Sequence information
Variant position: 373 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:
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human DRWQFKRSRLLDTQDKRSK-AD TGSSNQDKASKMSSPETDEE-
Mouse DQGSVKRPRLLETESRPSV-AA SRSRHQDKASS-SSLDIDI
Rat DQWPAKRPRLLESESRPG--PA FRGSHQDKASS-SSLDIDT
Bovine DGWQFKKSRLGGIQNRPSK-TD TNSSNQEQASTVSSPETDE
Chicken GPKSLKKLRSLQLDQELH--QD EEDCNQETKLALSSAETDE
Xenopus laevis GKTSTKKSRLPPFQRPQSDNSD SESSDSEKLLCTSGTETDG
Xenopus tropicalis GRTLTKKSRLLQLQKQHSQNGD SEGSDSERPLCNSGTETDG
Zebrafish FPQRLKRKR------------- -KTREVSESASESGSDTEI
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
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.