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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P38398: Variant p.Trp1837Arg

Breast cancer type 1 susceptibility protein
Gene: BRCA1
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Variant information Variant position: help 1837 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Tryptophan (W) to Arginine (R) at position 1837 (W1837R, p.Trp1837Arg). 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 large size and aromatic (W) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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: help In BC; pathogenic; functionally impaired in vitro. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 1837 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1863 The length of the canonical sequence.
Location on the sequence: help EDNGFHAIGQMCEAPVVTRE W VLDSVALYQCQELDTYLIPQ 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                         EDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTY-LIPQ

Gorilla                       EDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTY-LIP

                              EDSGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTY-LIP

Rhesus macaque                EDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTY-LIP

Chimpanzee                    EDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTY-LIP

Mouse                         EDSNCPDIGQLCKARLVMWDWVLDSLSSYRCRDLDAY-LVQ

Rat                           EDNDCPDIGQLCKGRLVMWDWVLDSISVYRCRDLDAY-LVQ

Bovine                        EDAGFHVIGQMCEAPVVTREWVLDSVALYQCQELDTY-LVP

Caenorhabditis elegans        ESKN---IENLYKCDVVTMEWVLDSISEYLILPTQPYKAVD
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 – 1863 Breast cancer type 1 susceptibility protein
Domain 1756 – 1855 BRCT 2
Alternative sequence 64 – 1863 Missing. In isoform 2.
Alternative sequence 1778 – 1863 DQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIPHSHY -> GCPPNCGCAARCLDRGQWLPCNWADV. In isoform 6.
Mutagenesis 1835 – 1835 R -> P. Mildly reduces affinity for a BRIP1 phosphopeptide.
Mutagenesis 1836 – 1836 E -> K. Slightly reduces affinity for a BRIP1 phosphopeptide.
Helix 1835 – 1844



Literature citations
A high-throughput functional complementation assay for classification of BRCA1 missense variants.
Bouwman P.; van der Gulden H.; van der Heijden I.; Drost R.; Klijn C.N.; Prasetyanti P.; Pieterse M.; Wientjens E.; Seibler J.; Hogervorst F.B.; Jonkers J.;
Cancer Discov. 3:1142-1155(2013)
Cited for: CHARACTERIZATION OF VARIANTS BC PHE-4; THR-18; GLN-45; GLY-61; GLY-64; TYR-67; LYS-132; HIS-142; PHE-147; PRO-165; TRP-170; TYR-186; ILE-191; MET-231; VAL-245; VAL-246; LEU-271; PHE-668; ASN-695; LEU-798; TYR-810; LYS-826; GLN-841; HIS-856; ASN-1101; ASN-1140; GLY-1140; LYS-1214; LYS-1236; SER-1267; VAL-1282; SER-1297 DEL; ARG-1301; LYS-1346; ILE-1378; VAL-1400; PRO-1407; THR-1411; GLY-1443; GLY-1448; CYS-1486; MET-1534; PRO-1589; THR-1628; PRO-1651; PHE-1651; PHE-1655; ARG-1686; GLN-1686; VAL-1688 DEL; ILE-1691; TRP-1699; GLN-1699; GLU-1706; ALA-1706; GLU-1708; CYS-1718; ALA-1720; LYS-1735; ALA-1736; GLY-1739; VAL-1739; GLN-1746; THR-1753; PRO-1764; SER-1767; VAL-1770; CYS-1782; THR-1789; ASP-1794; ASP-1804; ARG-1812; ARG-1837 AND LEU-1862; VARIANTS CYS-105; CYS-866; ALA-1060; LYS-1250 AND ILE-1652;
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.