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    APOBEC3G apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3G [ Homo sapiens (human) ]

    Gene ID: 60489, updated on 24-Aug-2015
    Official Symbol
    APOBEC3Gprovided by HGNC
    Official Full Name
    apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3Gprovided by HGNC
    Primary source
    HGNC:HGNC:17357
    See related
    Ensembl:ENSG00000239713; HPRD:06172; MIM:607113; Vega:OTTHUMG00000151081
    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
    A3G; ARCD; ARP9; ARP-9; CEM15; CEM-15; MDS019; bK150C2.7; dJ494G10.1
    Summary
    This gene is a member of the cytidine deaminase gene family. It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1. It is thought that the proteins may be RNA editing enzymes and have roles in growth or cell cycle control. The protein encoded by this gene has been found to be a specific inhibitor of human immunodeficiency virus-1 (HIV-1) infectivity. [provided by RefSeq, Jul 2008]
    Orthologs
    See APOBEC3G in Epigenomics, MapViewer
    Location:
    22q13.1-q13.2
    Exon count:
    8
    Annotation release Status Assembly Chr Location
    107 current GRCh38.p2 (GCF_000001405.28) 22 NC_000022.11 (39077005..39087743)
    105 previous assembly GRCh37.p13 (GCF_000001405.25) 22 NC_000022.10 (39473010..39483748)

    Chromosome 22 - NC_000022.11Genomic Context describing neighboring genes Neighboring gene apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3D Neighboring gene apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3F Neighboring gene uncharacterized LOC101927202 Neighboring gene apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3H

    GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

    NHGRI GWAS Catalog

    Description
    Host-microbe interactions have shaped the genetic architecture of inflammatory bowel disease.
    NHGRI GWA Catalog

    Protein interactions

    Protein Gene Interaction Pubs
    Envelope surface glycoprotein gp160, precursor env A significant level of APOBEC3G is upregulated when CD4+ T cells are stimulated with HIV-1 gp140 PubMed
    Gag-Pol gag-pol Residues N20, R24, L27, R30, Y59, K63, W94, R102, R122, W127, D128, D130, R136, F157, W175, E191 in the APOBEC3G N-terminal cytidine deaminase domain are involved in the interaction with HIV-1 GagPol PubMed
    gag-pol Residues Y222, Q237, R238, R239, V265, W269, and K270 in the C-terminal cytidine deaminase domain are involved in the interaction with HIV-1 GagPol PubMed
    Pr55(Gag) gag The N-terminus (residues 1-11) of HIV-1 nucleocapsid is critical for HIV-1 Gag and APOBEC3G interaction and virion packaging; the linker region (residues 121-161) of APOBEC3G is also important for efficient packaging into HIV-1 Gag virus like particles PubMed
    gag Single-virion fluorescence microscopy analysis demonstrates that the efficiency of A3G-YFP and A3F-YFP incorporation into HIV-1 Gag-CeFP virions is higher than that of A3C-YFP incorporation into HIV-1 Gag-CeFP virions PubMed
    gag Prostaglandin A1-treated HIV-1-infected cells induce HSP70 synthesis, which leads to block HIV-1 Vif-mediated A3G degradation and to reduce Gag levels in non-permissive cells PubMed
    gag The efficiency of incorporation of Mov10, A3G, and A3F into viral particles, which contains both HIV-1 Gag and genomic RNA, is much higher than that of the other P-body proteins AGO2, DCP1a, DCP2, and DDX6 PubMed
    gag Producer cell A3G complexes decrease HIV-1 pseudovirus production and intracellular HIV-1 Gag half-life PubMed
    gag HIV-1 Gag co-localizes with A3G complex in cells. C97A A3G mutant is delayed in A3G complex formation compared to the wild type PubMed
    gag Transient exposure of Pr(-) viral RNA to NCp7 in vitro returns the quality and quantity of tRNA(3)(Lys) annealing to Pr(+) levels. The presence of A3G prevents this rescue and creates a further reduction in tRNA(3)(Lys) annealing PubMed
    gag HIV-1 Gag chimeras formed by replacing HIV-1 nucleocapsid (NC) domain with SARS-CoV nucleocapsid (N) residues 2-213, 215-421, or 234-421 are capable of incorporating large amounts of human APOBEC3G (hA3G) into virus-like particles (VLPs) PubMed
    gag The amino-terminal half of A3G, which contains only a single cytidine deaminase domain (CDA), is able to bind to HIV-1 Gag and package into HIV-1 virions PubMed
    gag APOBEC3G in exosomes reduces accumulation of HIV-1 reverse transcription products and steady-state levels of HIV-1 Gag and Vif proteins PubMed
    gag Overexpression of A3G and Mov10 decreases the efficiency of HIV-1 Gag processing in virus-producing cells PubMed
    gag Approximately 7 (+/-4) molecules of A3G are incorporated into Delta-vif virions produced from human PBMCs; this incorporation is mediated by the nucleocapsid domain of HIV-1 Gag PubMed
    gag The basic linker region (Gag405-411) of NC is essential for the membrane association of APOBEC3G in a Gag-APOBEC3G complex. APOBEC3G is packaged as a multimer that is bound to packaged RNA PubMed
    Vif vif ASK1 restricts the replication of HIV-1 by inhibiting Vif activity and promoting APOBEC3G incorporation into virions in CD4+ T-cells PubMed
    vif ASK1 markedly inhibits HIV-1 Vif-induced ubiquitination of APOBEC3G by a reduction in the Vif-ELOC interaction PubMed
    vif ASK1 directly binds HIV-1 Vif and inhibits the anti-APOBEC3G activity by Vif PubMed
    vif HIV-1 Vif proteins derived from elite controllers display significantly reduced anti-APOBEC3G activities compared to those from noncontrollers PubMed
    vif Small molecular compound benzimidazole derivatives inhibit APOBEC3G degradation by HIV-1 Vif in H9 cells PubMed
    vif Rbx1 I44A and Rbx2 I52A mutants disrupt the level of HIV-1 Vif-mediated APOBEC3G degradation in cells PubMed
    vif Compound N.41 and its analogs inhibit the Vif-A3G interaction, and increase cellular A3G levels and incorporation of A3G into virions, thereby attenuating virus infectivity in a Vif-dependent manner PubMed
    vif UBE2F and RBX2 are required for activation of the polyubiquitin synthesis activity of Vif/CBF-beta/CUL5, leading to HIV-1 Vif-mediated degradation of A3G in cells PubMed
    vif CUL5/RBX2/ELOB/ELOC/Vif/CBF-beta complex catalyzes polyubiquitin chain formation on A3G in the presence of ubiquitin E2 UBE2R1 (CDC34) or UBCH5b (UBE2D2) PubMed
    vif HIV-1 Vif, CBF-beta, CUL5, and ELOB/C form a complex that is required for Vif-mediated downregulation of A3G and A3F. CBF-beta regulates HIV-1 infectivity only in the presence of A3G PubMed
    vif The ability of HIV-1 Vif to suppress the antiviral activity of APOBEC3G is dependent on the function of a Vif-Cul5-SCF complex involving Cul5, elongins B and C, and Rbx1 PubMed
    vif HIV-1 Vif binds to amino acids 54-124 of APOBEC3G and causes its degradation through a proteasome dependent pathway PubMed
    vif APOBEC3G, also known as CEM15, is a cellular inhibitor of HIV-1 replication which is suppressed by the viral Vif protein PubMed
    vif Residues N20, R24, L27, R30, Y59, K63, W94, R102, R122, W127, D128, D130, R136, F157, W175, and E191 in the APOBEC3G N-terminal cytidine deaminase domain are involved in the interaction with HIV-1 Vif PubMed
    vif HIV-1 Vif mutants carrying mutations or deletions in the conserved HCCH (residues 108-139), SLQ (residues 144-149), and PPLP (residues 161-164) motifs have the ability to dominantly interfere with the wild-type Vif function to inhibit A3G PubMed
    vif HIV-1 Vif W21A, S32A, W38A, Y40A, Y69A, H108A, C114S, C133S, and H139A mutants have no viral ability to neutralize APOBEC3G PubMed
    vif Mutations in the HIV-1 Vif HCCH motif (residues 108-139), BC box (residues 144-146), and Cul5-box (residues 163-169) result in the reduction of Vif-induced APOBEC3G degradation PubMed
    vif Two potent Vif inhibitors RN-18 and VEC5 specifically inhibits HIV-1 Vif-mediated downregulation of APOBEC3C/F/G proteins by decreasing Vif protein levels when Vif interacts with these proteins PubMed
    vif HIV-1 Vif mutants 84DVAAAA89, 88EW/AA89, G84A, G84D, W89A, D104A, L106S, and I107S are unable to efficiently degrade APOBEC3G, leading to Vif mutants that can not effectively inhibit the incorporation of APOBEC3G into virions PubMed
    vif Endogenous APOBEC3 proteins, particularly APOBEC3D, APOBEC3F, and APOBEC3G, can potently inhibit HIV-1 propagation in a mouse model by mutating 14DRMR17 and/or 40YRHHY44 motifs in Vif PubMed
    vif Small molecules identified by a multi-round screening recover APOBEC3G expression in the presence of HIV-1 Vif and increase APOBEC3G incorporation into Vif-proficient virus particles PubMed
    vif HIV-1 Vif(HXB2) interacts with and degrades the A3G D128K mutant in cells PubMed
    vif HIV-1 Vif mutant E88A/W89A fails to bind to CBF-beta, which impairs Vif-mediated degradation of both A3F and A3G proteins and HIV-1 replication in non-permissive CEM cells PubMed
    vif The T(Q/D/E)x(5)ADx(2)(I/L) motif, located at residues 96 to 107 in HIV-1 Vif, plays a critical role in neutralizing activity toward A3G. This motif regulates Vif interaction with Cul5 PubMed
    vif Significant levels of ubiquitinated A3G and A3G20K/R are detected in the presence of HIV-1 Vif. Vif-induced ubiquitination of A3G and A3G20K/R is inhibited by Cul5deltaNedd8 PubMed
    vif A single amino acid replacement of Asp-128 in human APOBEC3G with the Lys-128 of African green monkey (AGM) APOBEC3G causes the enzyme to switch its interaction, becoming sensitive to SIV(AGM) Vif and resistant to HIV-1 Vif PubMed
    vif HIV-1 Vif suppresses the inhibitory effects of APOBEC3G on HIV-1 replication by reducing its intracellular expression and inhibiting its virion encapsidation PubMed
    vif Both HIV-1 Vif-induced downregulation of APOBEC3G and efficient infectivity in the presence of APOBEC3G requires CUL4A neddylation PubMed
    vif HIV-1 Vif mutants W5S, W21S, W38S, W89S, F112S, and F115S have a reduced ability to interact with CBF-beta and still interact with A3G, but fail for Vif-mediated degradation of A3G PubMed
    vif Expression of CBF-beta from mouse, cattle, chicken, and zebrafish restores HIV-1 Vif-mediated A3G degradation ability in CBF-beta-silenced HEK293T cells PubMed
    vif The HIV-1 Vif N-terminal motif (residues 18-38) binds CUL5 in mammalian cells and is reguired for A3F and A3G degradation and HIV-1 infectivity PubMed
    vif HIV-1 Vif mutants C114S and C133A abolish the interaction with CUL5, which leads to fail to A3G degradation by Vif PubMed
    vif CBF-beta isoform 1 and isoform 2 stabilize HIV-1 Vif to degrade A3G and increase viral infectivity PubMed
    vif CBFbeta1-126 is fully functional in the HIV-1 Vif-mediated degradation of A3G, but a further deletion of the C-terminal six amino acid residues (CBFbeta1-120) almost completely abolish its ability to contribute to Vif-induced A3G degradation PubMed
    vif APOBEC3G C97A mutant binds to HIV-1 Vif but is resistant to degradation by Vif. Vif inhibits encapsidation of APOBEC3G C97A and restores viral infectivity PubMed
    vif The appropriate ratio of HIV-1 Vif to A3G protein levels is required for optimal virus replication under different physiological conditions PubMed
    vif The active site proximal loop extension (residues 124-129) in UBE2F is critical for HIV-1 Vif-mediated A3G degradation PubMed
    vif The conjugation of NEDD8 to Cullin-5 by UBE2F is required for HIV-1 Vif-mediated A3G degradation PubMed
    vif Putative serine/threonine phosphorylation point mutations in HIV-1 Vif (T96A, S144A/E, S165A/E, or T188A/E) do not alter Vif-mediated A3G degradation activity, with the exception of Vif T96E PubMed
    vif A patient-derived HIV-1 Vif I107T mutant impairs ability to mediate the degradation of A3G. HIV-1 carrying an I107T Vif mutation displays significantly reduced fitness in A3G(+) T cells and PBMCs PubMed
    vif The interaction of A3G with HIV-1 Vif affects Vif oligomerization in living cells PubMed
    vif SIVsmm Vif-mediated A3G degradation requires a region between A3G amino acid positions 122 and 148. Human A3G 129D and 129Q mutants reduce HIV-1, HIV-2, and SIVsmm Vif binding and are resistant to Vif-mediated degradation PubMed
    vif The inhibition of A3G's processivity and specific activity by HIV-1 Vif are two different functions mediated by an A3G-Vif or ssDNA-Vif interaction, respectively PubMed
    vif Prostaglandin A1-treated HIV-1-infected cells induce HSP70 synthesis, which leads to block HIV-1 Vif-mediated A3G degradation and to reduce Gag levels in non-permissive cells PubMed
    vif HIV-1 Vif co-localizes with A3G peptide 211-225 in cells and the A3G peptide impairs Vif-induced degradation of endogenous A3G PubMed
    vif A3G upregulates NKG2D ligands through an ATM pathway. HIV-1 Vif counteracts this upregulation by decreasing A3G expression PubMed
    vif The antiviral activity of A3G to HIV-1 vif mutants NL4-3 40YRHHY44>A5 and NL4-3 14DRMR17>A4 with G-to-A hypermutations confers a greater restriction than the combined antiviral activity of A3F and A3DE in activated CD4+ T cells and macrophages PubMed
    vif Unusual substitutions V13I, V55T, and L81M in HIV-1 Vif from children infected perinatally without progression to AIDS are located in three distinct Vif motifs important for the interaction with A3G/A3F PubMed
    vif Mutations in HIV-1 Vif PPLP motif (amino acids 161-164) reduces Vif binding to A3G without affecting its interaction with ElonginC and Cullin5 PubMed
    vif Arginine substitutions for Lys-297, 301, 303, and 334 cause A3G resistant to Vif-mediated degradation. The mutant displays normal Vif binding and inhibits HIV-1 infection PubMed
    vif An extensive mutational analysis of HIV-1 Vif reveals that two distinct regions of Vif, amino acids Y(40)RHHY(44) and D(14)RMR(17), are essential for binding to A3G and A3F, respectively PubMed
    vif HIV-1 Vif, which suppresses both APOBEC3G and APOBEC3F antiviral function by inducing their degradation, may selectively remove these proteins from, and/or restrict their localization to, P-bodies PubMed
    vif The binding of HIV-1 Vif to APOBEC3G is specifically mediated by a strong interacting domain encompassing amino acids 85-99 in APOBEC3G and 169-192 in Vif PubMed
    vif The C-terminal domain (amino acid residues 156-193) of APOBEC3G is required for binding with HIV-1 Vif PubMed
    vif Co-immunoprecipitation assays show that HIV-1 Vif directly binds APOBEC3G to form a complex in vivo that accelerates the degradation of APOBEC3G via the ubiquitin-proteasome pathway PubMed
    vif HIV-1 Vif alleles from seven HIV-1 subtypes show their abilities to degrade and counteract A3G efficiently PubMed
    vif Virion-encapsidated HIV-1 Vif, purified Vif protein and the Vif-derived peptide Vif25-39 inhibit the deamination activity of A3G PubMed
    vif The N-terminal HA tag stabilizes A3G20K/R degradation induced by HIV-1 Vif, at least in part, by blocking Vif-mediated A3G polyubiquitination PubMed
    vif A mutagenesis screen of CBF-beta surface residues reveals that a single amino acid change, F68D, disrupts HIV-1 Vif binding and its ability to degrade APOBEC3G PubMed
    vif Residues Y222, Q237, R238, R239, W269, and K270 in the C-terminal cytidine deaminase domain are involved in the interaction with HIV-1 Vif PubMed
    vif A potent small molecular compound VEC-5 protects APOBEC3G, APOBEC3F, and APOBEC3C from HIV-1 Vif-induced degradation and enhances A3G incorporation into HIV-1 virions by inhibiting the interaction between Vif and elongin C PubMed
    vif Highly conserved tryptophan residues in the N-terminal region of HIV-1 Vif are required for the suppression of both APOBEC3G and APOBEC3F PubMed
    vif HIV-1 Vif induces the gradual transition of APO3G translated in vitro or expressed in HeLa cells from a low molecular mass (LMM) conformation to puromycin-sensitive high molecular mass (HMM) complexes PubMed
    vif A VxIPLx(4-5)LxPhix(2)YWxL motif (amino acids 55-72) in HIV-1 Vif is required for efficient interaction between Vif and A3G, Vif-mediated A3G degradation and virion exclusion PubMed
    vif APOBEC3G fused with a virion-targeting polypeptide (amino acids 14-88) derived from HIV-1 Vpr is incorporated into Vif(+) HIV-1 particles and inhibits infectivity and spread of the virions among CD4(+) T cells PubMed
    vif APOBEC3G fused with ubiquitin-associated domain 2 (UBA2) in HHR23A protein is more resistant to Vif-mediated protein degradation than APOBEC3G PubMed
    vif HIV-1 Vif reduces cellular expression and packaging of A3G-3A chimera PubMed
    vif Suppression of viral infectivity by a peptide antagonist of Vif dimerization domain is dependent on the expression of Vif and hA3G PubMed
    vif Expression of hA3G fragments 1-156 or 157-384 dominantly inhibits the Vif-mediated degradation of full-length hA3G; only the N-terminal fragment inhibits the Vif/hA3G interaction PubMed
    vif In vitro biochemical and cell-based binding assays show residues 40 to 71 in the N terminus of Vif contain a nonlinear binding site for APOBEC3G. Mutation of the highly conserved residues His42/43 in this region inhibits Vif-APOBEC3G binding PubMed
    vif Vif-deficient HIV-1 replicates as equally well as wild-type virus in CEM-T4 cells expressing high levels of A3G and A3F, indicating CEM-T4 cells lack a cellular co-factor for these endogenous antiretroviral proteins PubMed
    vif A3G without ubiquitylation is still degraded by proteasomes in an HIV-1 Vif-dependent manner. Polyubiquitynated Vif is critical for A3G proteasomal degradation PubMed
    vif NF-IL6 facilitates the reverse transcription of HIV-1 by binding to and inhibiting the antiviral cytidine deaminase APOBEC3G. A mutation in NF-IL6 at Ser-288 weakens its binding to APOBEC3G and strongly inhibits HIV-1 replication PubMed
    vif Introduction of two Vif-binding mutants (D128K and P129A) into the R88-A3G fusion protein shows that both R88-A3GD128K and R88-A3GP129A possess very potent anti-HIV activity PubMed
    vif HIV-1 Vif-22H mutant uses APOBEC3G hypermutation to develop resistance in certain non-B variants PubMed
    vif N-terminal region (amino acids 21-43) of HIV-1 Vif is important for suppression of APOBEC3G PubMed
    vif Protein kinase A (PKA) binds and phosphorylates A3G at Thr32 in vitro and in vivo. This phosphorylation event reduces the binding of A3G to Vif and its subsequent ubiquitination and degradation PubMed
    vif MDM2 reduces cellular Vif levels and reversely increases A3G levels, because the interaction between MDM2 and Vif prevents A3G from binding to Vif PubMed
    vif A novel conserved 69YXXL72 motif in HIV-1 Vif mediates binding to human A3G and its subsequent degradation. Tyr69 and Trp70 residues in the YXXL motif are required for binding to A3G in vitro PubMed
    vif C-terminal half of HIV-1 Vif from subtype C virus possesses major determinant for A3G degradation PubMed
    vif Newly synthesized APOBEC3G is more sensitive to HIV-1 Vif-induced degradation than preexisting APOBEC3G PubMed
    vif Amino acids 121 to 149 of A3G are essential for binding to the 40YRHHY44 region of HIV-1 Vif but not sufficient for A3G degradation PubMed
    vif APOBEC3G in exosomes reduces accumulation of HIV-1 reverse transcription products and steady-state levels of HIV-1 Gag and Vif proteins PubMed
    vif The SLV portion of the Vif SLV/Ix4Yx9Y motif is required for Vif specificity for APOBEC3G degradation PubMed
    vif Residues K22, K26, Y30, and Y40 in the SLV/Ix4Yx9Y motif of HIV-1 Vif are important for the Vif-induced degradation and suppression of cellular APOBEC3G. The positively charged K26 is the most critical residue for A3G inactivation PubMed
    vif HIV-1 Vif K22E and RH41/42AA mutants are able to suppress the anti-viral activity of A3C, but are ineffective in suppressing the anti-viral activity of A3G. K22, R41, and H42 residues are important for Vif-mediated degradation of A3G, but not A3C PubMed
    vif 5' splice site D2 and an exonic splicing enhancer exist in the HIV-1 genome is to regulate the levels of vif mRNA and Vif protein in infected cells to counteract cellular restriction factor APOBEC3G PubMed
    vif Human T cell line CEM.NKR clones display inhibition of HIV-1 replication although these clones retain low levels of A3DE, A3F, A3G, and A3H expression, suggesting that a novel restriction factor distinct from APOBEC3s exists in CEM.NKR cells PubMed
    vif Incorporation of HIV-1 Vif into virions is dependent on its interaction with A3G/A3F PubMed
    vif Compounds IMB-26 and IMB-35 bind directly to the hA3G protein, suppress HIV-1 Vif/hA3G interaction, and therefore protect hA3G from Vif-mediated degradation PubMed
    vif Alternative splice removal of exon 2 or exons 3-5 of A3G produces proteins that do not interact with HIV-1 Vif and lack antiviral activity PubMed
    vif Residues G84, and, to a lesser extent, I87 and W89 within the (81)LGxGxxIxW(89) domain affect Vif binding to A3G and play very critical roles in A3G neutralizing activity PubMed
    vif HIV-1 Vif inhibits the antiviral function of A3G in a subtype-dependent manner. The N-terminal region (amino acids 1-31) of subtype C-derived Vif protein is crucial for the anti-A3G activity PubMed
    vif APOBEC3G can escape the inhibition from Vif and retain its antiviral activity when it is expressed high enough PubMed
    vif Approximately 7 (+/-4) molecules of APOBEC3G are incorporated into HIV-1 Vif-negative virions produced from human PBMCs; HIV-1 Vif inhibits this incorporation PubMed
    vif IFN-alpha enhances APOBEC3G expression and inhibits suppression of APOBEC3G by HIV-1 Vif PubMed
    vif HSP70 interacts with both APOBEC3G and HIV-1 Vif, which stabilizes APOBEC3G and blocks Vif-mediated degradation of APOBEC3G PubMed
    vif Human A3G is a host restriction factor against hepatitis C virus (HCV). Exogenous HIV-1 Vif decreases intracellular hA3G and therefore enhances HCV proliferation PubMed
    vif Three A3G mutants, containing duplicate CD1 domain (residues 65-100), duplicate CD2 domain (residues 257-291), or position switched CD domains, has no significant effect in A3G/Vif interaction and in incorporation into virions PubMed
    vif Mutation of amino acid S144 in HIV-1 HXB2 Vif significantly reduces the ability of Vif to inhibit the antiviral activity of APOBEC3G PubMed
    vif Binding of APOBEC3G with HIV-1 Vif influences the localization of Vif, and mutation of the isoleucine at Vif amino acid 9 disrupts this interaction PubMed
    vif The overall negative charge of the 3-amino-acid motif Asp128, Pro129, and Asp130 in APOBEC3G appears critical for recognition by Vif. The immediately adjacent 4 amino acids, residues 124 to 127, are important for the packaging of A3G into HIV-1 particles PubMed
    vif Treatment with the membrane-permeable zinc chelator TPEN prevents Vif function, and causes the blockage of Cul5 recruitment and APOBEC3G (A3G) degradation PubMed
    Vpr vpr Ubiquitination and degradation levels of APOBEC3G is upregulated in the presence of HIV-1 Vpr in the proviral backbone compared to the levels for control PubMed
    vpr HIV-1 Vpr induces the degradation of APOBEC3G through VprBP binding and participation of the proteasome, leading to a reduction in APOBEC3G encapsidation into virions PubMed
    vpr HIV-1 Vpr increases expression of HIV-1 Vif and APOBEC3G in cells PubMed
    Vpu vpu The expression of APOBEC3G is enhanced in Vpu-deficient HIV-1-infected cells as compared to that in wild-type-infected cells PubMed
    integrase gag-pol The C-terminal domain (amino acids 212-288) of HIV-1 IN and the first linker region (amino acids 104-156) of APOBEC3G are required for IN and APOBEC3G interaction PubMed
    gag-pol In HIV-1 virions, APOBEC3G interacts with HIV-1 IN and NC, which are known to be important for reverse transcription and integration PubMed
    gag-pol Newly synthesized A3G is incorporated into virion cores and assembles into a large RNA containing intravirion complex composed of IN, NC, and genomic RNA. Enzymatic activity of A3G is negatively regulated by RNA binding in the complex PubMed
    nucleocapsid gag The N-terminus (residues 1-11) of HIV-1 nucleocapsid is critical for HIV-1 Gag and APOBEC3G interaction and virion packaging; the linker region (residues 121-161) of APOBEC3G is also important for efficient packaging into HIV-1 Gag virus like particles PubMed
    gag Transient exposure of Pr(-) viral RNA to NCp7 in vitro returns the quality and quantity of tRNA(3)(Lys) annealing to Pr(+) levels. The presence of A3G prevents this rescue and creates a further reduction in tRNA(3)(Lys) annealing PubMed
    gag Interaction of APOBEC3G with HIV-1 nucleocapsid requires RNA, which may form a bridge between these two proteins PubMed
    gag Newly synthesized A3G is incorporated into virion cores and assembles into a large RNA containing intravirion complex composed of IN, NC, and genomic RNA. Enzymatic activity of A3G is negatively regulated by RNA binding in the complex PubMed
    gag Inhibition of tRNA3-Lys priming by A3G is associated with an inhibition of tRNA3-Lys annealing to viral RNA. The A3G-induced inhibition of tRNA-Lys priming occurs in a dose-dependent manner and can be rescued with increasing amounts of NC PubMed
    gag Overexpression of SRP19 reduces the incorporation of 7SL RNA and A3G into virions in a dose-dependent manner PubMed
    gag Efficient incorporation of 7SL RNA and A3G into virions is mediated by the RNA-binding nucleocapsid domain of HIV-1 Gag PubMed
    gag In vitro biochemical assays show A3G significantly inhibits all HIV-1 RT-catalyzed DNA elongation reactions with or without HIV-1 NC. In the case of (-) strong-stop DNA synthesis, the inhibition is independent of A3G's catalytic activity PubMed
    gag Formation of the NC and A3G complex in vitro is promoted by single-stranded RNAs (ssRNAs) containing G residues, human Y RNAs and 7SL RNA, but not promoted by highly structured tRNAs and rRNAs PubMed
    gag Approximately 7 (+/-4) molecules of APOBEC3G are incorporated into HIV-1 Vif-negative virions produced from human PBMCs; this incorporation is mediated by HIV-1 nucleocapsid PubMed
    gag The basic linker region (Gag405-411) of NC is essential for the membrane association of APOBEC3G in a Gag-APOBEC3G complex. APOBEC3G is packaged as a multimer that is bound to packaged RNA PubMed
    gag Interaction of APOBEC3G with the carboxy-terminal nucleocapsid/p6 domain of the Gag polyprotein precursor is observed by Western analysis PubMed
    p6 gag Interaction of APOBEC3G with the carboxy-terminal nucleocapsid/p6 domain of the Gag polyprotein precursor is observed by Western analysis PubMed
    reverse transcriptase gag-pol APOBEC3G decreases the efficiency of reverse transcriptase-mediated DNA synthesis by binding to the RNA template, rather than by physically interacting with reverse transcriptase PubMed
    gag-pol In vitro biochemical assays show A3G significantly inhibits all HIV-1 RT-catalyzed DNA elongation reactions with or without HIV-1 NC. In the case of (-) strong-stop DNA synthesis, the inhibition is independent of A3G's catalytic activity PubMed
    gag-pol Vif-negative HIV-1 produced from 293T cells transiently expressing hA3G are impaired in early and late viral DNA production, and in viral infectivity, which are correlated with an inability of tRNA(3)(Lys) to prime reverse transcription PubMed
    gag-pol The N-terminal fingers-palm domain (residues 1-243) of HIV-1 RT and the N-terminal first CDD and part of the linker domains (residues 65-132) of APOBEC3G are involved in the binding between RT and APOBEC3G PubMed
    gag-pol Both HIV-1 RTp66 and RTp51 proteins interact with APOBEC3G in the coimmunoprecipation assay and their interaction does not require the presence of viral RNA and HIV-1 IN PubMed
    gag-pol APOBEC3-driven mutagenesis contributes to the generation of both M184I and E138K mutations in HIV-1 RT in the absence of drug exposure PubMed
    gag-pol Enzymatic activity of A3G is negatively regulated by RNA binding in the intravirion complex. Inactive A3G is activated by viral RNase H during reverse transcription PubMed
    gag-pol The frequencies of G-to-A mutations induced by A3G are increased after infection with an HIV-1 K65R/M184V RT virus variant. Overall, the G-to-A mutation frequencies are lower in PBMCs than in H9 T-cells PubMed

    Go to the HIV-1, Human Interaction Database

    • APOBEC3G mediated resistance to HIV-1 infection, organism-specific biosystem (from REACTOME)
      APOBEC3G mediated resistance to HIV-1 infection, organism-specific biosystemRepresentatives of the apolipoprotein B mRNA editing enzyme catalytic polypeptide 3 (APOBEC3) family provide innate resistance to exogeneous and endogenous retroviruses (see Cullen 2006 for a recent ...
    • Disease, organism-specific biosystem (from REACTOME)
      Disease, organism-specific biosystemBiological processes are captured in Reactome by identifying the molecules (DNA, RNA, protein, small molecules) involved in them and describing the details of their interactions. From this molecular ...
    • HIV Infection, organism-specific biosystem (from REACTOME)
      HIV Infection, organism-specific biosystemThe global pandemic of Human Immunodeficiency Virus (HIV) infection has resulted in tens of millions of people infected by the virus and millions more affected. UNAIDS estimates around 40 million ...
    • Host Interactions of HIV factors, organism-specific biosystem (from REACTOME)
      Host Interactions of HIV factors, organism-specific biosystemLike all viruses, HIV-1 must co-opt the host cell macromolecular transport and processing machinery. HIV-1 Vpr and Rev proteins play key roles in this co-optation. Efficient HIV-1 replication likewis...
    • Infectious disease, organism-specific biosystem (from REACTOME)
      Infectious disease, organism-specific biosystem
      Infectious disease
    • Integrated Breast Cancer Pathway, organism-specific biosystem (from WikiPathways)
      Integrated Breast Cancer Pathway, organism-specific biosystemThis pathway incorporates the most important proteins for Breast Cancer. The Rp score from the Connectivity-Maps (C-Maps) webserver was used to determine the rank of the most important proteins in Br...
    • Vif-mediated degradation of APOBEC3G, organism-specific biosystem (from REACTOME)
      Vif-mediated degradation of APOBEC3G, organism-specific biosystemThe HIV-1 accessory protein Vif (Viral infectivity factor) is required for the efficient infection of primary cell populations (e.g., lymphocytes and macrophages) and 'non-permissive' cell lines. Vif...
    Products Interactant Other Gene Complex Source Pubs Description

    Markers

    Clone Names

    • FLJ12740

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    RNA binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    cytidine deaminase activity TAS
    Traceable Author Statement
    more info
    PubMed 
    deoxycytidine deaminase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    protein homodimerization activity NAS
    Non-traceable Author Statement
    more info
    PubMed 
    zinc ion binding IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Component Evidence Code Pubs
    apolipoprotein B mRNA editing enzyme complex TAS
    Traceable Author Statement
    more info
    PubMed 
    cytoplasm IDA
    Inferred from Direct Assay
    more info
    PubMed 
    cytoplasmic mRNA processing body IDA
    Inferred from Direct Assay
    more info
    PubMed 
    cytosol TAS
    Traceable Author Statement
    more info
     
    ribonucleoprotein complex IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Preferred Names
    DNA dC->dU-editing enzyme APOBEC-3G
    Names
    APOBEC-related cytidine deaminase
    APOBEC-related protein 9
    DNA dC->dU editing enzyme
    apolipoprotein B editing enzyme catalytic polypeptide-like 3G
    apolipoprotein B mRNA editing enzyme cytidine deaminase
    apolipoprotein B mRNA-editing enzyme catalytic polypeptide 3G
    deoxycytidine deaminase
    phorbolin-like protein MDS019
    NP_068594.1

    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.

    mRNA and Protein(s)

    1. NM_021822.3NP_068594.1  DNA dC->dU-editing enzyme APOBEC-3G

      See identical proteins and their annotated locations for NP_068594.1

      Status: REVIEWED

      Source sequence(s)
      AL022318, AL078641, BC009683
      Consensus CDS
      CCDS13984.1
      UniProtKB/Swiss-Prot
      Q9HC16
      Related
      ENSP00000385057, OTTHUMP00000199084, ENST00000407997, OTTHUMT00000321219
      Conserved Domains (3) summary
      pfam05240
      Location:318372
      APOBEC_C; APOBEC-like C-terminal domain
      cd01283
      Location:9133
      cytidine_deaminase; Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on ...
      pfam08210
      Location:202380
      APOBEC_N; APOBEC-like N-terminal domain

    RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 107

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

    Reference GRCh38.p2 Primary Assembly

    Genomic

    1. NC_000022.11 Reference GRCh38.p2 Primary Assembly

      Range
      39077005..39087743
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_006724290.1XP_006724353.1  

      Conserved Domains (3) summary
      pfam05240
      Location:251305
      APOBEC_C; APOBEC-like C-terminal domain
      cd01283
      Location:144235
      cytidine_deaminase; Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on ...
      pfam08210
      Location:135313
      APOBEC_N; APOBEC-like N-terminal domain

    Alternate CHM1_1.1

    Genomic

    1. NC_018933.2 Alternate CHM1_1.1

      Range
      39431972..39442708
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)