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Q9HC16 (ABC3G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA dC->dU-editing enzyme APOBEC-3G

EC=3.5.4.-
Alternative name(s):
APOBEC-related cytidine deaminase
Short name=APOBEC-related protein
Short name=ARCD
APOBEC-related protein 9
Short name=ARP-9
CEM-15
Short name=CEM15
Deoxycytidine deaminase
Short name=A3G
Gene names
Name:APOBEC3G
ORF Names:MDS019
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Protein existenceEvidence 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, AGO2, EIF4E, EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent manner. Interacts with AGO1, AGO3 and PKA/PRKACA. Interacts with HIV-1 VIF and reverse transcriptase/ribonuclease H. Interacts with hepatitis B virus capsid protein. 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. CytoplasmP-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 processAntiviral defense
Host-virus interaction
Immunity
Innate immunity
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA cytosine deamination

Inferred from direct assay Ref.24PubMed 16571802Ref.41. Source: UniProtKB

base conversion or substitution editing

Traceable author statement PubMed 17121840. Source: HGNC

cytidine deamination

Inferred from direct assay Ref.26. Source: UniProtKB

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 single stranded viral RNA replication via double stranded DNA intermediate

Inferred from direct assay PubMed 16571802Ref.41. Source: UniProtKB

negative regulation of transposition

Inferred from direct assay Ref.24. Source: UniProtKB

negative regulation of viral genome replication

Inferred from direct assay Ref.26. Source: UniProtKB

negative regulation of viral process

Inferred from direct assay PubMed 17121840. Source: HGNC

positive regulation of defense response to virus by host

Inferred from direct assay PubMed 17121840. Source: HGNC

viral process

Traceable author statement. Source: Reactome

   Cellular_componentapolipoprotein B mRNA editing enzyme complex

Traceable author statement PubMed 17121840. Source: HGNC

cytoplasm

Inferred from direct assay Ref.24Ref.27Ref.41. Source: UniProtKB

cytoplasmic mRNA processing body

Inferred from direct assay Ref.27Ref.48. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

ribonucleoprotein complex

Inferred from direct assay Ref.27. Source: UniProtKB

   Molecular_functionRNA 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 binding

Inferred from physical interaction Ref.27Ref.48. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384DNA dC->dU-editing enzyme APOBEC-3G
PRO_0000171761

Regions

Domain65 – 10036CMP/dCMP deaminase zinc-binding 1
Domain257 – 29135CMP/dCMP deaminase zinc-binding 2
Region1 – 6060Essential for cytoplasmic localization
Region209 – 336128Necessary for homooligomerization
Region213 – 2153Interaction with DNA Probable
Region313 – 3208Interaction with DNA Probable

Sites

Active site2591Proton donor Probable
Metal binding651Zinc By similarity
Metal binding971Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding2571Zinc; catalytic
Metal binding2881Zinc; catalytic
Metal binding2911Zinc; catalytic
Site2441Interaction with DNA Probable

Amino acid modifications

Modified residue321Phosphothreonine; by PKA Ref.32 Ref.39
Modified residue2181Phosphothreonine; by PKA and CAMK2 Ref.39

Natural variations

Alternative sequence58 – 7922VYSEL…SKWRK → VPPGLQSLCRQELSQLGKQT TH in isoform 3.
VSP_009588
Alternative sequence80 – 384305Missing in isoform 3.
VSP_009589
Natural variant1861H → R. Ref.5
Corresponds to variant rs8177832 [ dbSNP | Ensembl ].
VAR_017837
Natural variant2561R → H.
Corresponds to variant rs17000736 [ dbSNP | Ensembl ].
VAR_048723
Natural variant2751Q → E. Ref.5
Corresponds to variant rs17496046 [ dbSNP | Ensembl ].
VAR_025060

Experimental info

Mutagenesis671E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-259. Ref.11 Ref.15 Ref.25
Mutagenesis671E → A: No effect on cytidine deaminase and antiviral activity. Ref.11 Ref.15 Ref.25
Mutagenesis671E → Q: Decreases cytidine deaminase activity. Ref.11 Ref.15 Ref.25
Mutagenesis811H → A: Decreases cytidine deaminase activity. Ref.11 Ref.13
Mutagenesis851E → Q: Does not decrease cytidine deaminase activity. Ref.11
Mutagenesis971C → A: Decreases cytidine deaminase activity. Ref.11 Ref.13
Mutagenesis1001C → A or S: Decreases cytidine deaminase activity. Ref.11 Ref.13 Ref.15
Mutagenesis1281D → K: Complete loss of VIF-induced degradation. Ref.22
Mutagenesis2131R → A: Slightly reduces enzyme activity. Ref.54 Ref.55
Mutagenesis2131R → E: Reduces enzyme activity. Ref.54 Ref.55
Mutagenesis2151R → A or E: Abolishes enzyme activity. Ref.54 Ref.55
Mutagenesis2171E → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-247. Ref.40
Mutagenesis2181T → A: Loss of phosphorylation. No effect on cytidine deaminase activity or HIV-1 restriction activity. Ref.39
Mutagenesis2181T → E: Phosphomimetic mutant which shows loss of cytidine deaminase activity and HIV-1 restriction activity. Ref.39
Mutagenesis2211C → S: Does not decrease cytidine deaminase activity. Ref.11
Mutagenesis2441N → A: Abolishes enzyme activity. Ref.55
Mutagenesis2471P → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-217. Ref.40
Mutagenesis2561R → E: Strongly reduces enzyme activity.
Mutagenesis2571H → A: Decreases cytidine deaminase activity. Ref.11 Ref.13
Mutagenesis2591E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity. Ref.11 Ref.15 Ref.25 Ref.54
Mutagenesis2591E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-67.
Mutagenesis2591E → Q: Decreases cytidine deaminase activity and antiviral activity. Ref.11 Ref.15 Ref.25 Ref.54
Mutagenesis2851W → A: Abolishes enzyme activity. Ref.54 Ref.55
Mutagenesis2881C → A: Decreases cytidine deaminase activity. Ref.11 Ref.13
Mutagenesis2911C → A or S: Decreases cytidine deaminase activity. Ref.11 Ref.13 Ref.15
Mutagenesis3131R → A or E: Abolishes enzyme activity. Ref.54
Mutagenesis3151Y → A: Abolishes enzyme activity. Ref.55
Mutagenesis3201R → A: Slightly reduces enzyme activity. Ref.54
Mutagenesis3201R → E: Reduces enzyme activity. Ref.54
Mutagenesis3231E → Q: Does not decrease cytidine deaminase activity. Ref.11
Sequence conflict1621S → N no nucleotide entry Ref.1
Sequence conflict3701D → Y no nucleotide entry Ref.1

Secondary structure

..................................... 384
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 60525DC3B7D903D6

FASTA38446,408
        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 

« Hide

Isoform 3 [UniParc].

Checksum: 359E8ACA44AB074A
Show »

FASTA799,386

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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; AGO2; EIF4E; EIF4ENIF1; DCP2 AND DDX6.
[28]"The APOBEC3 cytidine deaminases: an innate defensive network opposing exogenous retroviruses and endogenous retroelements."
Chiu Y.L., Greene W.C.
Annu. Rev. Immunol. 26:317-353(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[29]"Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine deaminases as effectors in innate immunity against the hepatitis B virus."
Bonvin M., Greeve J.
Curr. Opin. Infect. Dis. 21:298-303(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN HBV RESTRICTION.
[30]"APOBEC3G subunits self-associate via the C-terminal deaminase domain."
Bennett R.P., Salter J.D., Liu X., Wedekind J.E., Smith H.C.
J. Biol. Chem. 283:33329-33336(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[31]"Two regions within the amino-terminal half of APOBEC3G cooperate to determine cytoplasmic localization."
Stenglein M.D., Matsuo H., Harris R.S.
J. Virol. 82:9591-9599(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[32]"Phosphorylation of APOBEC3G by protein kinase A regulates its interaction with HIV-1 Vif."
Shirakawa K., Takaori-Kondo A., Yokoyama M., Izumi T., Matsui M., Io K., Sato T., Sato H., Uchiyama T.
Nat. Struct. Mol. Biol. 15:1184-1191(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-32, INTERACTION WITH PRKACA.
[33]"Restriction of equine infectious anemia virus by equine APOBEC3 cytidine deaminases."
Zielonka J., Bravo I.G., Marino D., Conrad E., Perkovic M., Battenberg M., Cichutek K., Muenk C.
J. Virol. 83:7547-7559(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN EIAV RESTRICTION.
[34]"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 AGO1; AGO2 AND AGO3.
[49]"Endogenous origins of HIV-1 G-to-A hypermutation and restriction in the nonpermissive T cell line CEM2n."
Refsland E.W., Hultquist J.F., Harris R.S.
PLoS Pathog. 8:E1002800-E1002800(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN HIV-1 RESTRICTION.
[50]"Emerging complexities of APOBEC3G action on immunity and viral fitness during HIV infection and treatment."
Monajemi M., Woodworth C.F., Benkaroun J., Grant M., Larijani M.
Retrovirology 9:35-35(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[51]"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.
CCDSCCDS13984.1. [Q9HC16-1]
RefSeqNP_068594.1. NM_021822.3. [Q9HC16-1]
UniGeneHs.660143.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JYWNMR-A198-384[»]
2KBONMR-A193-384[»]
2KEMNMR-A191-384[»]
3E1UX-ray2.30A197-380[»]
3IQSX-ray2.30A197-380[»]
3IR2X-ray2.25A/B191-384[»]
3V4JX-ray2.04A/B191-384[»]
3V4KX-ray1.38A/B191-380[»]
ProteinModelPortalQ9HC16.
SMRQ9HC16. Positions 16-193, 197-380.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121920. 11 interactions.
128319. 5 interactions.
DIPDIP-37519N.
IntActQ9HC16. 2 interactions.
MINTMINT-1428867.
STRING9606.ENSP00000385057.

Chemistry

BindingDBQ9HC16.
ChEMBLCHEMBL1741217.

PTM databases

PhosphoSiteQ9HC16.

Polymorphism databases

DMDM44887683.

Proteomic databases

MaxQBQ9HC16.
PaxDbQ9HC16.
PRIDEQ9HC16.

Protocols and materials databases

DNASU200316.
60489.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000407997; ENSP00000385057; ENSG00000239713. [Q9HC16-1]
ENST00000452957; ENSP00000413376; ENSG00000239713. [Q9HC16-1]
GeneID60489.
KEGGhsa:60489.
UCSCuc003awx.3. human. [Q9HC16-1]

Organism-specific databases

CTD60489.
GeneCardsGC22P039437.
HGNCHGNC:17357. APOBEC3G.
HPAHPA001812.
MIM607113. gene.
neXtProtNX_Q9HC16.
PharmGKBPA24897.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG135704.
HOVERGENHBG050434.
InParanoidQ9HC16.
KOK01500.
OMAWDPDYQE.
OrthoDBEOG75QR3Z.
PhylomeDBQ9HC16.
TreeFamTF331356.

Enzyme and pathway databases

BRENDA3.5.4.5. 2681.
ReactomeREACT_116125. Disease.

Gene expression databases

ArrayExpressQ9HC16.
BgeeQ9HC16.
CleanExHS_APOBEC3G.
GenevestigatorQ9HC16.

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamPF08210. APOBEC_N. 2 hits.
[Graphical view]
SUPFAMSSF53927. SSF53927. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPOBEC3G. human.
EvolutionaryTraceQ9HC16.
GeneWikiAPOBEC3G.
GenomeRNAi60489.
NextBio65375.
PROQ9HC16.
SOURCESearch...

Entry information

Entry nameABC3G_HUMAN
AccessionPrimary (citable) accession number: Q9HC16
Secondary accession number(s): B2RDR9 expand/collapse secondary AC list , Q45F02, Q5TF77, Q7Z2N1, Q7Z2N4, Q9H9H8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM