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Q9HC16

- ABC3G_HUMAN

UniProt

Q9HC16 - ABC3G_HUMAN

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Protein

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

Gene
APOBEC3G, MDS019
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 651Zinc By similarity
Metal bindingi97 – 971Zinc By similarity
Metal bindingi100 – 1001Zinc By similarity
Sitei244 – 2441Interaction with DNA Inferred
Metal bindingi257 – 2571Zinc; catalytic
Active sitei259 – 2591Proton donor Inferred
Metal bindingi288 – 2881Zinc; catalytic
Metal bindingi291 – 2911Zinc; catalytic

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
Complete GO annotation...

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.7 Publications

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
Complete GO annotation...

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.
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.3 Publications
Phosphorylation at Thr-32 reduces its binding to HIV-1 VIF and subsequent ubiquitination and degradation thus promoting its antiviral activity.

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.2 Publications

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.12 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.

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 DNA Inferred
Regioni313 – 3208Interaction with DNA Inferred

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 (1 Publication).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.

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. VSP_009588Add
BLAST
Alternative sequencei80 – 384305Missing in isoform 3. VSP_009589Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621S → N no nucleotide entry 1 Publication
Sequence conflicti370 – 3701D → Y no nucleotide entry 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 131 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

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