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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q06609: Variant p.Arg150Gln

DNA repair protein RAD51 homolog 1
Gene: RAD51
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Variant information Variant position: help 150 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Arginine (R) to Glutamine (Q) at position 150 (R150Q, p.Arg150Gln). 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 large size and basic (R) to medium size and polar (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In BC; decreased ATPase activity in the presence of stoichiometric ss-DNA concentrations with respect to RAD51; 3 to 4-fold decrease of affinity for ATP. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 150 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 339 The length of the canonical sequence.
Location on the sequence: help RTGKTQICHTLAVTCQLPID R GGGEGKAMYIDTEGTFRPER 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                         RTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPER

                              RTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPER

Mouse                         RTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPER

Bovine                        RTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPER

Rabbit                        RTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPER

Chicken                       RTGKTQLCHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPER

Drosophila                    RCGKTQLCHTLAVTCQLPISQKGGEGKCMYIDTENTFRPER

Baker's yeast                 RTGKSQLCHTLAVTCQIPLDIGGGEGKCLYIDTEGTFRPVR

Fission yeast                 RTGKSQICHTLAVTCQLPIDMGGGEGKCLYIDTEGTFRPVR
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 2 – 339 DNA repair protein RAD51 homolog 1
Alternative sequence 77 – 173 Missing. In isoform 2.
Helix 148 – 150



Literature citations
Identification of Rad51 alteration in patients with bilateral breast cancer.
Kato M.; Yano K.; Matsuo F.; Saito H.; Katagiri T.; Kurumizaka H.; Yoshimoto M.; Kasumi F.; Akiyama F.; Sakamoto G.; Nagawa H.; Nakamura Y.; Miki Y.;
J. Hum. Genet. 45:133-137(2000)
Cited for: VARIANT BC GLN-150; Tumor-associated mutations in a conserved structural motif alter physical and biochemical properties of human RAD51 recombinase.
Chen J.; Morrical M.D.; Donigan K.A.; Weidhaas J.B.; Sweasy J.B.; Averill A.M.; Tomczak J.A.; Morrical S.W.;
Nucleic Acids Res. 43:1098-1111(2015)
Cited for: CHARACTERIZATION OF VARIANT BC GLN-150;
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.