ID   Q6FHS8_HUMAN            Unreviewed;       304 AA.
AC   Q6FHS8;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Uracil-DNA glycosylase {ECO:0000256|HAMAP-Rule:MF_03166, ECO:0000256|RuleBase:RU003780};
DE            Short=UDG {ECO:0000256|HAMAP-Rule:MF_03166};
DE            EC=3.2.2.27 {ECO:0000256|HAMAP-Rule:MF_03166, ECO:0000256|RuleBase:RU003780};
GN   Name=UNG {ECO:0000256|HAMAP-Rule:MF_03166,
GN   ECO:0000313|EMBL:CAG46474.1};
GN   Synonyms=UNG1 {ECO:0000256|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 {ECO:0000313|EMBL:CAG46474.1};
RN   [1] {ECO:0000313|EMBL:CAG46474.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_03166,
CC       ECO:0000256|RuleBase:RU003780}.
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:0000256|HAMAP-Rule:MF_03166,
CC         ECO:0000256|RuleBase:RU003780};
CC   -!- SUBUNIT: Monomer. Interacts with FAM72A. {ECO:0000256|HAMAP-
CC       Rule:MF_03166}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03166}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000256|ARBA:ARBA00008184, ECO:0000256|HAMAP-
CC       Rule:MF_03166, ECO:0000256|RuleBase:RU003780}.
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DR   EMBL; CR541673; CAG46474.1; -; mRNA.
DR   AlphaFoldDB; Q6FHS8; -.
DR   SMR; Q6FHS8; -.
DR   PeptideAtlas; Q6FHS8; -.
DR   ChiTaRS; UNG; human.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR   CDD; cd10027; UDG-F1-like; 1.
DR   Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 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   NCBIfam; TIGR00628; ung; 1.
DR   PANTHER; PTHR11264; URACIL-DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR11264:SF0; URACIL-DNA GLYCOSYLASE; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SMART; SM00987; UreE_C; 1.
DR   SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   2: Evidence at transcript level;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_03166};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_03166};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03166};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03166}.
FT   DOMAIN          130..291
FT                   /note="Uracil-DNA glycosylase-like"
FT                   /evidence="ECO:0000259|SMART:SM00986"
FT   REGION          40..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        145
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03166,
FT                   ECO:0000256|PROSITE-ProRule:PRU10072"
SQ   SEQUENCE   304 AA;  33926 MW;  059A296F611A87C7 CRC64;
     MGVFCLGPWG SGRKLRTPGK GPLQLLSRLC GDHLQAIPAK KAPAGQEEPG TPPSSPLSAE
     QLDRIQRNKA AALLRLAARN VPVGFGESWK KHLSGEFGKP YFIKLMGFVV EERKHYTVYP
     PPHQVFTWTQ MCDIKDVKVV ILGQDPYHGP NQAHGLCFSV QRPVPPPPSL ENIYKELSTD
     IEDFVHPGHG DLSGWAKQGV LLLNAVLTVR AHQANSHKER GWEQFTDAVV SWLNQNSNGL
     VFLLWGSYAQ KKGSAIDRKR HHVLQTAHPS PLSVYRGFFG CRHFSKTNEL LQKSGKKPID
     WKEL
//