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UniProtKB/Swiss-Prot Q13426: Variant p.Asp82Glu

DNA repair protein XRCC4
Gene: XRCC4
Variant information

Variant position:  82
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Aspartate (D) to Glutamate (E) at position 82 (D82E, p.Asp82Glu).
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:  Similar physico-chemical property. Both residues are medium size and acidic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  In SSMED; impaired ability to repair DNA double-strand breaks.
Any additional useful information about the variant.



Sequence information

Variant position:  82
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  336
The length of the canonical sequence.

Location on the sequence:   EKGKYVGELRKALLSGAGPA  D VYTFNFSKESCYFFFEKNLK
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                         EKGKYVGELRKALLSGAGPADVYTFNFS--KESCYFFFEKNLK

Mouse                         EKGKYIDELRKALVPGSGAAGTYKFLFS--KESQHFSLEKE

Slime mold                    SFDQYFQLLKKSLLKQDQTKREFDYKIDKYKRKNNNNINNN

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 – 336 DNA repair protein XRCC4
Region 1 – 213 Interaction with IFFO1
Mutagenesis 62 – 62 E -> R. Does not affect interaction with NHEJ1/XLF.
Mutagenesis 65 – 65 K -> E. Strongly decreased interaction with NHEJ1/XLF. Abolished interaction with NHEJ1/XLF; when associated with E-99. Abolished ability to bridge DNA; when associated with E-99. Abolished interaction with NHEJ1/XLF; when associated with E-102.
Mutagenesis 69 – 69 E -> R. Does not affect interaction with NHEJ1/XLF.
Mutagenesis 71 – 71 R -> E. Abolished interaction with NHEJ1/XLF; when associated with E-99.
Mutagenesis 72 – 72 K -> E. Abolished interaction with NHEJ1/XLF; when associated with E-99. Abolished ability to bridge DNA; when associated with E-90 and E-99.
Mutagenesis 90 – 90 K -> E. Abolished ability to bridge DNA; when associated with E-72 and E-99.
Mutagenesis 99 – 99 K -> E. Abolished interaction with NHEJ1/XLF; when associated with E-4 or E-26 or E-65 or E-71 or E-72. Abolished ability to bridge DNA; when associated with E-65. Abolished ability to bridge DNA; when associated with E-72 and E-90.
Mutagenesis 102 – 102 K -> E. Abolished interaction with NHEJ1/XLF; when associated with E-65.


Literature citations

An XRCC4 splice mutation associated with severe short stature, gonadal failure, and early-onset metabolic syndrome.
de Bruin C.; Mericq V.; Andrew S.F.; van Duyvenvoorde H.A.; Verkaik N.S.; Losekoot M.; Porollo A.; Garcia H.; Kuang Y.; Hanson D.; Clayton P.; van Gent D.C.; Wit J.M.; Hwa V.; Dauber A.;
J. Clin. Endocrinol. Metab. 100:E789-E798(2015)
Cited for: VARIANT SSMED GLU-82; CHARACTERIZATION OF VARIANT SSMED GLU-82; FUNCTION;

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.