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-KHKALDLDDRWQFKRSR LLDTQDKRSK-ADTGSSNQDK
Mouse AQLR-KRKALDTHDQGSVKRPR LLETESRPSV-AASRSRHQ
Rat APLS-KRKALDTQDQWPAKRPR LLESESRPG--PAFRGSHQ
Bovine ALLVTKRKASDTDDGWQFKKSR LGGIQNRPSK-TDTNSSNQ
Chicken KLVTKRKVRVTTTGPKSLKKLR SLQLDQELH--QDEEDCNQ
Xenopus laevis RQAGKRKAHSKQLGKTSTKKSR LPPFQRPQSDNSDSESSDS
Xenopus tropicalis RQAGKRKACSKQLGRTLTKKSR LLQLQKQHSQNGDSEGSDS
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;
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.