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UNG uracil-DNA glycosylase [ Homo sapiens (human) ]

Gene ID: 7374, updated on 11-Sep-2014
Official Symbol
UNGprovided by HGNC
Official Full Name
uracil-DNA glycosylaseprovided by HGNC
Primary source
HGNC:HGNC:12572
See related
Ensembl:ENSG00000076248; HPRD:01881; MIM:191525; Vega:OTTHUMG00000169247
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
DGU; UDG; UNG1; UNG2; HIGM4; HIGM5; UNG15
Summary
This gene encodes one of several uracil-DNA glycosylases. One important function of uracil-DNA glycosylases is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil bases occur from cytosine deamination or misincorporation of dUMP residues. Alternative promoter usage and splicing of this gene leads to two different isoforms: the mitochondrial UNG1 and the nuclear UNG2. The UNG2 term was used as a previous symbol for the CCNO gene (GeneID 10309), which has been confused with this gene, in the literature and some databases. [provided by RefSeq, Nov 2010]
Annotation information
Note: Due to a common symbol (UNG2) for the specific nuclear isoform of the UNG gene (GeneID 7374) and as a previous symbol for the CCNO gene (GeneID 10309), incorrect attributions of uracil DNA glycosylase activity have been made for CCNO in the scientific literature and some databases. CCNO was correctly identified as a cyclin protein family member in PubMed ID: 8419333. [13 Feb 2013]
Location:
12q23-q24.1
Exon count:
7
Annotation release Status Assembly Chr Location
106 current GRCh38 (GCF_000001405.26) 12 NC_000012.12 (109097594..109110993)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 12 NC_000012.11 (109535399..109548798)

Chromosome 12 - NC_000012.12Genomic Context describing neighboring genes Neighboring gene RNA, 5S ribosomal pseudogene 372 Neighboring gene ubiquitin specific peptidase 30 Neighboring gene alkB, alkylation repair homolog 2 (E. coli) Neighboring gene acetyl-CoA carboxylase beta Neighboring gene forkhead box N4

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Replication interactions

Interaction Pubs
Depletion of UNG2 by shRNA in HIV-1-producing 293T cells inhibits viral infectivity and replication PubMed

Protein interactions

Protein Gene Interaction Pubs
Tat tat The antiviral activity of UNG2 requires the integrity of its catalytic domain (residues 153 and 154). Depletion of endogenous UMG2 promotes Tat-mediated LTR transcription PubMed
Vpr vpr High levels of HIV-1 Vpr expression leads to the accumulation of phosphorylated UNG2 and the redistribution of UNG2 into the cell nucleus PubMed
vpr HIV-1-Vpr induced upregulation of NKG2D ligands in HIV-infected T cells by activating UNG2-dependent repair of uridine-containing DNA PubMed
vpr W54R/S79A Vpr mutant impairs interaction with UNG2, but is still able to recruit DCAF1 PubMed
vpr Downregulation of UNG2 by Vpr is related to a transcriptional regulation and is independent of Vpr binding, Vpr-induced G2 arrest, and the proteasome degradation PubMed
vpr In a yeast two-hybrid assay, tryptophan in position 54 of HIV-1 Vpr is critical for maintaining the interaction of Vpr with UNG2, and the WXXF motif (residues 231-234) of UNG2 is involved in this binding to Vpr PubMed
vpr The interaction of HIV-1 Vpr with UNG2 leads to virion incorporation of catalytically active UNG2, which is directly involved with Vpr in modulating the HIV-1 mutation rate PubMed
vpr HIV-1 Vpr-induced reduction in uracil DNA glycosylase (UNG) is mediated through proteasomal degradation PubMed
vpr HIV-1 Vpr induces the ubiquitination of UNG and forms a complex with UNG PubMed
vpr Expression of exogenous HIV-1 Vpr inhibits class switch recombination (CSR) by competing with some endogenous factors for the WXXF site (residues 222-225) of uracil-DNA glycosylase PubMed
vpr DCAF1 interacts with DDB1 as well as the Vpr-UNG2 complex, which leads to polyubiquitination of UNG2 via Vpr PubMed
vpr One report indicates incorporation of uracil DNA glycosylase (UNG) into HIV-1 virions is mediated by binding of HIV-1 Vpr to UNG, however another indicates virion incorporation of UNG is independent of Vpr and is mediated by the HIV-1 Integrase protein PubMed
vpr HIV-1 Vpr (amino acids 15-77) binds to the uracil DNA glycosylase DNA repair enzyme (amino acids 222-225) and thereby modulates the HIV-1 mutation rate PubMed
integrase gag-pol HIV-1 L172A/K173A mutant virus is deficient for Uracil DNA Glycosylase (UNG2) incorporation into virions and is defective for replication due to a blockage at the stage of proviral DNA integration PubMed
gag-pol Uracil DNA Glycosylase (UNG2; amino acids 1-51) binds to HIV-1 integrase (amino acids 170-180) and is incorporated into HIV-1 particles by binding to the integrase domain of the HIV-1 Gag-Pol polyprotein PubMed

Go to the HIV-1, Human Protein Interaction Database

  • Base excision repair, organism-specific biosystem (from KEGG)
    Base excision repair, organism-specific biosystemBase excision repair (BER) is the predominant DNA damage repair pathway for the processing of small base lesions, derived from oxidation and alkylation damages. BER is normally defined as DNA repair ...
  • Base excision repair, conserved biosystem (from KEGG)
    Base excision repair, conserved biosystemBase excision repair (BER) is the predominant DNA damage repair pathway for the processing of small base lesions, derived from oxidation and alkylation damages. BER is normally defined as DNA repair ...
  • Primary immunodeficiency, organism-specific biosystem (from KEGG)
    Primary immunodeficiency, organism-specific biosystemPrimary immunodeficiencies (PIs) are a heterogeneous group of disorders, which affect cellular and humoral immunity or non-specific host defense mechanisms mediated by complement proteins, and cells ...
  • Primary immunodeficiency, conserved biosystem (from KEGG)
    Primary immunodeficiency, conserved biosystemPrimary immunodeficiencies (PIs) are a heterogeneous group of disorders, which affect cellular and humoral immunity or non-specific host defense mechanisms mediated by complement proteins, and cells ...
Products Interactant Other Gene Complex Source Pubs Description

Markers

Homology

Clone Names

  • DKFZp781L1143

Gene Ontology Provided by GOA

Function Evidence Code Pubs
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
uracil DNA N-glycosylase activity NAS
Non-traceable Author Statement
more info
PubMed 
Process Evidence Code Pubs
DNA repair TAS
Traceable Author Statement
more info
PubMed 
base-excision repair IEA
Inferred from Electronic Annotation
more info
 
negative regulation of apoptotic process IEA
Inferred from Electronic Annotation
more info
 
somatic hypermutation of immunoglobulin genes IEA
Inferred from Electronic Annotation
more info
 
somatic recombination of immunoglobulin gene segments IEA
Inferred from Electronic Annotation
more info
 
viral process IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
mitochondrion IEA
Inferred from Electronic Annotation
more info
 
nucleus NAS
Non-traceable Author Statement
more info
PubMed 
Preferred Names
uracil-DNA glycosylase
Names
uracil-DNA glycosylase
uracil-DNA glycosylase 1, uracil-DNA glycosylase 2
NP_003353.1
NP_550433.1

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

  1. NG_007284.1 

    Range
    4985..18384
    Download
    GenBank, FASTA, Sequence Viewer (Graphics), LRG_124

mRNA and Protein(s)

  1. NM_003362.3NP_003353.1  uracil-DNA glycosylase isoform UNG1 precursor

    See proteins identical to NP_003353.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) uses the downstream promoter and a full-length exon 1B. It encodes the UNG1 isoform, which includes a mitochondrial targeting sequence.
    Source sequence(s)
    AC007637, BM928006, BU622689, DB045515
    Consensus CDS
    CCDS9125.1
    UniProtKB/TrEMBL
    E5KTA6
    UniProtKB/Swiss-Prot
    P13051
    Related
    ENSP00000337398, OTTHUMP00000240528, ENST00000336865, OTTHUMT00000403069
    Conserved Domains (1) summary
    cd10027
    Location:100301
    Blast Score: 953
    UDG_F1; Family 1 of Uracil-DNA glycosylase (UDG) enzymes
  2. NM_080911.2NP_550433.1  uracil-DNA glycosylase isoform UNG2

    See proteins identical to NP_550433.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) uses an upstream promoter and an alternate splice site for exon 1B when compared to variant 1. It encodes the nuclear UNG2 isoform, which has a different N-terminal sequence than the UNG1 isoform.
    Source sequence(s)
    BQ950839, BU622689, Y09008
    Consensus CDS
    CCDS9124.1
    UniProtKB/TrEMBL
    E5KTA5
    UniProtKB/Swiss-Prot
    P13051
    Related
    ENSP00000242576, OTTHUMP00000240527, ENST00000242576, OTTHUMT00000403067
    Conserved Domains (1) summary
    cd10027
    Location:109310
    Blast Score: 957
    UDG_F1; Family 1 of Uracil-DNA glycosylase (UDG) enzymes

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 106

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38 Primary Assembly

Genomic

  1. NC_000012.12 

    Range
    109097594..109110993
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

  1. AC_000144.1 

    Range
    106553817..106567575
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate CHM1_1.1

Genomic

  1. NC_018923.2 

    Range
    109503049..109516448
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)