UNG_MOUSE
ID UNG_MOUSE Reviewed; 306 AA.
AC P97931; P97285; P97509; Q7TPW8; Q9JIW8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 167.
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; Synonyms=Ung1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=9168124; DOI=10.1016/s0378-1119(96)00797-4;
RA Svendsen P.C., Yee H.A., Winkfein R.J., van de Sande J.H.;
RT "The mouse uracil-DNA glycosylase gene: isolation of cDNA and genomic
RT clones and mapping ung to mouse chromosome 5.";
RL Gene 189:175-181(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129/Sv;
RX PubMed=10871356; DOI=10.1093/nar/28.12.2277;
RA Nilsen H., Steinsbekk K.S., Otterlei M., Slupphaug G., Aas P.A.,
RA Krokan H.E.;
RT "Analysis of uracil-DNA glycosylases from the murine Ung gene reveals
RT differential expression in tissues and in embryonic development and a
RT subcellular sorting pattern that differs from the human homologues.";
RL Nucleic Acids Res. 28:2277-2285(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=DBA/2J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C3H/He, and Czech II; TISSUE=Mammary tumor, and Osteoblast;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
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=P97931-1; Sequence=Displayed;
CC Name=1; Synonyms=UNG1;
CC IsoId=P97931-2; Sequence=VSP_008514;
CC -!- PTM: Isoform 1 is processed by cleavage of a transit peptide.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000255|HAMAP-Rule:MF_03166}.
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DR EMBL; U55040; AAB39511.1; -; Genomic_DNA.
DR EMBL; U55041; AAC53197.1; -; mRNA.
DR EMBL; X99018; CAA67489.1; -; mRNA.
DR EMBL; Y08975; CAA70168.1; -; mRNA.
DR EMBL; AF174485; AAF76936.1; -; Genomic_DNA.
DR EMBL; AK146178; BAE26956.1; -; mRNA.
DR EMBL; CH466529; EDL19920.1; -; Genomic_DNA.
DR EMBL; BC011039; AAH11039.1; -; mRNA.
DR EMBL; BC052853; AAH52853.1; -; mRNA.
DR CCDS; CCDS19560.1; -. [P97931-2]
DR CCDS; CCDS39221.1; -. [P97931-1]
DR RefSeq; NP_001035781.1; NM_001040691.1. [P97931-1]
DR RefSeq; NP_035807.2; NM_011677.2. [P97931-2]
DR AlphaFoldDB; P97931; -.
DR SMR; P97931; -.
DR IntAct; P97931; 1.
DR STRING; 10090.ENSMUSP00000031587; -.
DR iPTMnet; P97931; -.
DR PhosphoSitePlus; P97931; -.
DR EPD; P97931; -.
DR PaxDb; P97931; -.
DR PeptideAtlas; P97931; -.
DR PRIDE; P97931; -.
DR ProteomicsDB; 297969; -. [P97931-1]
DR ProteomicsDB; 297970; -. [P97931-2]
DR Antibodypedia; 3173; 553 antibodies from 35 providers.
DR DNASU; 22256; -.
DR Ensembl; ENSMUST00000031587; ENSMUSP00000031587; ENSMUSG00000029591. [P97931-1]
DR Ensembl; ENSMUST00000102584; ENSMUSP00000099644; ENSMUSG00000029591. [P97931-2]
DR GeneID; 22256; -.
DR KEGG; mmu:22256; -.
DR UCSC; uc008yzf.1; mouse. [P97931-1]
DR CTD; 7374; -.
DR MGI; MGI:109352; Ung.
DR VEuPathDB; HostDB:ENSMUSG00000029591; -.
DR eggNOG; KOG2994; Eukaryota.
DR GeneTree; ENSGT00390000003405; -.
DR HOGENOM; CLU_032162_2_1_1; -.
DR InParanoid; P97931; -.
DR OMA; PDNGYLM; -.
DR OrthoDB; 832568at2759; -.
DR PhylomeDB; P97931; -.
DR TreeFam; TF315028; -.
DR Reactome; R-MMU-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-MMU-110357; Displacement of DNA glycosylase by APEX1.
DR BioGRID-ORCS; 22256; 5 hits in 109 CRISPR screens.
DR ChiTaRS; Ung; mouse.
DR PRO; PR:P97931; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P97931; protein.
DR Bgee; ENSMUSG00000029591; Expressed in indifferent gonad and 241 other tissues.
DR ExpressionAtlas; P97931; baseline and differential.
DR Genevisible; P97931; MM.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR GO; GO:0043024; F:ribosomal small subunit binding; ISO:MGI.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:MGI.
DR GO; GO:0006284; P:base-excision repair; ISO:MGI.
DR GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; TAS:MGI.
DR GO; GO:0045190; P:isotype switching; IGI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IMP:MGI.
DR GO; GO:0016447; P:somatic recombination of immunoglobulin gene segments; IMP:MGI.
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 Acetylation; Alternative splicing; DNA damage; DNA repair; Hydrolase;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..306
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176174"
FT REGION 11..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03166"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13051"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13051"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13051"
FT MOD_RES 288
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13051"
FT VAR_SEQ 1..41
FT /note="MIGQKTLYSFFSPTPTGKRTTRSPEPVPGSGVAAEIGGDAV -> MGVLGRR
FT SLRLARRAGLRSLTPNPDSDSRQ (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10871356,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9016624, ECO:0000303|PubMed:9168124"
FT /id="VSP_008514"
FT CONFLICT 277
FT /note="H -> Y (in Ref. 2; CAA67489/CAA70168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 33926 MW; CE2D5192936CE6EA CRC64;
MIGQKTLYSF FSPTPTGKRT TRSPEPVPGS GVAAEIGGDA VASPAKKARV EQNEQGSPLS
AEQLVRIQRN KAAALLRLAA RNVPAGFGES WKQQLCGEFG KPYFVKLMGF VAEERNHHKV
YPPPEQVFTW TQMCDIRDVK VVILGQDPYH GPNQAHGLCF SVQRPVPPPP SLENIFKELS
TDIDGFVHPG HGDLSGWARQ GVLLLNAVLT VRAHQANSHK ERGWEQFTDA VVSWLNQNLS
GLVFLLWGSY AQKKGSVIDR KRHHVLQTAH PSPLSVHRGF LGCRHFSKAN ELLQKSGKKP
INWKEL
