UniProtKB/SwissProt variant VAR

Variant information

Variant position:

361

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 Arginine (R) to Glutamine (Q) at position 361 (R361Q, p.Arg361Gln).

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 (Q)

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 BC; results in reduced DSB repair efficiency; primarily localizes to the cytoplasm and has reduced nuclear localization; does not affect interaction with BRCA1; results in highly reduced interaction with UIMC1/RAP80.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs201627097 [ dbSNP | Ensembl ]

Sequence information

Variant position:

361

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

Protein sequence length:

409

The length of the canonical sequence.

Location on the sequence:

PQIIKHKALDLDDRWQFKRS R LLDTQDKRSKADTGSSNQDK

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                         PQII-KHKALDLDDRWQFKRSRLLDTQDKRSK-ADTGSSNQDK

Mouse                         AQLR-KRKALDTHDQGSVKRPRLLETESRPSV-AASRSRHQ

Rat                           APLS-KRKALDTQDQWPAKRPRLLESESRPG--PAFRGSHQ

Bovine                        ALLVTKRKASDTDDGWQFKKSRLGGIQNRPSK-TDTNSSNQ

Chicken                       KLVTKRKVRVTTTGPKSLKKLRSLQLDQELH--QDEEDCNQ

Xenopus laevis                RQAGKRKAHSKQLGKTSTKKSRLPPFQRPQSDNSDSESSDS

Xenopus tropicalis            RQAGKRKACSKQLGRTLTKKSRLLQLQKQHSQNGDSEGSDS

Zebrafish                     L----RKKCLVASFPQRLKRKR--------------KTREV

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 – 409	BRCA1-A complex subunit Abraxas 1

Literature citations

Breast cancer-associated Abraxas mutation disrupts nuclear localization and DNA damage response functions.
Solyom S.; Aressy B.; Pylkas K.; Patterson-Fortin J.; Hartikainen J.M.; Kallioniemi A.; Kauppila S.; Nikkila J.; Kosma V.M.; Mannermaa A.; Greenberg R.A.; Winqvist R.;
Sci. Transl. Med. 4:122ra23-122ra23(2012)
Cited for: FUNCTION; VARIANTS THR-348 AND ASN-373; VARIANT BC GLN-361; CHARACTERIZATION OF VARIANT BC GLN-361;

Mislocalization of BRCA1-complex due to ABRAXAS Arg361Gln mutation.
Kumar R.V.; Siddiqui Q.; Singh N.; Waghmare S.K.; Varma A.K.;
J. Biomol. Struct. Dyn. 33:1291-1301(2015)
Cited for: CHARACTERIZATION OF VARIANT BC GLN-361;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q6UWZ7: Variant p.Arg361Gln