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

Gene ID: 60489, updated on 6-Jul-2014
Official Symbol
APOBEC3Gprovided by HGNC
Official Full Name
apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3Gprovided by HGNC
Primary source
HGNC:17357
Locus tag
MDS019
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]
See APOBEC3G in Epigenomics, MapViewer
Location:
22q13.1-q13.2
Exon count :
8
Annotation release Status Assembly Chr Location
106 current GRCh38 (GCF_000001405.26) 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
Gag, Pr55 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 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 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, p23 vif The appropriate ratio of HIV-1 Vif to A3G protein levels is required for optimal virus replication under different physiological conditions 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 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 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 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 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 CBF-beta isoform 1 and isoform 2 stabilize HIV-1 Vif to degrade A3G and increase viral infectivity 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 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 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 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 suppresses the inhibitory effects of APOBEC3G on HIV-1 replication by reducing its intracellular expression and inhibiting its virion encapsidation PubMed
vif HIV-1 Vif binds to amino acids 54-124 of APOBEC3G and causes its degradation through a proteasome dependent 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 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 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 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 Small molecule RN-18 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 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 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 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 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 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 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 W21A, S32A, W38A, Y40A, Y69A, H108A, C114S, C133S, and H139A mutants have no viral ability to neutralize APOBEC3G 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 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 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
vif APOBEC3G, also known as CEM15, is a cellular inhibitor of HIV-1 replication which is suppressed by the viral Vif protein PubMed
Vpr, p15 vpr HIV-1 Vpr increases expression of HIV-1 Vif and APOBEC3G in cells PubMed
Vpu, p16 vpu The expression of APOBEC3G is enhanced in Vpu-deficient HIV-1-infected cells as compared to that in wild-type-infected cells PubMed
nucleocapsid 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 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 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
pol 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 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
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 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 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 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-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 Protein 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...
  • 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 ââ?¬Å?non-permissiveââ?¬Â? cel...
Products Interactant Other Gene Complex Source Pubs Description

Markers

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
DNA dC->dU-editing enzyme APOBEC-3G
deoxycytidine deaminase
APOBEC-related protein 9
DNA dC->dU editing enzyme
phorbolin-like protein MDS019
APOBEC-related cytidine deaminase
apolipoprotein B mRNA editing enzyme cytidine deaminase
apolipoprotein B editing enzyme catalytic polypeptide-like 3G
apolipoprotein B mRNA-editing enzyme catalytic polypeptide 3G
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 proteins identical to 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
    Blast Score: 249
    APOBEC_C; APOBEC-like C-terminal domain
    cd01283
    Location:9133
    Blast Score: 165
    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
    Blast Score: 323
    APOBEC_N; APOBEC-like N-terminal domain

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_000022.11 

    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
    Blast Score: 249
    APOBEC_C; APOBEC-like C-terminal domain
    cd01283
    Location:144235
    Blast Score: 112
    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
    Blast Score: 322
    APOBEC_N; APOBEC-like N-terminal domain

Alternate HuRef

Genomic

  1. AC_000154.1 

    Range
    22440372..22451110
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate CHM1_1.1

Genomic

  1. NC_018933.2 

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

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