UNG_HUMAN
ID UNG_HUMAN Reviewed; 313 AA.
AC P13051; A8K5M6; B2R8Y1; O00637; O00719; Q93028;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166};
DE Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166};
DE EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
GN Name=UNG {ECO:0000255|HAMAP-Rule:MF_03166};
GN Synonyms=DGU, UNG1 {ECO:0000255|HAMAP-Rule:MF_03166},
GN UNG15 {ECO:0000255|HAMAP-Rule:MF_03166};
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), AND PROTEIN SEQUENCE OF 87-113.
RC TISSUE=Placenta;
RX PubMed=2555154; DOI=10.1002/j.1460-2075.1989.tb08464.x;
RA Olsen L.C., Aasland R., Wittwer C.U., Krokan H.E., Helland D.E.;
RT "Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA
RT repair enzyme.";
RL EMBO J. 8:3121-3125(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7926048; DOI=10.1016/0014-5793(94)01042-0;
RA Haug T., Skorpen F., Lund H., Krokan H.E.;
RT "Structure of the gene for human uracil-DNA glycosylase and analysis of the
RT promoter function.";
RL FEBS Lett. 353:180-184(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND ALTERNATIVE
RP SPLICING.
RX PubMed=9016624; DOI=10.1093/nar/25.4.750;
RA Nilsen H., Solum K., Haug T., Krokan H.E.;
RT "Nuclear and mitochondrial uracil-DNA glycosylases are generated by
RT alternative splicing and transcription from different positions in the UNG
RT gene.";
RL Nucleic Acids Res. 25:750-755(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Tongue;
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 [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 1).
RC TISSUE=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 SUBCELLULAR LOCATION.
RX PubMed=8332455; DOI=10.1093/nar/21.11.2579;
RA Slupphaug G., Markussen F.-H., Olsen L.C., Aasland R., Aarsaether N.,
RA Bakke O., Krokan H.E., Helland D.E.;
RT "Nuclear and mitochondrial forms of human uracil-DNA glycosylase are
RT encoded by the same gene.";
RL Nucleic Acids Res. 21:2579-2584(1993).
RN [9]
RP MUTAGENESIS.
RX PubMed=8670846; DOI=10.1002/j.1460-2075.1996.tb00710.x;
RA Kavli B., Slupphaug G., Mol C.D., Arvai A.S., Petersen S.B., Tainer J.A.,
RA Krohan H.E.;
RT "Excision of cytosine and thymine from DNA by mutants of human uracil-DNA
RT glycosylase.";
RL EMBO J. 15:3442-3447(1996).
RN [10]
RP INTERACTION WITH HIV-1 VPR (MICROBIAL INFECTION).
RX PubMed=8551605; DOI=10.1128/jvi.70.2.697-704.1996;
RA Bouhamdan M., Benichou S., Rey F., Navarro J.-M., Agostini I., Spire B.,
RA Camonis J., Slupphaug G., Vigne R., Benarous R., Sire J.;
RT "Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA
RT glycosylase DNA repair enzyme.";
RL J. Virol. 70:697-704(1996).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=9753728; DOI=10.1093/nar/26.20.4611;
RA Otterlei M., Haug T., Nagelhus T.A., Slupphaug G., Lindmo T., Krokan H.E.;
RT "Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase
RT contain a complex nuclear localisation signal and a strong classical
RT mitochondrial localisation signal, respectively.";
RL Nucleic Acids Res. 26:4611-4617(1998).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [13]
RP INTERACTION WITH FAM72A.
RX PubMed=18676834; DOI=10.1158/0008-5472.can-08-1259;
RA Guo C., Zhang X., Fink S.P., Platzer P., Wilson K., Willson J.K., Wang Z.,
RA Markowitz S.D.;
RT "Ugene, a newly identified protein that is commonly overexpressed in cancer
RT and binds uracil DNA glycosylase.";
RL Cancer Res. 68:6118-6126(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-14; SER-23; THR-60
RP AND SER-64, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-23; THR-60 AND
RP SER-64, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-295, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-14; SER-23 AND
RP THR-60, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND THR-60, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-14; SER-23; THR-60
RP AND SER-64, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=7697717; DOI=10.1016/0092-8674(95)90290-2;
RA Mol C.D., Arvai A.S., Slupphaug G., Kavli B., Alseth I., Krohan H.E.,
RA Tainer J.A.;
RT "Crystal structure and mutational analysis of human uracil-DNA glycosylase:
RT structural basis for specificity and catalysis.";
RL Cell 80:869-878(1995).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=7671300; DOI=10.1016/0092-8674(95)90467-0;
RA Mol C.D., Arvai A.S., Sanderson R.J., Slupphaug G., Kavli B., Krokan H.E.,
RA Mosbaugh D.W., Tainer J.A.;
RT "Crystal structure of human uracil-DNA glycosylase in complex with a
RT protein inhibitor: protein mimicry of DNA.";
RL Cell 82:701-708(1995).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=8900285; DOI=10.1038/384087a0;
RA Slupphaug G., Mol C.D., Kavli B., Arvai A.S., Krohan H.E., Tainer J.A.;
RT "A nucleotide-flipping mechanism from the structure of human uracil-DNA
RT glycosylase bound to DNA.";
RL Nature 384:87-92(1996).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 94-313.
RX PubMed=9724657; DOI=10.1093/emboj/17.17.5214;
RA Parikh S.S., Mol C.D., Slupphaug G., Bharati S., Krokan H.E., Tainer J.A.;
RT "Base excision repair initiation revealed by crystal structures and binding
RT kinetics of human uracil-DNA glycosylase with DNA.";
RL EMBO J. 17:5214-5226(1998).
RN [26]
RP VARIANT HIGM5 SER-251.
RX PubMed=12958596; DOI=10.1038/ni974;
RA Imai K., Slupphaug G., Lee W.-I., Revy P., Nonoyama S., Catalan N., Yel L.,
RA Forveille M., Kavli B., Krokan H.E., Ochs H.D., Fischer A., Durandy A.;
RT "Human uracil-DNA glycosylase deficiency associated with profoundly
RT impaired immunoglobulin class-switch recombination.";
RL Nat. Immunol. 4:1023-1028(2003).
RN [27]
RP CHARACTERIZATION OF VARIANT HIGM5 SER-251.
RX PubMed=15967827; DOI=10.1084/jem.20050042;
RA Kavli B., Andersen S., Otterlei M., Liabakk N.B., Imai K., Fischer A.,
RA Durandy A., Krokan H.E., Slupphaug G.;
RT "B cells from hyper-IgM patients carrying UNG mutations lack ability to
RT remove uracil from ssDNA and have elevated genomic uracil.";
RL J. Exp. Med. 201:2011-2021(2005).
CC -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC result of misincorporation of dUMP residues by DNA polymerase or due to
CC deamination of cytosine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03166};
CC -!- SUBUNIT: Monomer. Interacts with FAM72A. {ECO:0000255|HAMAP-
CC Rule:MF_03166, ECO:0000269|PubMed:18676834}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Vpr.
CC {ECO:0000269|PubMed:8551605}.
CC -!- INTERACTION:
CC P13051; P15927: RPA2; NbExp=6; IntAct=EBI-1025947, EBI-621404;
CC P13051-2; P61158: ACTR3; NbExp=3; IntAct=EBI-25834258, EBI-351428;
CC P13051-2; P05067: APP; NbExp=3; IntAct=EBI-25834258, EBI-77613;
CC P13051-2; P54252: ATXN3; NbExp=3; IntAct=EBI-25834258, EBI-946046;
CC P13051-2; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-25834258, EBI-1383687;
CC P13051-2; Q14790: CASP8; NbExp=3; IntAct=EBI-25834258, EBI-78060;
CC P13051-2; P16671: CD36; NbExp=3; IntAct=EBI-25834258, EBI-2808214;
CC P13051-2; P25685: DNAJB1; NbExp=3; IntAct=EBI-25834258, EBI-357034;
CC P13051-2; Q969H0-2: FBXW7; NbExp=3; IntAct=EBI-25834258, EBI-359594;
CC P13051-2; P06241: FYN; NbExp=3; IntAct=EBI-25834258, EBI-515315;
CC P13051-2; P27361: MAPK3; NbExp=3; IntAct=EBI-25834258, EBI-73995;
CC P13051-2; Q13765: NACA; NbExp=3; IntAct=EBI-25834258, EBI-712216;
CC P13051-2; O14939: PLD2; NbExp=3; IntAct=EBI-25834258, EBI-1053996;
CC P13051-2; P17252: PRKCA; NbExp=3; IntAct=EBI-25834258, EBI-1383528;
CC P13051-2; Q14257: RCN2; NbExp=3; IntAct=EBI-25834258, EBI-356710;
CC P13051-2; P23443: RPS6KB1; NbExp=3; IntAct=EBI-25834258, EBI-1775921;
CC P13051-2; P04271: S100B; NbExp=3; IntAct=EBI-25834258, EBI-458391;
CC P13051-2; Q15545: TAF7; NbExp=3; IntAct=EBI-25834258, EBI-1560194;
CC P13051-2; P61812: TGFB2; NbExp=3; IntAct=EBI-25834258, EBI-779581;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=UNG2;
CC IsoId=P13051-1; Sequence=Displayed;
CC Name=1; Synonyms=UNG1;
CC IsoId=P13051-2; Sequence=VSP_008513;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed with the highest
CC expression in skeletal muscle, heart and testicles. Isoform 2 has the
CC highest expression levels in tissues containing proliferating cells.
CC -!- PTM: Isoform 1 is processed by cleavage of a transit peptide.
CC -!- DISEASE: Immunodeficiency with hyper-IgM 5 (HIGM5) [MIM:608106]: A rare
CC immunodeficiency syndrome characterized by normal or elevated serum IgM
CC levels with absence of IgG, IgA, and IgE. It results in a profound
CC susceptibility to bacterial infections. {ECO:0000269|PubMed:12958596,
CC ECO:0000269|PubMed:15967827}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000255|HAMAP-Rule:MF_03166}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ung/";
CC -!- WEB RESOURCE: Name=UNGbase; Note=UNG mutation db;
CC URL="http://structure.bmc.lu.se/idbase/UNGbase/";
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; X15653; CAA33679.1; -; mRNA.
DR EMBL; X89398; CAA61578.1; -; Genomic_DNA.
DR EMBL; X89398; CAA61579.1; -; Genomic_DNA.
DR EMBL; Y09008; CAA70211.1; -; mRNA.
DR EMBL; AF526277; AAM77695.1; -; Genomic_DNA.
DR EMBL; AK291341; BAF84030.1; -; mRNA.
DR EMBL; AK313552; BAG36328.1; -; mRNA.
DR EMBL; CH471054; EAW97846.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW97847.1; -; Genomic_DNA.
DR EMBL; BC015205; AAH15205.1; -; mRNA.
DR EMBL; BC050634; AAH50634.1; -; mRNA.
DR CCDS; CCDS9124.1; -. [P13051-1]
DR CCDS; CCDS9125.1; -. [P13051-2]
DR PIR; S05964; A60472.
DR RefSeq; NP_003353.1; NM_003362.3. [P13051-2]
DR RefSeq; NP_550433.1; NM_080911.2. [P13051-1]
DR PDB; 1AKZ; X-ray; 1.57 A; A=94-313.
DR PDB; 1DPU; NMR; -; B=73-88.
DR PDB; 1EMH; X-ray; 1.80 A; A=94-313.
DR PDB; 1EMJ; X-ray; 2.00 A; A=94-313.
DR PDB; 1Q3F; X-ray; 1.90 A; A=94-313.
DR PDB; 1SSP; X-ray; 1.90 A; E=94-313.
DR PDB; 1UGH; X-ray; 1.90 A; E=94-313.
DR PDB; 1YUO; X-ray; 1.95 A; A=91-313.
DR PDB; 2HXM; X-ray; 1.30 A; A=94-313.
DR PDB; 2OXM; X-ray; 2.50 A; A=94-313.
DR PDB; 2OYT; X-ray; 2.00 A; A=94-313.
DR PDB; 2SSP; X-ray; 2.25 A; E=94-313.
DR PDB; 3FCF; X-ray; 1.84 A; A=94-313.
DR PDB; 3FCI; X-ray; 1.27 A; A=94-313.
DR PDB; 3FCK; X-ray; 1.64 A; B=94-313.
DR PDB; 3FCL; X-ray; 1.70 A; A/B=94-313.
DR PDB; 3TKB; X-ray; 1.50 A; A=94-313.
DR PDB; 4SKN; X-ray; 2.90 A; E=94-313.
DR PDB; 5AYR; X-ray; 2.40 A; A/C=94-313.
DR PDB; 5JK7; X-ray; 3.49 A; D/G=94-313.
DR PDB; 6VBA; X-ray; 1.80 A; A=94-313.
DR PDBsum; 1AKZ; -.
DR PDBsum; 1DPU; -.
DR PDBsum; 1EMH; -.
DR PDBsum; 1EMJ; -.
DR PDBsum; 1Q3F; -.
DR PDBsum; 1SSP; -.
DR PDBsum; 1UGH; -.
DR PDBsum; 1YUO; -.
DR PDBsum; 2HXM; -.
DR PDBsum; 2OXM; -.
DR PDBsum; 2OYT; -.
DR PDBsum; 2SSP; -.
DR PDBsum; 3FCF; -.
DR PDBsum; 3FCI; -.
DR PDBsum; 3FCK; -.
DR PDBsum; 3FCL; -.
DR PDBsum; 3TKB; -.
DR PDBsum; 4SKN; -.
DR PDBsum; 5AYR; -.
DR PDBsum; 5JK7; -.
DR PDBsum; 6VBA; -.
DR AlphaFoldDB; P13051; -.
DR SMR; P13051; -.
DR BioGRID; 113220; 31.
DR DIP; DIP-24194N; -.
DR ELM; P13051; -.
DR IntAct; P13051; 34.
DR MINT; P13051; -.
DR STRING; 9606.ENSP00000242576; -.
DR BindingDB; P13051; -.
DR ChEMBL; CHEMBL3277; -.
DR DrugBank; DB07116; 1-(2-DEOXY-5-O-PHOSPHONO-BETA-D-ERYTHRO-PENTOFURANOSYL)-4-METHYL-1H-INDOLE.
DR DrugBank; DB07760; 3-[(1E,7E)-8-(2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-3,6-dioxa-2,7-diazaocta-1,7-dien-1-yl]benzoic acid.
DR DrugBank; DB06990; 4-[(1E,7E)-8-(2,6-DIOXO-1,2,3,6-TETRAHYDROPYRIMIDIN-4-YL)-3,6-DIOXA-2,7-DIAZAOCTA-1,7-DIEN-1-YL]BENZOIC ACID.
DR iPTMnet; P13051; -.
DR PhosphoSitePlus; P13051; -.
DR BioMuta; UNG; -.
DR DMDM; 37999897; -.
DR EPD; P13051; -.
DR jPOST; P13051; -.
DR MassIVE; P13051; -.
DR MaxQB; P13051; -.
DR PaxDb; P13051; -.
DR PeptideAtlas; P13051; -.
DR PRIDE; P13051; -.
DR ProteomicsDB; 52891; -. [P13051-1]
DR ProteomicsDB; 52892; -. [P13051-2]
DR Antibodypedia; 3173; 553 antibodies from 35 providers.
DR DNASU; 7374; -.
DR Ensembl; ENST00000242576.7; ENSP00000242576.3; ENSG00000076248.11. [P13051-1]
DR Ensembl; ENST00000336865.6; ENSP00000337398.2; ENSG00000076248.11. [P13051-2]
DR GeneID; 7374; -.
DR KEGG; hsa:7374; -.
DR MANE-Select; ENST00000242576.7; ENSP00000242576.3; NM_080911.3; NP_550433.1.
DR UCSC; uc001tnz.3; human. [P13051-1]
DR CTD; 7374; -.
DR DisGeNET; 7374; -.
DR GeneCards; UNG; -.
DR HGNC; HGNC:12572; UNG.
DR HPA; ENSG00000076248; Low tissue specificity.
DR MalaCards; UNG; -.
DR MIM; 191525; gene.
DR MIM; 608106; phenotype.
DR neXtProt; NX_P13051; -.
DR OpenTargets; ENSG00000076248; -.
DR Orphanet; 101092; Hyper-IgM syndrome type 5.
DR PharmGKB; PA364; -.
DR VEuPathDB; HostDB:ENSG00000076248; -.
DR eggNOG; KOG2994; Eukaryota.
DR GeneTree; ENSGT00390000003405; -.
DR HOGENOM; CLU_032162_2_1_1; -.
DR InParanoid; P13051; -.
DR OMA; PDNGYLM; -.
DR OrthoDB; 1132313at2759; -.
DR PhylomeDB; P13051; -.
DR TreeFam; TF315028; -.
DR BRENDA; 3.2.2.27; 2681.
DR PathwayCommons; P13051; -.
DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine. [P13051-1]
DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine. [P13051-1]
DR Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1. [P13051-1]
DR SABIO-RK; P13051; -.
DR SignaLink; P13051; -.
DR SIGNOR; P13051; -.
DR BioGRID-ORCS; 7374; 15 hits in 1085 CRISPR screens.
DR ChiTaRS; UNG; human.
DR EvolutionaryTrace; P13051; -.
DR GeneWiki; Uracil-DNA_glycosylase; -.
DR GenomeRNAi; 7374; -.
DR Pharos; P13051; Tbio.
DR PRO; PR:P13051; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P13051; protein.
DR Bgee; ENSG00000076248; Expressed in secondary oocyte and 210 other tissues.
DR ExpressionAtlas; P13051; baseline and differential.
DR Genevisible; P13051; HS.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HGNC.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0043024; F:ribosomal small subunit binding; IPI:UniProtKB.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:HGNC.
DR GO; GO:0006284; P:base-excision repair; IDA:HGNC.
DR GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IDA:UniProtKB.
DR GO; GO:0045008; P:depyrimidination; TAS:Reactome.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0045190; P:isotype switching; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IEA:Ensembl.
DR CDD; cd10027; UDG-F1-like; 1.
DR Gene3D; 3.40.470.10; -; 1.
DR HAMAP; MF_00148; UDG; 1.
DR InterPro; IPR002043; UDG_fam1.
DR InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR PANTHER; PTHR11264; PTHR11264; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
DR TIGRFAMs; TIGR00628; ung; 1.
DR PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Disease variant; DNA damage; DNA repair; Host-virus interaction; Hydrolase;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..313
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176173"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..25
FT /note="FAM72A-binding"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03166"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 60
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 295
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..44
FT /note="MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESGDAA -> MGVF
FT CLGPWGLGRKLRTPGKGPLQLLSRLCGDHLQ (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2555154"
FT /id="VSP_008513"
FT VARIANT 4
FT /note="Q -> R (in dbSNP:rs7488798)"
FT /id="VAR_052697"
FT VARIANT 251
FT /note="F -> S (in HIGM5; fully active and stable when
FT expressed in E.coli; mistargeted to mitochondria rather
FT than the nucleus; dbSNP:rs104894380)"
FT /evidence="ECO:0000269|PubMed:12958596,
FT ECO:0000269|PubMed:15967827"
FT /id="VAR_017094"
FT MUTAGEN 154
FT /note="D->E,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8670846"
FT MUTAGEN 156
FT /note="Y->A,C,S: Thymine-DNA glycosylase activity."
FT /evidence="ECO:0000269|PubMed:8670846"
FT MUTAGEN 213
FT /note="N->D: Cytosine-DNA glycosylase activity."
FT /evidence="ECO:0000269|PubMed:8670846"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:1DPU"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:3FCI"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3FCI"
FT HELIX 109..124
FT /evidence="ECO:0007829|PDB:3FCI"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3FCI"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3FCI"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3FCI"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1EMH"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3FCI"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:3FCI"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:3FCI"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3FCK"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:3FCI"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:3TKB"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:3FCI"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:3FCI"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:3FCI"
FT TURN 223..228
FT /evidence="ECO:0007829|PDB:3FCI"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:3FCI"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:3FCI"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:3FCI"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:3FCI"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:3FCI"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:3FCI"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:3FCI"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:3FCI"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:3FCI"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:3FCI"
FT TURN 310..313
FT /evidence="ECO:0007829|PDB:5AYR"
SQ SEQUENCE 313 AA; 34645 MW; A4B27E6198AFE9C0 CRC64;
MIGQKTLYSF FSPSPARKRH APSPEPAVQG TGVAGVPEES GDAAAIPAKK APAGQEEPGT
PPSSPLSAEQ LDRIQRNKAA ALLRLAARNV PVGFGESWKK HLSGEFGKPY FIKLMGFVAE
ERKHYTVYPP PHQVFTWTQM CDIKDVKVVI LGQDPYHGPN QAHGLCFSVQ RPVPPPPSLE
NIYKELSTDI EDFVHPGHGD LSGWAKQGVL LLNAVLTVRA HQANSHKERG WEQFTDAVVS
WLNQNSNGLV FLLWGSYAQK KGSAIDRKRH HVLQTAHPSP LSVYRGFFGC RHFSKTNELL
QKSGKKPIDW KEL
