Q9HC16 (ABC3G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA dC->dU-editing enzyme APOBEC-3G
EC=3.5.4.14

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 names

Name:	APOBEC3G
ORF Names:	MDS019

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.23 Ref.24 Ref.26 Ref.33 Ref.35 Ref.36 Ref.40 Ref.41 Ref.46 Ref.48 Ref.49 Ref.52 Ref.53 Ref.54
Catalytic activity	Deoxycytidine + H2O = deoxyuridine + NH3. Ref.13 Ref.54 Ref.55 Ref.56
Cofactor	Zinc.
Enzyme regulation	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. Ref.41
Subunit structure	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, EIF2C2/AGO2, EIF4E, EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent manner. Interacts with EIF2C1/AGO1, EIF2C3/AGO3 and PKA/PRKACA. Interacts with HIV-1 VIF and reverse transcriptase/ribonuclease H. Interacts with hepatitis B virus capsid protein. Ref.9 Ref.14 Ref.16 Ref.17 Ref.25 Ref.27 Ref.30 Ref.32 Ref.38 Ref.46 Ref.47 Ref.48
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › P-body. Note: Mainly cytoplasmic. Small amount are found in the nucleus. During HIV-1 infection, virion-encapsidated in absence of HIV-1 VIF. Ref.11 Ref.24 Ref.27 Ref.31 Ref.39 Ref.41 Ref.48
Tissue specificity	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. Ref.9 Ref.10 Ref.37
Induction	Up-regulated by IFN-alpha. Ref.15 Ref.41
Domain	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 (Ref.25). Ref.25 Ref.43
Post-translational modification	Ubiquitinated in the presence of HIV-1 VIF. Association with VIF targets the protein for proteolysis by the ubiquitin-dependent proteasome pathway. Ref.16 Ref.17 Ref.18 Phosphorylation at Thr-32 reduces its binding to HIV-1 VIF and subsequent ubiquitination and degradation thus promoting its antiviral activity.
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.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family. Contains 2 CMP/dCMP deaminase zinc-binding domains.
Sequence caution	The sequence CAB45274.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Antiviral defense Host-virus interaction Immunity Innate immunity
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA cytosine deamination Inferred from direct assay Ref.24PubMed 16571802Ref.41. Source: UniProtKB base conversion or substitution editing Traceable author statement PubMed 17121840. Source: HGNC defense response to virus Inferred from direct assay Ref.13Ref.41Ref.48. Source: UniProtKB innate immune response Inferred from direct assay PubMed 17121840. Source: HGNC negative regulation of retroviral genome replication Inferred from direct assay PubMed 16571802Ref.41. Source: UniProtKB negative regulation of transposition Inferred from direct assay Ref.24. Source: UniProtKB positive regulation of defense response to virus by host Inferred from direct assay PubMed 17121840. Source: HGNC viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	apolipoprotein B mRNA editing enzyme complex Traceable author statement PubMed 17121840. Source: HGNC cytoplasmic mRNA processing body Inferred from direct assay Ref.27Ref.48. Source: UniProtKB cytosol Traceable author statement. Source: Reactome mitochondrion Inferred from direct assay. Source: HPA
Molecular_function	RNA binding Inferred from direct assay Ref.9. Source: UniProtKB cytidine deaminase activity Traceable author statement PubMed 17121840. Source: HGNC deoxycytidine deaminase activity Inferred from direct assay Ref.13. Source: UniProtKB protein homodimerization activity Non-traceable author statement Ref.9. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.9. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9HC16-1)

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.

Isoform 3 (identifier: Q9HC16-3)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 384

384

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

PRO_0000171761

Regions

Domain

65 – 100

36

CMP/dCMP deaminase zinc-binding 1

Domain

257 – 291

35

CMP/dCMP deaminase zinc-binding 2

Region

1 – 60

60

Essential for cytoplasmic localization

Region

209 – 336

128

Necessary for homooligomerization

Region

213 – 215

3

Interaction with DNA Probable

Region

313 – 320

8

Interaction with DNA Probable

Sites

Active site

259

1

Proton donor Probable

Metal binding

65

1

Zinc By similarity

Metal binding

97

1

Zinc By similarity

Metal binding

100

1

Zinc By similarity

Metal binding

257

1

Zinc; catalytic

Metal binding

288

1

Zinc; catalytic

Metal binding

291

1

Zinc; catalytic

Site

244

1

Interaction with DNA Probable

Amino acid modifications

Modified residue

32

1

Phosphothreonine; by PKA Ref.32 Ref.39

Modified residue

218

1

Phosphothreonine; by PKA and CAMK2 Ref.39

Natural variations

Alternative sequence

58 – 79

22

VYSEL…SKWRK → VPPGLQSLCRQELSQLGKQT TH in isoform 3.

VSP_009588

Alternative sequence

80 – 384

305

Missing in isoform 3.

VSP_009589

Natural variant

186

1

H → R. Ref.5
Corresponds to variant rs8177832 [ dbSNP | Ensembl ].

VAR_017837

Natural variant

256

1

R → H.
Corresponds to variant rs17000736 [ dbSNP | Ensembl ].

VAR_048723

Natural variant

275

1

Q → E. Ref.5
Corresponds to variant rs17496046 [ dbSNP | Ensembl ].

VAR_025060

Experimental info

Mutagenesis

67

1

E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-259. Ref.11 Ref.15 Ref.25

Mutagenesis

67

1

E → A: No effect on cytidine deaminase and antiviral activity. Ref.11 Ref.15 Ref.25

Mutagenesis

67

1

E → Q: Decreases cytidine deaminase activity. Ref.11 Ref.15 Ref.25

Mutagenesis

81

1

H → A: Decreases cytidine deaminase activity. Ref.11 Ref.13

Mutagenesis

85

1

E → Q: Does not decrease cytidine deaminase activity. Ref.11

Mutagenesis

97

1

C → A: Decreases cytidine deaminase activity. Ref.11 Ref.13

Mutagenesis

100

1

C → A or S: Decreases cytidine deaminase activity. Ref.11 Ref.13 Ref.15

Mutagenesis

128

1

D → K: Complete loss of VIF-induced degradation. Ref.22

Mutagenesis

213

1

R → A: Slightly reduces enzyme activity. Ref.54 Ref.55

Mutagenesis

213

1

R → E: Reduces enzyme activity. Ref.54 Ref.55

Mutagenesis

215

1

R → A or E: Abolishes enzyme activity. Ref.54 Ref.55

Mutagenesis

217

1

E → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-247. Ref.40

Mutagenesis

218

1

T → A: Loss of phosphorylation. No effect on cytidine deaminase activity or HIV-1 restriction activity. Ref.39

Mutagenesis

218

1

T → E: Phosphomimetic mutant which shows loss of cytidine deaminase activity and HIV-1 restriction activity. Ref.39

Mutagenesis

221

1

C → S: Does not decrease cytidine deaminase activity. Ref.11

Mutagenesis

244

1

N → A: Abolishes enzyme activity. Ref.55

Mutagenesis

247

1

P → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-217. Ref.40

Mutagenesis

256

1

R → E: Strongly reduces enzyme activity.

Mutagenesis

257

1

H → A: Decreases cytidine deaminase activity. Ref.11 Ref.13

Mutagenesis

259

1

E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity. Ref.11 Ref.15 Ref.25 Ref.54

Mutagenesis

259

1

E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-67.

Mutagenesis

259

1

E → Q: Decreases cytidine deaminase activity and antiviral activity. Ref.11 Ref.15 Ref.25 Ref.54

Mutagenesis

285

1

W → A: Abolishes enzyme activity. Ref.54 Ref.55

Mutagenesis

288

1

C → A: Decreases cytidine deaminase activity. Ref.11 Ref.13

Mutagenesis

291

1

C → A or S: Decreases cytidine deaminase activity. Ref.11 Ref.13 Ref.15

Mutagenesis

313

1

R → A or E: Abolishes enzyme activity. Ref.54

Mutagenesis

315

1

Y → A: Abolishes enzyme activity. Ref.55

Mutagenesis

320

1

R → A: Slightly reduces enzyme activity. Ref.54

Mutagenesis

320

1

R → E: Reduces enzyme activity. Ref.54

Mutagenesis

323

1

E → Q: Does not decrease cytidine deaminase activity. Ref.11

Sequence conflict

162

1

S → N no nucleotide entry Ref.1

Sequence conflict

370

1

D → Y no nucleotide entry Ref.1

Secondary structure

1

.

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.

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.

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.

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384

Helix Strand Turn

Details...

Beta strand

195 – 197

3

Helix

199 – 206

8

Beta strand

213 – 217

5

Beta strand

219 – 228

10

Beta strand

231 – 234

4

Helix

236 – 238

3

Beta strand

240 – 243

4

Beta strand

247 – 250

4

Helix

258 – 265

8

Helix

266 – 269

4

Beta strand

273 – 275

3

Beta strand

277 – 285

9

Helix

289 – 301

13

Beta strand

305 – 313

9

Beta strand

318 – 320

3

Helix

321 – 330

10

Beta strand

334 – 337

4

Helix

340 – 350

11

Helix

364 – 379

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 60525DC3B7D903D6	FASTA	384	46,408
	10 20 30 40 50 60 MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPPLD AKIFRGQVYS 70 80 90 100 110 120 ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC TRDMATFLAE DPKVTLTIFV 130 140 150 160 170 180 ARLYYFWDPD YQEALRSLCQ KRDGPRATMK IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK 190 200 210 220 230 240 YYILLHIMLG EILRHSMDPP TFTFNFNNEP WVRGRHETYL CYEVERMHND TWVLLNQRRG 250 260 270 280 290 300 FLCNQAPHKH GFLEGRHAEL CFLDVIPFWK LDLDQDYRVT CFTSWSPCFS CAQEMAKFIS 310 320 330 340 350 360 KNKHVSLCIF TARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF VDHQGCPFQP 370 380 WDGLDEHSQD LSGRLRAILQ NQEN
	Isoform 3 [UniParc]. Checksum: 359E8ACA44AB074A	FASTA	79	9,386
	10 20 30 40 50 60 MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPPLD AKIFRGQVPP 70 GLQSLCRQEL SQLGKQTTH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"DNA deamination mediates innate immunity to retroviral infection." Harris R.S., Bishop K.N., Sheehy A.M., Craig H.M., Petersen-Mahrt S.K., Watt I.N., Neuberger M.S., Malim M.H. Cell 113:803-809(2003) [PubMed] [Europe PMC] [Abstract] 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]	"Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif." Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B., Muenk C., Nymark-McMahon H., Landau N.R. Cell 114:21-31(2003) [PubMed] [Europe PMC] [Abstract] 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]	"Death and the retrovirus." Vartanian J.P., Sommer P., Wain-Hobson S. Trends Mol. Med. 9:409-413(2003) [PubMed] [Europe PMC] [Abstract] 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]	"Restriction of foamy viruses by APOBEC cytidine deaminases." Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A., Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O. J. Virol. 80:605-614(2006) [PubMed] [Europe PMC] [Abstract] 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; EIF2C2; 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]	"APOBEC3G: an intracellular centurion." Chiu Y.L., Greene W.C. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 364:689-703(2009) [PubMed] [Europe PMC] [Abstract] 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]	"APOBEC3G: a double agent in defense." Smith H.C. Trends Biochem. Sci. 36:239-244(2011) [PubMed] [Europe PMC] [Abstract] 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 EIF2C1; EIF2C2 AND EIF2C3.
[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]	"Functions and regulation of the APOBEC family of proteins." Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M. Semin. Cell Dev. Biol. 23:258-268(2012) [PubMed] [Europe PMC] [Abstract] 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]	"First-in-class small molecule inhibitors of the single-strand DNA cytosine deaminase APOBEC3G." Li M., Shandilya S.M., Carpenter M.A., Rathore A., Brown W.L., Perkins A.L., Harki D.A., Solberg J., Hook D.J., Pandey K.K., Parniak M.A., Johnson J.R., Krogan N.J., Somasundaran M., Ali A., Schiffer C.A., Harris R.S. ACS Chem. Biol. 7:506-517(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 191-380.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Protein Spotlight

Protein wars - Issue 45 of April 2004

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00396656.
IPI00401132.

RefSeq

NP_001006667.1. NM_001006666.1.
NP_068594.1. NM_021822.3.

UniGene

Hs.659809.
Hs.660143.

3D structure databases

PDBe
RCSB PDB
PDBj

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	196-380	[»]
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	[»]

ProteinModelPortal

Q9HC16.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37519N.

IntAct

Q9HC16. 2 interactions.

MINT

MINT-1428867.

STRING

9606.ENSP00000385057.

PTM databases

PhosphoSite

Q9HC16.

Polymorphism databases

DMDM

44887683.

Proteomic databases

PaxDb

Q9HC16.

PRIDE

Q9HC16.

Protocols and materials databases

DNASU

200316.
60489.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000407997; ENSP00000385057; ENSG00000239713.
ENST00000452957; ENSP00000413376; ENSG00000239713.

GeneID

200316.
60489.

KEGG

hsa:200316.
hsa:60489.

UCSC

uc003awx.3. human.

Organism-specific databases

CTD

200316.
60489.

GeneCards

GC22P039437.

HGNC

HGNC:17357. APOBEC3G.

HPA

HPA001812.

MIM

607113. gene.

neXtProt

NX_Q9HC16.

PharmGKB

PA24897.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG135704.

HOVERGEN

HBG050434.

InParanoid

Q9HC16.

KO

K01500.

OMA

WDPDYQE.

OrthoDB

EOG480HX1.

PhylomeDB

Q9HC16.

Enzyme and pathway databases

BRENDA

3.5.4.5. 2681.

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q9HC16.

Bgee

Q9HC16.

CleanEx

HS_APOBEC3G.

Genevestigator

Q9HC16.

GermOnline

ENSG00000128394. Homo sapiens.

Family and domain databases

InterPro

IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR016193. Cytidine_deaminase-like.
[Graphical view]

Pfam

PF08210. APOBEC_N. 2 hits.
[Graphical view]

SUPFAM

SSF53927. Cytidine_deaminase-like. 1 hit.

PROSITE

PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9HC16.

ChEMBL

CHEMBL1741217.

ChiTaRS

APOBEC3G. human.

EvolutionaryTrace

Q9HC16.

NextBio

65375.

SOURCE

Search...

Entry information

Entry name

ABC3G_HUMAN

Accession

Primary (citable) accession number: Q9HC16
Secondary accession number(s): B2RDR9 , Q45F02, Q5TF77, Q7Z2N1, Q7Z2N4, Q9H9H8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.