HUMAN:ABC3G

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	APOBEC3G
Protein Name(s)	DNA dC->dU-editing enzyme APOBEC-3G APOBEC-related cytidine deaminase APOBEC-related protein ARCD APOBEC-related protein 9 ARP-9 CEM-15 CEM15 Deoxycytidine deaminase A3G
External Links
UniProt	Q9HC16
EMBL	AK022802 AK315650 AF182420 CR456472 DQ147772 AL022318 AL078641 AL022318 AL022318 AL078641 CH471095 BC024268 BC061914
CCDS	CCDS13984.1
RefSeq	NP_068594.1
UniGene	Hs.660143
PDB	2JYW 2KBO 2KEM 3E1U 3IQS 3IR2 3V4J 3V4K
PDBsum	2JYW 2KBO 2KEM 3E1U 3IQS 3IR2 3V4J 3V4K
ProteinModelPortal	Q9HC16
SMR	Q9HC16
BioGrid	121920 128319
DIP	DIP-37519N
IntAct	Q9HC16
MINT	MINT-1428867
STRING	9606.ENSP00000385057
BindingDB	Q9HC16
ChEMBL	CHEMBL1741217
PhosphoSite	Q9HC16
DMDM	44887683
MaxQB	Q9HC16
PaxDb	Q9HC16
PRIDE	Q9HC16
DNASU	200316 60489
Ensembl	ENST00000407997 ENST00000452957
GeneID	60489
KEGG	hsa:60489
UCSC	uc003awx.3
CTD	60489
GeneCards	GC22P039437
HGNC	HGNC:17357
HPA	HPA001812
MIM	607113
neXtProt	NX_Q9HC16
PharmGKB	PA24897
eggNOG	NOG135704
GeneTree	ENSGT00530000062933
HOVERGEN	HBG050434
KO	K01500
OMA	WDPDYQE
OrthoDB	EOG75QR3Z
PhylomeDB	Q9HC16
TreeFam	TF331356
BRENDA	3.5.4.5
Reactome	REACT_9406 REACT_9453
ChiTaRS	APOBEC3G
EvolutionaryTrace	Q9HC16
GeneWiki	APOBEC3G
GenomeRNAi	60489
NextBio	65375
PRO	PR:Q9HC16
Proteomes	UP000005640
Bgee	Q9HC16
CleanEx	HS_APOBEC3G
ExpressionAtlas	Q9HC16
Genevestigator	Q9HC16
GO	GO:0030895 GO:0005737 GO:0000932 GO:0005829 GO:0030529 GO:0004126 GO:0047844 GO:0042803 GO:0003723 GO:0008270 GO:0016553 GO:0009972 GO:0051607 GO:0070383 GO:0045087 GO:0045869 GO:0010529 GO:0045071 GO:0048525 GO:0002230 GO:0016032
InterPro	IPR016192 IPR013158 IPR016193
Pfam	PF08210
SUPFAM	SSF53927
PROSITE	PS00903

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0045071	negative regulation of viral genome replication	PMID:17121840^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0048525	negative regulation of viral process	PMID:17121840^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045869	negative regulation of single stranded viral RNA replication via double stranded DNA intermediate	PMID:17121840^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	PMID:17121840^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0002230	positive regulation of defense response to virus by host	PMID:17121840^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0070383	DNA cytosine deamination	PMID:21835787^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0070383	DNA cytosine deamination	PMID:16571802^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0070383	DNA cytosine deamination	PMID:16527742^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	PMID:22915799^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	PMID:21835787^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	PMID:12808465^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0047844	deoxycytidine deaminase activity	PMID:12808465^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0045869	negative regulation of single stranded viral RNA replication via double stranded DNA intermediate	PMID:21835787^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045869	negative regulation of single stranded viral RNA replication via double stranded DNA intermediate	PMID:16571802^[3]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045071	negative regulation of viral genome replication	PMID:16378963^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:11863358^[8]	ECO:0000303	author statement without traceable support used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:16699599^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0010529	negative regulation of transposition	PMID:16527742^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009972	cytidine deamination	PMID:16378963^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:11863358^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21835787^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16699599^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16527742^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:11863358^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0000932	P-body	PMID:22915799^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0000932	P-body	PMID:16699599^[9]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0080111	DNA demethylation	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:103298 PANTHER:PTN000355219 UniProtKB:P31941 UniProtKB:Q8IUX4 UniProtKB:Q9GZX7 UniProtKB:Q9NRW3 UniProtKB:Q9Y235	P	Seeded From UniProt	complete
involved_in	GO:0016554	cytidine to uridine editing	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:103298 MGI:MGI:1343178 PANTHER:PTN000355219 RGD:2133 UniProtKB:Q9Y235	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1933111 PANTHER:PTN000355219 RGD:2133 UniProtKB:P31941 UniProtKB:P41238 UniProtKB:Q19Q52 UniProtKB:Q6NTF7 UniProtKB:Q7YR23 UniProtKB:Q8IUX4 UniProtKB:Q96AK3 UniProtKB:Q9GZX7 UniProtKB:Q9HC16 UniProtKB:Q9NRW3	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000355219 RGD:2133 UniProtKB:P31941 UniProtKB:Q6NTF7 UniProtKB:Q9GZX7 UniProtKB:Q9NRW3 UniProtKB:Q9UH17	C	Seeded From UniProt	complete
enables	GO:0004126	cytidine deaminase activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1342279 MGI:MGI:1343178 PANTHER:PTN000355219 RGD:2133 UniProtKB:P31941 UniProtKB:Q19Q52 UniProtKB:Q6NTF7 UniProtKB:Q8IUX4 UniProtKB:Q9GZX7 UniProtKB:Q9Y235	F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000355219 UniProtKB:Q8IUX4 UniProtKB:Q9HC16	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20152150^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HC16	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15152192^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9HC16	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016193	F	Seeded From UniProt	complete
enables	GO:0004126	cytidine deaminase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR040551	F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016192	F	Seeded From UniProt	complete
involved_in	GO:0016553	base conversion or substitution editing	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR040551	P	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016192	F	Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR040551	P	Seeded From UniProt	complete
part_of	GO:0030895	apolipoprotein B mRNA editing enzyme complex	PMID:17121840^[1]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0016553	base conversion or substitution editing	PMID:17121840^[1]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004126	cytidine deaminase activity	PMID:17121840^[1]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-180634 Reactome:R-HSA-180632 Reactome:R-HSA-180630 Reactome:R-HSA-180603 Reactome:R-HSA-180602 Reactome:R-HSA-180555 Reactome:R-HSA-180540	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
involved_in	GO:0051607	defense response to virus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0051	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
involved_in	GO:0002376	immune system process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0391	P	Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P	Seeded From UniProt	complete
involved_in	GO:0045087	innate immune response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0399	P	Seeded From UniProt	complete
part_of	GO:0000932	P-body	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0230	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 Holmes, RK et al. (2007) APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. J. Biol. Chem. 282 2587-95 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Hultquist, JF et al. (2011) Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1. J. Virol. 85 11220-34 PubMed GONUTS page
↑ ^3.0 ^3.1 OhAinle, M et al. (2006) Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H. J. Virol. 80 3853-62 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Chen, H et al. (2006) APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons. Curr. Biol. 16 480-5 PubMed GONUTS page
↑ ^5.0 ^5.1 Phalora, PK et al. (2012) HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies. J. Virol. 86 11712-24 PubMed GONUTS page
↑ ^6.0 ^6.1 Zhang, H et al. (2003) The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424 94-8 PubMed GONUTS page
↑ ^7.0 ^7.1 Delebecque, F et al. (2006) Restriction of foamy viruses by APOBEC cytidine deaminases. J. Virol. 80 605-14 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Jarmuz, A et al. (2002) An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics 79 285-96 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Wichroski, MJ et al. (2006) Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies. PLoS Pathog. 2 e41 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Shandilya, SM et al. (2010) Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces. Structure 18 28-38 PubMed GONUTS page
↑ Wiegand, HL et al. (2004) A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J. 23 2451-8 PubMed GONUTS page

[PMID:17121840-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 Holmes, RK et al. (2007) APOBEC3F can inhibit the accumulation of HIV-1 reverse transcription products in the absence of hypermutation. Comparisons with APOBEC3G. J. Biol. Chem. 282 2587-95 PubMed GONUTS page

[PMID:21835787-2] 2.0 ^2.1 ^2.2 ^2.3 Hultquist, JF et al. (2011) Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a conserved capacity to restrict Vif-deficient HIV-1. J. Virol. 85 11220-34 PubMed GONUTS page

[PMID:16571802-3] 3.0 ^3.1 OhAinle, M et al. (2006) Adaptive evolution and antiviral activity of the conserved mammalian cytidine deaminase APOBEC3H. J. Virol. 80 3853-62 PubMed GONUTS page

[PMID:16527742-4] 4.0 ^4.1 ^4.2 Chen, H et al. (2006) APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons. Curr. Biol. 16 480-5 PubMed GONUTS page

[PMID:22915799-5] 5.0 ^5.1 Phalora, PK et al. (2012) HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies. J. Virol. 86 11712-24 PubMed GONUTS page

[PMID:12808465-6] 6.0 ^6.1 Zhang, H et al. (2003) The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. Nature 424 94-8 PubMed GONUTS page

[PMID:16378963-7] 7.0 ^7.1 Delebecque, F et al. (2006) Restriction of foamy viruses by APOBEC cytidine deaminases. J. Virol. 80 605-14 PubMed GONUTS page

[PMID:11863358-8] 8.0 ^8.1 ^8.2 Jarmuz, A et al. (2002) An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics 79 285-96 PubMed GONUTS page

[PMID:16699599-9] 9.0 ^9.1 ^9.2 Wichroski, MJ et al. (2006) Human retroviral host restriction factors APOBEC3G and APOBEC3F localize to mRNA processing bodies. PLoS Pathog. 2 e41 PubMed GONUTS page

[PMID:21873635-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:20152150-11] Shandilya, SM et al. (2010) Crystal structure of the APOBEC3G catalytic domain reveals potential oligomerization interfaces. Structure 18 28-38 PubMed GONUTS page

[PMID:15152192-12] Wiegand, HL et al. (2004) A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J. 23 2451-8 PubMed GONUTS page

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HUMAN:ABC3G

Contents

Annotations

Notes

References

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