SMUG1_HUMAN
ID SMUG1_HUMAN Reviewed; 270 AA.
AC Q53HV7; A8K2K9; O95862; Q0D2M0; Q8NB71; Q9BWC8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Single-strand selective monofunctional uracil DNA glycosylase;
DE EC=3.2.2.-;
GN Name=SMUG1;
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 [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Ovary;
RX PubMed=10074426; DOI=10.1016/s0960-9822(99)80087-6;
RA Haushalter K.A., Stukenberg P.T., Kirschner M.W., Verdine G.L.;
RT "Identification of a new uracil-DNA glycosylase family by expression
RT cloning using synthetic inhibitors.";
RL Curr. Biol. 9:174-185(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=12718543; DOI=10.1021/bi0273213;
RA Masaoka A., Matsubara M., Hasegawa R., Tanaka T., Kurisu S., Terato H.,
RA Ohyama Y., Karino N., Matsuda A., Ide H.;
RT "Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA
RT glycosylase in repair of 5-formyluracil and other oxidized and deaminated
RT base lesions.";
RL Biochemistry 42:5003-5012(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-15 AND TRP-105.
RG NIEHS SNPs program;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle, and Uterus;
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 PROTEIN SEQUENCE OF 13-21; 26-37; 46-66; 79-105; 124-140; 141-146; 147-157;
RP 188-200; 201-208; 224-243 AND 259-270, FUNCTION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11526119; DOI=10.1074/jbc.m106953200;
RA Boorstein R.J., Cummings A. Jr., Marenstein D.R., Chan M.K., Ma Y.,
RA Neubert T.A., Brown S.M., Teebor G.W.;
RT "Definitive identification of mammalian 5-hydroxymethyluracil DNA N-
RT glycosylase activity as SMUG1.";
RL J. Biol. Chem. 276:41991-41997(2001).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12161446; DOI=10.1074/jbc.m207107200;
RA Kavli B., Sundheim O., Akbari M., Otterlei M., Nilsen H., Skorpen F.,
RA Aas P.A., Hagen L., Krokan H.E., Slupphaug G.;
RT "hUNG2 is the major repair enzyme for removal of uracil from U:A matches,
RT U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad
RT specificity backup.";
RL J. Biol. Chem. 277:39926-39936(2002).
RN [10]
RP MUTAGENESIS OF ASN-85; GLY-87; PHE-89; GLY-90; MET-91; PHE-98; ASN-163 AND
RP HIS-239.
RX PubMed=15466595; DOI=10.1093/nar/gkh859;
RA Matsubara M., Tanaka T., Terato H., Ohmae E., Izumi S., Katayanagi K.,
RA Ide H.;
RT "Mutational analysis of the damage-recognition and catalytic mechanism of
RT human SMUG1 DNA glycosylase.";
RL Nucleic Acids Res. 32:5291-5302(2004).
CC -!- FUNCTION: Recognizes base lesions in the genome and initiates base
CC excision DNA repair. Acts as a monofunctional DNA glycosylase specific
CC for uracil (U) residues in DNA with a preference for single-stranded
CC DNA substrates. The activity is greater toward mismatches (U/G)
CC compared to matches (U/A). Excises uracil (U), 5-formyluracil (fU) and
CC uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil
CC (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not
CC analogous cytosine derivatives (5-hydroxycytosine and 5-
CC formylcytosine), nor other oxidized bases. The activity is damage-
CC specific and salt-dependent. The substrate preference is the following:
CC ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and
CC dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration.
CC {ECO:0000269|PubMed:10074426, ECO:0000269|PubMed:11526119,
CC ECO:0000269|PubMed:12161446, ECO:0000269|PubMed:12718543}.
CC -!- INTERACTION:
CC Q53HV7; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-749970, EBI-396137;
CC Q53HV7; O43186: CRX; NbExp=3; IntAct=EBI-749970, EBI-748171;
CC Q53HV7; Q93062: RBPMS; NbExp=2; IntAct=EBI-749970, EBI-740322;
CC Q53HV7; P12757: SKIL; NbExp=3; IntAct=EBI-749970, EBI-2902468;
CC Q53HV7; Q08AM6: VAC14; NbExp=4; IntAct=EBI-749970, EBI-2107455;
CC Q53HV7-2; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-12275818, EBI-12809220;
CC Q53HV7-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12275818, EBI-3867333;
CC Q53HV7-2; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-12275818, EBI-2807642;
CC Q53HV7-2; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-12275818, EBI-748515;
CC Q53HV7-2; Q13227: GPS2; NbExp=3; IntAct=EBI-12275818, EBI-713355;
CC Q53HV7-2; P52597: HNRNPF; NbExp=3; IntAct=EBI-12275818, EBI-352986;
CC Q53HV7-2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-12275818, EBI-6509505;
CC Q53HV7-2; Q7L273: KCTD9; NbExp=3; IntAct=EBI-12275818, EBI-4397613;
CC Q53HV7-2; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-12275818, EBI-9478422;
CC Q53HV7-2; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-12275818, EBI-11953846;
CC Q53HV7-2; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-12275818, EBI-11992140;
CC Q53HV7-2; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-12275818, EBI-3957672;
CC Q53HV7-2; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-12275818, EBI-11962084;
CC Q53HV7-2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-12275818, EBI-10261141;
CC Q53HV7-2; P25791-3: LMO2; NbExp=4; IntAct=EBI-12275818, EBI-11959475;
CC Q53HV7-2; Q15345: LRRC41; NbExp=3; IntAct=EBI-12275818, EBI-721408;
CC Q53HV7-2; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-12275818, EBI-11750983;
CC Q53HV7-2; Q86UR1-2: NOXA1; NbExp=4; IntAct=EBI-12275818, EBI-12025760;
CC Q53HV7-2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-12275818, EBI-748974;
CC Q53HV7-2; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-12275818, EBI-11022007;
CC Q53HV7-2; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-12275818, EBI-724639;
CC Q53HV7-2; Q99697-2: PITX2; NbExp=3; IntAct=EBI-12275818, EBI-12138495;
CC Q53HV7-2; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-12275818, EBI-1389308;
CC Q53HV7-2; O43741: PRKAB2; NbExp=3; IntAct=EBI-12275818, EBI-1053424;
CC Q53HV7-2; O75360: PROP1; NbExp=3; IntAct=EBI-12275818, EBI-9027467;
CC Q53HV7-2; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-12275818, EBI-740924;
CC Q53HV7-2; P0CG20: PRR35; NbExp=3; IntAct=EBI-12275818, EBI-11986293;
CC Q53HV7-2; Q93062-3: RBPMS; NbExp=6; IntAct=EBI-12275818, EBI-740343;
CC Q53HV7-2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-12275818, EBI-358489;
CC Q53HV7-2; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-12275818, EBI-12275818;
CC Q53HV7-2; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-12275818, EBI-11959123;
CC Q53HV7-2; Q9NQB0-10: TCF7L2; NbExp=3; IntAct=EBI-12275818, EBI-11746252;
CC Q53HV7-2; Q96M29: TEKT5; NbExp=3; IntAct=EBI-12275818, EBI-10239812;
CC Q53HV7-2; Q92734: TFG; NbExp=3; IntAct=EBI-12275818, EBI-357061;
CC Q53HV7-2; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-12275818, EBI-11064654;
CC Q53HV7-2; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-12275818, EBI-8451480;
CC Q53HV7-2; Q08AM6: VAC14; NbExp=3; IntAct=EBI-12275818, EBI-2107455;
CC Q53HV7-2; O95231: VENTX; NbExp=3; IntAct=EBI-12275818, EBI-10191303;
CC Q53HV7-2; Q15915: ZIC1; NbExp=3; IntAct=EBI-12275818, EBI-11963196;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10074426,
CC ECO:0000269|PubMed:12161446}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q53HV7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53HV7-2; Sequence=VSP_015150, VSP_015151;
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC SMUG1 family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/smug1/";
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DR EMBL; AF125182; AAD17301.1; -; mRNA.
DR EMBL; AK001235; BAA91571.1; -; mRNA.
DR EMBL; AK091468; BAC03670.1; -; mRNA.
DR EMBL; AK222473; BAD96193.1; -; mRNA.
DR EMBL; AK290274; BAF82963.1; -; mRNA.
DR EMBL; AF489699; AAL86910.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96752.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96756.1; -; Genomic_DNA.
DR EMBL; BC000417; AAH00417.1; -; mRNA.
DR EMBL; BC088352; AAH88352.1; -; mRNA.
DR EMBL; BC105607; AAI05608.1; -; mRNA.
DR CCDS; CCDS58239.1; -. [Q53HV7-2]
DR CCDS; CCDS8874.1; -. [Q53HV7-1]
DR RefSeq; NP_001230716.1; NM_001243787.1. [Q53HV7-1]
DR RefSeq; NP_001230717.1; NM_001243788.1. [Q53HV7-1]
DR RefSeq; NP_001230718.1; NM_001243789.1. [Q53HV7-2]
DR RefSeq; NP_001230719.1; NM_001243790.1. [Q53HV7-2]
DR RefSeq; NP_001230720.1; NM_001243791.1. [Q53HV7-2]
DR RefSeq; NP_055126.1; NM_014311.2. [Q53HV7-1]
DR RefSeq; XP_006719382.1; XM_006719319.3. [Q53HV7-1]
DR RefSeq; XP_006719383.1; XM_006719320.3.
DR RefSeq; XP_006719384.1; XM_006719321.3.
DR RefSeq; XP_006719385.1; XM_006719322.3.
DR RefSeq; XP_011536411.1; XM_011538109.2.
DR RefSeq; XP_011536412.1; XM_011538110.2.
DR RefSeq; XP_011536413.1; XM_011538111.2.
DR RefSeq; XP_011536414.1; XM_011538112.2. [Q53HV7-1]
DR RefSeq; XP_011536415.1; XM_011538113.2.
DR RefSeq; XP_011536416.1; XM_011538114.2.
DR RefSeq; XP_011536417.1; XM_011538115.2.
DR RefSeq; XP_011536418.1; XM_011538116.2. [Q53HV7-1]
DR RefSeq; XP_011536419.1; XM_011538117.2.
DR RefSeq; XP_011536420.1; XM_011538118.2. [Q53HV7-1]
DR RefSeq; XP_011536421.1; XM_011538119.2. [Q53HV7-1]
DR RefSeq; XP_011536422.1; XM_011538120.2.
DR RefSeq; XP_011536423.1; XM_011538121.2. [Q53HV7-1]
DR RefSeq; XP_011536424.1; XM_011538122.2.
DR RefSeq; XP_016874602.1; XM_017019113.1.
DR RefSeq; XP_016874603.1; XM_017019114.1.
DR RefSeq; XP_016874604.1; XM_017019115.1.
DR RefSeq; XP_016874605.1; XM_017019116.1.
DR RefSeq; XP_016874606.1; XM_017019117.1.
DR RefSeq; XP_016874607.1; XM_017019118.1.
DR RefSeq; XP_016874608.1; XM_017019119.1. [Q53HV7-2]
DR RefSeq; XP_016874609.1; XM_017019120.1.
DR AlphaFoldDB; Q53HV7; -.
DR SMR; Q53HV7; -.
DR BioGRID; 117118; 48.
DR IntAct; Q53HV7; 45.
DR STRING; 9606.ENSP00000424191; -.
DR iPTMnet; Q53HV7; -.
DR PhosphoSitePlus; Q53HV7; -.
DR BioMuta; SMUG1; -.
DR EPD; Q53HV7; -.
DR jPOST; Q53HV7; -.
DR MassIVE; Q53HV7; -.
DR MaxQB; Q53HV7; -.
DR PaxDb; Q53HV7; -.
DR PeptideAtlas; Q53HV7; -.
DR PRIDE; Q53HV7; -.
DR ProteomicsDB; 62508; -. [Q53HV7-1]
DR ProteomicsDB; 62509; -. [Q53HV7-2]
DR TopDownProteomics; Q53HV7-2; -. [Q53HV7-2]
DR Antibodypedia; 27322; 289 antibodies from 31 providers.
DR DNASU; 23583; -.
DR Ensembl; ENST00000243112.9; ENSP00000243112.5; ENSG00000123415.16. [Q53HV7-2]
DR Ensembl; ENST00000337581.7; ENSP00000338606.3; ENSG00000123415.16. [Q53HV7-1]
DR Ensembl; ENST00000401977.6; ENSP00000384828.2; ENSG00000123415.16. [Q53HV7-1]
DR Ensembl; ENST00000506595.5; ENSP00000421206.1; ENSG00000123415.16. [Q53HV7-2]
DR Ensembl; ENST00000508394.6; ENSP00000424191.1; ENSG00000123415.16. [Q53HV7-1]
DR Ensembl; ENST00000513838.5; ENSP00000423629.1; ENSG00000123415.16. [Q53HV7-2]
DR Ensembl; ENST00000514685.5; ENSP00000421139.1; ENSG00000123415.16. [Q53HV7-2]
DR Ensembl; ENST00000682136.1; ENSP00000507590.1; ENSG00000123415.16. [Q53HV7-1]
DR GeneID; 23583; -.
DR KEGG; hsa:23583; -.
DR MANE-Select; ENST00000682136.1; ENSP00000507590.1; NM_001243787.2; NP_001230716.1.
DR UCSC; uc001sfb.5; human. [Q53HV7-1]
DR CTD; 23583; -.
DR DisGeNET; 23583; -.
DR GeneCards; SMUG1; -.
DR HGNC; HGNC:17148; SMUG1.
DR HPA; ENSG00000123415; Low tissue specificity.
DR MIM; 607753; gene.
DR neXtProt; NX_Q53HV7; -.
DR OpenTargets; ENSG00000123415; -.
DR PharmGKB; PA142670895; -.
DR VEuPathDB; HostDB:ENSG00000123415; -.
DR eggNOG; ENOG502QT20; Eukaryota.
DR GeneTree; ENSGT00390000004897; -.
DR HOGENOM; CLU_134151_0_0_1; -.
DR InParanoid; Q53HV7; -.
DR OMA; VANYCPL; -.
DR PhylomeDB; Q53HV7; -.
DR TreeFam; TF324356; -.
DR BRENDA; 3.2.2.27; 2681.
DR PathwayCommons; Q53HV7; -.
DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1.
DR SignaLink; Q53HV7; -.
DR BioGRID-ORCS; 23583; 74 hits in 1082 CRISPR screens.
DR ChiTaRS; SMUG1; human.
DR GeneWiki; SMUG1; -.
DR GenomeRNAi; 23583; -.
DR Pharos; Q53HV7; Tbio.
DR PRO; PR:Q53HV7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q53HV7; protein.
DR Bgee; ENSG00000123415; Expressed in lower esophagus mucosa and 136 other tissues.
DR ExpressionAtlas; Q53HV7; baseline and differential.
DR Genevisible; Q53HV7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IDA:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0017065; F:single-strand selective uracil DNA N-glycosylase activity; IDA:HGNC-UCL.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:HGNC-UCL.
DR GO; GO:0006284; P:base-excision repair; IDA:HGNC-UCL.
DR GO; GO:0045008; P:depyrimidination; TAS:Reactome.
DR CDD; cd19374; UDG-F3_SMUG1-like; 1.
DR Gene3D; 3.40.470.10; -; 1.
DR InterPro; IPR039134; SMUG1.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR PANTHER; PTHR13235; PTHR13235; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; DNA damage; DNA repair;
KW DNA-binding; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..270
FT /note="Single-strand selective monofunctional uracil DNA
FT glycosylase"
FT /id="PRO_0000071992"
FT REGION 173..187
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="substrate"
FT BINDING 163
FT /ligand="substrate"
FT BINDING 239
FT /ligand="substrate"
FT VAR_SEQ 136..177
FT /note="VSGARFWGFFRNLCGQPEVFFHHCFVHNLCPLLFLAPSGRNL -> GPRQSM
FT GHEIKSELLMGGCSWIRGKIQCDRVQVRRPGFSSQL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015150"
FT VAR_SEQ 178..270
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015151"
FT VARIANT 15
FT /note="G -> V (in dbSNP:rs2233920)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023243"
FT VARIANT 105
FT /note="R -> W (in dbSNP:rs3136389)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_023244"
FT MUTAGEN 85
FT /note="N->A: Markedly impaired damage-excising activity for
FT U/G, hoU/G, hmU/A and fU/A. No cytosine-excising activity
FT for C/G, C/A, C/T and C/C."
FT /evidence="ECO:0000269|PubMed:15466595"
FT MUTAGEN 87
FT /note="G->A,S: Impaired the damage-excising activity for
FT U/G, hoU/G, hmU/A and fU/A."
FT /evidence="ECO:0000269|PubMed:15466595"
FT MUTAGEN 87
FT /note="G->F: Loss of damage-excising activity."
FT /evidence="ECO:0000269|PubMed:15466595"
FT MUTAGEN 89
FT /note="F->A,G,S: No effect on damage-excising activity for
FT U/G, hoU/G, hmU/A and fU/A."
FT /evidence="ECO:0000269|PubMed:15466595"
FT MUTAGEN 90
FT /note="G->A: Loss of damage-excising activity for U/G.
FT Weak, but significant activity toward hoU/G, hmU/A and
FT fU/A."
FT /evidence="ECO:0000269|PubMed:15466595"
FT MUTAGEN 91
FT /note="M->A: No effect on damage-excising activity for U/G,
FT hoU/G, hmU/A and fU/A."
FT /evidence="ECO:0000269|PubMed:15466595"
FT MUTAGEN 98
FT /note="F->L: Impaired the damage-excising activity for U/G,
FT hoU/G, hmU/A and fU/A."
FT /evidence="ECO:0000269|PubMed:15466595"
FT MUTAGEN 163
FT /note="N->D: Impaired the damage-excising activity for U/G,
FT hoU/G, hmU/A and fU/A. No cytosine-excising activity for
FT C/G, C/A, C/T and C/C. hoC-excising activity for hoC/A,
FT hoC/T and hoC/C."
FT /evidence="ECO:0000269|PubMed:15466595"
FT MUTAGEN 239
FT /note="H->L,N: Markedly impaired the damage-excising
FT activity for U/G, hoU/G, hmU/A and fU/A."
FT /evidence="ECO:0000269|PubMed:15466595"
FT CONFLICT 30
FT /note="S -> G (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="S -> L (in Ref. 3; BAC03670)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="P -> I (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="I -> V (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 66..174
FT /note="Missing (in Ref. 3; BAC03670)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="T -> I (in Ref. 4; BAD96193)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="M -> V (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="H -> R (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="I -> V (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="G -> S (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 259..260
FT /note="LN -> NL (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..270
FT /note="LK -> TS (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 29862 MW; 2AB18F6F757F6DD7 CRC64;
MPQAFLLGSI HEPAGALMEP QPCPGSLAES FLEEELRLNA ELSQLQFSEP VGIIYNPVEY
AWEPHRNYVT RYCQGPKEVL FLGMNPGPFG MAQTGVPFGE VSMVRDWLGI VGPVLTPPQE
HPKRPVLGLE CPQSEVSGAR FWGFFRNLCG QPEVFFHHCF VHNLCPLLFL APSGRNLTPA
ELPAKQREQL LGICDAALCR QVQLLGVRLV VGVGRLAEQR ARRALAGLMP EVQVEGLLHP
SPRNPQANKG WEAVAKERLN ELGLLPLLLK
