UniProtKB/Swiss-Prot P02489: Variant p.Arg119His

Alpha-crystallin A chain
Gene: CRYAA
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Variant information Variant position:

119 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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:

From Arginine (R) to Histidine (H) at position 119 (R119H, p.Arg119His). 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:

Change from large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 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:

In CTRCT9; uncertain significance. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs760170206 [ dbSNP | Ensembl ]

Sequence information Variant position:

119 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

173 The length of the canonical sequence.
Location on the sequence:

KHNERQDDHGYISREFHRRY R LPSNVDQSALSCSLSADGML 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:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         KHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGML

                              KHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGML

Rhesus macaque                KHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGML

Mouse                         KHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGML

Rat                           KHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGML

Pig                           KHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGML

Bovine                        KHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGML

Rabbit                        KHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGML

Sheep                         KHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGML

Cat                           KHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGML

Horse                         KHNERQDDHGYISREFHRRYRLPSNVDQTALSCSVSADGML

Chicken                       KHSERQDDHGYISREFHRRYRLPANVDQSAITCSLSSDGML

Sequence annotation in neighborhood:

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.

Type	Positions	Description
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
Site	138 – 138	Susceptible to oxidation
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
Novel Mutations in the Crystallin Gene in Age-Related Cataract Patients from a North Indian Population.
Patel R.; Zenith R.K.; Chandra A.; Ali A.;
Mol. Syndromol. 8:179-186(2017)
Cited for: VARIANTS CTRCT9 GLN-65 AND HIS-119;

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.