Selected-GenAtlas references SOURCE GeneCards NCBI Gene Swiss-Prot Ensembl
HGNC UniGene Nucleotide OMIM UCSC
Home Page
Symbol APOBEC3G contributors: mct/pgu - updated : 15-02-2015
HGNC name apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G
HGNC id 17357
Location 22q13.1      Physical location : 39.473.009 - 39.483.747
Synonym name
  • phorbolin-like protein MDS019
  • APOBEC-related cytidine deaminase
  • DNA dC->dU editing enzyme
  • phorbolin-like protein MDS019
  • Synonym symbol(s) ARP9, CEM15, MDS019, FLJ12740, A3G, bK150C2.7, dJ494G10.1, ARCD
    EC.number 3.5.4.-
    TYPE functioning gene
    SPECIAL FEATURE arranged in tandem, component of a cluster
    text one of seven related genes or pseudogenes found in a cluster
    STRUCTURE 10.72 kb     8 Exon(s)
    10 Kb 5' upstream gene genomic sequence study
    regulatory sequence Promoter
    Binding site   transcription factor
    text structure
  • a GC-box mediates transcriptional activity of the 180 bp core promoter
  • Sp1 and Sp3 bind to the GC-box present in the promoter
  • controlled by a promoter with multiple transcriptional start sites
  • TATA-less core promoter with an NFATC1, NFATC2/IRF4 composite binding site that confers cell type-specific transcriptional regulation
  • MAPPING cloned Y linked N status provisional
    Physical map
    DNAL4 22q13.1 dynein, axonemal, light polypeptide 4 LOC388901 22 LOC388901 NPTXR 22q13.1 neuronal pentraxin receptor CBX6 22q13.1 chromobox homolog 6 APOBEC3A 22q13.1-q13.2 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3A APOBEC3B 22q12-q13 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3B APOBEC3C 22q12-q13 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C APOBEC3D 22q12-q13 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3D APOBEC3E 22q12-q13 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3E pseudogene APOBEC3F 22q12-q13 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3F APOBEC3G 22q12-q13 apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G ARP10 22q13.1 ARP10 protein COX5BL7 22pter-p13 cytochrome c oxidase subunit Vb-like 7 CBX7 22q13.1 chromobox homolog 7 LOC391332 22 similar to hepatitis C virus core-binding protein 6; cervical cancer oncogene 3 FLJ23865 22q13.1 hypothetical protein FLJ23865 PDGFB 22q13.1 platelet-derived growth factor beta polypeptide (simian sarcoma viral (v-sis) oncogene homolog) RPL3 22q13.1 ribosomal protein L3 SYNGR1 22q13.1 synaptogyrin 1
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    8 - 1848 - 384 - 2009 19389408
    6 - - 38 - - 2010 20624919
    lacking exon 2
    4 - - 10 - - 2010 20624919
    5 - - 23 - - 2010 20624919
    Type widely
       expressed in (based on citations)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Endocrineadrenal gland   highly
    Lymphoid/Immunelymph node   highly
     spleen   highly
     tonsils   highly
    Reproductivefemale systemovary   
     male systemtestis   
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Blood / hematopoieticbone marrow  highly
    SystemCellPubmedSpeciesStageRna symbol
    Lymphoid/ImmuneT cell Homo sapiens
    Reproductivegerm cell
    cell lineage
    cell lines colorectal adenocarcinoma cells and Burkitt lymphoma cells
    at STAGE
    physiological period embryo
    Text early embryo
  • N-terminal domains which were unable to multimerize but remained functional for Gag and viral infectivity factor (Vif) interactions when expressed apart from the C terminus , domain that interacts with the Vif YRHHY region is located between AAs 126 and 132
  • a zinc-binding domain and the glutamate involved in proton shuttling found in the active site of all cytidine deaminases
  • two critical aromatic residues involved in RNA binding
  • two cytidine deaminase domains (CDD) (both active sites are required for antiviral function but serve separate functions)
  • a 37-AAs linker peptide connecting the active site and pseudoactive site domains of E. coli cytidine deaminase
  • AAs 198-384 are sufficient for DNA deamination but are similarly insoluble
  • a ZDD domain of the C terminus, involved in the homoligomerization (forms RNA-independent oligomers through interactions within its C terminus)
  • dual conserved catalytic domains located in the N- and C-terminal regions termed CD1 and CD2, respectively
  • N-terminal and C-terminal ZDD required for nucleic acid-dependent higher-order oligomerization as well as many other interactions necessary for antiviral activity
  • secondary structure a helix-strand-helix supersecondary structure containing conserved residues (His/Cys)-Xaa-Glu-Xaa2530Pro-Cys-Xaa-Xaa-Cys that are integral to the function of the zinc-dependent deaminase domain
    mono polymer homomer , dimer , oligo
  • cytidine and deoxycytidylate deaminase family
  • membre of the APOBEC family of nucleic-acid editing enzymes
  • CATEGORY enzyme , RNA associated
    SUBCELLULAR LOCALIZATION     intracellular
  • strongly retained in the cytoplasm through a mechanism that involves both the N and C-terminal regions of the protein
  • both APOBEC3G and MOV10 have been found to co-localize with AGO1 and AGO2 in P-bodies and stress granules
  • MOV10 and APOBEC3G (A3G) localize to cytoplasmic granules called processing bodies (P bodies)
  • basic FUNCTION
  • cytidine deaminase that catalyzes the deamination of cytidine to uridine in the context of single-stranded (ss) DNA, activity that is critical to its function as a host defense factor against HIV infection
  • endogenous inhibitor of HIV-1 replication, acting as a cytidine deaminase and able to induce G-to-A hypermutation in newly synthesized viral DNA
  • functioning as a natural defense against endogenous retrotransposons and a multitude of retroviruses, most notably human immunodeficiency virus type 1 (HIV-1)
  • antiretroviral deoxycytidine deaminase, broad antiviral enzyme
  • inhibiting retrotransposition of IAP and MusD elements
  • cellular restriction factor that is responsible for inhibition of virion infectivity factor (Vif)-deleted human immunodeficiency virus-1 (HIV-1) replication in non-permissive cells
  • mediates intrinsic resistance of monocyte-derived dendritic cells to HIV-1 infection
  • restrict retroviral infection by deaminating cytosine residues in the first cDNA strand of a replicating virus
  • deaminates cytidines to uridines in single-strand DNA and inhibits the replication of human immunodeficiency virus-1, other retroviruses, and retrotransposons
  • capable of associating with different species of viral structural proteins through a potentially common, RNA-mediated mechanism
  • having intracellular expression and regulation in the neuronal cells, which may be one of innate defense mechanisms involved in the neuronal protection in the CNS
  • APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms
  • have strong antiviral activity and together with APOBEC3F, it is considered the most potent cytidine deaminase targeting HIV
  • cytidine deaminase whose expression has been implicated in host defense and conditionally in viral resistance
  • catalyzes deamination of deoxycytidine (dC) on single-stranded DNA (ssDNA)
  • APOBEC3F and APOBEC3G are the most potent inhibitors of HIV-1, but only in the absence of the virus-encoded protein, Vif
  • antiretroviral activity of cellular proteins APOBEC3F and APOBEC3G requires their inclusion within HIV-1 virions
  • APOBEC3F (A3F) and APOBEC3G (A3G) inhibit human immunodeficiency virus type-1 (HIV-1) replication
  • unlike APOBEC3G, signals in N- and C-terminal deaminase domains of APOBEC3F each contribute to virion encapsidation
  • potent restrictive factor for human immunodeficiency virus type 1 (HIV-1) and many other retroviruses
  • MOV10 and APOBEC3G localization to processing bodies is not required for virion incorporation and antiviral activity
  • APOBEC3F, APOBEC3G are host factors that incorporate into virions and restrict virus replication
  • cellular cytidine deaminase that restricts HIV-1 replication by inducing G-to-A hypermutation in viral DNA and by deamination-independent mechanisms
  • APOBEC3F and APOBEC3G are two of the most potent A3 enzymes in humans with each having a different target DNA specificity: A3G prefers to deaminate cytosines preceded by a cytosine (5'-CC), whereas A3F preferentially targets cytosines preceded by a thymine (5'-TC)
  • cellular cytidine deaminase APOBEC3G (A3G) was first described as an anti-HIV-1 restriction factor, acting by directly deaminating reverse transcripts of the viral genome
  • APOBEC3 proteins function within the innate immune system by mutating DNA of viral genomes and retroelements to restrict infection and retrotransposition
    a component
    small molecule
  • with Vif protein of lentiviruses (to induce its degradation by proteasomes)
  • conserved motif VxIPLx(4-5)LxPhix(2)YWxL motif in HIV-1 Vif required for APOBEC3G and APOBEC3F interaction and inhibition
  • interacting with NGF (NGF reduced the synthesis of the cellular HIV-1 restriction factor APOBEC3G and also overrode its IFNG-induced up-regulation)
  • binds to a domain at the C terminus in MOV10, where it competitively inhibits the binding of AGO2 to that same domain
  • HIV-1 Vif binds to APOBEC3G, resulting in its degradation via the 26 S proteasome
  • cell & other
    inhibited by HIV Vif protein which promoting proteasomal degradation of APOBEC3G
    Other controlled by the PKCalpha/betaI/MEK/ERK protein kinase cascade in human T lymphocytes
    its expression is critically dependent on NFATC1/NFATC2 and IRF4 (when either NFATC1 or NFATC2 and IRF4 were co-expressed, APOBEC3G promoter activity was observed in cells that normally lack APOBEC3G expression
    phosphorylation of a conserved threonine attenuates the intrinsic activity of APOBEC3G (Thr-218)
    corresponding disease(s)
    Variant & Polymorphism
    Candidate gene
    Therapy target
    promising target for future HIV/AIDS therapies