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Q9HC16

- ABC3G_HUMAN

UniProt

Q9HC16 - ABC3G_HUMAN

Protein

DNA dC->dU-editing enzyme APOBEC-3G

Gene

APOBEC3G

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits potent antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double-stranded RNA. Exhibits antiviral activity also against simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV). May inhibit the mobility of LTR and non-LTR retrotransposons.22 Publications

    Catalytic activityi

    Deoxycytidine + H2O = deoxyuridine + NH3.4 Publications

    Cofactori

    Zinc.

    Enzyme regulationi

    Assembly into ribonucleoprotein complexes of high-molecular-mass (HMM) inhibits its enzymatic activity. Antiviral activity is neutralized by the HIV-1 virion infectivity factor (VIF), that prevents its incorporation into progeny HIV-1 virions by both inhibiting its translation and/or by inducing its ubiquitination and subsequent degradation by the 26S proteasome. Can also be neutralized by simian immunodeficiency virus sooty mangabey monkey virus (SIV-sm) and chimpanzee immunodeficiency virus (SIV-cpz) VIF.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi65 – 651ZincBy similarity
    Metal bindingi97 – 971ZincBy similarity
    Metal bindingi100 – 1001ZincBy similarity
    Sitei244 – 2441Interaction with DNACurated
    Metal bindingi257 – 2571Zinc; catalytic3 Publications
    Active sitei259 – 2591Proton donorCurated
    Metal bindingi288 – 2881Zinc; catalytic3 Publications
    Metal bindingi291 – 2911Zinc; catalytic3 Publications

    GO - Molecular functioni

    1. cytidine deaminase activity Source: HGNC
    2. deoxycytidine deaminase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB
    5. RNA binding Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. base conversion or substitution editing Source: HGNC
    2. cytidine deamination Source: UniProtKB
    3. defense response to virus Source: UniProtKB
    4. DNA cytosine deamination Source: UniProtKB
    5. innate immune response Source: HGNC
    6. negative regulation of single stranded viral RNA replication via double stranded DNA intermediate Source: UniProtKB
    7. negative regulation of transposition Source: UniProtKB
    8. negative regulation of viral genome replication Source: UniProtKB
    9. negative regulation of viral process Source: HGNC
    10. positive regulation of defense response to virus by host Source: HGNC
    11. viral process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antiviral defense, Host-virus interaction, Immunity, Innate immunity

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.5.4.5. 2681.
    ReactomeiREACT_9406. APOBEC3G mediated resistance to HIV-1 infection.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA dC->dU-editing enzyme APOBEC-3G (EC:3.5.4.-)
    Alternative name(s):
    APOBEC-related cytidine deaminase
    Short name:
    APOBEC-related protein
    Short name:
    ARCD
    APOBEC-related protein 9
    Short name:
    ARP-9
    CEM-15
    Short name:
    CEM15
    Deoxycytidine deaminase
    Short name:
    A3G
    Gene namesi
    ORF Names:MDS019
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:17357. APOBEC3G.

    Subcellular locationi

    Cytoplasm. Nucleus. CytoplasmP-body
    Note: Mainly cytoplasmic. Small amount are found in the nucleus. During HIV-1 infection, virion-encapsidated in absence of HIV-1 VIF.

    GO - Cellular componenti

    1. apolipoprotein B mRNA editing enzyme complex Source: HGNC
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic mRNA processing body Source: UniProtKB
    4. cytosol Source: Reactome
    5. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-259. 3 Publications
    Mutagenesisi67 – 671E → A: No effect on cytidine deaminase and antiviral activity. 3 Publications
    Mutagenesisi67 – 671E → Q: Decreases cytidine deaminase activity. 3 Publications
    Mutagenesisi81 – 811H → A: Decreases cytidine deaminase activity. 2 Publications
    Mutagenesisi85 – 851E → Q: Does not decrease cytidine deaminase activity. 1 Publication
    Mutagenesisi97 – 971C → A: Decreases cytidine deaminase activity. 2 Publications
    Mutagenesisi100 – 1001C → A or S: Decreases cytidine deaminase activity. 3 Publications
    Mutagenesisi128 – 1281D → K: Complete loss of VIF-induced degradation. 1 Publication
    Mutagenesisi213 – 2131R → A: Slightly reduces enzyme activity. 2 Publications
    Mutagenesisi213 – 2131R → E: Reduces enzyme activity. 2 Publications
    Mutagenesisi215 – 2151R → A or E: Abolishes enzyme activity. 2 Publications
    Mutagenesisi217 – 2171E → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-247. 1 Publication
    Mutagenesisi218 – 2181T → A: Loss of phosphorylation. No effect on cytidine deaminase activity or HIV-1 restriction activity. 1 Publication
    Mutagenesisi218 – 2181T → E: Phosphomimetic mutant which shows loss of cytidine deaminase activity and HIV-1 restriction activity. 1 Publication
    Mutagenesisi221 – 2211C → S: Does not decrease cytidine deaminase activity. 1 Publication
    Mutagenesisi244 – 2441N → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi247 – 2471P → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-217. 1 Publication
    Mutagenesisi256 – 2561R → E: Strongly reduces enzyme activity.
    Mutagenesisi257 – 2571H → A: Decreases cytidine deaminase activity. 2 Publications
    Mutagenesisi259 – 2591E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity. 4 Publications
    Mutagenesisi259 – 2591E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-67. 4 Publications
    Mutagenesisi259 – 2591E → Q: Decreases cytidine deaminase activity and antiviral activity. 4 Publications
    Mutagenesisi285 – 2851W → A: Abolishes enzyme activity. 2 Publications
    Mutagenesisi288 – 2881C → A: Decreases cytidine deaminase activity. 2 Publications
    Mutagenesisi291 – 2911C → A or S: Decreases cytidine deaminase activity. 3 Publications
    Mutagenesisi313 – 3131R → A or E: Abolishes enzyme activity. 1 Publication
    Mutagenesisi315 – 3151Y → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi320 – 3201R → A: Slightly reduces enzyme activity. 1 Publication
    Mutagenesisi320 – 3201R → E: Reduces enzyme activity. 1 Publication
    Mutagenesisi323 – 3231E → Q: Does not decrease cytidine deaminase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA24897.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 384384DNA dC->dU-editing enzyme APOBEC-3GPRO_0000171761Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321Phosphothreonine; by PKA2 Publications
    Modified residuei218 – 2181Phosphothreonine; by PKA and CAMK21 Publication

    Post-translational modificationi

    Ubiquitinated in the presence of HIV-1 VIF. Association with VIF targets the protein for proteolysis by the ubiquitin-dependent proteasome pathway.
    Phosphorylation at Thr-32 reduces its binding to HIV-1 VIF and subsequent ubiquitination and degradation thus promoting its antiviral activity.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9HC16.
    PaxDbiQ9HC16.
    PRIDEiQ9HC16.

    PTM databases

    PhosphoSiteiQ9HC16.

    Expressioni

    Tissue specificityi

    Expressed in spleen, testes, ovary and peripheral blood leukocytes and CD4+ lymphocytes. Also expressed in non-permissive peripheral blood mononuclear cells, and several tumor cell lines; no expression detected in permissive lymphoid and non-lymphoid cell lines. Exists only in the LMM form in peripheral blood-derived resting CD4 T-cells and monocytes, both of which are refractory to HIV-1 infection. LMM is converted to a HMM complex when resting CD4 T-cells are activated or when monocytes are induced to differentiate into macrophages. This change correlates with increased susceptibility of these cells to HIV-1 infection.3 Publications

    Inductioni

    Up-regulated by IFN-alpha.

    Gene expression databases

    ArrayExpressiQ9HC16.
    BgeeiQ9HC16.
    CleanExiHS_APOBEC3G.
    GenevestigatoriQ9HC16.

    Organism-specific databases

    HPAiHPA001812.

    Interactioni

    Subunit structurei

    Homodimer. Homooligomer. Can bind RNA to form ribonucleoprotein complexes of high-molecular-mass (HMM) or low-molecular-mass (LMM). HMM is inactive and heterogeneous in protein composition because of binding nonselectively to cellular RNAs, which in turn are associated with variety of cellular proteins. The LMM form which is enzymatically active has few or no RNAs associated. Its ability to form homooligomer is distinct from its ability to assemble into HMM. Interacts with APOBEC3B, APOBEC3F, MOV10, AGO2, EIF4E, EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent manner. Interacts with AGO1, AGO3 and PKA/PRKACA. Interacts with HIV-1 VIF and reverse transcriptase/ribonuclease H. Interacts with hepatitis B virus capsid protein.15 Publications

    Protein-protein interaction databases

    BioGridi121920. 11 interactions.
    128319. 5 interactions.
    DIPiDIP-37519N.
    IntActiQ9HC16. 2 interactions.
    MINTiMINT-1428867.
    STRINGi9606.ENSP00000385057.

    Structurei

    Secondary structure

    1
    384
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi195 – 1973
    Helixi199 – 2068
    Beta strandi213 – 2175
    Beta strandi219 – 22810
    Beta strandi231 – 2344
    Helixi236 – 2383
    Beta strandi240 – 2434
    Beta strandi247 – 2504
    Helixi258 – 2658
    Helixi266 – 2694
    Beta strandi273 – 2753
    Beta strandi277 – 2859
    Helixi289 – 30113
    Beta strandi305 – 3139
    Beta strandi318 – 3203
    Helixi321 – 33010
    Beta strandi334 – 3374
    Helixi340 – 35011
    Helixi364 – 37916

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JYWNMR-A198-384[»]
    2KBONMR-A193-384[»]
    2KEMNMR-A191-384[»]
    3E1UX-ray2.30A197-380[»]
    3IQSX-ray2.30A197-380[»]
    3IR2X-ray2.25A/B191-384[»]
    3V4JX-ray2.04A/B191-384[»]
    3V4KX-ray1.38A/B191-380[»]
    ProteinModelPortaliQ9HC16.
    SMRiQ9HC16. Positions 16-193, 197-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HC16.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 10036CMP/dCMP deaminase zinc-binding 1Add
    BLAST
    Domaini257 – 29135CMP/dCMP deaminase zinc-binding 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 6060Essential for cytoplasmic localizationAdd
    BLAST
    Regioni209 – 336128Necessary for homooligomerizationAdd
    BLAST
    Regioni213 – 2153Interaction with DNACurated
    Regioni313 – 3208Interaction with DNACurated

    Domaini

    The CMP/dCMP deaminase zinc-binding 1 domain mediates RNA binding, RNA-dependent oligomerization and virion incorporation whereas the CMP/dCMP deaminase zinc-binding 2 domain confers deoxycytidine deaminase activity and substrate sequence specificity.2 Publications

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG135704.
    HOVERGENiHBG050434.
    InParanoidiQ9HC16.
    KOiK01500.
    OMAiWDPDYQE.
    OrthoDBiEOG75QR3Z.
    PhylomeDBiQ9HC16.
    TreeFamiTF331356.

    Family and domain databases

    InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR013158. APOBEC_N.
    IPR016193. Cytidine_deaminase-like.
    [Graphical view]
    PfamiPF08210. APOBEC_N. 2 hits.
    [Graphical view]
    SUPFAMiSSF53927. SSF53927. 1 hit.
    PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HC16-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPPLD    50
    AKIFRGQVYS ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC 100
    TRDMATFLAE DPKVTLTIFV ARLYYFWDPD YQEALRSLCQ KRDGPRATMK 150
    IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK YYILLHIMLG EILRHSMDPP 200
    TFTFNFNNEP WVRGRHETYL CYEVERMHND TWVLLNQRRG FLCNQAPHKH 250
    GFLEGRHAEL CFLDVIPFWK LDLDQDYRVT CFTSWSPCFS CAQEMAKFIS 300
    KNKHVSLCIF TARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF 350
    VDHQGCPFQP WDGLDEHSQD LSGRLRAILQ NQEN 384
    Length:384
    Mass (Da):46,408
    Last modified:March 1, 2001 - v1
    Checksum:i60525DC3B7D903D6
    GO
    Isoform 3 (identifier: Q9HC16-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         58-79: VYSELKYHPEMRFFHWFSKWRK → VPPGLQSLCRQELSQLGKQTTH
         80-384: Missing.

    Note: May be due to a competing donor splice site.

    Show »
    Length:79
    Mass (Da):9,386
    Checksum:i359E8ACA44AB074A
    GO

    Sequence cautioni

    The sequence CAB45274.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621S → N no nucleotide entry (PubMed:14557625)Curated
    Sequence conflicti370 – 3701D → Y no nucleotide entry (PubMed:14557625)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti186 – 1861H → R.1 Publication
    Corresponds to variant rs8177832 [ dbSNP | Ensembl ].
    VAR_017837
    Natural varianti256 – 2561R → H.
    Corresponds to variant rs17000736 [ dbSNP | Ensembl ].
    VAR_048723
    Natural varianti275 – 2751Q → E.1 Publication
    Corresponds to variant rs17496046 [ dbSNP | Ensembl ].
    VAR_025060

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei58 – 7922VYSEL…SKWRK → VPPGLQSLCRQELSQLGKQT TH in isoform 3. 1 PublicationVSP_009588Add
    BLAST
    Alternative sequencei80 – 384305Missing in isoform 3. 1 PublicationVSP_009589Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK022802 mRNA. No translation available.
    AK315650 mRNA. Translation: BAG38016.1.
    AF182420 mRNA. Translation: AAG14956.1.
    CR456472 mRNA. Translation: CAG30358.1.
    DQ147772 Genomic DNA. Translation: AAZ38722.1.
    AL022318 Genomic DNA. Translation: CAB45274.1. Sequence problems.
    AL078641, AL022318 Genomic DNA. Translation: CAI21556.1.
    AL022318, AL078641 Genomic DNA. Translation: CAI17900.1.
    CH471095 Genomic DNA. Translation: EAW60292.1.
    BC024268 mRNA. Translation: AAH24268.1.
    BC061914 mRNA. Translation: AAH61914.1.
    CCDSiCCDS13984.1. [Q9HC16-1]
    RefSeqiNP_068594.1. NM_021822.3. [Q9HC16-1]
    UniGeneiHs.660143.

    Genome annotation databases

    EnsembliENST00000407997; ENSP00000385057; ENSG00000239713. [Q9HC16-1]
    ENST00000452957; ENSP00000413376; ENSG00000239713. [Q9HC16-1]
    GeneIDi60489.
    KEGGihsa:60489.
    UCSCiuc003awx.3. human. [Q9HC16-1]

    Polymorphism databases

    DMDMi44887683.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    Protein Spotlight

    Protein wars - Issue 45 of April 2004

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK022802 mRNA. No translation available.
    AK315650 mRNA. Translation: BAG38016.1 .
    AF182420 mRNA. Translation: AAG14956.1 .
    CR456472 mRNA. Translation: CAG30358.1 .
    DQ147772 Genomic DNA. Translation: AAZ38722.1 .
    AL022318 Genomic DNA. Translation: CAB45274.1 . Sequence problems.
    AL078641 , AL022318 Genomic DNA. Translation: CAI21556.1 .
    AL022318 , AL078641 Genomic DNA. Translation: CAI17900.1 .
    CH471095 Genomic DNA. Translation: EAW60292.1 .
    BC024268 mRNA. Translation: AAH24268.1 .
    BC061914 mRNA. Translation: AAH61914.1 .
    CCDSi CCDS13984.1. [Q9HC16-1 ]
    RefSeqi NP_068594.1. NM_021822.3. [Q9HC16-1 ]
    UniGenei Hs.660143.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JYW NMR - A 198-384 [» ]
    2KBO NMR - A 193-384 [» ]
    2KEM NMR - A 191-384 [» ]
    3E1U X-ray 2.30 A 197-380 [» ]
    3IQS X-ray 2.30 A 197-380 [» ]
    3IR2 X-ray 2.25 A/B 191-384 [» ]
    3V4J X-ray 2.04 A/B 191-384 [» ]
    3V4K X-ray 1.38 A/B 191-380 [» ]
    ProteinModelPortali Q9HC16.
    SMRi Q9HC16. Positions 16-193, 197-380.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121920. 11 interactions.
    128319. 5 interactions.
    DIPi DIP-37519N.
    IntActi Q9HC16. 2 interactions.
    MINTi MINT-1428867.
    STRINGi 9606.ENSP00000385057.

    Chemistry

    BindingDBi Q9HC16.
    ChEMBLi CHEMBL1741217.

    PTM databases

    PhosphoSitei Q9HC16.

    Polymorphism databases

    DMDMi 44887683.

    Proteomic databases

    MaxQBi Q9HC16.
    PaxDbi Q9HC16.
    PRIDEi Q9HC16.

    Protocols and materials databases

    DNASUi 200316.
    60489.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000407997 ; ENSP00000385057 ; ENSG00000239713 . [Q9HC16-1 ]
    ENST00000452957 ; ENSP00000413376 ; ENSG00000239713 . [Q9HC16-1 ]
    GeneIDi 60489.
    KEGGi hsa:60489.
    UCSCi uc003awx.3. human. [Q9HC16-1 ]

    Organism-specific databases

    CTDi 60489.
    GeneCardsi GC22P039437.
    HGNCi HGNC:17357. APOBEC3G.
    HPAi HPA001812.
    MIMi 607113. gene.
    neXtProti NX_Q9HC16.
    PharmGKBi PA24897.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG135704.
    HOVERGENi HBG050434.
    InParanoidi Q9HC16.
    KOi K01500.
    OMAi WDPDYQE.
    OrthoDBi EOG75QR3Z.
    PhylomeDBi Q9HC16.
    TreeFami TF331356.

    Enzyme and pathway databases

    BRENDAi 3.5.4.5. 2681.
    Reactomei REACT_9406. APOBEC3G mediated resistance to HIV-1 infection.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Miscellaneous databases

    ChiTaRSi APOBEC3G. human.
    EvolutionaryTracei Q9HC16.
    GeneWikii APOBEC3G.
    GenomeRNAii 60489.
    NextBioi 65375.
    PROi Q9HC16.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HC16.
    Bgeei Q9HC16.
    CleanExi HS_APOBEC3G.
    Genevestigatori Q9HC16.

    Family and domain databases

    InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR013158. APOBEC_N.
    IPR016193. Cytidine_deaminase-like.
    [Graphical view ]
    Pfami PF08210. APOBEC_N. 2 hits.
    [Graphical view ]
    SUPFAMi SSF53927. SSF53927. 1 hit.
    PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity."
      Kao S., Khan M.A., Miyagi E., Plishka R., Buckler-White A., Strebel K.
      J. Virol. 77:11398-11407(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN HIV-1 INFECTION INHIBITION.
      Tissue: Kidney.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Synovium and Teratocarcinoma.
    3. "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
      Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hematopoietic stem cell.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. SeattleSNPs program for genomic applications
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-186 AND GLU-275.
    6. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Skin and Uterus.
    9. "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22."
      Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J., Navaratnam N.
      Genomics 79:285-296(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY ORGANIZATION, TISSUE SPECIFICITY, SUBUNIT, RNA-BINDING, ZINC-BINDING.
    10. "Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein."
      Sheehy A.M., Gaddis N.C., Choi J.D., Malim M.H.
      Nature 418:646-650(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, FUNCTION IN HIV-1 INFECTION INHIBITION.
      Tissue: T-cell lymphoma.
    11. "Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts."
      Mangeat B., Turelli P., Caron G., Friedli M., Perrin L., Trono D.
      Nature 424:99-103(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION IN DNA C TO U EDITING, MUTAGENESIS OF GLU-67; HIS-81; GLU-85; CYS-97; CYS-100; CYS-221; HIS-257; GLU-259; CYS-288; CYS-291 AND GLU-323.
    12. Cited for: FUNCTION IN DNA C TO U EDITING, MLV INFECTION INHIBITION.
    13. "The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA."
      Zhang H., Yang B., Pomerantz R.J., Zhang C., Arunachalam S.C., Gao L.
      Nature 424:94-98(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION IN DNA C TO U EDITING, MUTAGENESIS OF HIS-81; CYS-97; CYS-100; HIS-257; CYS-288 AND CYS-291.
    14. Cited for: FUNCTION IN DNA C TO U EDITING, INTERACTION WITH VIF.
    15. "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."
      Shindo K., Takaori-Kondo A., Kobayashi M., Abudu A., Fukunaga K., Uchiyama T.
      J. Biol. Chem. 278:44412-44416(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA C TO U EDITING, INFECTION REGULATION OF HIV-1, MUTAGENESIS OF GLU-67; CYS-100; GLU-259 AND CYS-291.
      Tissue: T-cell lymphoma.
    16. "HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability."
      Stopak K., de Noronha C., Yonemoto W., Greene W.C.
      Mol. Cell 12:591-601(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VIF, PROTEASOME MEDIATED DEGRADATION, TRANSLATION INHIBITION.
    17. "HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation."
      Marin M., Rose K.M., Kozak S.L., Kabat D.
      Nat. Med. 9:1398-1403(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VIF, UBIQUITINATION.
    18. "The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif."
      Sheehy A.M., Gaddis N.C., Malim M.H.
      Nat. Med. 9:1404-1407(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA C TO U EDITING, UBIQUITINATION.
    19. "Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business."
      Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.
      Trends Genet. 19:207-216(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON APOBEC FAMILY.
    20. Cited for: REVIEW.
    21. "HIV-1 Vif: counteracting innate antiretroviral defenses."
      Cullen B.R.
      Mol. Ther. 8:525-527(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    22. "A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion."
      Xu H., Svarovskaia E.S., Barr R., Zhang Y., Khan M.A., Strebel K., Pathak V.K.
      Proc. Natl. Acad. Sci. U.S.A. 101:5652-5657(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-128.
    23. "Inhibition of hepatitis B virus replication by APOBEC3G."
      Turelli P., Mangeat B., Jost S., Vianin S., Trono D.
      Science 303:1829-1829(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HBV INHIBITION.
    24. "APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons."
      Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., Landau N.R., Weitzman M.D.
      Curr. Biol. 16:480-485(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RETROTRANSPOSITION, SUBCELLULAR LOCATION.
    25. "Reversed functional organization of mouse and human APOBEC3 cytidine deaminase domains."
      Hakata Y., Landau N.R.
      J. Biol. Chem. 281:36624-36631(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN CMP/DCMP DEAMINASE ZINC-BINDING, SUBUNIT, MUTAGENESIS OF GLU-67 AND GLU-259.
    26. Cited for: FUNCTION IN SFV RESTRICTION.
    27. "Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies."
      Wichroski M.J., Robb G.B., Rana T.M.
      PLoS Pathog. 2:E41-E41(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH APOBEC3F; AGO2; EIF4E; EIF4ENIF1; DCP2 AND DDX6.
    28. "The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements."
      Chiu Y.L., Greene W.C.
      Annu. Rev. Immunol. 26:317-353(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    29. "Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine deaminases as effectors in innate immunity against the hepatitis B virus."
      Bonvin M., Greeve J.
      Curr. Opin. Infect. Dis. 21:298-303(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION IN HBV RESTRICTION.
    30. "APOBEC3G subunits self-associate via the C-terminal deaminase domain."
      Bennett R.P., Salter J.D., Liu X., Wedekind J.E., Smith H.C.
      J. Biol. Chem. 283:33329-33336(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    31. "Two regions within the amino-terminal half of APOBEC3G cooperate to determine cytoplasmic localization."
      Stenglein M.D., Matsuo H., Harris R.S.
      J. Virol. 82:9591-9599(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    32. "Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif."
      Shirakawa K., Takaori-Kondo A., Yokoyama M., Izumi T., Matsui M., Io K., Sato T., Sato H., Uchiyama T.
      Nat. Struct. Mol. Biol. 15:1184-1191(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-32, INTERACTION WITH PRKACA.
    33. "Restriction of equine infectious anemia virus by equine APOBEC3 cytidine deaminases."
      Zielonka J., Bravo I.G., Marino D., Conrad E., Perkovic M., Battenberg M., Cichutek K., Muenk C.
      J. Virol. 83:7547-7559(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EIAV RESTRICTION.
    34. Cited for: REVIEW.
    35. "APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different mechanisms."
      Mbisa J.L., Bu W., Pathak V.K.
      J. Virol. 84:5250-5259(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HIV-1 RESTRICTION.
    36. "Inhibition of xenotropic murine leukemia virus-related virus by APOBEC3 proteins and antiviral drugs."
      Paprotka T., Venkatachari N.J., Chaipan C., Burdick R., Delviks-Frankenberry K.A., Hu W.S., Pathak V.K.
      J. Virol. 84:5719-5729(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN XMRV RESTRICTION.
    37. "Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes and tissues: implications for HIV-1 restriction."
      Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L., Harris R.S.
      Nucleic Acids Res. 38:4274-4284(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    38. "APOBEC3G directly binds Hepatitis B virus core protein in cell and cell free systems."
      Zhao D., Wang X., Lou G., Peng G., Li J., Zhu H., Chen F., Li S., Liu D., Chen Z., Yang Z.
      Virus Res. 151:213-219(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HEPATITIS B VIRUS CAPSID PROTEIN.
    39. "Phosphorylation directly regulates the intrinsic DNA cytidine deaminase activity of activation-induced deaminase and APOBEC3G protein."
      Demorest Z.L., Li M., Harris R.S.
      J. Biol. Chem. 286:26568-26575(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-32 AND THR-218, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-218.
    40. "Structure-function analyses point to a polynucleotide-accommodating groove essential for APOBEC3A restriction activities."
      Bulliard Y., Narvaiza I., Bertero A., Peddi S., Roehrig U.F., Ortiz M., Zoete V., Castro-Diaz N., Turelli P., Telenti A., Michielin O., Weitzman M.D., Trono D.
      J. Virol. 85:1765-1776(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HOST DEFENSE, MUTAGENESIS OF GLU-217 AND PRO-247.
    41. "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1."
      Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L., Brown W.L., Harris R.S.
      J. Virol. 85:11220-11234(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HIV-1 RESTRICTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
    42. Cited for: REVIEW.
    43. "Functional analysis of the two cytidine deaminase domains in APOBEC3G."
      Li X., Ma J., Zhang Q., Zhou J., Yin X., Zhai C., You X., Yu L., Guo F., Zhao L., Li Z., Zeng Y., Cen S.
      Virology 414:130-136(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN CMP/DCMP DEAMINASE ZINC-BINDING.
    44. "Antiviral mechanism and biochemical basis of the human APOBEC3 family."
      Imahashi M., Nakashima M., Iwatani Y.
      Front. Microbiol. 3:250-250(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    45. "Retroelements versus APOBEC3 family members: No great escape from the magnificent seven."
      Arias J.F., Koyama T., Kinomoto M., Tokunaga K.
      Front. Microbiol. 3:275-275(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    46. "APOBEC3G inhibits microRNA-mediated repression of translation by interfering with the interaction between Argonaute-2 and MOV10."
      Liu C., Zhang X., Huang F., Yang B., Li J., Liu B., Luo H., Zhang P., Zhang H.
      J. Biol. Chem. 287:29373-29383(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MOV10.
    47. "The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse transcriptase and inhibits its function during viral replication."
      Wang X., Ao Z., Chen L., Kobinger G., Peng J., Yao X.
      J. Virol. 86:3777-3786(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 REVERSE TRANSCRIPTASE/RIBONUCLEASE H.
    48. "HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies."
      Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.
      J. Virol. 86:11712-11724(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AGO1; AGO2 AND AGO3.
    49. "Endogenous origins of HIV-1 G-to-A hypermutation and restriction in the nonpermissive T cell line CEM2n."
      Refsland E.W., Hultquist J.F., Harris R.S.
      PLoS Pathog. 8:E1002800-E1002800(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HIV-1 RESTRICTION.
    50. "Emerging complexities of APOBEC3G action on immunity and viral fitness during HIV infection and treatment."
      Monajemi M., Woodworth C.F., Benkaroun J., Grant M., Larijani M.
      Retrovirology 9:35-35(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    51. Cited for: REVIEW.
    52. "APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and APOBEC3DE in human primary CD4+ t cells and macrophages."
      Chaipan C., Smith J.L., Hu W.S., Pathak V.K.
      J. Virol. 87:444-453(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HIV-1 RESTRICTION.
    53. "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."
      Gillick K., Pollpeter D., Phalora P., Kim E.Y., Wolinsky S.M., Malim M.H.
      J. Virol. 87:1508-1517(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HIV-1 RESTRICTION.
    54. "Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G."
      Chen K.M., Harjes E., Gross P.J., Fahmy A., Lu Y., Shindo K., Harris R.S., Matsuo H.
      Nature 452:116-119(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 198-384 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ARG-213; ARG-215; GLU-259; TRP-285; ARG-313 AND ARG-320.
    55. "Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications."
      Holden L.G., Prochnow C., Chang Y.P., Bransteitter R., Chelico L., Sen U., Stevens R.C., Goodman M.F., Chen X.S.
      Nature 456:121-124(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 197-380 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-213; ARG-215; ASN-244; TRP-285 AND TYR-315.
    56. "Structure, interaction and real-time monitoring of the enzymatic reaction of wild-type APOBEC3G."
      Furukawa A., Nagata T., Matsugami A., Habu Y., Sugiyama R., Hayashi F., Kobayashi N., Yokoyama S., Takaku H., Katahira M.
      EMBO J. 28:440-451(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 193-384 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY.
    57. Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 191-380.

    Entry informationi

    Entry nameiABC3G_HUMAN
    AccessioniPrimary (citable) accession number: Q9HC16
    Secondary accession number(s): B2RDR9
    , Q45F02, Q5TF77, Q7Z2N1, Q7Z2N4, Q9H9H8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Accumulation of APOBEC3G induced non-lethal hypermutation could contribute to the genetic variation of primate lentiviral populations.
    It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3