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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O43502: Variant p.Ala126Thr

DNA repair protein RAD51 homolog 3
Gene: RAD51C
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Variant information Variant position: help 126 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B 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 Alanine (A) to Threonine (T) at position 126 (A126T, p.Ala126Thr). 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 small size and hydrophobic (A) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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

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


Sequence information Variant position: help 126 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 376 The length of the canonical sequence.
Location on the sequence: help ALDDILGGGVPLMKTTEICG A PGVGKTQLCMQLAVDVQIPE 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                         ALDDILGGGVPLMKTTEICGAPGVGKTQLCMQLAVDVQIPE

Mouse                         ALDNILGGGIPLMKTTEVCGVPGVGKTQLCMQLAVDVQIPE

Slime mold                    EIDQMLNGGTPLKKITEICGVPGIGKTNMAFQLLVNTSIPF

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 – 376 DNA repair protein RAD51 homolog 3
Region 1 – 126 Required for Holliday junction resolution activity
Region 79 – 136 Interaction with RAD51B, RAD51D and XRCC3
Binding site 125 – 132
Alternative sequence 135 – 135 C -> W. In isoform 2.
Mutagenesis 131 – 131 K -> A. Significant loss of function; abolishes Holliday junction resolution activity.
Mutagenesis 131 – 131 K -> R. Partial loss of function.



Literature citations
Germline mutations in breast and ovarian cancer pedigrees establish RAD51C as a human cancer susceptibility gene.
Meindl A.; Hellebrand H.; Wiek C.; Erven V.; Wappenschmidt B.; Niederacher D.; Freund M.; Lichtner P.; Hartmann L.; Schaal H.; Ramser J.; Honisch E.; Kubisch C.; Wichmann H.E.; Kast K.; Deissler H.; Engel C.; Muller-Myhsok B.; Neveling K.; Kiechle M.; Mathew C.G.; Schindler D.; Schmutzler R.K.; Hanenberg H.;
Nat. Genet. 42:410-414(2010)
Cited for: VARIANTS ARG-3; THR-126; ASN-159; ALA-169; SER-264; VAL-264; ALA-287 AND GLN-366; VARIANTS BROVCA3 VAL-125 AND PHE-138; Analysis of RAD51C germline mutations in high-risk breast and ovarian cancer families and ovarian cancer patients.
Thompson E.R.; Boyle S.E.; Johnson J.; Ryland G.L.; Sawyer S.; Choong D.Y.; Chenevix-Trench G.; Trainer A.H.; Lindeman G.J.; Mitchell G.; James P.A.; Campbell I.G.;
Hum. Mutat. 33:95-99(2012)
Cited for: VARIANTS LEU-52; PHE-103 DEL; VAL-114; THR-126; ALA-169; THR-175; CYS-249; VAL-262 AND SER-264; VARIANTS BROVCA3 GLU-162; PRO-178 AND ALA-287;
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.