAI

Horse                         RLPSNVDQTALSCSVSADGMLTFSGPKIPSGMDAGHSERAI

Chicken                       RLPANVDQSAITCSLSSDGMLTFSGPKVPSNMDPSHSERPI
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 154 – 154
Site 138 – 138 Susceptible to oxidation
Modified residue 122 – 122 Phosphoserine
Modified residue 123 – 123 Deamidated asparagine; partial
Modified residue 147 – 147 Deamidated glutamine; partial
Disulfide bond 131 – 142
Mutagenesis 123 – 123 N -> D. Impairs chaperone activity.



Literature citations
Mutation analysis of two families with inherited congenital cataracts.
Liang C.; Liang H.; Yang Y.; Ping L.; Jie Q.;
Mol. Med. Report. 12:3469-3475(2015)
Cited for: VARIANT CTRCT9 PRO-139; SUBCELLULAR LOCATION;
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.