UniProtKB/Swiss-Prot Q13426: Variant p.Ala247Ser

DNA repair protein XRCC4
Gene: XRCC4
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Variant information Variant position:

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

LB/B 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 Alanine (A) to Serine (S) at position 247 (A247S, p.Ala247Ser). 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 small size and hydrophobic (A) to small size and polar (S) 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
Other resources:

Links to websites of interest for the variant.

Variant rs3734091 [ dbSNP | Ensembl ]

Sequence information Variant position:

247 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:

PVYDESTDEESENQTDLSGL A SAAVSKDDSIISSLDVTDIA 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                         PVY-----------------DESTDEESENQTDLSGLASAAVSKDD-----------------------------------------------------------SIISSL--DVTDIA

Mouse                         GLY-----------------DGSTDEESGAPVQ----AAET

Slime mold                    QVYTTPKKKKRNYQSNLINIDNDDDDDLGNNDNVNNINDEN

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 – 336	DNA repair protein XRCC4
Region	212 – 249	Disordered
Modified residue	229 – 229	Phosphotyrosine
Modified residue	232 – 232	Phosphoserine
Modified residue	233 – 233	Phosphothreonine; by CK2
Modified residue	237 – 237	Phosphoserine
Modified residue	256 – 256	Phosphoserine
Modified residue	260 – 260	Phosphoserine; by PRKDC
Mutagenesis	233 – 233	T -> A. Abolished phosphorylation by CK2, leading to strongly reduced interaction with PNKP.
Mutagenesis	235 – 235	E -> F. Impaired ability mediate double-strand break repair.
Mutagenesis	260 – 260	S -> A. Reduced phosphorylation by PRKDC. In XRCC4-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with NHEJ1/XLF phosphorylation-defective mutant; when associated with A-193, A-304, A-315, A-320, A-323, A-327 and A-328.
Mutagenesis	260 – 260	S -> D. In XRCC4-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with NHEJ1/XLF phospho-mimetic mutant; when associated with D-193, D-304, D-315, D-320, D-323, D-327 and D-328.
Mutagenesis	264 – 264	T -> A. Does not affect phosphorylation by CK2.
Mutagenesis	266 – 266	I -> G. Abolished cleavage by caspase and ability to regulate phospholipid scramblase activity.

Literature citations
Submission
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS CYS-12; THR-56; THR-134; GLN-142 AND SER-247;

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.