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Adenine DNA glycosylase (EC 3.2.2.-) (MutY homolog) (hMYH)

 MUTYH_HUMAN             Reviewed;         546 AA.
Q9UIF7; D3DPZ4; Q15830; Q9UBP2; Q9UBS7; Q9UIF4; Q9UIF5; Q9UIF6;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-FEB-2018, entry version 171.
RecName: Full=Adenine DNA glycosylase;
EC=3.2.2.-;
AltName: Full=MutY homolog;
Short=hMYH;
Name=MUTYH; Synonyms=MYH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-3).
PubMed=8682794;
Slupska M.M., Baikalov C., Luther W.M., Chiang J.H., Wei Y.F.,
Miller J.H.;
"Cloning and sequencing a human homolog (hMYH) of the Escherichia coli
mutY gene whose function is required for the repair of oxidative DNA
damage.";
J. Bacteriol. 178:3885-3892(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1; ALPHA-2; ALPHA-3;
BETA-1; GAMMA-2 AND GAMMA-3), AND FUNCTION.
PubMed=10684930; DOI=10.1093/nar/28.6.1355;
Ohtsubo T., Nishioka K., Imaiso Y., Iwai S., Shimokawa H., Oda H.,
Fujikawa T., Nakabeppu Y.;
"Identification of human MutY homolog (hMYH) as a repair enzyme for 2-
hydroxyadenine in DNA and detection of multiple forms of hMYH located
in nuclei and mitochondria.";
Nucleic Acids Res. 28:1355-1364(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=20843780; DOI=10.1093/nar/gkq750;
Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R.,
Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W.,
Mindrinos M., Speed T.P., Scharfe C.;
"Identification of rare DNA variants in mitochondrial disorders with
improved array-based sequencing.";
Nucleic Acids Res. 39:44-58(2011).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-22; HIS-335;
GLU-500; MET-526 AND GLN-531.
NIEHS SNPs program;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-3).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
STRUCTURE BY NMR OF 356-497.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the NUDIX domain from human A/G-specific
adenine DNA glycosylase alpha-3 splice isoform.";
Submitted (NOV-2005) to the PDB data bank.
[9]
VARIANTS FAP2 CYS-176 AND ASP-393.
PubMed=11818965; DOI=10.1038/ng828;
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.;
"Inherited variants of MYH associated with somatic G:C-->T:A mutations
in colorectal tumors.";
Nat. Genet. 30:227-232(2002).
[10]
VARIANTS FAP2 ARG-128; CYS-176 AND ASP-393.
PubMed=12853198; DOI=10.1016/S0140-6736(03)13805-6;
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.;
"Autosomal recessive colorectal adenomatous polyposis due to inherited
mutations of MYH.";
Lancet 362:39-41(2003).
[11]
VARIANTS FAP2 CYS-176 AND ASP-393, AND VARIANTS MET-22; HIS-335 AND
PHE-512.
PubMed=12606733; DOI=10.1056/NEJMoa025283;
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.;
"Multiple colorectal adenomas, classic adenomatous polyposis, and
germ-line mutations in MYH.";
N. Engl. J. Med. 348:791-799(2003).
[12]
VARIANTS FAP2 HIS-125; HIS-179 AND TRP-238.
PubMed=15366000; DOI=10.1002/humu.9282;
Isidro G., Laranjeira F., Pires A., Leite J., Regateiro F.,
Castro e Sousa F., Soares J., Castro C., Giria J., Brito M.J.,
Medeira A., Teixeira R., Morna H., Gaspar I., Marinho C., Jorge R.,
Brehm A., Ramos J.S., Boavida M.G.;
"Germline MUTYH (MYH) mutations in Portuguese individuals with
multiple colorectal adenomas.";
Hum. Mutat. 24:353-354(2004).
[13]
VARIANTS GASC SER-402 AND ARG-411.
PubMed=15273732; DOI=10.1038/sj.onc.1207574;
Kim C.J., Cho Y.G., Park C.H., Kim S.Y., Nam S.W., Lee S.H., Yoo N.J.,
Lee J.Y., Park W.S.;
"Genetic alterations of the MYH gene in gastric cancer.";
Oncogene 23:6820-6822(2004).
[14]
VARIANTS FAP2 CYS-176; HIS-242; TRP-271; PRO-385; ASP-393; CYS-423 AND
GLU-477 DEL, AND VARIANTS MET-22 AND HIS-335.
PubMed=16134147; DOI=10.1002/humu.9370;
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.;
"Mutations of APC and MYH in unrelated Italian patients with
adenomatous polyposis coli.";
Hum. Mutat. 26:394-394(2005).
[15]
VARIANTS FAP2 CYS-176; SER-177; VAL-280; LEU-292; PRO-385 AND ASP-393,
AND VARIANTS MET-22; HIS-335 AND PHE-512.
PubMed=16941501; DOI=10.1002/humu.9460;
PAFNORD Group;
Lejeune S., Guillemot F., Triboulet J.P., Cattan S., Mouton C.,
Porchet N., Manouvrier S., Buisine M.P.;
"Low frequency of AXIN2 mutations and high frequency of MUTYH
mutations in patients with multiple polyposis.";
Hum. Mutat. 27:1064-1064(2006).
[16]
VARIANTS FAP2 ILE-TRP-148 INS; CYS-176; GLN-182; VAL-220; HIS-242 AND
ASP-393, AND VARIANTS MET-22 AND HIS-335.
PubMed=16287072; DOI=10.1002/ijc.21470;
Russell A.M., Zhang J., Luz J., Hutter P., Chappuis P.O.,
Berthod C.R., Maillet P., Mueller H., Heinimann K.;
"Prevalence of MYH germline mutations in Swiss APC mutation-negative
polyposis patients.";
Int. J. Cancer 118:1937-1940(2006).
[17]
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.
PubMed=16557584; DOI=10.1002/ijc.21905;
Aretz S., Uhlhaas S., Goergens H., Siberg K., Vogel M.,
Pagenstecher C., Mangold E., Caspari R., Propping P., Friedl W.;
"MUTYH-associated polyposis: 70 of 71 patients with biallelic
mutations present with an attenuated or atypical phenotype.";
Int. J. Cancer 119:807-814(2006).
[18]
VARIANTS FAP2 CYS-176; CYS-179; TRP-182 AND ASP-393.
PubMed=18091433; DOI=10.1097/GIM.0b013e31815bf940;
Cattaneo F., Molatore S., Mihalatos M., Apessos A., Venesio T.,
Bione S., Grignani P., Nasioulas G., Ranzani G.N.;
"Heterogeneous molecular mechanisms underlie attenuated familial
adenomatous polyposis.";
Genet. Med. 9:836-841(2007).
[19]
VARIANTS FAP2 GLU-213; SER-235 AND MET-474.
PubMed=18515411; DOI=10.1136/gut.2007.145748;
Dallosso A.R., Dolwani S., Jones N., Jones S., Colley J., Maynard J.,
Idziaszczyk S., Humphreys V., Arnold J., Donaldson A., Eccles D.,
Ellis A., Evans D.G., Frayling I.M., Hes F.J., Houlston R.S.,
Maher E.R., Nielsen M., Parry S., Tyler E., Moskvina V., Cheadle J.P.,
Sampson J.R.;
"Inherited predisposition to colorectal adenomas caused by multiple
rare alleles of MUTYH but not OGG1, NUDT1, NTH1 or NEIL 1, 2 or 3.";
Gut 57:1252-1255(2008).
[20]
CHARACTERIZATION OF VARIANTS FAP2 ILE-TRP-148 INS; CYS-176; TRP-182;
ASP-393 AND GLU-477 DEL, AND FUNCTION.
PubMed=20418187; DOI=10.1016/j.dnarep.2010.03.008;
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.;
"Functional analysis of MUTYH mutated proteins associated with
familial adenomatous polyposis.";
DNA Repair 9:700-707(2010).
[21]
VARIANTS FAP2 ILE-TRP-148 INS; TRP-182 AND GLU-477 DEL, AND
CHARACTERIZATION OF VARIANTS FAP2 ILE-TRP-148 INS; CYS-176; TRP-182;
ASP-393 AND GLU-477 DEL.
PubMed=19953527; DOI=10.1002/humu.21158;
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.;
"MUTYH mutations associated with familial adenomatous polyposis:
functional characterization by a mammalian cell-based assay.";
Hum. Mutat. 31:159-166(2010).
[22]
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, AND MUTAGENESIS OF
ASP-233.
PubMed=20848659; DOI=10.1002/humu.21363;
Goto M., Shinmura K., Nakabeppu Y., Tao H., Yamada H., Tsuneyoshi T.,
Sugimura H.;
"Adenine DNA glycosylase activity of 14 human MutY homolog (MUTYH)
variant proteins found in patients with colorectal polyposis and
cancer.";
Hum. Mutat. 31:E1861-E1874(2010).
[23]
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, AND SUBCELLULAR LOCATION.
PubMed=25820570; DOI=10.1002/humu.22794;
Komine K., Shimodaira H., Takao M., Soeda H., Zhang X., Takahashi M.,
Ishioka C.;
"Functional complementation assay for 47 MUTYH variants in a MutY-
disrupted Escherichia coli strain.";
Hum. Mutat. 36:704-711(2015).
[24]
CHARACTERIZATION OF VARIANT FAP2 SER-235, CHARACTERIZATION OF VARIANT
ASN-102; GLY-121; MET-231; GLY-244; ASN-319; HIS-520 AND ALA-536, AND
FUNCTION.
PubMed=26694661; DOI=10.1002/humu.22949;
Shinmura K., Kato H., Goto M., Yamada H., Tao H., Nakamura S.,
Sugimura H.;
"Functional evaluation of nine missense-type variants of the human DNA
glycosylase enzyme MUTYH in the Japanese population.";
Hum. Mutat. 37:350-353(2016).
-!- FUNCTION: Involved in oxidative DNA damage repair. Initiates
repair of A*oxoG to C*G by removing the inappropriately paired
adenine base from the DNA backbone. Possesses both adenine and 2-
OH-A DNA glycosylase activities. {ECO:0000269|PubMed:10684930,
ECO:0000269|PubMed:20418187, ECO:0000269|PubMed:20848659,
ECO:0000269|PubMed:25820570, ECO:0000269|PubMed:26694661}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000250};
Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play
a role in catalysis, but is probably involved in the proper
positioning of the enzyme along the DNA strand. {ECO:0000250};
-!- INTERACTION:
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-10321956, EBI-741181;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25820570}.
Mitochondrion {ECO:0000250|UniProtKB:Q99P21}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=Alpha-1;
IsoId=Q9UIF7-1; Sequence=Displayed;
Name=Alpha-2;
IsoId=Q9UIF7-2; Sequence=VSP_010549;
Name=Alpha-3;
IsoId=Q9UIF7-3; Sequence=VSP_010550;
Name=Beta-1;
IsoId=Q9UIF7-4; Sequence=VSP_010548;
Name=Gamma-2;
IsoId=Q9UIF7-5; Sequence=VSP_010548, VSP_010549;
Name=Gamma-3;
IsoId=Q9UIF7-6; Sequence=VSP_010548, VSP_010550;
-!- DISEASE: Familial adenomatous polyposis 2 (FAP2) [MIM:608456]: A
condition characterized by the development of multiple colorectal
adenomatous polyps, benign neoplasms derived from glandular
epithelium. Some affected individuals may develop colorectal
carcinoma. {ECO:0000269|PubMed:11818965,
ECO:0000269|PubMed:12606733, ECO:0000269|PubMed:12853198,
ECO:0000269|PubMed:15366000, ECO:0000269|PubMed:16134147,
ECO:0000269|PubMed:16287072, ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:16941501, ECO:0000269|PubMed:18091433,
ECO:0000269|PubMed:18515411, ECO:0000269|PubMed:19953527,
ECO:0000269|PubMed:20418187, ECO:0000269|PubMed:20848659,
ECO:0000269|PubMed:25820570, ECO:0000269|PubMed:26694661}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease
which starts in the stomach, can spread to the esophagus or the
small intestine, and can extend through the stomach wall to nearby
lymph nodes and organs. It also can metastasize to other parts of
the body. The term gastric cancer or gastric carcinoma refers to
adenocarcinoma of the stomach that accounts for most of all
gastric malignant tumors. Two main histologic types are
recognized, diffuse type and intestinal type carcinomas. Diffuse
tumors are poorly differentiated infiltrating lesions, resulting
in thickening of the stomach. In contrast, intestinal tumors are
usually exophytic, often ulcerating, and associated with
intestinal metaplasia of the stomach, most often observed in
sporadic disease. {ECO:0000269|PubMed:15273732,
ECO:0000269|PubMed:25820570}. Note=The gene represented in this
entry may be involved in disease pathogenesis. Somatic mutations
contribute to the development of a sub-set of sporadic gastric
cancers in carriers of Helicobacter pylori (PubMed:15273732).
{ECO:0000269|PubMed:15273732}.
-!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA89339.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA89339.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=BAA89345.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA89345.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MUTYHID41464ch1p34.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mutyh/";
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EMBL; U63329; AAC50618.1; -; Genomic_DNA.
EMBL; AB032920; BAA89336.1; -; mRNA.
EMBL; AB032921; BAA89337.1; -; mRNA.
EMBL; AB032922; BAA89338.1; -; mRNA.
EMBL; AB032923; BAA89339.1; ALT_SEQ; mRNA.
EMBL; AB032924; BAA89340.1; -; mRNA.
EMBL; AB032925; BAA89341.1; -; mRNA.
EMBL; AB032926; BAA89342.1; -; mRNA.
EMBL; AB032927; BAA89343.1; -; mRNA.
EMBL; AB032928; BAA89344.1; -; mRNA.
EMBL; AB032929; BAA89345.1; ALT_SEQ; mRNA.
EMBL; HQ205466; ADP90937.1; -; Genomic_DNA.
EMBL; HQ205468; ADP90947.1; -; Genomic_DNA.
EMBL; HQ205469; ADP90952.1; -; Genomic_DNA.
EMBL; HQ205470; ADP90957.1; -; Genomic_DNA.
EMBL; HQ205472; ADP90967.1; -; Genomic_DNA.
EMBL; HQ205473; ADP90972.1; -; Genomic_DNA.
EMBL; HQ205474; ADP90977.1; -; Genomic_DNA.
EMBL; HQ205475; ADP90982.1; -; Genomic_DNA.
EMBL; HQ205476; ADP90987.1; -; Genomic_DNA.
EMBL; HQ205477; ADP90992.1; -; Genomic_DNA.
EMBL; HQ205479; ADP91002.1; -; Genomic_DNA.
EMBL; HQ205480; ADP91007.1; -; Genomic_DNA.
EMBL; HQ205481; ADP91012.1; -; Genomic_DNA.
EMBL; HQ205482; ADP91017.1; -; Genomic_DNA.
EMBL; HQ205483; ADP91022.1; -; Genomic_DNA.
EMBL; HQ205484; ADP91027.1; -; Genomic_DNA.
EMBL; HQ205485; ADP91032.1; -; Genomic_DNA.
EMBL; HQ205486; ADP91037.1; -; Genomic_DNA.
EMBL; HQ205487; ADP91042.1; -; Genomic_DNA.
EMBL; HQ205488; ADP91047.1; -; Genomic_DNA.
EMBL; HQ205489; ADP91052.1; -; Genomic_DNA.
EMBL; HQ205490; ADP91057.1; -; Genomic_DNA.
EMBL; HQ205491; ADP91062.1; -; Genomic_DNA.
EMBL; HQ205492; ADP91067.1; -; Genomic_DNA.
EMBL; HQ205493; ADP91072.1; -; Genomic_DNA.
EMBL; HQ205494; ADP91077.1; -; Genomic_DNA.
EMBL; HQ205495; ADP91082.1; -; Genomic_DNA.
EMBL; HQ205496; ADP91087.1; -; Genomic_DNA.
EMBL; HQ205497; ADP91092.1; -; Genomic_DNA.
EMBL; HQ205498; ADP91097.1; -; Genomic_DNA.
EMBL; HQ205499; ADP91102.1; -; Genomic_DNA.
EMBL; HQ205500; ADP91107.1; -; Genomic_DNA.
EMBL; HQ205501; ADP91112.1; -; Genomic_DNA.
EMBL; HQ205502; ADP91117.1; -; Genomic_DNA.
EMBL; HQ205503; ADP91122.1; -; Genomic_DNA.
EMBL; HQ205505; ADP91132.1; -; Genomic_DNA.
EMBL; AF527839; AAM78555.1; -; Genomic_DNA.
EMBL; AL359540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06993.1; -; Genomic_DNA.
EMBL; CH471059; EAX06996.1; -; Genomic_DNA.
EMBL; CH471059; EAX06997.1; -; Genomic_DNA.
EMBL; BC003178; AAH03178.1; -; mRNA.
CCDS; CCDS41320.1; -. [Q9UIF7-3]
CCDS; CCDS41321.1; -. [Q9UIF7-5]
CCDS; CCDS41322.1; -. [Q9UIF7-6]
CCDS; CCDS520.1; -. [Q9UIF7-1]
CCDS; CCDS72776.1; -. [Q9UIF7-4]
CCDS; CCDS72777.1; -. [Q9UIF7-2]
RefSeq; NP_001041636.1; NM_001048171.1. [Q9UIF7-3]
RefSeq; NP_001041637.1; NM_001048172.1. [Q9UIF7-5]
RefSeq; NP_001041638.1; NM_001048173.1. [Q9UIF7-6]
RefSeq; NP_001041639.1; NM_001048174.1. [Q9UIF7-6]
RefSeq; NP_001121897.1; NM_001128425.1.
RefSeq; NP_001280119.1; NM_001293190.1. [Q9UIF7-2]
RefSeq; NP_001280120.1; NM_001293191.1. [Q9UIF7-4]
RefSeq; NP_001280121.1; NM_001293192.1.
RefSeq; NP_001280124.1; NM_001293195.1. [Q9UIF7-6]
RefSeq; NP_001280125.1; NM_001293196.1.
RefSeq; NP_036354.1; NM_012222.2. [Q9UIF7-1]
RefSeq; XP_011539806.1; XM_011541504.2. [Q9UIF7-4]
RefSeq; XP_016856823.1; XM_017001334.1. [Q9UIF7-5]
RefSeq; XP_016856824.1; XM_017001335.1.
UniGene; Hs.271353; -.
PDB; 1X51; NMR; -; A=356-497.
PDB; 3N5N; X-ray; 2.30 A; X/Y=76-362.
PDBsum; 1X51; -.
PDBsum; 3N5N; -.
ProteinModelPortal; Q9UIF7; -.
SMR; Q9UIF7; -.
BioGrid; 110681; 10.
DIP; DIP-41972N; -.
IntAct; Q9UIF7; 14.
MINT; Q9UIF7; -.
STRING; 9606.ENSP00000361170; -.
iPTMnet; Q9UIF7; -.
PhosphoSitePlus; Q9UIF7; -.
BioMuta; MUTYH; -.
DMDM; 48428272; -.
PaxDb; Q9UIF7; -.
PeptideAtlas; Q9UIF7; -.
PRIDE; Q9UIF7; -.
Ensembl; ENST00000354383; ENSP00000346354; ENSG00000132781. [Q9UIF7-5]
Ensembl; ENST00000355498; ENSP00000347685; ENSG00000132781. [Q9UIF7-6]
Ensembl; ENST00000372098; ENSP00000361170; ENSG00000132781. [Q9UIF7-1]
Ensembl; ENST00000372104; ENSP00000361176; ENSG00000132781. [Q9UIF7-6]
Ensembl; ENST00000372110; ENSP00000361182; ENSG00000132781. [Q9UIF7-2]
Ensembl; ENST00000372115; ENSP00000361187; ENSG00000132781. [Q9UIF7-3]
Ensembl; ENST00000448481; ENSP00000409718; ENSG00000132781. [Q9UIF7-4]
Ensembl; ENST00000456914; ENSP00000407590; ENSG00000132781. [Q9UIF7-6]
GeneID; 4595; -.
KEGG; hsa:4595; -.
UCSC; uc001cnf.4; human. [Q9UIF7-1]
CTD; 4595; -.
DisGeNET; 4595; -.
EuPathDB; HostDB:ENSG00000132781.17; -.
GeneCards; MUTYH; -.
GeneReviews; MUTYH; -.
HGNC; HGNC:7527; MUTYH.
HPA; HPA008732; -.
MalaCards; MUTYH; -.
MIM; 604933; gene.
MIM; 608456; phenotype.
MIM; 613659; phenotype.
neXtProt; NX_Q9UIF7; -.
OpenTargets; ENSG00000132781; -.
Orphanet; 26106; Familial gastric cancer.
Orphanet; 247798; MUTYH-related attenuated familial adenomatous polyposis.
PharmGKB; PA31328; -.
eggNOG; KOG2457; Eukaryota.
eggNOG; COG1194; LUCA.
GeneTree; ENSGT00510000047220; -.
HOVERGEN; HBG052540; -.
InParanoid; Q9UIF7; -.
KO; K03575; -.
PhylomeDB; Q9UIF7; -.
TreeFam; TF328549; -.
Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
Reactome; R-HSA-110331; Cleavage of the damaged purine.
Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1.
SIGNOR; Q9UIF7; -.
EvolutionaryTrace; Q9UIF7; -.
GeneWiki; MUTYH; -.
GenomeRNAi; 4595; -.
PRO; PR:Q9UIF7; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000132781; -.
CleanEx; HS_MUTYH; -.
ExpressionAtlas; Q9UIF7; baseline and differential.
Genevisible; Q9UIF7; HS.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0019104; F:DNA N-glycosylase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032407; F:MutSalpha complex binding; IDA:HGNC.
GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IMP:UniProtKB.
GO; GO:0045007; P:depurination; TAS:Reactome.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0006298; P:mismatch repair; TAS:ProtInc.
CDD; cd03431; DNA_Glycosylase_C; 1.
CDD; cd00056; ENDO3c; 1.
Gene3D; 1.10.1670.10; -; 2.
InterPro; IPR011257; DNA_glycosylase.
InterPro; IPR004036; Endonuclease-III-like_CS2.
InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
InterPro; IPR003265; HhH-GPD_domain.
InterPro; IPR000445; HhH_motif.
InterPro; IPR023170; HTH_base_excis_C.
InterPro; IPR029119; MutY_C.
InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
InterPro; IPR000086; NUDIX_hydrolase_dom.
Pfam; PF00633; HHH; 1.
Pfam; PF00730; HhH-GPD; 1.
Pfam; PF14815; NUDIX_4; 1.
SMART; SM00478; ENDO3c; 1.
SMART; SM00525; FES; 1.
SUPFAM; SSF48150; SSF48150; 1.
SUPFAM; SSF55811; SSF55811; 1.
PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PROSITE; PS51462; NUDIX; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Alternative splicing; Complete proteome;
Disease mutation; DNA damage; DNA repair; Glycosidase; Hydrolase;
Iron; Iron-sulfur; Metal-binding; Mitochondrion; Nucleus;
Polymorphism; Reference proteome; Tumor suppressor.
CHAIN 1 546 Adenine DNA glycosylase.
/FTId=PRO_0000102239.
DOMAIN 364 495 Nudix hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00794}.
MOTIF 404 426 Nudix box.
ACT_SITE 131 131 Proton donor/acceptor.
{ECO:0000250|UniProtKB:P83847}.
METAL 287 287 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 294 294 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 297 297 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 303 303 Iron-sulfur (4Fe-4S). {ECO:0000250}.
SITE 233 233 Transition state stabilizer.
{ECO:0000250|UniProtKB:P83847}.
VAR_SEQ 1 14 Missing (in isoform Beta-1, isoform
Gamma-2 and isoform Gamma-3).
{ECO:0000303|PubMed:10684930}.
/FTId=VSP_010548.
VAR_SEQ 53 63 Missing (in isoform Alpha-3 and isoform
Gamma-3). {ECO:0000303|PubMed:10684930,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010550.
VAR_SEQ 53 62 Missing (in isoform Alpha-2 and isoform
Gamma-2). {ECO:0000303|PubMed:10684930}.
/FTId=VSP_010549.
VARIANT 18 18 P -> L (in FAP2; also found in multiple
polyposis, colorectal and lung cancer
cases; unknown pathological significance;
decreased function in DNA repair;
dbSNP:rs79777494).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077640.
VARIANT 22 22 V -> M (polymorphism; does not affect
function in DNA repair; dbSNP:rs3219484).
{ECO:0000269|PubMed:12606733,
ECO:0000269|PubMed:16134147,
ECO:0000269|PubMed:16287072,
ECO:0000269|PubMed:16941501,
ECO:0000269|PubMed:25820570,
ECO:0000269|Ref.4}.
/FTId=VAR_018872.
VARIANT 25 25 G -> D (polymorphism; does not affect
function in DNA repair;
dbSNP:rs75321043).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077641.
VARIANT 72 72 V -> E (polymorphism; does not affect DNA
glycosylase activity).
{ECO:0000269|PubMed:20848659}.
/FTId=VAR_077642.
VARIANT 100 100 W -> R (found in sporadic hepatocellular
carcinoma; unknown pathological
significance; loss of function in DNA
repair; dbSNP:rs1140507).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077643.
VARIANT 102 102 D -> N (found in multiple polyposis and
sporadic colorectal cancer cases; unknown
pathological significance; does not
affect DNA glycosylase activity; does not
affect function in DNA repair;
dbSNP:rs587780746).
{ECO:0000269|PubMed:25820570,
ECO:0000269|PubMed:26694661}.
/FTId=VAR_077644.
VARIANT 121 121 D -> G (polymorphism; does not affect DNA
glycosylase activity; does not affect
function in DNA repair).
{ECO:0000269|PubMed:26694661}.
/FTId=VAR_077645.
VARIANT 125 125 Y -> H (in FAP2; decreased function in
DNA repair).
{ECO:0000269|PubMed:15366000,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_026045.
VARIANT 128 128 W -> R (in FAP2; loss of function in DNA
repair; dbSNP:rs730881832).
{ECO:0000269|PubMed:12853198,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_026046.
VARIANT 148 148 G -> GIW (in FAP2; reduced DNA
glycosylase activity; decreased DNA
binding; loss of function in DNA repair).
{ECO:0000269|PubMed:16287072,
ECO:0000269|PubMed:19953527,
ECO:0000269|PubMed:20418187}.
/FTId=VAR_064938.
VARIANT 154 154 P -> L (in FAP2; decreased function in
DNA repair; dbSNP:rs777184451).
{ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_077646.
VARIANT 176 176 Y -> C (in FAP2; loss of DNA glycosylase
activity; decreased DNA binding; loss of
function in DNA repair;
dbSNP:rs34612342).
{ECO:0000269|PubMed:11818965,
ECO:0000269|PubMed:12606733,
ECO:0000269|PubMed:12853198,
ECO:0000269|PubMed:16134147,
ECO:0000269|PubMed:16287072,
ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:16941501,
ECO:0000269|PubMed:18091433,
ECO:0000269|PubMed:19953527,
ECO:0000269|PubMed:20418187,
ECO:0000269|PubMed:20848659,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_018873.
VARIANT 177 177 Y -> S (in FAP2).
{ECO:0000269|PubMed:16941501}.
/FTId=VAR_077647.
VARIANT 179 179 R -> C (in FAP2; also found in multiple
polyposis and colorectal cancer cases;
loss of function in DNA repair;
dbSNP:rs747993448).
{ECO:0000269|PubMed:18091433,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_064939.
VARIANT 179 179 R -> H (in FAP2; loss of DNA glycosylase
activity; loss of function in DNA repair;
dbSNP:rs143353451).
{ECO:0000269|PubMed:15366000,
ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:20848659,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_026047.
VARIANT 182 182 R -> Q (in FAP2; loss of function in DNA
repair; dbSNP:rs533899702).
{ECO:0000269|PubMed:16287072,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_077648.
VARIANT 182 182 R -> W (in FAP2; loss of DNA glycosylase
activity; loss of DNA binding; loss of
function in DNA repair;
dbSNP:rs750592289).
{ECO:0000269|PubMed:18091433,
ECO:0000269|PubMed:19953527,
ECO:0000269|PubMed:20418187}.
/FTId=VAR_064940.
VARIANT 186 186 G -> E (in FAP2; decreased function in
DNA repair; dbSNP:rs754155145).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077649.
VARIANT 213 213 G -> E (in FAP2; dbSNP:rs768553551).
{ECO:0000269|PubMed:18515411}.
/FTId=VAR_077650.
VARIANT 220 220 I -> V (in FAP2; also found in multiple
polyposis case; unknown pathological
significance; reduced DNA glycosylase
activity; no effect on function in DNA
repair; dbSNP:rs200872702).
{ECO:0000269|PubMed:16287072,
ECO:0000269|PubMed:20848659,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_077651.
VARIANT 224 224 A -> V (functional polymorphism;
decreased function in DNA repair;
dbSNP:rs11545695).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077652.
VARIANT 231 231 V -> M (probable disease-associated
mutation found in a case of familial
colorectal cancer; no significant effect
on DNA glycosylase activity; slightly
decreased function in DNA repair;
dbSNP:rs200165598).
{ECO:0000269|PubMed:25820570,
ECO:0000269|PubMed:26694661}.
/FTId=VAR_077653.
VARIANT 235 235 N -> S (in FAP2; loss of DNA glycosylase
activity; loss of function in DNA repair;
dbSNP:rs1057517765).
{ECO:0000269|PubMed:18515411,
ECO:0000269|PubMed:26694661}.
/FTId=VAR_077654.
VARIANT 238 238 R -> W (in FAP2; also found in a case of
sporadic colorectal cancer; unknown
pathological significance; decreased
function in DNA repair;
dbSNP:rs34126013).
{ECO:0000269|PubMed:15366000,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_026048.
VARIANT 242 242 R -> C (probable disease-associated
mutation found in multiple polyposis
cases; decreased function in DNA repair;
dbSNP:rs200495564).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077655.
VARIANT 242 242 R -> H (in FAP2; loss of function in DNA
repair; dbSNP:rs140342925).
{ECO:0000269|PubMed:16134147,
ECO:0000269|PubMed:16287072,
ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_077656.
VARIANT 243 243 V -> F (polymorphism; does not affect
function; dbSNP:rs587780749).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077657.
VARIANT 244 244 R -> G (functional polymorphism; reduced
DNA glycosylase activity; decreased
function in DNA repair).
{ECO:0000269|PubMed:26694661}.
/FTId=VAR_077658.
VARIANT 271 271 R -> W (in FAP2; loss of function in DNA
repair; dbSNP:rs769237459).
{ECO:0000269|PubMed:16134147,
ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_077659.
VARIANT 280 280 M -> V (in FAP2; reduced DNA glycosylase
activity; dbSNP:rs876659676).
{ECO:0000269|PubMed:16941501,
ECO:0000269|PubMed:20848659}.
/FTId=VAR_077660.
VARIANT 283 283 G -> E (in FAP2; also found in a patient
with multiple polyps; unknown
pathological significance; does not
affect function in DNA repair;
dbSNP:rs730881833).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077661.
VARIANT 287 287 C -> W (found in a case of sporadic lung
cancer; unknown pathological
significance; loss of function in DNA
repair). {ECO:0000269|PubMed:25820570}.
/FTId=VAR_077662.
VARIANT 292 292 P -> L (in FAP2; also found in multiple
polyposis cases; loss of function in DNA
repair; dbSNP:rs374950566).
{ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:16941501,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_077663.
VARIANT 306 306 R -> C (in FAP2; also found in multiple
polyposis cases; unknown pathological
significance; does not affect DNA
glycosylase activity; slightly decreased
function in DNA repair;
dbSNP:rs138089183).
{ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:20848659,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_077664.
VARIANT 319 319 S -> N (polymorphism; does not affect DNA
glycosylase activity; does not affect
function in DNA repair).
{ECO:0000269|PubMed:26694661}.
/FTId=VAR_077665.
VARIANT 335 335 Q -> H (polymorphism; does not affect
function in DNA repair; dbSNP:rs3219489).
{ECO:0000269|PubMed:12606733,
ECO:0000269|PubMed:16134147,
ECO:0000269|PubMed:16287072,
ECO:0000269|PubMed:16941501,
ECO:0000269|PubMed:25820570,
ECO:0000269|Ref.4}.
/FTId=VAR_018874.
VARIANT 335 335 Q -> R (found in a family with non-
polyposis colorectal cancer-like
syndrome; unknown pathological
significance; does not affect function in
DNA repair; dbSNP:rs199742231).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077666.
VARIANT 370 370 A -> V (polymorphism; does not affect DNA
glycosylase activity; dbSNP:rs35352891).
{ECO:0000269|PubMed:20848659}.
/FTId=VAR_048262.
VARIANT 377 377 P -> T (in FAP2; decreased function in
DNA repair).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077667.
VARIANT 385 385 L -> P (in FAP2; also found in multiple
polyposis cases; loss of DNA glycosylase
activity; loss of function in DNA
repair). {ECO:0000269|PubMed:16134147,
ECO:0000269|PubMed:16941501,
ECO:0000269|PubMed:20848659,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_077668.
VARIANT 393 393 G -> D (in FAP2; reduced DNA glycosylase
activity; decreased DNA binding;
decreased function in DNA repair;
dbSNP:rs36053993).
{ECO:0000269|PubMed:11818965,
ECO:0000269|PubMed:12606733,
ECO:0000269|PubMed:12853198,
ECO:0000269|PubMed:16134147,
ECO:0000269|PubMed:16287072,
ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:16941501,
ECO:0000269|PubMed:18091433,
ECO:0000269|PubMed:19953527,
ECO:0000269|PubMed:20418187,
ECO:0000269|PubMed:20848659,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_018875.
VARIANT 402 402 P -> L (in FAP2; also found in multiple
polyposis and colorectal cancer cases;
loss of DNA glycosylase activity; loss of
function in DNA repair;
dbSNP:rs529008617).
{ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:20848659,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_077669.
VARIANT 402 402 P -> S (in GASC; sporadic; decreased
function in DNA repair;
dbSNP:rs121908382).
{ECO:0000269|PubMed:15273732,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_026049.
VARIANT 411 411 Q -> R (in GASC; sporadic; unknown
pathological significance; does not
affect function in DNA repair;
dbSNP:rs121908383).
{ECO:0000269|PubMed:15273732,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_026050.
VARIANT 417 417 L -> M (in FAP2; also found in patient
with multiple polyps and in a family with
non-polyposis colorectal cancer-like
syndrome; unknown pathological
significance; does not affect function in
DNA repair; dbSNP:rs144079536).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077670.
VARIANT 423 423 R -> C (in FAP2; unknown pathological
significance; does not affect function in
DNA repair; dbSNP:rs150792276).
{ECO:0000269|PubMed:16134147,
ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_077671.
VARIANT 434 434 R -> P (found in sporadic colorectal
cancer cases; unknown pathological
significance; decreased function in DNA
repair). {ECO:0000269|PubMed:25820570}.
/FTId=VAR_077672.
VARIANT 434 434 R -> Q (polymorphism; does not affect
function in DNA repair;
dbSNP:rs587782120).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077673.
VARIANT 470 470 A -> D (in FAP2; loss of function in DNA
repair; dbSNP:rs200844166).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077674.
VARIANT 470 470 A -> T (found in patient with multiple
polyposis; unknown pathological
significance; does not affect function in
DNA repair; dbSNP:rs192816572).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077675.
VARIANT 474 474 T -> M (in FAP2; unknown pathological
significance; dbSNP:rs767747402).
{ECO:0000269|PubMed:18515411}.
/FTId=VAR_077676.
VARIANT 477 477 Missing (in FAP2; also found in a case of
sporadic colorectal cancer; loss of DNA
glycosylase activity; loss of DNA
binding; loss of function in DNA repair).
{ECO:0000269|PubMed:16134147,
ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:19953527,
ECO:0000269|PubMed:20418187,
ECO:0000269|PubMed:20848659,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_064941.
VARIANT 486 486 A -> T (in FAP2; decreased function in
DNA repair; dbSNP:rs587782263).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077677.
VARIANT 490 490 V -> F (in FAP2; found also in sporadic
colorectal cancer cases; unknown
pathological significance; decreased
function in DNA repair;
dbSNP:rs587782228).
{ECO:0000269|PubMed:16557584,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_077678.
VARIANT 500 500 G -> E (functional polymorphism;
decreased function in DNA repair;
dbSNP:rs3219494).
{ECO:0000269|PubMed:25820570,
ECO:0000269|Ref.4}.
/FTId=VAR_018876.
VARIANT 512 512 S -> F (polymorphism; does not affect DNA
glycosylase activity; does not affect
function in DNA repair;
dbSNP:rs140118273).
{ECO:0000269|PubMed:12606733,
ECO:0000269|PubMed:16941501,
ECO:0000269|PubMed:20848659,
ECO:0000269|PubMed:25820570}.
/FTId=VAR_026051.
VARIANT 513 513 P -> L (polymorphism; does not affect
function in DNA repair;
dbSNP:rs587778542).
{ECO:0000269|PubMed:25820570}.
/FTId=VAR_077679.
VARIANT 520 520 R -> H (polymorphism; does not affect DNA
glycosylase activity; does not affect
function in DNA repair;
dbSNP:rs374655042).
{ECO:0000269|PubMed:26694661}.
/FTId=VAR_077680.
VARIANT 526 526 L -> M (polymorphism; does not affect
function in DNA repair; dbSNP:rs3219496).
{ECO:0000269|PubMed:25820570,
ECO:0000269|Ref.4}.
/FTId=VAR_018877.
VARIANT 531 531 R -> Q (polymorphism; does not affect
function in DNA repair; dbSNP:rs3219497).
{ECO:0000269|PubMed:25820570,
ECO:0000269|Ref.4}.
/FTId=VAR_018878.
VARIANT 536 536 T -> A (polymorphism; does not affect DNA
glycosylase activity; does not affect
function in DNA repair;
dbSNP:rs151196169).
{ECO:0000269|PubMed:26694661}.
/FTId=VAR_077681.
MUTAGEN 233 233 D->N: Loss of DNA glycosylase activity.
{ECO:0000269|PubMed:20848659}.
HELIX 87 104 {ECO:0000244|PDB:3N5N}.
HELIX 109 116 {ECO:0000244|PDB:3N5N}.
HELIX 120 135 {ECO:0000244|PDB:3N5N}.
HELIX 139 152 {ECO:0000244|PDB:3N5N}.
HELIX 156 160 {ECO:0000244|PDB:3N5N}.
HELIX 164 171 {ECO:0000244|PDB:3N5N}.
HELIX 177 193 {ECO:0000244|PDB:3N5N}.
HELIX 202 208 {ECO:0000244|PDB:3N5N}.
HELIX 214 224 {ECO:0000244|PDB:3N5N}.
HELIX 234 243 {ECO:0000244|PDB:3N5N}.
HELIX 253 266 {ECO:0000244|PDB:3N5N}.
HELIX 272 285 {ECO:0000244|PDB:3N5N}.
STRAND 289 291 {ECO:0000244|PDB:3N5N}.
HELIX 300 302 {ECO:0000244|PDB:3N5N}.
HELIX 304 316 {ECO:0000244|PDB:3N5N}.
HELIX 330 332 {ECO:0000244|PDB:3N5N}.
STRAND 358 360 {ECO:0000244|PDB:1X51}.
STRAND 366 377 {ECO:0000244|PDB:1X51}.
STRAND 379 388 {ECO:0000244|PDB:1X51}.
STRAND 403 405 {ECO:0000244|PDB:1X51}.
HELIX 410 424 {ECO:0000244|PDB:1X51}.
STRAND 447 456 {ECO:0000244|PDB:1X51}.
STRAND 470 474 {ECO:0000244|PDB:1X51}.
HELIX 475 480 {ECO:0000244|PDB:1X51}.
HELIX 485 495 {ECO:0000244|PDB:1X51}.
SEQUENCE 546 AA; 60069 MW; 6C79BDB34345DD10 CRC64;
MTPLVSRLSR LWAIMRKPRA AVGSGHRKQA ASQEGRQKHA KNNSQAKPSA CDGMIAECPG
APAGLARQPE EVVLQASVSS YHLFRDVAEV TAFRGSLLSW YDQEKRDLPW RRRAEDEMDL
DRRAYAVWVS EVMLQQTQVA TVINYYTGWM QKWPTLQDLA SASLEEVNQL WAGLGYYSRG
RRLQEGARKV VEELGGHMPR TAETLQQLLP GVGRYTAGAI ASIAFGQATG VVDGNVARVL
CRVRAIGADP SSTLVSQQLW GLAQQLVDPA RPGDFNQAAM ELGATVCTPQ RPLCSQCPVE
SLCRARQRVE QEQLLASGSL SGSPDVEECA PNTGQCHLCL PPSEPWDQTL GVVNFPRKAS
RKPPREESSA TCVLEQPGAL GAQILLVQRP NSGLLAGLWE FPSVTWEPSE QLQRKALLQE
LQRWAGPLPA THLRHLGEVV HTFSHIKLTY QVYGLALEGQ TPVTTVPPGA RWLTQEEFHT
AAVSTAMKKV FRVYQGQQPG TCMGSKRSQV SSPCSRKKPR MGQQVLDNFF RSHISTDAHS
LNSAAQ


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