Details for: APOBEC3G
Associated with
Other Information
Genular Protein ID: 237150312
Symbol: ABC3G_HUMAN
Name: DNA dC->dU-editing enzyme APOBEC-3G
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 14557625
Title: The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity.
PubMed ID: 14557625
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 15461802
Title: A genome annotation-driven approach to cloning the human ORFeome.
PubMed ID: 15461802
PubMed ID: 10591208
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 11863358
Title: An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22.
PubMed ID: 11863358
PubMed ID: 12167863
Title: Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein.
PubMed ID: 12167863
DOI: 10.1038/nature00939
PubMed ID: 12808466
Title: Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.
PubMed ID: 12808466
DOI: 10.1038/nature01709
PubMed ID: 12809610
Title: DNA deamination mediates innate immunity to retroviral infection.
PubMed ID: 12809610
PubMed ID: 12808465
Title: The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA.
PubMed ID: 12808465
DOI: 10.1038/nature01707
PubMed ID: 12859895
Title: Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.
PubMed ID: 12859895
PubMed ID: 12970355
Title: The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity.
PubMed ID: 12970355
PubMed ID: 14527406
Title: HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability.
PubMed ID: 14527406
PubMed ID: 14528301
Title: HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation.
PubMed ID: 14528301
DOI: 10.1038/nm946
PubMed ID: 14528300
Title: The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif.
PubMed ID: 14528300
DOI: 10.1038/nm945
PubMed ID: 12683974
Title: Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business.
PubMed ID: 12683974
PubMed ID: 14557052
PubMed ID: 14565218
Title: HIV-1 Vif: counteracting innate antiretroviral defenses.
PubMed ID: 14565218
PubMed ID: 15054139
Title: A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion.
PubMed ID: 15054139
PubMed ID: 15031497
Title: Inhibition of hepatitis B virus replication by APOBEC3G.
PubMed ID: 15031497
PubMed ID: 16527742
Title: APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons.
PubMed ID: 16527742
PubMed ID: 17020885
Title: Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains.
PubMed ID: 17020885
PubMed ID: 16378963
Title: Restriction of foamy viruses by APOBEC cytidine deaminases.
PubMed ID: 16378963
PubMed ID: 16699599
Title: Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies.
PubMed ID: 16699599
PubMed ID: 18304004
Title: The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements.
PubMed ID: 18304004
PubMed ID: 18448976
Title: Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine deaminases as effectors in innate immunity against the hepatitis B virus.
PubMed ID: 18448976
PubMed ID: 18842592
Title: APOBEC3G subunits self-associate via the C-terminal deaminase domain.
PubMed ID: 18842592
PubMed ID: 18667511
Title: Two regions within the amino-terminal half of APOBEC3G cooperate to determine cytoplasmic localization.
PubMed ID: 18667511
DOI: 10.1128/jvi.02471-07
PubMed ID: 18836454
Title: Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif.
PubMed ID: 18836454
DOI: 10.1038/nsmb.1497
PubMed ID: 19458006
Title: Restriction of equine infectious anemia virus by equine APOBEC3 cytidine deaminases.
PubMed ID: 19458006
DOI: 10.1128/jvi.00015-09
PubMed ID: 19008196
PubMed ID: 20219927
Title: APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms.
PubMed ID: 20219927
DOI: 10.1128/jvi.02358-09
PubMed ID: 20335265
Title: Inhibition of xenotropic murine leukemia virus-related virus by APOBEC3 proteins and antiviral drugs.
PubMed ID: 20335265
DOI: 10.1128/jvi.00134-10
PubMed ID: 20308164
Title: Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes and tissues: implications for HIV-1 restriction.
PubMed ID: 20308164
DOI: 10.1093/nar/gkq174
PubMed ID: 20510315
Title: APOBEC3G directly binds Hepatitis B virus core protein in cell and cell free systems.
PubMed ID: 20510315
PubMed ID: 21659520
Title: Phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein.
PubMed ID: 21659520
PubMed ID: 21123384
Title: Structure-function analyses point to a polynucleotide-accommodating groove essential for APOBEC3A restriction activities.
PubMed ID: 21123384
DOI: 10.1128/jvi.01651-10
PubMed ID: 21835787
Title: Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1.
PubMed ID: 21835787
DOI: 10.1128/jvi.05238-11
PubMed ID: 21239176
PubMed ID: 21489586
Title: Functional analysis of the two cytidine deaminase domains in APOBEC3G.
PubMed ID: 21489586
PubMed ID: 22787460
Title: Antiviral mechanism and biochemical basis of the human APOBEC3 family.
PubMed ID: 22787460
PubMed ID: 22912627
Title: Retroelements versus APOBEC3 family members: No great escape from the magnificent seven.
PubMed ID: 22912627
PubMed ID: 22791714
Title: APOBEC3G inhibits microRNA-mediated repression of translation by interfering with the interaction between Argonaute-2 and MOV10.
PubMed ID: 22791714
PubMed ID: 22301159
Title: The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse transcriptase and inhibits its function during viral replication.
PubMed ID: 22301159
DOI: 10.1128/jvi.06594-11
PubMed ID: 22915799
Title: HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies.
PubMed ID: 22915799
DOI: 10.1128/jvi.00595-12
PubMed ID: 23001005
Title: The APOBEC3C crystal structure and the interface for HIV-1 Vif binding.
PubMed ID: 23001005
DOI: 10.1038/nsmb.2378
PubMed ID: 22807680
Title: Endogenous origins of HIV-1 G-to-A hypermutation and restriction in the nonpermissive T cell line CEM2n.
PubMed ID: 22807680
PubMed ID: 22546055
Title: Emerging complexities of APOBEC3G action on immunity and viral fitness during HIV infection and treatment.
PubMed ID: 22546055
PubMed ID: 22001110
Title: Functions and regulation of the APOBEC family of proteins.
PubMed ID: 22001110
PubMed ID: 23097438
Title: APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ t cells and macrophages.
PubMed ID: 23097438
DOI: 10.1128/jvi.00676-12
PubMed ID: 23152537
Title: The suppression of HIV-1 infection by APOBEC3 proteins in primary human CD4+ T cells is associated with the inhibition of processive reverse transcription as well as excessive cytidine deamination.
PubMed ID: 23152537
DOI: 10.1128/jvi.02587-12
PubMed ID: 18288108
Title: Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G.
PubMed ID: 18288108
DOI: 10.1038/nature06638
PubMed ID: 18849968
Title: Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications.
PubMed ID: 18849968
DOI: 10.1038/nature07357
PubMed ID: 19153609
Title: Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G.
PubMed ID: 19153609
PubMed ID: 22181350
Title: First-in-class small molecule inhibitors of the single-strand DNA cytosine deaminase APOBEC3G.
PubMed ID: 22181350
DOI: 10.1021/cb200440y
Sequence Information:
- Length: 384
- Mass: 46408
- Checksum: 60525DC3B7D903D6
- Sequence:
MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPPLD AKIFRGQVYS ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC TRDMATFLAE DPKVTLTIFV ARLYYFWDPD YQEALRSLCQ KRDGPRATMK IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK YYILLHIMLG EILRHSMDPP TFTFNFNNEP WVRGRHETYL CYEVERMHND TWVLLNQRRG FLCNQAPHKH GFLEGRHAEL CFLDVIPFWK LDLDQDYRVT CFTSWSPCFS CAQEMAKFIS KNKHVSLCIF TARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF VDHQGCPFQP WDGLDEHSQD LSGRLRAILQ NQEN
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.