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

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Summary

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: ARCD; ARP9; ARP-9; CEM15; CEM-15; MDS019; bK150C2.7; dJ494G10.1; FLJ12740
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]

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Genomic context

Location :: 22q13.1-q13.2

Sequence :: Chromosome: 22; NC_000022.10 (39473010..39483748)

See APOBEC3G in Epigenomics, MapViewer

Chromosome 22 - NC_000022.10 Genomic Context describing neighboring genes

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Genomic regions, transcripts, and products

Genomic Sequence

Go to nucleotideGraphics FASTA GenBank

Go to reference sequence details

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Bibliography

GeneRIFs: Gene References Into Functions What's a GeneRIF?

G-to-A mutations on V3 HIV peptide caused by APOBEC3F and APOBEC3G facilitate co-receptor switch of HIV from R5 to X4 strains.
Title: APOBEC3G/F as one possible driving force for co-receptor switch of the human immunodeficiency virus-1.
In summary, our results cast doubt on all previous structure-function predictions for APOBEC3G that were based on the crystal structure of APOBEC2.
Title: APOBEC2 is a monomer in solution: implications for APOBEC3G models.
APOBEC3G/3F and BST-2 mRNA expression was significantly elevated during IFN-alpha/riba treatment in patient-derived CD4+ T cells (P < 0.04 and P < 0.008, paired Wilcoxon), and extent of BST-2 induction was correlated with reduction in HIV-1 viral...
Title: Role of retroviral restriction factors in the interferon-α-mediated suppression of HIV-1 in vivo.
Vif proteins of human and simian immunodeficiency viruses require cellular CBFbeta to degrade APOBEC3G.
Title: Vif proteins of human and simian immunodeficiency viruses require cellular CBFβ to degrade APOBEC3 restriction factors.
CBF-beta is required for Vif-mediated degradation of APOBEC3G and therefore for preserving HIV-1 infectivity
Title: Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection.
Study propose that RPA plays a role in the protection of the human genome cell from A3G and other deaminases when they are inadvertently diverged from their natural targets.
Title: Replication protein A (RPA) hampers the processive action of APOBEC3G cytosine deaminase on single-stranded DNA.
A significant inhibition of HIV-1 infection was observed in PBMCs and macrophages transduced with R14-88 APOBEC3G mutant fusion proteins.
Title: Characterization of anti-HIV activity mediated by R88-APOBEC3G mutant fusion proteins in CD4+ T cells, peripheral blood mononuclear cells, and macrophages.
Most Vif proteins counteract APOBEC3G and APOBEC3F efficiently but display differences with respect to the inhibition of APOBEC3H.
Title: The activity spectrum of Vif from multiple HIV-1 subtypes against APOBEC3G, APOBEC3F, and APOBEC3H.
novel mechanism in which APOBEC3G promotes colorectal cancer hepatic metastasis through inhibition of miR-29-mediated suppression of MMP2
Title: APOBEC3G promotes liver metastasis in an orthotopic mouse model of colorectal cancer and predicts human hepatic metastasis.
levels of A3G and A3F expression and induced G-to-A hypermutation in a group of children with distinct profiles of disease progression
Title: Expression of APOBEC3G/3F and G-to-A hypermutation levels in HIV-1-infected children with different profiles of disease progression.

Submit: New GeneRIF Correction See all (203)

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Phenotypes

Review eQTL and phenotype association data in this region using PheGenI

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HIV-1 protein interactions

Protein	Gene	Interaction	Pubs
Vif	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	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	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	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	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	APOBEC3G, also know as CEM15, is a cellular inhibitor of HIV-1 replication which is suppressed by the viral Vif protein	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	IFN-alpha enhances APOBEC3G expression and inhibits suppression of APOBEC3G by HIV-1 Vif	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	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	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
nucleocapsid	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	Interaction of APOBEC3G with HIV-1 nucleocapsid requires RNA, which may form a bridge between these two proteins	PubMed
	gag	Interaction of APOBEC3G with the carboxy-terminal nucleocapsid/p6 domain of the Gag polyprotein precursor is observed by Western analysis	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
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	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

Go to the HIV-1, Human Protein Interaction Database

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Products	Interactant	Other Gene	Source	Pubs	Description
NP_068594.1	NP_068594.1	APOBEC3G	BIND	PubMed	CEM15 forms homo-dimer.
NP_068594.1	UQHU	UBA52	BIND	PubMed	Ubiquitin interacts with APOBEC3G.
NP_068594.1	NP_057850.1	gag	BIND	PubMed	Gag interacts with APOBEC3G.
NP_068594.1	AAM96931.1		BIND	PubMed	APOBEC3G interacts with HBcAg.
Phorbolin like protein MDS019	Q9HC16	APOBEC3G	HPRD	PubMed
Phorbolin like protein MDS019	P21246	PTN	HPRD	PubMed
Q9HC16	Phorbolin like protein MDS019	APOBEC3G	HPRD	PubMed
BioGRID:121920	BioGRID:121920	APOBEC3G	BioGRID	PubMed	PCA
BioGRID:121920	BioGRID:109540	HSPA4	BioGRID	PubMed	Affinity Capture-Western
BioGRID:121920	BioGRID:111553	PRKACA	BioGRID	PubMed	Affinity Capture-Western; Biochemical Activity
BioGRID:121920	BioGRID:111731	PTN	BioGRID	PubMed	Two-hybrid
BioGRID:121920	BioGRID:113164	UBC	BioGRID	PubMed	Affinity Capture-MS; Affinity Capture-Western
BioGRID:121920	BioGRID:1205537	gag	BioGRID	PubMed	Protein-RNA
BioGRID:121920	BioGRID:1205539	vif	BioGRID	PubMed	Affinity Capture-Western; Biochemical Activity; PCA; Reconstituted Complex

Function	Evidence Code	Pubs
RNA binding	IDA Inferred from Direct Assay more info	PubMed
cytidine deaminase activity	TAS Traceable Author Statement more info	PubMed
hydrolase activity	IEA Inferred from Electronic Annotation more info
metal ion binding	IEA Inferred from Electronic Annotation more info
protein homodimerization activity	NAS Non-traceable Author Statement more info	PubMed
zinc ion binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
DNA cytosine deamination	IDA Inferred from Direct Assay more info	PubMed
base conversion or substitution editing	TAS Traceable Author Statement more info	PubMed
cytidine deamination	TAS Traceable Author Statement more info	PubMed
innate immune response	IDA Inferred from Direct Assay more info	PubMed
interspecies interaction between organisms	IEA Inferred from Electronic Annotation more info
negative regulation of retroviral genome replication	IDA Inferred from Direct Assay more info	PubMed
negative regulation of transposition	IDA Inferred from Direct Assay more info	PubMed
negative regulation of viral genome replication	IDA Inferred from Direct Assay more info	PubMed
negative regulation of viral reproduction	IDA Inferred from Direct Assay more info	PubMed
positive regulation of defense response to virus by host	IDA Inferred from Direct Assay more info	PubMed
response to virus	IEA Inferred from Electronic Annotation more info
viral reproduction	TAS Traceable Author Statement more info

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
cytosol	TAS Traceable Author Statement more info
mitochondrion	IDA Inferred from Direct Assay more info	PubMed
nucleus	IEA Inferred from Electronic Annotation more info

General protein information

Preferred Names: DNA dC->dU-editing enzyme APOBEC-3G

Names: DNA dC->dU-editing enzyme APOBEC-3G; APOBEC-related protein 9; DNA dC->dU editing enzyme; phorbolin-like protein MDS019; APOBEC-related cytidine deaminase; apolipoprotein B mRNA editing enzyme cytidine deaminase

NP_068594.1

EC 3.5.4.-

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NCBI Reference Sequences (RefSeq)

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)

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

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

cd01283
Location:9 – 133
Blast Score: 143

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 ...

pfam05240
Location:318 – 372
Blast Score: 238

APOBEC_C; APOBEC-like C-terminal domain

pfam08210
Location:202 – 380
Blast Score: 309

APOBEC_N; APOBEC-like N-terminal domain

RefSeqs of Annotated Genomes: Build 37.3

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

Reference GRCh37.p5 Primary Assembly

Genomic

NC_000022.10 Reference GRCh37.p5 Primary Assembly

Range

39473010..39483748

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

AC_000154.1 Alternate HuRef

Range

22440372..22451110

Download

GenBank, FASTA, Sequence Viewer (Graphics)

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Related Sequences

Nucleotide		Protein
Heading	Accession and Version	Protein
genomic	AL022318.2	CAI17900.1
genomic	AL078641.2	CAI21556.1
genomic	CH471095.1	EAW60292.1
genomic	DQ147772.1	AAZ38722.1
mRNA	AB266487.1	BAF34652.1
mRNA	AF182420.1	AAG14956.1
mRNA	AK022802.1	None
mRNA	AK092614.1	None
mRNA	AK093635.1	None
mRNA	AK310279.1	None
mRNA	AK315650.1	BAG38016.1
mRNA	BC009683.1	None
mRNA	BC024268.1	AAH24268.1
mRNA	BC061914.1	AAH61914.1
mRNA	CR456472.1	CAG30358.1
mRNA	DA457434.1	None
mRNA	JF262036.1	AEA39616.1
other-genetic	CU013022.1	CAK54453.1
other-genetic	CU013310.1	CAK54752.1