Variant position: 47 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:
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 AMMNSILRGLNSKQHCLLES PTGSGKSLALLCSALAWQQSL
Mouse AMMNSIVRGLNSSQHCLLES PTGSGKSLALLCSALAWQQSL
Chicken AMMNAIVKGLNNRQHCLLES PTGSGKSLALLCSALSWQQSL
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
1 – 1249 Fanconi anemia group J protein
11 – 442 Helicase ATP-binding
52 – 52 K -> R. Disrupts BRCA1-mediated double-strand break repair. Loss of ATPase and DNA helicase activities.
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.;
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;
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