Variant position: 138 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 376 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 MKTTEICGAPGVGKTQLCMQ LAVDVQIPECFGGVAGEAVFI
Mouse MKTTEVCGVPGVGKTQLCMQ LAVDVQIPECFGGVAGEAVFI
Slime mold KKITEICGVPGIGKTNMAFQ LLVNTSIPFDLGGVQGKAIYI
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 – 376 DNA repair protein RAD51 homolog 3
135 – 135 C -> W. In isoform 2.
136 – 376 Missing. In isoform 2.
131 – 131 K -> A. Significant loss of function; abolishes Holliday junction resolution activity.
131 – 131 K -> R. Partial loss of function.
Breast cancer-associated missense mutants of the PALB2 WD40 domain, which directly binds RAD51C, RAD51 and BRCA2, disrupt DNA repair.
Park J.Y.; Singh T.R.; Nassar N.; Zhang F.; Freund M.; Hanenberg H.; Meetei A.R.; Andreassen P.R.;
Cited for: INTERACTION WITH BRCA2; RAD51 AND PALB2; IDENTIFICATION IN A PALB2-CONTAINING HR COMPLEX; CHARACTERIZATION OF VARIANT BROVCA3 PHE-138; CHARACTERIZATION OF VARIANT ASN-159; CHARACTERIZATION OF VARIANT FANCO HIS-258;
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;
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.