ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9HC16

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ABC3G_HUMAN
Primary accession number Q9HC16
Secondary accession numbers Q45F02 Q5TF77 Q7Z2N1 Q7Z2N4 Q9H9H8
Integrated into Swiss-Prot on March 1, 2004
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    July 1, 2008 (Entry version 64)
Name and origin of the protein
Protein name DNA dC->dU-editing enzyme APOBEC-3G
Synonyms EC 3.5.4.-
APOBEC-related cytidine deaminase
ARCD
APOBEC-related protein
ARP-9
CEM-15
CEM15
Gene name
Name: APOBEC3G
ORFNames: MDS019
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION IN HIV-1 INFECTION INHIBITION.
TISSUE=Kidney;
DOI=10.1128/JVI.77.21.11398-11407.2003; PubMed=14557625 [NCBI, ExPASy, EBI, Israel, Japan]
Kao S., Khan M.A., Miyagi E., Plishka R., Buckler-White A., Strebel K.;
"The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity.";
J. Virol. 77:11398-11407(2003).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hematopoietic stem cell;
Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
"Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Teratocarcinoma;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[5]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-186 AND GLU-275.
SeattleSNPs program for genomic applications;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Skin, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
 GENE FAMILY ORGANIZATION, TISSUE SPECIFICITY, SUBUNIT, RNA-BINDING, AND ZINC-BINDING.
DOI=10.1006/geno.2002.6718; PubMed=11863358 [NCBI, ExPASy, EBI, Israel, Japan]
Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J., Navaratnam N.;
"An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22.";
Genomics 79:285-296(2002).
[9]
 TISSUE SPECIFICITY, AND FUNCTION IN HIV-1 INFECTION INHIBITION.
TISSUE=T-cell lymphoma;
DOI=10.1038/nature00939; PubMed=12167863 [NCBI, ExPASy, EBI, Israel, Japan]
Sheehy A.M., Gaddis N.C., Choi J.D., Malim M.H.;
"Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein.";
Nature 418:646-650(2002).
[10]
 SUBCELLULAR LOCATION, FUNCTION IN DNA C TO U EDITING, AND 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.
DOI=10.1038/nature01709; PubMed=12808466 [NCBI, ExPASy, EBI, Israel, Japan]
Mangeat B., Turelli P., Caron G., Friedli M., Perrin L., Trono D.;
"Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts.";
Nature 424:99-103(2003).
[11]
 FUNCTION IN DNA C TO U EDITING, AND MLV INFECTION INHIBITION.
DOI=10.1016/S0092-8674(03)00423-9; PubMed=12809610 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"DNA deamination mediates innate immunity to retroviral infection.";
Cell 113:803-809(2003).
[12]
 FUNCTION IN DNA C TO U EDITING, AND MUTAGENESIS OF HIS-81; CYS-97; CYS-100; HIS-257; CYS-288 AND CYS-291.
DOI=10.1038/nature01707; PubMed=12808465 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang H., Yang B., Pomerantz R.J., Zhang C., Arunachalam S.C., Gao L.;
"The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA.";
Nature 424:94-98(2003).
[13]
 FUNCTION IN DNA C TO U EDITING, AND INTERACTION WITH VIF.
DOI=10.1016/S0092-8674(03)00515-4; PubMed=12859895 [NCBI, ExPASy, EBI, Israel, Japan]
Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B., Muenk C., Nymark-McMahon H., Landau N.R.;
"Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.";
Cell 114:21-31(2003).
[14]
 FUNCTION IN DNA C TO U EDITING, INFECTION REGULATION OF HIV-1, AND MUTAGENESIS OF GLU-67; CYS-100; GLU-259 AND CYS-291.
TISSUE=T-cell lymphoma;
DOI=10.1074/jbc.C300376200; PubMed=12970355 [NCBI, ExPASy, EBI, Israel, Japan]
Shindo K., Takaori-Kondo A., Kobayashi M., Abudu A., Fukunaga K., Uchiyama T.;
"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.";
J. Biol. Chem. 278:44412-44416(2003).
[15]
 INTERACTION WITH VIF, PROTEASOME MEDIATED DEGRADATION, AND TRANSLATION INHIBITION.
DOI=10.1016/S1097-2765(03)00353-8; PubMed=14527406 [NCBI, ExPASy, EBI, Israel, Japan]
Stopak K., de Noronha C., Yonemoto W., Greene W.C.;
"HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability.";
Mol. Cell 12:591-601(2003).
[16]
 INTERACTION WITH VIF, AND UBIQUITINATION.
DOI=10.1038/nm946; PubMed=14528301 [NCBI, ExPASy, EBI, Israel, Japan]
Marin M., Rose K.M., Kozak S.L., Kabat D.;
"HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation.";
Nat. Med. 9:1398-1403(2003).
[17]
 FUNCTION IN DNA C TO U EDITING, AND UBIQUITINATION.
DOI=10.1038/nm945; PubMed=14528300 [NCBI, ExPASy, EBI, Israel, Japan]
Sheehy A.M., Gaddis N.C., Malim M.H.;
"The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif.";
Nat. Med. 9:1404-1407(2003).
[18]
 REVIEW ON APOBEC FAMILY.
DOI=10.1016/S0168-9525(03)00054-4; PubMed=12683974 [NCBI, ExPASy, EBI, Israel, Japan]
Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.;
"Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business.";
Trends Genet. 19:207-216(2003).
[19]
 REVIEW.
DOI=10.1016/j.molmed.2003.08.008; PubMed=14557052 [NCBI, ExPASy, EBI, Israel, Japan]
Vartanian J.P., Sommer P., Wain-Hobson S.;
"Death and the retrovirus.";
Trends Mol. Med. 9:409-413(2003).
[20]
 REVIEW.
DOI=10.1016/j.ymthe.2003.08.010; PubMed=14565218 [NCBI, ExPASy, EBI, Israel, Japan]
Cullen B.R.;
"HIV-1 Vif: counteracting innate antiretroviral defenses.";
Mol. Ther. 8:525-527(2003).
[21]
 MUTAGENESIS OF ASP-128.
DOI=10.1073/pnas.0400830101; PubMed=15054139 [NCBI, ExPASy, EBI, Israel, Japan]
Xu H., Svarovskaia E.S., Barr R., Zhang Y., Khan M.A., Strebel K., Pathak V.K.;
"A single amino acid substitution in human APOBEC3G antiretroviral enzyme confers resistance to HIV-1 virion infectivity factor-induced depletion.";
Proc. Natl. Acad. Sci. U.S.A. 101:5652-5657(2004).
[22]
 FUNCTION IN HBV INHIBITION.
DOI=10.1126/science.1092066; PubMed=15031497 [NCBI, ExPASy, EBI, Israel, Japan]
Turelli P., Mangeat B., Jost S., Vianin S., Trono D.;
"Inhibition of hepatitis B virus replication by APOBEC3G.";
Science 303:1829-1829(2004).
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. APOBEC3G binds a variety of RNAs, but does not display detectable APOB, NF1 and NAT1 mRNA editing.
  • COFACTOR: Zinc.
  • SUBUNIT: Homodimer. Interacts with APOBEC3B, APOBEC3F and HIV-1 VIF in a species specific manner.
  • INTERACTION:
    P12504:vif (xeno); NbExp=1; IntAct=EBI-717839, EBI-779991;
  • 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.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ9HC16-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ9HC16-2
    Note: May be due to a competing donor and acceptor splice sites and intron retentions. No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_009587, VSP_009590.
    Name3
    Isoform IDQ9HC16-3
    Note: May be due to a competing donor splice site.
    Features which should be applied to build the isoform sequence: VSP_009588, VSP_009589.
  • 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.
  • PTM: Ubiquitinated in the presence of HIV-1 VIF. Association with VIF targets the protein for proteolysis by the ubiquitin-dependent proteasome pathway.
  • 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).
  • MISCELLANEOUS: HIV-1 does not replicate productively in nonhuman 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.
  • MISCELLANEOUS: Accumulation of APOBEC3G induced non-lethal hypermutation could contribute to the genetic variation of primate lentiviral populations.
  • MISCELLANEOUS: It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22.
  • SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family.
  • SEQUENCE CAUTION:
    • Sequence=CAB45274.1; Type=Erroneous gene model prediction;
  • WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/apobec3g/";.
  • WEB RESOURCE: Name=Protein Spotlight; Note=Protein wars - Issue 45 of April 2004; URL="http://www.expasy.org/spotlight/back_issues/sptlt045.shtml";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF182420; AAG14956.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK022802; BAB14251.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456472; CAG30358.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ147772; AAZ38722.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022318; CAB45274.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL078641; CAI21556.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022318; CAI21556.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022318; CAI17900.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL078641; CAI17900.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024268; AAH24268.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC061914; AAH61914.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_068594.1; -.
UniGene Hs.659991
3D structure databases
ModBase Q9HC16.
Protein-protein interaction databases
IntAct Q9HC16; -.
Enzyme and pathway databases
Reactome REACT_6185; HIV Infection.
Organism-specific databases
H-InvDB HIX0018289; -.
HIX0080287; -.
HGNC HGNC:17357; APOBEC3G.
GeneLynx APOBEC3G; Homo sapiens.
GenAtlas APOBEC3G.
HPA HPA001812; -.
MIM 607113; gene. [NCBI / EBI]
PharmGKB PA24897; -.
GeneCards Q9HC16.
Gene expression databases
ArrayExpress Q9HC16; -.
CleanEx HS_APOBEC3G; -.
GermOnline ENSG00000128394; Homo sapiens.
Ontologies
GO
GO:0030895; Cellular component: apolipoprotein B mRNA editing enzyme complex (traceable author statement from HGNC).
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0004126; Molecular function: cytidine deaminase activity (traceable author statement from HGNC).
GO:0042803; Molecular function: protein homodimerization activity (non-traceable author statement from UniProtKB).
GO:0003723; Molecular function: RNA binding (inferred from direct assay from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from direct assay from UniProtKB).
GO:0016553; Biological process: base conversion or substitution editing (traceable author statement from HGNC).
GO:0045087; Biological process: innate immune response (inferred from direct assay from HGNC).
GO:0045869; Biological process: negative regulation of retroviral genome replication (inferred from direct assay from HGNC).
GO:0002230; Biological process: positive regulation of defense response to virus by host (inferred from direct assay from HGNC).
GO:0006410; Biological process: transcription, RNA-dependent (inferred from direct assay from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR016192; APOBEC/CMP_deaminase_Zn-bd.
IPR007904; APOBEC_C.
IPR013158; APOBEC_N.
Graphical view of domain structure.
Pfam PF05240; APOBEC_C; 2.
PF08210; APOBEC_N; 2.
Pfam graphical view of domain structure.
PROSITE PS00903; CYT_DCMP_DEAMINASES; 1.
BLOCKS Q9HC16.
Genome annotation databases
Ensembl ENSG00000128394; Homo sapiens. [Contig view]
GeneID 60489; -.
KEGG hsa:60489; -.
Phylogenomic databases
HOGENOM Q9HC16; -.
HOVERGEN Q9HC16; -.
Other
LinkHub Q9HC16; -.
SOURCE APOBEC3G; Homo sapiens.
ProtoNet Q9HC16.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Antiviral defense; Cytoplasm; Host-virus interaction; Hydrolase; Metal-binding; Nucleus; Polymorphism; Ubl conjugation; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   384  384     DNA dC->dU-editing enzyme APOBEC-3G. PRO_0000171761
ACT_SITE   259   259        Proton donor (By similarity). 
METAL   65    65        Zinc (By similarity). 
METAL   97    97        Zinc (By similarity). 
METAL   100   100        Zinc (By similarity). 
METAL   257   257        Zinc (By similarity). 
METAL   288   288        Zinc (By similarity). 
METAL   291   291        Zinc (By similarity). 
VAR_SEQ   1    67        Missing (in isoform 2). VSP_009587
VAR_SEQ   58    79        VYSELKYHPEMRFFHWFSKWRK -> VPPGLQSLCRQELSQLGKQTTH (in isoform 3). VSP_009588
VAR_SEQ   80   384        Missing (in isoform 3). VSP_009589
VAR_SEQ   195   384        Missing (in isoform 2). VSP_009590
VARIANT   186   186  1     H -> R (in dbSNP:rs8177832 [NCBI]). VAR_017837 
VARIANT   275   275  1     Q -> E (in dbSNP:rs17496046 [NCBI]). VAR_025060 
MUTAGEN   67    67        E->Q: Decreases cytidine deaminase activity. 
MUTAGEN   81    81        H->A: Decreases cytidine deaminase activity. 
MUTAGEN   85    85        E->Q: Does not decrease cytidine deaminase activity. 
MUTAGEN   97    97        C->A: Decreases cytidine deaminase activity. 
MUTAGEN   100   100        C->A,S: Decreases cytidine deaminase activity. 
MUTAGEN   128   128        D->K: Complete loss of VIF-induced degradation. 
MUTAGEN   221   221        C->S: Does not decrease cytidine deaminase activity. 
MUTAGEN   257   257        H->A: Decreases cytidine deaminase activity. 
MUTAGEN   259   259        E->Q: Decreases cytidine deaminase activity. 
MUTAGEN   288   288        C->A: Decreases cytidine deaminase activity. 
MUTAGEN   291   291        C->A,S: Decreases cytidine deaminase activity. 
MUTAGEN   323   323        E->Q: Does not decrease cytidine deaminase activity. 
CONFLICT   162   162        S -> N (in Ref. 1). 
CONFLICT   370   370        D -> Y (in Ref. 1). 
Sequence information
Length: 384 AA [This is the length of the unprocessed precursor] Molecular weight: 46408 Da [This is the MW of the unprocessed precursor] CRC64: 60525DC3B7D903D6 [This is a checksum on the sequence] 
        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
Q9HC16 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland