UniProtKB/Swiss-Prot Q9UIF7: Variant p.Gly393Asp

Adenine DNA glycosylase
Gene: MUTYH
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Variant information Variant position:

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

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:

From Glycine (G) to Aspartate (D) at position 393 (G393D, p.Gly393Asp). 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 glycine (G) to medium size and acidic (D) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-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:

In FAP2; reduced DNA glycosylase activity; decreased DNA binding; decreased function in DNA repair. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs36053993 [ dbSNP | Ensembl ]

Sequence information Variant position:

393 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:

VLEQPGALGAQILLVQRPNS G LLAGLWEFPSVTWEPSEQLQ 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                         VLEQPGALGAQ-ILLVQRPNSGLLAGLWEFPSVTWEPSEQLQ

Mouse                         VVEQPGAIGGPLVLLVQRPDSGLLAGLWEFPSVTLEPSEQH

Rat                           VVEQPGATGGPLILLVQRPNSGLLAGLWEFPSVTLEPSGQH

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
Domain	364 – 495	Nudix hydrolase

Literature citations
Inherited variants of MYH associated with somatic G:C-->T:A mutations in colorectal tumors.
Al-Tassan N.; Chmiel N.H.; Maynard J.; Fleming N.; Livingston A.L.; Williams G.T.; Hodges A.K.; Davies D.R.; David S.S.; Sampson J.R.; Cheadle J.P.;
Nat. Genet. 30:227-232(2002)
Cited for: VARIANTS FAP2 CYS-176 AND ASP-393; Autosomal recessive colorectal adenomatous polyposis due to inherited mutations of MYH.
Sampson J.R.; Dolwani S.; Jones S.; Eccles D.; Ellis A.; Evans D.G.; Frayling I.; Jordan S.; Maher E.R.; Mak T.; Maynard J.; Pigatto F.; Shaw J.; Cheadle J.P.;
Lancet 362:39-41(2003)
Cited for: VARIANTS FAP2 ARG-128; CYS-176 AND ASP-393; 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; Mutations of APC and MYH in unrelated Italian patients with adenomatous polyposis coli.
Aceto G.; Curia M.C.; Veschi S.; De Lellis L.; Mammarella S.; Catalano T.; Stuppia L.; Palka G.; Valanzano R.; Tonelli F.; Casale V.; Stigliano V.; Cetta F.; Battista P.; Mariani-Costantini R.; Cama A.;
Hum. Mutat. 26:394-394(2005)
Cited for: VARIANTS FAP2 CYS-176; HIS-242; TRP-271; PRO-385; ASP-393; CYS-423 AND GLU-477 DEL; VARIANTS MET-22 AND HIS-335; 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; Prevalence of MYH germline mutations in Swiss APC mutation-negative polyposis patients.
Russell A.M.; Zhang J.; Luz J.; Hutter P.; Chappuis P.O.; Berthod C.R.; Maillet P.; Mueller H.; Heinimann K.;
Int. J. Cancer 118:1937-1940(2006)
Cited for: VARIANTS FAP2 ILE-TRP-148 INS; CYS-176; GLN-182; VAL-220; HIS-242 AND ASP-393; VARIANTS MET-22 AND HIS-335; MUTYH-associated polyposis: 70 of 71 patients with biallelic mutations present with an attenuated or atypical phenotype.
Aretz S.; Uhlhaas S.; Goergens H.; Siberg K.; Vogel M.; Pagenstecher C.; Mangold E.; Caspari R.; Propping P.; Friedl W.;
Int. J. Cancer 119:807-814(2006)
Cited for: VARIANTS FAP2 LEU-154; CYS-176; HIS-179; HIS-242; TRP-271; LEU-292; CYS-306; ASP-393; LEU-402; CYS-423; GLU-477 DEL AND PHE-490; Heterogeneous molecular mechanisms underlie attenuated familial adenomatous polyposis.
Cattaneo F.; Molatore S.; Mihalatos M.; Apessos A.; Venesio T.; Bione S.; Grignani P.; Nasioulas G.; Ranzani G.N.;
Genet. Med. 9:836-841(2007)
Cited for: VARIANTS FAP2 CYS-176; CYS-179; TRP-182 AND ASP-393; Functional analysis of MUTYH mutated proteins associated with familial adenomatous polyposis.
D'Agostino V.G.; Minoprio A.; Torreri P.; Marinoni I.; Bossa C.; Petrucci T.C.; Albertini A.M.; Ranzani G.N.; Bignami M.; Mazzei F.;
DNA Repair 9:700-707(2010)
Cited for: CHARACTERIZATION OF VARIANTS FAP2 ILE-TRP-148 INS; CYS-176; TRP-182; ASP-393 AND GLU-477 DEL; FUNCTION; CATALYTIC ACTIVITY; MUTYH mutations associated with familial adenomatous polyposis: functional characterization by a mammalian cell-based assay.
Molatore S.; Russo M.T.; D'Agostino V.G.; Barone F.; Matsumoto Y.; Albertini A.M.; Minoprio A.; Degan P.; Mazzei F.; Bignami M.; Ranzani G.N.;
Hum. Mutat. 31:159-166(2010)
Cited for: VARIANTS FAP2 ILE-TRP-148 INS; TRP-182 AND GLU-477 DEL; CHARACTERIZATION OF VARIANTS FAP2 ILE-TRP-148 INS; CYS-176; TRP-182; ASP-393 AND GLU-477 DEL; 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;

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.