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UniProtKB/Swiss-Prot P02489: Variant p.Asp105His

Alpha-crystallin A chain
Gene: CRYAA
Variant information

Variant position:  105
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Unclassified
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Aspartate (D) to Histidine (H) at position 105 (D105H, p.Asp105His).
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 medium size and acidic (D) to medium size and polar (H)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -1
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 a breast cancer sample; somatic mutation.
Any additional useful information about the variant.



Sequence information

Variant position:  105
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:   LTVKVQDDFVEIHGKHNERQ  D DHGYISREFHRRYRLPSNVD
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                         LTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVD

                              LTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVD

Rhesus macaque                LTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVD

Mouse                         LTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVD

Rat                           LTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVD

Pig                           LTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVD

Bovine                        LTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVD

Rabbit                        LTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVD

Sheep                         LTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVD

Cat                           LTVKVLEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVD

Horse                         LTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVD

Chicken                       LSVKIIDDFVEIHGKHSERQDDHGYISREFHRRYRLPANVD

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.

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
Metal binding 100 – 100 Zinc 2
Metal binding 102 – 102 Zinc 2
Metal binding 107 – 107 Zinc 1
Metal binding 115 – 115 Zinc 1
Modified residue 90 – 90 Deamidated glutamine; partial
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

The consensus coding sequences of human breast and colorectal cancers.
Sjoeblom T.; Jones S.; Wood L.D.; Parsons D.W.; Lin J.; Barber T.D.; Mandelker D.; Leary R.J.; Ptak J.; Silliman N.; Szabo S.; Buckhaults P.; Farrell C.; Meeh P.; Markowitz S.D.; Willis J.; Dawson D.; Willson J.K.V.; Gazdar A.F.; Hartigan J.; Wu L.; Liu C.; Parmigiani G.; Park B.H.; Bachman K.E.; Papadopoulos N.; Vogelstein B.; Kinzler K.W.; Velculescu V.E.;
Science 314:268-274(2006)
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-105;

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.