ID MUTYH_HUMAN Reviewed; 546 AA. AC Q9UIF7; D3DPZ4; Q15830; Q9UBP2; Q9UBS7; Q9UIF4; Q9UIF5; Q9UIF6; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 208. DE RecName: Full=Adenine DNA glycosylase; DE EC=3.2.2.31 {ECO:0000269|PubMed:20418187}; DE AltName: Full=MutY homolog; DE Short=hMYH; GN Name=MUTYH; Synonyms=MYH; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-3). RX PubMed=8682794; DOI=10.1128/jb.178.13.3885-3892.1996; RA Slupska M.M., Baikalov C., Luther W.M., Chiang J.H., Wei Y.F., Miller J.H.; RT "Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY RT gene whose function is required for the repair of oxidative DNA damage."; RL J. Bacteriol. 178:3885-3892(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1; ALPHA-2; ALPHA-3; BETA-1; RP GAMMA-2 AND GAMMA-3), AND FUNCTION. RX PubMed=10684930; DOI=10.1093/nar/28.6.1355; RA Ohtsubo T., Nishioka K., Imaiso Y., Iwai S., Shimokawa H., Oda H., RA Fujikawa T., Nakabeppu Y.; RT "Identification of human MutY homolog (hMYH) as a repair enzyme for 2- RT hydroxyadenine in DNA and detection of multiple forms of hMYH located in RT nuclei and mitochondria."; RL Nucleic Acids Res. 28:1355-1364(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=20843780; DOI=10.1093/nar/gkq750; RA Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., RA Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., RA Speed T.P., Scharfe C.; RT "Identification of rare DNA variants in mitochondrial disorders with RT improved array-based sequencing."; RL Nucleic Acids Res. 39:44-58(2011). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-22; HIS-335; GLU-500; RP MET-526 AND GLN-531. RG NIEHS SNPs program; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-3). RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP STRUCTURE BY NMR OF 356-497. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the NUDIX domain from human A/G-specific adenine DNA RT glycosylase alpha-3 splice isoform."; RL Submitted (NOV-2005) to the PDB data bank. RN [9] RP VARIANTS FAP2 CYS-176 AND ASP-393. RX PubMed=11818965; DOI=10.1038/ng828; RA Al-Tassan N., Chmiel N.H., Maynard J., Fleming N., Livingston A.L., RA Williams G.T., Hodges A.K., Davies D.R., David S.S., Sampson J.R., RA Cheadle J.P.; RT "Inherited variants of MYH associated with somatic G:C-->T:A mutations in RT colorectal tumors."; RL Nat. Genet. 30:227-232(2002). RN [10] RP VARIANTS FAP2 ARG-128; CYS-176 AND ASP-393. RX PubMed=12853198; DOI=10.1016/s0140-6736(03)13805-6; RA Sampson J.R., Dolwani S., Jones S., Eccles D., Ellis A., Evans D.G., RA Frayling I., Jordan S., Maher E.R., Mak T., Maynard J., Pigatto F., RA Shaw J., Cheadle J.P.; RT "Autosomal recessive colorectal adenomatous polyposis due to inherited RT mutations of MYH."; RL Lancet 362:39-41(2003). RN [11] RP VARIANTS FAP2 CYS-176 AND ASP-393, AND VARIANTS MET-22; HIS-335 AND RP PHE-512. RX PubMed=12606733; DOI=10.1056/nejmoa025283; RA Sieber O.M., Lipton L., Crabtree M., Heinimann K., Fidalgo P., RA Phillips R.K.S., Bisgaard M.-L., Orntoft T.F., Aaltonen L.A., Hodgson S.V., RA Thomas H.J.W., Tomlinson I.P.M.; RT "Multiple colorectal adenomas, classic adenomatous polyposis, and germ-line RT mutations in MYH."; RL N. Engl. J. Med. 348:791-799(2003). RN [12] RP VARIANTS FAP2 HIS-125; HIS-179 AND TRP-238. RX PubMed=15366000; DOI=10.1002/humu.9282; RA Isidro G., Laranjeira F., Pires A., Leite J., Regateiro F., RA Castro e Sousa F., Soares J., Castro C., Giria J., Brito M.J., Medeira A., RA Teixeira R., Morna H., Gaspar I., Marinho C., Jorge R., Brehm A., RA Ramos J.S., Boavida M.G.; RT "Germline MUTYH (MYH) mutations in Portuguese individuals with multiple RT colorectal adenomas."; RL Hum. Mutat. 24:353-354(2004). RN [13] RP VARIANTS GASC SER-402 AND ARG-411. RX PubMed=15273732; DOI=10.1038/sj.onc.1207574; RA Kim C.J., Cho Y.G., Park C.H., Kim S.Y., Nam S.W., Lee S.H., Yoo N.J., RA Lee J.Y., Park W.S.; RT "Genetic alterations of the MYH gene in gastric cancer."; RL Oncogene 23:6820-6822(2004). RN [14] RP VARIANTS FAP2 CYS-176; HIS-242; TRP-271; PRO-385; ASP-393; CYS-423 AND RP GLU-477 DEL, AND VARIANTS MET-22 AND HIS-335. RX PubMed=16134147; DOI=10.1002/humu.9370; RA Aceto G., Curia M.C., Veschi S., De Lellis L., Mammarella S., Catalano T., RA Stuppia L., Palka G., Valanzano R., Tonelli F., Casale V., Stigliano V., RA Cetta F., Battista P., Mariani-Costantini R., Cama A.; RT "Mutations of APC and MYH in unrelated Italian patients with adenomatous RT polyposis coli."; RL Hum. Mutat. 26:394-394(2005). RN [15] RP VARIANTS FAP2 CYS-176; SER-177; VAL-280; LEU-292; PRO-385 AND ASP-393, AND RP VARIANTS MET-22; HIS-335 AND PHE-512. RX PubMed=16941501; DOI=10.1002/humu.9460; RG PAFNORD Group; RA Lejeune S., Guillemot F., Triboulet J.P., Cattan S., Mouton C., Porchet N., RA Manouvrier S., Buisine M.P.; RT "Low frequency of AXIN2 mutations and high frequency of MUTYH mutations in RT patients with multiple polyposis."; RL Hum. Mutat. 27:1064-1064(2006). RN [16] RP VARIANTS FAP2 ILE-TRP-148 INS; CYS-176; GLN-182; VAL-220; HIS-242 AND RP ASP-393, AND VARIANTS MET-22 AND HIS-335. RX PubMed=16287072; DOI=10.1002/ijc.21470; RA Russell A.M., Zhang J., Luz J., Hutter P., Chappuis P.O., Berthod C.R., RA Maillet P., Mueller H., Heinimann K.; RT "Prevalence of MYH germline mutations in Swiss APC mutation-negative RT polyposis patients."; RL Int. J. Cancer 118:1937-1940(2006). RN [17] RP VARIANTS FAP2 LEU-154; CYS-176; HIS-179; HIS-242; TRP-271; LEU-292; RP CYS-306; ASP-393; LEU-402; CYS-423; GLU-477 DEL AND PHE-490. RX PubMed=16557584; DOI=10.1002/ijc.21905; RA Aretz S., Uhlhaas S., Goergens H., Siberg K., Vogel M., Pagenstecher C., RA Mangold E., Caspari R., Propping P., Friedl W.; RT "MUTYH-associated polyposis: 70 of 71 patients with biallelic mutations RT present with an attenuated or atypical phenotype."; RL Int. J. Cancer 119:807-814(2006). RN [18] RP VARIANTS FAP2 CYS-176; CYS-179; TRP-182 AND ASP-393. RX PubMed=18091433; DOI=10.1097/gim.0b013e31815bf940; RA Cattaneo F., Molatore S., Mihalatos M., Apessos A., Venesio T., Bione S., RA Grignani P., Nasioulas G., Ranzani G.N.; RT "Heterogeneous molecular mechanisms underlie attenuated familial RT adenomatous polyposis."; RL Genet. Med. 9:836-841(2007). RN [19] RP VARIANTS FAP2 GLU-213; SER-235 AND MET-474. RX PubMed=18515411; DOI=10.1136/gut.2007.145748; RA Dallosso A.R., Dolwani S., Jones N., Jones S., Colley J., Maynard J., RA Idziaszczyk S., Humphreys V., Arnold J., Donaldson A., Eccles D., Ellis A., RA Evans D.G., Frayling I.M., Hes F.J., Houlston R.S., Maher E.R., Nielsen M., RA Parry S., Tyler E., Moskvina V., Cheadle J.P., Sampson J.R.; RT "Inherited predisposition to colorectal adenomas caused by multiple rare RT alleles of MUTYH but not OGG1, NUDT1, NTH1 or NEIL 1, 2 or 3."; RL Gut 57:1252-1255(2008). RN [20] RP CHARACTERIZATION OF VARIANTS FAP2 ILE-TRP-148 INS; CYS-176; TRP-182; RP ASP-393 AND GLU-477 DEL, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20418187; DOI=10.1016/j.dnarep.2010.03.008; RA D'Agostino V.G., Minoprio A., Torreri P., Marinoni I., Bossa C., RA Petrucci T.C., Albertini A.M., Ranzani G.N., Bignami M., Mazzei F.; RT "Functional analysis of MUTYH mutated proteins associated with familial RT adenomatous polyposis."; RL DNA Repair 9:700-707(2010). RN [21] RP VARIANTS FAP2 ILE-TRP-148 INS; TRP-182 AND GLU-477 DEL, AND RP CHARACTERIZATION OF VARIANTS FAP2 ILE-TRP-148 INS; CYS-176; TRP-182; RP ASP-393 AND GLU-477 DEL. RX PubMed=19953527; DOI=10.1002/humu.21158; RA Molatore S., Russo M.T., D'Agostino V.G., Barone F., Matsumoto Y., RA Albertini A.M., Minoprio A., Degan P., Mazzei F., Bignami M., Ranzani G.N.; RT "MUTYH mutations associated with familial adenomatous polyposis: functional RT characterization by a mammalian cell-based assay."; RL Hum. Mutat. 31:159-166(2010). RN [22] RP CHARACTERIZATION OF VARIANTS FAP2 CYS-176; HIS-179; VAL-220; VAL-280; RP CYS-306; PRO-385; ASP-393; LEU-402 AND GLU-477 DEL, CHARACTERIZATION OF RP VARIANTS GLU-72; VAL-370 AND PHE-512, FUNCTION, AND MUTAGENESIS OF ASP-233. RX PubMed=20848659; DOI=10.1002/humu.21363; RA Goto M., Shinmura K., Nakabeppu Y., Tao H., Yamada H., Tsuneyoshi T., RA Sugimura H.; RT "Adenine DNA glycosylase activity of 14 human MutY homolog (MUTYH) variant RT proteins found in patients with colorectal polyposis and cancer."; RL Hum. Mutat. 31:E1861-E1874(2010). RN [23] RP CHARACTERIZATION OF VARIANTS FAP2 LEU-18; HIS-125; ARG-128; LEU-154; RP CYS-176; CYS-179; HIS-179; GLN-182; GLU-186; VAL-220; TRP-238; HIS-242; RP TRP-271; GLU-283; LEU-292; CYS-306; THR-377; PRO-385; ASP-393; LEU-402; RP MET-417; CYS-423; ASP-470; THR-470; GLU-477 DEL; THR-486 AND PHE-490, RP CHARACTERIZATION OF VARIANTS GASC SER-402 AND ARG-411, CHARACTERIZATION OF RP VARIANTS MET-22; ASP-25; ARG-100; ASN-102; VAL-224; MET-231; CYS-242; RP PHE-243; TRP-287; HIS-335; ARG-335; GLN-434; PRO-434; GLU-500; PHE-512; RP LEU-513; MET-526 AND GLN-531, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=25820570; DOI=10.1002/humu.22794; RA Komine K., Shimodaira H., Takao M., Soeda H., Zhang X., Takahashi M., RA Ishioka C.; RT "Functional complementation assay for 47 MUTYH variants in a MutY-disrupted RT Escherichia coli strain."; RL Hum. Mutat. 36:704-711(2015). RN [24] RP CHARACTERIZATION OF VARIANT FAP2 SER-235, CHARACTERIZATION OF VARIANTS RP ASN-102; MET-231; GLY-244; ASN-319; HIS-520 AND ALA-536, FUNCTION, AND RP MUTAGENESIS OF ASP-121. RX PubMed=26694661; DOI=10.1002/humu.22949; RA Shinmura K., Kato H., Goto M., Yamada H., Tao H., Nakamura S., Sugimura H.; RT "Functional evaluation of nine missense-type variants of the human DNA RT glycosylase enzyme MUTYH in the Japanese population."; RL Hum. Mutat. 37:350-353(2016). CC -!- FUNCTION: Involved in oxidative DNA damage repair. Initiates repair of CC A*oxoG to C*G by removing the inappropriately paired adenine base from CC the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase CC activities. {ECO:0000269|PubMed:10684930, ECO:0000269|PubMed:20418187, CC ECO:0000269|PubMed:20848659, ECO:0000269|PubMed:25820570, CC ECO:0000269|PubMed:26694661}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolyzes free adenine bases from 7,8-dihydro-8- CC oxoguanine:adenine mismatched double-stranded DNA, leaving an CC apurinic site.; EC=3.2.2.31; Evidence={ECO:0000269|PubMed:20418187}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a CC role in catalysis, but is probably involved in the proper positioning CC of the enzyme along the DNA strand. {ECO:0000250}; CC -!- INTERACTION: CC Q9UIF7-3; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-10321956, EBI-741181; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25820570}. CC Mitochondrion {ECO:0000250|UniProtKB:Q99P21}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=Alpha-1; CC IsoId=Q9UIF7-1; Sequence=Displayed; CC Name=Alpha-2; CC IsoId=Q9UIF7-2; Sequence=VSP_010549; CC Name=Alpha-3; CC IsoId=Q9UIF7-3; Sequence=VSP_010550; CC Name=Beta-1; CC IsoId=Q9UIF7-4; Sequence=VSP_010548; CC Name=Gamma-2; CC IsoId=Q9UIF7-5; Sequence=VSP_010548, VSP_010549; CC Name=Gamma-3; CC IsoId=Q9UIF7-6; Sequence=VSP_010548, VSP_010550; CC -!- DISEASE: Familial adenomatous polyposis 2 (FAP2) [MIM:608456]: A CC condition characterized by the development of multiple colorectal CC adenomatous polyps, benign neoplasms derived from glandular epithelium. CC Some affected individuals may develop colorectal carcinoma. CC {ECO:0000269|PubMed:11818965, ECO:0000269|PubMed:12606733, CC ECO:0000269|PubMed:12853198, ECO:0000269|PubMed:15366000, CC ECO:0000269|PubMed:16134147, ECO:0000269|PubMed:16287072, CC ECO:0000269|PubMed:16557584, ECO:0000269|PubMed:16941501, CC ECO:0000269|PubMed:18091433, ECO:0000269|PubMed:18515411, CC ECO:0000269|PubMed:19953527, ECO:0000269|PubMed:20418187, CC ECO:0000269|PubMed:20848659, ECO:0000269|PubMed:25820570, CC ECO:0000269|PubMed:26694661}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which CC starts in the stomach, can spread to the esophagus or the small CC intestine, and can extend through the stomach wall to nearby lymph CC nodes and organs. It also can metastasize to other parts of the body. CC The term gastric cancer or gastric carcinoma refers to adenocarcinoma CC of the stomach that accounts for most of all gastric malignant tumors. CC Two main histologic types are recognized, diffuse type and intestinal CC type carcinomas. Diffuse tumors are poorly differentiated infiltrating CC lesions, resulting in thickening of the stomach. In contrast, CC intestinal tumors are usually exophytic, often ulcerating, and CC associated with intestinal metaplasia of the stomach, most often CC observed in sporadic disease. {ECO:0000269|PubMed:15273732, CC ECO:0000269|PubMed:25820570}. Note=The gene represented in this entry CC may be involved in disease pathogenesis. Somatic mutations contribute CC to the development of a sub-set of sporadic gastric cancers in carriers CC of Helicobacter pylori (PubMed:15273732). CC {ECO:0000269|PubMed:15273732}. CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA89339.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA89339.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC Sequence=BAA89345.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA89345.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41464/mutyh-(muty-homolog-(e-coli))"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/mutyh/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U63329; AAC50618.1; -; Genomic_DNA. DR EMBL; AB032920; BAA89336.1; -; mRNA. DR EMBL; AB032921; BAA89337.1; -; mRNA. DR EMBL; AB032922; BAA89338.1; -; mRNA. DR EMBL; AB032923; BAA89339.1; ALT_SEQ; mRNA. DR EMBL; AB032924; BAA89340.1; -; mRNA. DR EMBL; AB032925; BAA89341.1; -; mRNA. DR EMBL; AB032926; BAA89342.1; -; mRNA. DR EMBL; AB032927; BAA89343.1; -; mRNA. DR EMBL; AB032928; BAA89344.1; -; mRNA. DR EMBL; AB032929; BAA89345.1; ALT_SEQ; mRNA. DR EMBL; HQ205466; ADP90937.1; -; Genomic_DNA. DR EMBL; HQ205468; ADP90947.1; -; Genomic_DNA. DR EMBL; HQ205469; ADP90952.1; -; Genomic_DNA. DR EMBL; HQ205470; ADP90957.1; -; Genomic_DNA. DR EMBL; HQ205472; ADP90967.1; -; Genomic_DNA. DR EMBL; HQ205473; ADP90972.1; -; Genomic_DNA. DR EMBL; HQ205474; ADP90977.1; -; Genomic_DNA. DR EMBL; HQ205475; ADP90982.1; -; Genomic_DNA. DR EMBL; HQ205476; ADP90987.1; -; Genomic_DNA. DR EMBL; HQ205477; ADP90992.1; -; Genomic_DNA. DR EMBL; HQ205479; ADP91002.1; -; Genomic_DNA. DR EMBL; HQ205480; ADP91007.1; -; Genomic_DNA. DR EMBL; HQ205481; ADP91012.1; -; Genomic_DNA. DR EMBL; HQ205482; ADP91017.1; -; Genomic_DNA. DR EMBL; HQ205483; ADP91022.1; -; Genomic_DNA. DR EMBL; HQ205484; ADP91027.1; -; Genomic_DNA. DR EMBL; HQ205485; ADP91032.1; -; Genomic_DNA. DR EMBL; HQ205486; ADP91037.1; -; Genomic_DNA. DR EMBL; HQ205487; ADP91042.1; -; Genomic_DNA. DR EMBL; HQ205488; ADP91047.1; -; Genomic_DNA. DR EMBL; HQ205489; ADP91052.1; -; Genomic_DNA. DR EMBL; HQ205490; ADP91057.1; -; Genomic_DNA. DR EMBL; HQ205491; ADP91062.1; -; Genomic_DNA. DR EMBL; HQ205492; ADP91067.1; -; Genomic_DNA. DR EMBL; HQ205493; ADP91072.1; -; Genomic_DNA. DR EMBL; HQ205494; ADP91077.1; -; Genomic_DNA. DR EMBL; HQ205495; ADP91082.1; -; Genomic_DNA. DR EMBL; HQ205496; ADP91087.1; -; Genomic_DNA. DR EMBL; HQ205497; ADP91092.1; -; Genomic_DNA. DR EMBL; HQ205498; ADP91097.1; -; Genomic_DNA. DR EMBL; HQ205499; ADP91102.1; -; Genomic_DNA. DR EMBL; HQ205500; ADP91107.1; -; Genomic_DNA. DR EMBL; HQ205501; ADP91112.1; -; Genomic_DNA. DR EMBL; HQ205502; ADP91117.1; -; Genomic_DNA. DR EMBL; HQ205503; ADP91122.1; -; Genomic_DNA. DR EMBL; HQ205505; ADP91132.1; -; Genomic_DNA. DR EMBL; AF527839; AAM78555.1; -; Genomic_DNA. DR EMBL; AL359540; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX06993.1; -; Genomic_DNA. DR EMBL; CH471059; EAX06996.1; -; Genomic_DNA. DR EMBL; CH471059; EAX06997.1; -; Genomic_DNA. DR EMBL; BC003178; AAH03178.1; -; mRNA. DR CCDS; CCDS41321.1; -. [Q9UIF7-5] DR CCDS; CCDS41322.1; -. [Q9UIF7-6] DR CCDS; CCDS520.1; -. [Q9UIF7-1] DR CCDS; CCDS72776.1; -. [Q9UIF7-4] DR CCDS; CCDS72777.1; -. [Q9UIF7-2] DR RefSeq; NP_001041636.1; NM_001048171.1. [Q9UIF7-6] DR RefSeq; NP_001041637.1; NM_001048172.1. [Q9UIF7-5] DR RefSeq; NP_001041638.1; NM_001048173.1. [Q9UIF7-6] DR RefSeq; NP_001041639.1; NM_001048174.1. [Q9UIF7-6] DR RefSeq; NP_001121897.1; NM_001128425.1. DR RefSeq; NP_001280119.1; NM_001293190.1. [Q9UIF7-2] DR RefSeq; NP_001280120.1; NM_001293191.1. [Q9UIF7-4] DR RefSeq; NP_001280121.1; NM_001293192.1. DR RefSeq; NP_001280124.1; NM_001293195.1. [Q9UIF7-6] DR RefSeq; NP_001280125.1; NM_001293196.1. DR RefSeq; NP_036354.1; NM_012222.2. [Q9UIF7-1] DR RefSeq; XP_011539806.1; XM_011541504.2. DR RefSeq; XP_016856823.1; XM_017001334.1. DR RefSeq; XP_016856824.1; XM_017001335.1. DR PDB; 1X51; NMR; -; A=356-497. DR PDB; 3N5N; X-ray; 2.30 A; X/Y=76-362. DR PDBsum; 1X51; -. DR PDBsum; 3N5N; -. DR AlphaFoldDB; Q9UIF7; -. DR SMR; Q9UIF7; -. DR BioGRID; 110681; 28. DR DIP; DIP-41972N; -. DR IntAct; Q9UIF7; 16. DR MINT; Q9UIF7; -. DR STRING; 9606.ENSP00000500891; -. DR iPTMnet; Q9UIF7; -. DR PhosphoSitePlus; Q9UIF7; -. DR BioMuta; MUTYH; -. DR DMDM; 48428272; -. DR EPD; Q9UIF7; -. DR jPOST; Q9UIF7; -. DR MassIVE; Q9UIF7; -. DR MaxQB; Q9UIF7; -. DR PaxDb; 9606-ENSP00000361170; -. DR PeptideAtlas; Q9UIF7; -. DR ProteomicsDB; 84500; -. [Q9UIF7-1] DR ProteomicsDB; 84501; -. [Q9UIF7-2] DR ProteomicsDB; 84502; -. [Q9UIF7-3] DR ProteomicsDB; 84503; -. [Q9UIF7-4] DR ProteomicsDB; 84504; -. [Q9UIF7-5] DR ProteomicsDB; 84505; -. [Q9UIF7-6] DR Pumba; Q9UIF7; -. DR Antibodypedia; 1869; 360 antibodies from 41 providers. DR CPTC; Q9UIF7; 1 antibody. DR DNASU; 4595; -. DR Ensembl; ENST00000354383.10; ENSP00000346354.6; ENSG00000132781.21. [Q9UIF7-5] DR Ensembl; ENST00000355498.6; ENSP00000347685.2; ENSG00000132781.21. [Q9UIF7-6] DR Ensembl; ENST00000372098.7; ENSP00000361170.3; ENSG00000132781.21. [Q9UIF7-1] DR Ensembl; ENST00000372104.5; ENSP00000361176.1; ENSG00000132781.21. [Q9UIF7-6] DR Ensembl; ENST00000372110.7; ENSP00000361182.3; ENSG00000132781.21. [Q9UIF7-2] DR Ensembl; ENST00000372115.7; ENSP00000361187.3; ENSG00000132781.21. [Q9UIF7-3] DR Ensembl; ENST00000435155.2; ENSP00000403655.2; ENSG00000132781.21. [Q9UIF7-4] DR Ensembl; ENST00000448481.5; ENSP00000409718.1; ENSG00000132781.21. [Q9UIF7-4] DR Ensembl; ENST00000456914.7; ENSP00000407590.2; ENSG00000132781.21. [Q9UIF7-6] DR Ensembl; ENST00000672314.2; ENSP00000500828.2; ENSG00000132781.21. [Q9UIF7-6] DR Ensembl; ENST00000672818.3; ENSP00000500891.1; ENSG00000132781.21. [Q9UIF7-1] DR GeneID; 4595; -. DR KEGG; hsa:4595; -. DR MANE-Select; ENST00000456914.7; ENSP00000407590.2; NM_001048174.2; NP_001041639.1. [Q9UIF7-6] DR UCSC; uc001cnf.4; human. [Q9UIF7-1] DR AGR; HGNC:7527; -. DR CTD; 4595; -. DR DisGeNET; 4595; -. DR GeneCards; MUTYH; -. DR GeneReviews; MUTYH; -. DR HGNC; HGNC:7527; MUTYH. DR HPA; ENSG00000132781; Low tissue specificity. DR MalaCards; MUTYH; -. DR MIM; 604933; gene. DR MIM; 608456; phenotype. DR MIM; 613659; phenotype. DR neXtProt; NX_Q9UIF7; -. DR OpenTargets; ENSG00000132781; -. DR Orphanet; 440437; Familial colorectal cancer Type X. DR Orphanet; 247798; MUTYH-related attenuated familial adenomatous polyposis. DR PharmGKB; PA31328; -. DR VEuPathDB; HostDB:ENSG00000132781; -. DR eggNOG; KOG2457; Eukaryota. DR GeneTree; ENSGT00510000047220; -. DR HOGENOM; CLU_012862_0_0_1; -. DR InParanoid; Q9UIF7; -. DR OMA; QQTRMET; -. DR OrthoDB; 123472at2759; -. DR PhylomeDB; Q9UIF7; -. DR TreeFam; TF328549; -. DR PathwayCommons; Q9UIF7; -. DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine. DR Reactome; R-HSA-110331; Cleavage of the damaged purine. DR Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1. DR Reactome; R-HSA-9608287; Defective MUTYH substrate binding. [Q9UIF7-3] DR Reactome; R-HSA-9608290; Defective MUTYH substrate processing. DR SignaLink; Q9UIF7; -. DR SIGNOR; Q9UIF7; -. DR BioGRID-ORCS; 4595; 18 hits in 1164 CRISPR screens. DR EvolutionaryTrace; Q9UIF7; -. DR GeneWiki; MUTYH; -. DR GenomeRNAi; 4595; -. DR Pharos; Q9UIF7; Tbio. DR PRO; PR:Q9UIF7; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9UIF7; Protein. DR Bgee; ENSG00000132781; Expressed in cerebellar hemisphere and 95 other cell types or tissues. DR ExpressionAtlas; Q9UIF7; baseline and differential. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IBA:GO_Central. DR GO; GO:0035485; F:adenine/guanine mispair binding; IBA:GO_Central. DR GO; GO:0019104; F:DNA N-glycosylase activity; TAS:Reactome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0032407; F:MutSalpha complex binding; IDA:HGNC-UCL. DR GO; GO:0032357; F:oxidized purine DNA binding; IBA:GO_Central. DR GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IMP:UniProtKB. DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central. DR GO; GO:0045007; P:depurination; TAS:Reactome. DR GO; GO:0006281; P:DNA repair; TAS:ProtInc. DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central. DR GO; GO:0060546; P:negative regulation of necroptotic process; IEA:Ensembl. DR CDD; cd03431; DNA_Glycosylase_C; 1. DR CDD; cd00056; ENDO3c; 1. DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1. DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR004036; Endonuclease-III-like_CS2. DR InterPro; IPR003651; Endonuclease3_FeS-loop_motif. DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR023170; HhH_base_excis_C. DR InterPro; IPR000445; HhH_motif. DR InterPro; IPR044298; MIG/MutY. DR InterPro; IPR029119; MutY_C. DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1. DR PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1. DR Pfam; PF00633; HHH; 1. DR Pfam; PF00730; HhH-GPD; 1. DR Pfam; PF14815; NUDIX_4; 1. DR SMART; SM00478; ENDO3c; 1. DR SMART; SM00525; FES; 1. DR SUPFAM; SSF48150; DNA-glycosylase; 1. DR SUPFAM; SSF55811; Nudix; 1. DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1. DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1. DR PROSITE; PS51462; NUDIX; 1. DR Genevisible; Q9UIF7; HS. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Alternative splicing; Disease variant; DNA damage; KW DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur; Metal-binding; KW Mitochondrion; Nucleus; Reference proteome; Tumor suppressor. FT CHAIN 1..546 FT /note="Adenine DNA glycosylase" FT /id="PRO_0000102239" FT DOMAIN 364..495 FT /note="Nudix hydrolase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794" FT REGION 19..51 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 404..426 FT /note="Nudix box" FT ACT_SITE 131 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P83847" FT BINDING 287 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 294 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 297 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 303 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT SITE 233 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P83847" FT VAR_SEQ 1..14 FT /note="Missing (in isoform Beta-1, isoform Gamma-2 and FT isoform Gamma-3)" FT /evidence="ECO:0000303|PubMed:10684930" FT /id="VSP_010548" FT VAR_SEQ 53..63 FT /note="Missing (in isoform Alpha-3 and isoform Gamma-3)" FT /evidence="ECO:0000303|PubMed:10684930, FT ECO:0000303|PubMed:15489334" FT /id="VSP_010550" FT VAR_SEQ 53..62 FT /note="Missing (in isoform Alpha-2 and isoform Gamma-2)" FT /evidence="ECO:0000303|PubMed:10684930" FT /id="VSP_010549" FT VARIANT 18 FT /note="P -> L (in FAP2; uncertain significance; decreased FT function in DNA repair; dbSNP:rs79777494)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077640" FT VARIANT 22 FT /note="V -> M (does not affect function in DNA repair; FT dbSNP:rs3219484)" FT /evidence="ECO:0000269|PubMed:12606733, FT ECO:0000269|PubMed:16134147, ECO:0000269|PubMed:16287072, FT ECO:0000269|PubMed:16941501, ECO:0000269|PubMed:25820570, FT ECO:0000269|Ref.4" FT /id="VAR_018872" FT VARIANT 25 FT /note="G -> D (does not affect function in DNA repair; FT dbSNP:rs75321043)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077641" FT VARIANT 72 FT /note="V -> E (does not affect DNA glycosylase activity; FT dbSNP:rs1557487179)" FT /evidence="ECO:0000269|PubMed:20848659" FT /id="VAR_077642" FT VARIANT 100 FT /note="W -> R (found in sporadic hepatocellular carcinoma; FT uncertain significance; loss of function in DNA repair; FT dbSNP:rs1140507)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077643" FT VARIANT 102 FT /note="D -> N (found in multiple polyposis and sporadic FT colorectal cancer cases; uncertain significance; does not FT affect DNA glycosylase activity; does not affect function FT in DNA repair; dbSNP:rs587780746)" FT /evidence="ECO:0000269|PubMed:25820570, FT ECO:0000269|PubMed:26694661" FT /id="VAR_077644" FT VARIANT 125 FT /note="Y -> H (in FAP2; decreased function in DNA repair)" FT /evidence="ECO:0000269|PubMed:15366000, FT ECO:0000269|PubMed:25820570" FT /id="VAR_026045" FT VARIANT 128 FT /note="W -> R (in FAP2; loss of function in DNA repair; FT dbSNP:rs730881832)" FT /evidence="ECO:0000269|PubMed:12853198, FT ECO:0000269|PubMed:25820570" FT /id="VAR_026046" FT VARIANT 148 FT /note="G -> GIW (in FAP2; reduced DNA glycosylase activity; FT decreased DNA binding; loss of function in DNA repair)" FT /evidence="ECO:0000269|PubMed:16287072, FT ECO:0000269|PubMed:19953527, ECO:0000269|PubMed:20418187" FT /id="VAR_064938" FT VARIANT 154 FT /note="P -> L (in FAP2; decreased function in DNA repair; FT dbSNP:rs777184451)" FT /evidence="ECO:0000269|PubMed:16557584, FT ECO:0000269|PubMed:25820570" FT /id="VAR_077646" FT VARIANT 176 FT /note="Y -> C (in FAP2; loss of DNA glycosylase activity; FT decreased DNA binding; loss of function in DNA repair; FT dbSNP:rs34612342)" FT /evidence="ECO:0000269|PubMed:11818965, FT ECO:0000269|PubMed:12606733, ECO:0000269|PubMed:12853198, FT ECO:0000269|PubMed:16134147, ECO:0000269|PubMed:16287072, FT ECO:0000269|PubMed:16557584, ECO:0000269|PubMed:16941501, FT ECO:0000269|PubMed:18091433, ECO:0000269|PubMed:19953527, FT ECO:0000269|PubMed:20418187, ECO:0000269|PubMed:20848659, FT ECO:0000269|PubMed:25820570" FT /id="VAR_018873" FT VARIANT 177 FT /note="Y -> S (in FAP2)" FT /evidence="ECO:0000269|PubMed:16941501" FT /id="VAR_077647" FT VARIANT 179 FT /note="R -> C (in FAP2; also found in multiple polyposis FT and colorectal cancer cases; loss of function in DNA FT repair; dbSNP:rs747993448)" FT /evidence="ECO:0000269|PubMed:18091433, FT ECO:0000269|PubMed:25820570" FT /id="VAR_064939" FT VARIANT 179 FT /note="R -> H (in FAP2; loss of DNA glycosylase activity; FT loss of function in DNA repair; dbSNP:rs143353451)" FT /evidence="ECO:0000269|PubMed:15366000, FT ECO:0000269|PubMed:16557584, ECO:0000269|PubMed:20848659, FT ECO:0000269|PubMed:25820570" FT /id="VAR_026047" FT VARIANT 182 FT /note="R -> Q (in FAP2; loss of function in DNA repair; FT dbSNP:rs533899702)" FT /evidence="ECO:0000269|PubMed:16287072, FT ECO:0000269|PubMed:25820570" FT /id="VAR_077648" FT VARIANT 182 FT /note="R -> W (in FAP2; loss of DNA glycosylase activity; FT loss of DNA binding; loss of function in DNA repair; FT dbSNP:rs750592289)" FT /evidence="ECO:0000269|PubMed:18091433, FT ECO:0000269|PubMed:19953527, ECO:0000269|PubMed:20418187" FT /id="VAR_064940" FT VARIANT 186 FT /note="G -> E (in FAP2; decreased function in DNA repair; FT dbSNP:rs754155145)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077649" FT VARIANT 213 FT /note="G -> E (in FAP2; dbSNP:rs768553551)" FT /evidence="ECO:0000269|PubMed:18515411" FT /id="VAR_077650" FT VARIANT 220 FT /note="I -> V (in FAP2; uncertain significance; reduced DNA FT glycosylase activity; no effect on function in DNA repair; FT dbSNP:rs200872702)" FT /evidence="ECO:0000269|PubMed:16287072, FT ECO:0000269|PubMed:20848659, ECO:0000269|PubMed:25820570" FT /id="VAR_077651" FT VARIANT 224 FT /note="A -> V (decreased function in DNA repair; FT dbSNP:rs11545695)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077652" FT VARIANT 231 FT /note="V -> M (found in familial colorectal cancer; likely FT pathogenic; no significant effect on DNA glycosylase FT activity; slightly decreased function in DNA repair; FT dbSNP:rs200165598)" FT /evidence="ECO:0000269|PubMed:25820570, FT ECO:0000269|PubMed:26694661" FT /id="VAR_077653" FT VARIANT 235 FT /note="N -> S (in FAP2; loss of DNA glycosylase activity; FT loss of function in DNA repair; dbSNP:rs1057517765)" FT /evidence="ECO:0000269|PubMed:18515411, FT ECO:0000269|PubMed:26694661" FT /id="VAR_077654" FT VARIANT 238 FT /note="R -> W (in FAP2; uncertain significance; decreased FT function in DNA repair; dbSNP:rs34126013)" FT /evidence="ECO:0000269|PubMed:15366000, FT ECO:0000269|PubMed:25820570" FT /id="VAR_026048" FT VARIANT 242 FT /note="R -> C (found in colorectal polyposis; likely FT pathogenic; decreased function in DNA repair; FT dbSNP:rs200495564)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077655" FT VARIANT 242 FT /note="R -> H (in FAP2; loss of function in DNA repair; FT dbSNP:rs140342925)" FT /evidence="ECO:0000269|PubMed:16134147, FT ECO:0000269|PubMed:16287072, ECO:0000269|PubMed:16557584, FT ECO:0000269|PubMed:25820570" FT /id="VAR_077656" FT VARIANT 243 FT /note="V -> F (does not affect function; FT dbSNP:rs587780749)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077657" FT VARIANT 244 FT /note="R -> G (reduced DNA glycosylase activity; decreased FT function in DNA repair; dbSNP:rs587782885)" FT /evidence="ECO:0000269|PubMed:26694661" FT /id="VAR_077658" FT VARIANT 271 FT /note="R -> W (in FAP2; loss of function in DNA repair; FT dbSNP:rs769237459)" FT /evidence="ECO:0000269|PubMed:16134147, FT ECO:0000269|PubMed:16557584, ECO:0000269|PubMed:25820570" FT /id="VAR_077659" FT VARIANT 280 FT /note="M -> V (in FAP2; reduced DNA glycosylase activity; FT dbSNP:rs876659676)" FT /evidence="ECO:0000269|PubMed:16941501, FT ECO:0000269|PubMed:20848659" FT /id="VAR_077660" FT VARIANT 283 FT /note="G -> E (in FAP2; uncertain significance; does not FT affect function in DNA repair; dbSNP:rs730881833)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077661" FT VARIANT 287 FT /note="C -> W (found in a case of sporadic lung cancer; FT uncertain significance; loss of function in DNA repair)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077662" FT VARIANT 292 FT /note="P -> L (in FAP2; also found in multiple polyposis FT cases; loss of function in DNA repair; dbSNP:rs374950566)" FT /evidence="ECO:0000269|PubMed:16557584, FT ECO:0000269|PubMed:16941501, ECO:0000269|PubMed:25820570" FT /id="VAR_077663" FT VARIANT 306 FT /note="R -> C (in FAP2; uncertain significance; does not FT affect DNA glycosylase activity; slightly decreased FT function in DNA repair; dbSNP:rs138089183)" FT /evidence="ECO:0000269|PubMed:16557584, FT ECO:0000269|PubMed:20848659, ECO:0000269|PubMed:25820570" FT /id="VAR_077664" FT VARIANT 319 FT /note="S -> N (does not affect DNA glycosylase activity; FT does not affect function in DNA repair; dbSNP:rs587781810)" FT /evidence="ECO:0000269|PubMed:26694661" FT /id="VAR_077665" FT VARIANT 335 FT /note="Q -> H (does not affect function in DNA repair; FT dbSNP:rs3219489)" FT /evidence="ECO:0000269|PubMed:12606733, FT ECO:0000269|PubMed:16134147, ECO:0000269|PubMed:16287072, FT ECO:0000269|PubMed:16941501, ECO:0000269|PubMed:25820570, FT ECO:0000269|Ref.4" FT /id="VAR_018874" FT VARIANT 335 FT /note="Q -> R (found in a family with non-polyposis FT colorectal cancer-like syndrome; uncertain significance; FT does not affect function in DNA repair; dbSNP:rs199742231)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077666" FT VARIANT 370 FT /note="A -> V (does not affect DNA glycosylase activity; FT dbSNP:rs35352891)" FT /evidence="ECO:0000269|PubMed:20848659" FT /id="VAR_048262" FT VARIANT 377 FT /note="P -> T (in FAP2; decreased function in DNA repair)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077667" FT VARIANT 385 FT /note="L -> P (in FAP2; also found in multiple polyposis FT cases; loss of DNA glycosylase activity; loss of function FT in DNA repair; dbSNP:rs1060501335)" FT /evidence="ECO:0000269|PubMed:16134147, FT ECO:0000269|PubMed:16941501, ECO:0000269|PubMed:20848659, FT ECO:0000269|PubMed:25820570" FT /id="VAR_077668" FT VARIANT 393 FT /note="G -> D (in FAP2; reduced DNA glycosylase activity; FT decreased DNA binding; decreased function in DNA repair; FT dbSNP:rs36053993)" FT /evidence="ECO:0000269|PubMed:11818965, FT ECO:0000269|PubMed:12606733, ECO:0000269|PubMed:12853198, FT ECO:0000269|PubMed:16134147, ECO:0000269|PubMed:16287072, FT ECO:0000269|PubMed:16557584, ECO:0000269|PubMed:16941501, FT ECO:0000269|PubMed:18091433, ECO:0000269|PubMed:19953527, FT ECO:0000269|PubMed:20418187, ECO:0000269|PubMed:20848659, FT ECO:0000269|PubMed:25820570" FT /id="VAR_018875" FT VARIANT 402 FT /note="P -> L (in FAP2; also found in multiple polyposis FT and colorectal cancer cases; loss of DNA glycosylase FT activity; loss of function in DNA repair; FT dbSNP:rs529008617)" FT /evidence="ECO:0000269|PubMed:16557584, FT ECO:0000269|PubMed:20848659, ECO:0000269|PubMed:25820570" FT /id="VAR_077669" FT VARIANT 402 FT /note="P -> S (in GASC; sporadic; decreased function in DNA FT repair; dbSNP:rs121908382)" FT /evidence="ECO:0000269|PubMed:15273732, FT ECO:0000269|PubMed:25820570" FT /id="VAR_026049" FT VARIANT 411 FT /note="Q -> R (in GASC; uncertain significance; does not FT affect function in DNA repair; dbSNP:rs121908383)" FT /evidence="ECO:0000269|PubMed:15273732, FT ECO:0000269|PubMed:25820570" FT /id="VAR_026050" FT VARIANT 417 FT /note="L -> M (in FAP2; uncertain significance; also found FT in a family with non-polyposis colorectal cancer-like FT syndrome; uncertain significance; does not affect function FT in DNA repair; dbSNP:rs144079536)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077670" FT VARIANT 423 FT /note="R -> C (in FAP2; uncertain significance; does not FT affect function in DNA repair; dbSNP:rs150792276)" FT /evidence="ECO:0000269|PubMed:16134147, FT ECO:0000269|PubMed:16557584, ECO:0000269|PubMed:25820570" FT /id="VAR_077671" FT VARIANT 434 FT /note="R -> P (found in sporadic colorectal cancer cases; FT uncertain significance; decreased function in DNA repair)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077672" FT VARIANT 434 FT /note="R -> Q (does not affect function in DNA repair; FT dbSNP:rs587782120)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077673" FT VARIANT 470 FT /note="A -> D (in FAP2; loss of function in DNA repair; FT dbSNP:rs200844166)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077674" FT VARIANT 470 FT /note="A -> T (found in patient with multiple polyposis; FT uncertain significance; does not affect function in DNA FT repair; dbSNP:rs192816572)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077675" FT VARIANT 474 FT /note="T -> M (in FAP2; uncertain significance; FT dbSNP:rs767747402)" FT /evidence="ECO:0000269|PubMed:18515411" FT /id="VAR_077676" FT VARIANT 477 FT /note="Missing (in FAP2; also found in a case of sporadic FT colorectal cancer; loss of DNA glycosylase activity; loss FT of DNA binding; loss of function in DNA repair)" FT /evidence="ECO:0000269|PubMed:16134147, FT ECO:0000269|PubMed:16557584, ECO:0000269|PubMed:19953527, FT ECO:0000269|PubMed:20418187, ECO:0000269|PubMed:20848659, FT ECO:0000269|PubMed:25820570" FT /id="VAR_064941" FT VARIANT 486 FT /note="A -> T (in FAP2; decreased function in DNA repair; FT dbSNP:rs587782263)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077677" FT VARIANT 490 FT /note="V -> F (in FAP2; uncertain significance; decreased FT function in DNA repair; dbSNP:rs587782228)" FT /evidence="ECO:0000269|PubMed:16557584, FT ECO:0000269|PubMed:25820570" FT /id="VAR_077678" FT VARIANT 500 FT /note="G -> E (decreased function in DNA repair; FT dbSNP:rs3219494)" FT /evidence="ECO:0000269|PubMed:25820570, ECO:0000269|Ref.4" FT /id="VAR_018876" FT VARIANT 512 FT /note="S -> F (does not affect DNA glycosylase activity; FT does not affect function in DNA repair; dbSNP:rs140118273)" FT /evidence="ECO:0000269|PubMed:12606733, FT ECO:0000269|PubMed:16941501, ECO:0000269|PubMed:20848659, FT ECO:0000269|PubMed:25820570" FT /id="VAR_026051" FT VARIANT 513 FT /note="P -> L (does not affect function in DNA repair; FT dbSNP:rs587778542)" FT /evidence="ECO:0000269|PubMed:25820570" FT /id="VAR_077679" FT VARIANT 520 FT /note="R -> H (does not affect DNA glycosylase activity; FT does not affect function in DNA repair; dbSNP:rs374655042)" FT /evidence="ECO:0000269|PubMed:26694661" FT /id="VAR_077680" FT VARIANT 526 FT /note="L -> M (does not affect function in DNA repair; FT dbSNP:rs3219496)" FT /evidence="ECO:0000269|PubMed:25820570, ECO:0000269|Ref.4" FT /id="VAR_018877" FT VARIANT 531 FT /note="R -> Q (does not affect function in DNA repair; FT dbSNP:rs3219497)" FT /evidence="ECO:0000269|PubMed:25820570, ECO:0000269|Ref.4" FT /id="VAR_018878" FT VARIANT 536 FT /note="T -> A (does not affect DNA glycosylase activity; FT does not affect function in DNA repair; dbSNP:rs151196169)" FT /evidence="ECO:0000269|PubMed:26694661" FT /id="VAR_077681" FT MUTAGEN 121 FT /note="D->G: Does not affect DNA glycosylase activity. Does FT not affect function in DNA repair." FT /evidence="ECO:0000269|PubMed:26694661" FT MUTAGEN 233 FT /note="D->N: Loss of DNA glycosylase activity." FT /evidence="ECO:0000269|PubMed:20848659" FT HELIX 87..104 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 109..116 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 120..135 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 139..152 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 156..160 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 164..171 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 177..193 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 202..208 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 214..224 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 234..243 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 253..266 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 272..285 FT /evidence="ECO:0007829|PDB:3N5N" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 304..316 FT /evidence="ECO:0007829|PDB:3N5N" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:3N5N" FT STRAND 358..360 FT /evidence="ECO:0007829|PDB:1X51" FT STRAND 366..377 FT /evidence="ECO:0007829|PDB:1X51" FT STRAND 379..388 FT /evidence="ECO:0007829|PDB:1X51" FT STRAND 403..405 FT /evidence="ECO:0007829|PDB:1X51" FT HELIX 410..424 FT /evidence="ECO:0007829|PDB:1X51" FT STRAND 447..456 FT /evidence="ECO:0007829|PDB:1X51" FT STRAND 470..474 FT /evidence="ECO:0007829|PDB:1X51" FT HELIX 475..480 FT /evidence="ECO:0007829|PDB:1X51" FT HELIX 485..495 FT /evidence="ECO:0007829|PDB:1X51" SQ 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 //