Variant position: 524 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 934 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 GLDPGKQIKLDSSAQFGYYF RVTCKEEKVLR-NNKNFSTVDI
Mouse GLDPGKQIKLDSSAQFGYYF RVTCKEEKVLR-NNKNFSTVD
Rat GLDPGKQIKLDSSAQFGYYF RVTCKEEKVLR-NNKNFSTVD
Bovine GLDPGKQIKLDSSTQFGYYF RVTCKEEKVLR-NNKNFSTVD
Drosophila NLDGKNQVKLESVAKLGHHF RITVKDDSVLR-KNKNYRIVD
Slime mold NLD-EAKVKLHYSEKDMFLL RISRKDEVAIR-DKKKYIVHA
Baker's yeast GFDPDKKLKLENHHLHGWCM RLTRNDAKELR-KHKKYIELS
Fission yeast HQDTEKKLHLEQHHLYGWCL RLTRTEAGCLRGRSSHYTELS
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
2 – 934 DNA mismatch repair protein Msh2
521 – 525
Functional analysis of human MutSalpha and MutSbeta complexes in yeast.
Clark A.B.; Cook M.E.; Tran H.T.; Gordenin D.A.; Resnick M.A.; Kunkel T.A.;
Nucleic Acids Res. 27:736-742(1999)
Cited for: MISMATCH-BINDING; CHARACTERIZATION OF VARIANT HNPCC1 PRO-524;
Mutator phenotypes of common polymorphisms and missense mutations in MSH2.
Drotschmann K.; Clark A.B.; Kunkel T.A.;
Curr. Biol. 9:907-910(1999)
Cited for: CHARACTERIZATION OF VARIANTS ASP-322; PHE-390; LYS-419; TYR-506; PRO-524; LEU-622 AND PHE-697;
HNPCC mutations in hMSH2 result in reduced hMSH2-hMSH6 molecular switch functions.
Heinen C.D.; Wilson T.; Mazurek A.; Berardini M.; Butz C.; Fishel R.;
Cancer Cell 1:469-478(2002)
Cited for: VARIANTS HNPCC1 HIS-167; MET-393; PRO-524; ASN-596 DEL; LEU-622; SER-674 AND ARG-905; CHARACTERIZATION OF VARIANTS HNPCC1 HIS-167; MET-393; PRO-524; ASN-596 DEL; LEU-622; SER-674 AND ARG-905;
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.