UniProtKB/SwissProt variant VAR

Variant information

Variant position:

512

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 Serine (S) to Phenylalanine (F) at position 512 (S512F, p.Ser512Phe).

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 small size and polar (S) to large size and aromatic (F)

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

-2

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:

Does not affect DNA glycosylase activity; does not affect function in DNA repair.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs140118273 [ dbSNP | Ensembl ]

Sequence information

Variant position:

512

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:

546

The length of the canonical sequence.

Location on the sequence:

RVYQGQQPGTCMGSKRSQVS S PCSRKKPRMGQQVLDNFFRS

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                         RVYQGQQPGTCMGSKRSQVSSPCSRKKPRMGQQVLDNFFRS

Mouse                         RMYEDHRQGTRKGSKRSQVCPPSSRKKPSLGQQVLDTFFQR

Rat                           RVYEEHRRGTCKGSKRPQVCTPSSRKKPSRGQQVLDRFFQR

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	1 – 546	Adenine DNA glycosylase

Literature citations

Multiple colorectal adenomas, classic adenomatous polyposis, and germ-line mutations in MYH.
Sieber O.M.; Lipton L.; Crabtree M.; Heinimann K.; Fidalgo P.; Phillips R.K.S.; Bisgaard M.-L.; Orntoft T.F.; Aaltonen L.A.; Hodgson S.V.; Thomas H.J.W.; Tomlinson I.P.M.;
N. Engl. J. Med. 348:791-799(2003)
Cited for: VARIANTS FAP2 CYS-176 AND ASP-393; VARIANTS MET-22; HIS-335 AND PHE-512;

Low frequency of AXIN2 mutations and high frequency of MUTYH mutations in patients with multiple polyposis.
Lejeune S.; Guillemot F.; Triboulet J.P.; Cattan S.; Mouton C.; Porchet N.; Manouvrier S.; Buisine M.P.;
Hum. Mutat. 27:1064-1064(2006)
Cited for: VARIANTS FAP2 CYS-176; SER-177; VAL-280; LEU-292; PRO-385 AND ASP-393; VARIANTS MET-22; HIS-335 AND PHE-512;

Adenine DNA glycosylase activity of 14 human MutY homolog (MUTYH) variant proteins found in patients with colorectal polyposis and cancer.
Goto M.; Shinmura K.; Nakabeppu Y.; Tao H.; Yamada H.; Tsuneyoshi T.; Sugimura H.;
Hum. Mutat. 31:E1861-E1874(2010)
Cited for: CHARACTERIZATION OF VARIANTS FAP2 CYS-176; HIS-179; VAL-220; VAL-280; CYS-306; PRO-385; ASP-393; LEU-402 AND GLU-477 DEL; CHARACTERIZATION OF VARIANTS GLU-72; VAL-370 AND PHE-512; FUNCTION; MUTAGENESIS OF ASP-233;

Functional complementation assay for 47 MUTYH variants in a MutY-disrupted Escherichia coli strain.
Komine K.; Shimodaira H.; Takao M.; Soeda H.; Zhang X.; Takahashi M.; Ishioka C.;
Hum. Mutat. 36:704-711(2015)
Cited for: CHARACTERIZATION OF VARIANTS FAP2 LEU-18; HIS-125; ARG-128; LEU-154; CYS-176; CYS-179; HIS-179; GLN-182; GLU-186; VAL-220; TRP-238; HIS-242; TRP-271; GLU-283; LEU-292; CYS-306; THR-377; PRO-385; ASP-393; LEU-402; MET-417; CYS-423; ASP-470; THR-470; GLU-477 DEL; THR-486 AND PHE-490; CHARACTERIZATION OF VARIANTS GASC SER-402 AND ARG-411; CHARACTERIZATION OF VARIANTS MET-22; ASP-25; ARG-100; ASN-102; VAL-224; MET-231; CYS-242; PHE-243; TRP-287; HIS-335; ARG-335; GLN-434; PRO-434; GLU-500; PHE-512; LEU-513; MET-526 AND GLN-531; FUNCTION; SUBCELLULAR LOCATION;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UIF7: Variant p.Ser512Phe