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    UNG uracil DNA glycosylase [ Homo sapiens (human) ]

    Gene ID: 7374, updated on 22-Apr-2017
    Official Symbol
    UNGprovided by HGNC
    Official Full Name
    uracil DNA glycosylaseprovided by HGNC
    Primary source
    HGNC:HGNC:12572
    See related
    Ensembl:ENSG00000076248 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]
    Orthologs
    Location:
    12q24.11
    Exon count:
    7
    Annotation release Status Assembly Chr Location
    108 current GRCh38.p7 (GCF_000001405.33) 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 ubiquitin specific peptidase 30 Neighboring gene RNA, 5S ribosomal pseudogene 372 Neighboring gene alkB homolog 2, alpha-ketoglutarate dependent dioxygenase Neighboring gene uncharacterized LOC105369974 Neighboring gene acetyl-CoA carboxylase beta Neighboring gene forkhead box N4

    • Project title: HPA RNA-seq normal tissues
    • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
    • BioProject: PRJEB4337
    • Publication: PMID 24309898
    • Analysis date: Wed Jun 15 11:32:44 2016

    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 HIV-1 Vpr downregulates the gene expression of UNG2 and amino-acid residues A30/V31 are critical for the Vpr-mediated downregulation of UNG2 PubMed
    vpr HIV-1 Vpr-induced reduction in uracil DNA glycosylase (UNG) is mediated through proteasomal degradation PubMed
    vpr HIV-1 Vpr complexes with DCAF1, DDB1, CUL4A, CUL4B, and UNG2 proteins in the cullin4 (CUL4)-containing ubiquitin ligase complex in HEK293T cells PubMed
    vpr Ubiquitination levels of UNG2 is upregulated in the presence of HIV-1 Vpr in the proviral backbone compared to the levels for control PubMed
    vpr The coexpression of UNG2 with a dominant negative CUL4 molecule prevents UNG2 degradation from the presence of HIV-1 Vpr PubMed
    vpr HIV-1 Vpr-mediated UNG2 degradation and constitutive UNG2 turnover are dependent on DCAF1 or DDB1 but not on CUL4a or CUL4B in the cullin4 (CUL4)-containing ubiquitin ligase complex in HEK293T cells PubMed
    vpr HIV-1 Vpr-mediated degradation of UNG2 is dependent on CUL4A neddylation PubMed
    vpr HIV-1 Vpr binding to UNG2 results in a rapid reduced level of UNG2 protein and a significant loss of uracil-DNA glycosylate activity 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 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 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 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 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 Interaction Database

    • Base Excision Repair, organism-specific biosystem (from REACTOME)
      Base Excision Repair, organism-specific biosystemOf the three major pathways involved in the repair of nucleotide damage in DNA, base excision repair (BER) involves the greatest number of individual enzymatic activities. This is the consequence of ...
    • 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 ...
    • Base-Excision Repair, AP Site Formation, organism-specific biosystem (from REACTOME)
      Base-Excision Repair, AP Site Formation, organism-specific biosystemBase excision repair is initiated by DNA glycosylases that hydrolytically cleave the base-deoxyribose glycosyl bond of a damaged nucleotide residue, releasing the damaged base (Lindahl and Wood 1999,...
    • Cleavage of the damaged pyrimidine, organism-specific biosystem (from REACTOME)
      Cleavage of the damaged pyrimidine, organism-specific biosystemDamaged pyrimidines are cleaved by pyrimide-specific glycosylases (Lindahl and Wood 1999).
    • DNA Repair, organism-specific biosystem (from REACTOME)
      DNA Repair, organism-specific biosystemDNA repair is a phenomenal multi-enzyme, multi-pathway system required to ensure the integrity of the cellular genome. Living organisms are constantly exposed to harmful metabolic by-products, enviro...
    • Depyrimidination, organism-specific biosystem (from REACTOME)
      Depyrimidination, organism-specific biosystemDepyrimidination of a damaged nucleotide in DNA is mediated by a pyrimidine-specific DNA glycosylase. The glycosylase cleaves the N-C1' glycosidic bond between the damaged DNA base and the deoxyribos...
    • Displacement of DNA glycosylase by APEX1, organism-specific biosystem (from REACTOME)
      Displacement of DNA glycosylase by APEX1, organism-specific biosystemFollowing cleavage of the damaged base, DNA glycosylase is displaced by APEX1, an AP endonuclease (Parikh et al. 1998).
    • 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 ...
    • Recognition and association of DNA glycosylase with site containing an affected pyrimidine, organism-specific biosystem (from REACTOME)
      Recognition and association of DNA glycosylase with site containing an affected pyrimidine, organism-specific biosystemBase excision repair is initiated by a DNA glycosylase which first recognizes and removes a damaged or incorrect (e.g. mismatched) base (Sokhansanj et al. 2002).
    • Resolution of Abasic Sites (AP sites), organism-specific biosystem (from REACTOME)
      Resolution of Abasic Sites (AP sites), organism-specific biosystemResolution of AP sites can occur through the single nucleotide replacement pathway or through the multiple nucleotide patch replacement pathway, also known as the long-patch base excision repair (BER...
    Products Interactant Other Gene Complex Source Pubs Description

    Markers

    Homology

    Clone Names

    • DKFZp781L1143

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    damaged DNA binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enzyme binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    uracil DNA N-glycosylase activity NAS
    Non-traceable Author Statement
    more info
    PubMed 
    uracil DNA N-glycosylase activity TAS
    Traceable Author Statement
    more info
     
    Process Evidence Code Pubs
    DNA repair TAS
    Traceable Author Statement
    more info
    PubMed 
    base-excision repair TAS
    Traceable Author Statement
    more info
    PubMed 
    base-excision repair, AP site formation via deaminated base removal IDA
    Inferred from Direct Assay
    more info
    PubMed 
    depyrimidination TAS
    Traceable Author Statement
    more info
     
    negative regulation of apoptotic process IEA
    Inferred from Electronic Annotation
    more info
     
    positive regulation of isotype switching 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
     
    nucleoplasm TAS
    Traceable Author Statement
    more info
     
    nucleus NAS
    Non-traceable Author Statement
    more info
    PubMed 
    Preferred Names
    uracil-DNA glycosylase
    Names
    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 RefSeqGene

      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 identical proteins and their annotated locations for 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/Swiss-Prot
      P13051
      UniProtKB/TrEMBL
      E5KTA6
      Related
      ENSP00000337398.2, OTTHUMP00000240528, ENST00000336865.6, OTTHUMT00000403069
      Conserved Domains (1) summary
      TIGR00628
      Location:87296
      ung; uracil-DNA glycosylase
    2. NM_080911.2NP_550433.1  uracil-DNA glycosylase isoform UNG2

      See identical proteins and their annotated locations for 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/Swiss-Prot
      P13051
      UniProtKB/TrEMBL
      E5KTA5
      Related
      ENSP00000242576.2, OTTHUMP00000240527, ENST00000242576.6, OTTHUMT00000403067
      Conserved Domains (1) summary
      TIGR00628
      Location:96305
      ung; uracil-DNA glycosylase

    RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 108 details...Open this link in a new tab

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

    Reference GRCh38.p7 Primary Assembly

    Genomic

    1. NC_000012.12 Reference GRCh38.p7 Primary Assembly

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

    Alternate CHM1_1.1

    Genomic

    1. NC_018923.2 Alternate CHM1_1.1

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