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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q6UWZ7: Variant p.Asp373Asn

BRCA1-A complex subunit Abraxas 1
Gene: ABRAXAS1
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Variant information Variant position: help 373 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Aspartate (D) to Asparagine (N) at position 373 (D373N, p.Asp373Asn). 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: help Change from medium size and acidic (D) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help Links to websites of interest for the variant.


Sequence information Variant position: help 373 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 409 The length of the canonical sequence.
Location on the sequence: help DRWQFKRSRLLDTQDKRSKA D TGSSNQDKASKMSSPETDEE 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         DRWQFKRSRLLDTQDKRSK-ADTGSSNQDKASKMSSPETDEE-

Mouse                         DQGSVKRPRLLETESRPSV-AASRSRHQDKASS-SSLDIDI

Rat                           DQWPAKRPRLLESESRPG--PAFRGSHQDKASS-SSLDIDT

Bovine                        DGWQFKKSRLGGIQNRPSK-TDTNSSNQEQASTVSSPETDE

Chicken                       GPKSLKKLRSLQLDQELH--QDEEDCNQETKLALSSAETDE

Xenopus laevis                GKTSTKKSRLPPFQRPQSDNSDSESSDSEKLLCTSGTETDG

Xenopus tropicalis            GRTLTKKSRLLQLQKQHSQNGDSEGSDSERPLCNSGTETDG

Zebrafish                     FPQRLKRKR--------------KTREVSESASESGSDTEI

Sequence annotation in neighborhood: help 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 – 409 BRCA1-A complex subunit Abraxas 1
Region 362 – 409 Disordered
Modified residue 386 – 386 Phosphoserine
Modified residue 387 – 387 Phosphoserine
Modified residue 390 – 390 Phosphothreonine



Literature citations
The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.
Clark H.F.; Gurney A.L.; Abaya E.; Baker K.; Baldwin D.T.; Brush J.; Chen J.; Chow B.; Chui C.; Crowley C.; Currell B.; Deuel B.; Dowd P.; Eaton D.; Foster J.S.; Grimaldi C.; Gu Q.; Hass P.E.; Heldens S.; Huang A.; Kim H.S.; Klimowski L.; Jin Y.; Johnson S.; Lee J.; Lewis L.; Liao D.; Mark M.R.; Robbie E.; Sanchez C.; Schoenfeld J.; Seshagiri S.; Simmons L.; Singh J.; Smith V.; Stinson J.; Vagts A.; Vandlen R.L.; Watanabe C.; Wieand D.; Woods K.; Xie M.-H.; Yansura D.G.; Yi S.; Yu G.; Yuan J.; Zhang M.; Zhang Z.; Goddard A.D.; Wood W.I.; Godowski P.J.; Gray A.M.;
Genome Res. 13:2265-2270(2003)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1); VARIANT ASN-373; Analysis of the genes coding for the BRCA1-interacting proteins, RAP80 and Abraxas (CCDC98), in high-risk, non-BRCA1/2, multiethnic breast cancer cases.
Novak D.J.; Sabbaghian N.; Maillet P.; Chappuis P.O.; Foulkes W.D.; Tischkowitz M.;
Breast Cancer Res. Treat. 117:453-459(2009)
Cited for: VARIANTS THR-348 AND ASN-373; 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;
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.