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UniProtKB/Swiss-Prot Q9BX63: Variant p.Met299Ile

Fanconi anemia group J protein
Gene: BRIP1
Variant information

Variant position:  299
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 Methionine (M) to Isoleucine (I) at position 299 (M299I, p.Met299Ile).
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 hydrophobic.
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; early onset; reduces helicase efficiency on longer substrates.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  299
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  1249
The length of the canonical sequence.

Location on the sequence:   RDHTCVHPEVVGNFNRNEKC  M ELLDGKNGKSCYFYHGVHKI
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                         RDHTCVHPEVV-GNFNRNEKCMELLDGKNGKSCYFYHGVHKI

Mouse                         RDHSCVHPEVV-GNFNRKEKCMELLDGKHGKSCYFYHGVHK

Chicken                       RDYTCIHPVVSSSNSNRNELCVELLEGKHGKSCLYYHGVHK

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 – 1249 Fanconi anemia group J protein
Domain 11 – 442 Helicase ATP-binding
Metal binding 283 – 283 Iron-sulfur (4Fe-4S)
Metal binding 298 – 298 Iron-sulfur (4Fe-4S)
Metal binding 310 – 310 Iron-sulfur (4Fe-4S)


Literature citations

BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function.
Cantor S.B.; Bell D.W.; Ganesan S.; Kass E.M.; Drapkin R.; Grossman S.; Wahrer D.C.R.; Sgroi D.C.; Lane W.S.; Haber D.A.; Livingston D.M.;
Cell 105:149-160(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); PROTEIN SEQUENCE OF 708-747; 765-790; 815-831; 1079-1085; 1169-1174 AND 1215-1225; FUNCTION; TISSUE SPECIFICITY; SUBCELLULAR LOCATION; INTERACTION WITH BRCA1; MUTAGENESIS OF LYS-52; VARIANTS BC ALA-47 AND ILE-299; VARIANTS ILE-193 AND PRO-919; IDENTIFICATION BY MASS SPECTROMETRY;

The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations.
Cantor S.B.; Drapkin R.; Zhang F.; Lin Y.; Han J.; Pamidi S.; Livingston D.M.;
Proc. Natl. Acad. Sci. U.S.A. 101:2357-2362(2004)
Cited for: FUNCTION; MUTAGENESIS OF LYS-52; CHARACTERIZATION OF VARIANTS BC ALA-47 AND ILE-299;

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.