UniProtKB/Swiss-Prot P40692: Variant p.Val384Asp

DNA mismatch repair protein Mlh1
Gene: MLH1
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Variant information Variant position:

384 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Valine (V) to Aspartate (D) at position 384 (V384D, p.Val384Asp). 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:

Change from medium size and hydrophobic (V) to medium size and acidic (D) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-3 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:

Probable risk factor for HNPCC in some populations. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs63750447 [ dbSNP | Ensembl ]

Sequence information Variant position:

384 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

756 The length of the canonical sequence.
Location on the sequence:

TSLTSSSTSGSSDKVYAHQM V RTDSREQKLDAFLQPLSKPL 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                         TSLTSSSTSGSSD----KVYAHQMVRTDSREQKLDAFLQPL---SKPL

Mouse                         TGVASSSTSGSGD----KVYAYQMVRTDSREQKLDAFLQPV

Rat                           TGIASSSTSGSGD----KVHAYQMVRTDSRDQKLDAFMQPV

Slime mold                    TNNNNNPTSRKEP----IEYAKDKIRSDSKSQTLDAFLNPM

Baker's yeast                 QVVENSYTTANSQLRKAKRQENKLVRIDASQAKITSFLSSS

Fission yeast                 NTKNAESSSQKAV----RTYENYLVRTDPRERSIKSMLS--

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	2 – 756	DNA mismatch repair protein Mlh1

Literature citations
Mutational analysis of mismatch repair genes, hMLH1 and hMSH2, in sporadic endometrial carcinomas with microsatellite instability.
Kobayashi K.; Matsushima M.; Koi S.; Saito H.; Sagae S.; Kudo R.; Nakamura Y.;
Jpn. J. Cancer Res. 87:141-145(1996)
Cited for: VARIANTS LEU-ASN-HIS-37 INS AND ASP-384; A novel missense mutation in the DNA mismatch repair gene hMLH1 present among East Asians but not among Europeans.
Wang Y.; Friedl W.; Lamberti C.; Noethen M.M.; Kruse R.; Propping P.;
Hum. Hered. 48:87-91(1998)
Cited for: VARIANT ASP-384; ASSOCIATION WITH HNPCC; Enhanced detection of deleterious and other germline mutations of hMSH2 and hMLH1 in Japanese hereditary nonpolyposis colorectal cancer kindreds.
Nomura S.; Sugano K.; Kashiwabara H.; Taniguchi T.; Fukayama N.; Fujita S.; Akasu T.; Moriya Y.; Ohhigashi S.; Kakizoe T.; Sekiya T.;
Biochem. Biophys. Res. Commun. 271:120-129(2000)
Cited for: VARIANTS LYNCH2 VAL-111 AND PRO-588; VARIANTS VAL-219 AND ASP-384;

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.