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.-

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

Gene names

Name:	APOBEC3G
ORF Names:	MDS019

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

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

General annotation (Comments)

Function	DNA deaminase (cytidine deaminase) that mediates a form of innate resistance to retroviral infections (at least to HIV-1 infection) by triggering G-to-A hypermutation in the newly synthesized viral DNA. The replacements C-to-U in the minus strand DNA of HIV-1 during reverse transcription, leads to G-to-A transitions in the plus strand. The inhibition of viral replication is either due to the degradation of the minus strand before its integration or to the lethality of the hypermutations. Modification of both DNA strands is not excluded. This antiviral activity is neutralized by the virion infectivity factor (VIF), that prevents the incorporation of APOBEC3G into progeny HIV-1 virions by both inhibiting its translation and/or by inducing its ubiquitination and subsequent degradation by the 26S proteasome. May also prevent the transposition of a subset of retroelements. Binds a variety of RNAs, but does not display detectable APOB, NF1 and NAT1 mRNA editing. Ref.1 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.23 Ref.24 Ref.26
Catalytic activity	Cytidine + H2O = uridine + NH3.
Cofactor	Zinc.
Subunit structure	Homodimer. Interacts with APOBEC3B, APOBEC3F and HIV-1 VIF in a species specific manner. Ref.9 Ref.14 Ref.16 Ref.17
Subcellular location	Cytoplasm. Nucleus. 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
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. Ref.9 Ref.10 Ref.25
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
Miscellaneous	Inhibits also the infectivity of retroviral particles only distantly related to HIV-1, such as the simian immunodeficiency virus (SIV), the equine infectious anemia virus (EIAV) and the murine leukemia virus (MLV). HIV-1 does not replicate productively in non-human primates with the exception of the chimpanzee. The primates APOBEC3G (rhesus macaque, chimpanzee and African green monkey) are active against HIV-1 without VIF. Only the chimpanzee APOBEC3G is inhibited by HIV-1 VIF. 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.
Sequence caution	The sequence CAB45274.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Antiviral defense Host-virus interaction
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA cytosine deamination Inferred from direct assay Ref.24. Source: UniProtKB base conversion or substitution editing Traceable author statement. Source: HGNC innate immune response Inferred from direct assay. Source: HGNC interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of retroviral genome replication Inferred from direct assay. 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. Source: HGNC response to virus Inferred from electronic annotation. Source: UniProtKB-KW viral reproduction Traceable author statement. Source: Reactome
Cellular component	apolipoprotein B mRNA editing enzyme complex Traceable author statement. Source: HGNC 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. Source: HGNC 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

Sites

Active site

259

1

Proton donor By similarity

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 By similarity

Metal binding

288

1

Zinc By similarity

Metal binding

291

1

Zinc By similarity

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

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

217

1

E → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-247. Ref.26

Mutagenesis

221

1

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

Mutagenesis

247

1

P → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-217. Ref.26

Mutagenesis

257

1

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

Mutagenesis

259

1

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

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

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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384

Helix Strand Turn

Details...

Beta strand

205 – 209

5

Beta strand

213 – 217

5

Beta strand

221 – 228

8

Beta strand

231 – 233

3

Beta strand

243 – 245

3

Beta strand

247 – 250

4

Helix

259 – 269

11

Beta strand

276 – 282

7

Beta strand

284 – 286

3

Helix

289 – 300

12

Beta strand

301 – 303

3

Beta strand

305 – 311

7

Turn

319 – 321

3

Helix

322 – 331

10

Beta strand

334 – 337

4

Helix

340 – 350

11

Helix

363 – 380

18

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: 14557625] [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: 14702039] [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: 15461802] [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: 10591208] [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: 15489334] [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: 11863358] [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: 12167863] [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: 12808466] [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: 12809610] [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: 12808465] [Abstract] Cited for: 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: 12859895] [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: 12970355] [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: 14527406] [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: 14528301] [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: 14528300] [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: 12683974] [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: 14557052] [Abstract] Cited for: REVIEW.
[21]	"HIV-1 Vif: counteracting innate antiretroviral defenses." Cullen B.R. Mol. Ther. 8:525-527(2003) [PubMed: 14565218] [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: 15054139] [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: 15031497] [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: 16527742] [Abstract] Cited for: FUNCTION IN RETROTRANSPOSITION, SUBCELLULAR LOCATION.
[25]	"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: 20308164] [Abstract] Cited for: TISSUE SPECIFICITY.
[26]	"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: 21123384] [Abstract] Cited for: FUNCTION IN HOST DEFENSE, MUTAGENESIS OF GLU-217 AND PRO-247.
+	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	[»]

ProteinModelPortal

Q9HC16.

SMR

Q9HC16. Positions 10-195, 197-380.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37519N.

IntAct

Q9HC16. 2 interactions.

MINT

MINT-1428867.

STRING

Q9HC16.

PTM databases

PhosphoSite

Q9HC16.

Polymorphism databases

DMDM

44887683.

Proteomic databases

PRIDE

Q9HC16.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000407997; ENSP00000385057; ENSG00000239713.

GeneID

200316.
60489.

KEGG

hsa:200316.
hsa:60489.

UCSC

uc003awx.1. human.

Organism-specific databases

CTD

200316.
60489.

GeneCards

GC22P039437.

H-InvDB

HIX0018289.
HIX0080287.

HGNC

HGNC:17357. APOBEC3G.

HPA

HPA001812.

MIM

607113. gene.

neXtProt

NX_Q9HC16.

PharmGKB

PA24897.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04109.

GeneTree

ENSGT00530000062933.

HOVERGEN

HBG050434.

InParanoid

Q9HC16.

OMA

HPEMRFF.

OrthoDB

EOG480HX1.

PhylomeDB

Q9HC16.

Enzyme and pathway databases

BRENDA

3.5.4.5. 2681.

Reactome

REACT_6185. HIV Infection.

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.
IPR007904. APOBEC_C.
IPR013158. APOBEC_N.
IPR016193. Cytidine_deaminase-like.
[Graphical view]

KO

K01500.

Pfam

PF05240. APOBEC_C. 2 hits.
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

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:	January 25, 2012
This is version 102 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.