Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

DNA dC->dU-editing enzyme APOBEC-3G (EC 3.5.4.-) (APOBEC-related cytidine deaminase) (APOBEC-related protein) (ARCD) (APOBEC-related protein 9) (ARP-9) (CEM-15) (CEM15) (Deoxycytidine deaminase) (A3G)

 ABC3G_HUMAN             Reviewed;         384 AA.
Q9HC16; B2RDR9; Q45F02; Q5TF77; Q7Z2N1; Q7Z2N4; Q9H9H8;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 161.
RecName: Full=DNA dC->dU-editing enzyme APOBEC-3G;
EC=3.5.4.-;
AltName: Full=APOBEC-related cytidine deaminase;
Short=APOBEC-related protein;
Short=ARCD;
AltName: Full=APOBEC-related protein 9;
Short=ARP-9;
AltName: Full=CEM-15;
Short=CEM15;
AltName: Full=Deoxycytidine deaminase;
Short=A3G;
Name=APOBEC3G; ORFNames=MDS019;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION IN HIV-1
INFECTION INHIBITION.
TISSUE=Kidney;
PubMed=14557625; DOI=10.1128/JVI.77.21.11398-11407.2003;
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=Synovium, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
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).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
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:R84.1-R84.11(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].
PubMed=10591208; DOI=10.1038/990031;
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 GENOMIC DNA].
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[9]
GENE FAMILY ORGANIZATION, TISSUE SPECIFICITY, SUBUNIT, RNA-BINDING,
AND ZINC-BINDING.
PubMed=11863358; DOI=10.1006/geno.2002.6718;
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).
[10]
TISSUE SPECIFICITY, AND FUNCTION IN HIV-1 INFECTION INHIBITION.
TISSUE=T-cell lymphoma;
PubMed=12167863; DOI=10.1038/nature00939;
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).
[11]
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.
PubMed=12808466; DOI=10.1038/nature01709;
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).
[12]
FUNCTION IN DNA C TO U EDITING, AND MLV INFECTION INHIBITION.
PubMed=12809610; DOI=10.1016/S0092-8674(03)00423-9;
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).
[13]
CATALYTIC ACTIVITY, FUNCTION IN DNA C TO U EDITING, AND MUTAGENESIS OF
HIS-81; CYS-97; CYS-100; HIS-257; CYS-288 AND CYS-291.
PubMed=12808465; DOI=10.1038/nature01707;
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).
[14]
FUNCTION IN DNA C TO U EDITING, AND INTERACTION WITH VIF.
PubMed=12859895; DOI=10.1016/S0092-8674(03)00515-4;
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).
[15]
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;
PubMed=12970355; DOI=10.1074/jbc.C300376200;
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).
[16]
INTERACTION WITH VIF, PROTEASOME MEDIATED DEGRADATION, AND TRANSLATION
INHIBITION.
PubMed=14527406; DOI=10.1016/S1097-2765(03)00353-8;
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).
[17]
INTERACTION WITH VIF, AND UBIQUITINATION.
PubMed=14528301; DOI=10.1038/nm946;
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).
[18]
FUNCTION IN DNA C TO U EDITING, AND UBIQUITINATION.
PubMed=14528300; DOI=10.1038/nm945;
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).
[19]
REVIEW ON APOBEC FAMILY.
PubMed=12683974; DOI=10.1016/S0168-9525(03)00054-4;
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).
[20]
REVIEW.
PubMed=14557052; DOI=10.1016/j.molmed.2003.08.008;
Vartanian J.P., Sommer P., Wain-Hobson S.;
"Death and the retrovirus.";
Trends Mol. Med. 9:409-413(2003).
[21]
REVIEW.
PubMed=14565218; DOI=10.1016/j.ymthe.2003.08.010;
Cullen B.R.;
"HIV-1 Vif: counteracting innate antiretroviral defenses.";
Mol. Ther. 8:525-527(2003).
[22]
MUTAGENESIS OF ASP-128.
PubMed=15054139; DOI=10.1073/pnas.0400830101;
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).
[23]
FUNCTION IN HBV INHIBITION.
PubMed=15031497; DOI=10.1126/science.1092066;
Turelli P., Mangeat B., Jost S., Vianin S., Trono D.;
"Inhibition of hepatitis B virus replication by APOBEC3G.";
Science 303:1829-1829(2004).
[24]
FUNCTION IN RETROTRANSPOSITION, AND SUBCELLULAR LOCATION.
PubMed=16527742; DOI=10.1016/j.cub.2006.01.031;
Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I.,
Landau N.R., Weitzman M.D.;
"APOBEC3A is a potent inhibitor of adeno-associated virus and
retrotransposons.";
Curr. Biol. 16:480-485(2006).
[25]
DOMAIN CMP/DCMP DEAMINASE, SUBUNIT, AND MUTAGENESIS OF GLU-67 AND
GLU-259.
PubMed=17020885; DOI=10.1074/jbc.M604980200;
Hakata Y., Landau N.R.;
"Reversed functional organization of mouse and human APOBEC3 cytidine
deaminase domains.";
J. Biol. Chem. 281:36624-36631(2006).
[26]
FUNCTION IN SFV RESTRICTION.
PubMed=16378963; DOI=10.1128/JVI.80.2.605-614.2006;
Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A.,
Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O.;
"Restriction of foamy viruses by APOBEC cytidine deaminases.";
J. Virol. 80:605-614(2006).
[27]
SUBCELLULAR LOCATION, AND INTERACTION WITH APOBEC3F; AGO2; EIF4E;
EIF4ENIF1; DCP2 AND DDX6.
PubMed=16699599; DOI=10.1371/journal.ppat.0020041;
Wichroski M.J., Robb G.B., Rana T.M.;
"Human retroviral host restriction factors APOBEC3G and APOBEC3F
localize to mRNA processing bodies.";
PLoS Pathog. 2:E41-E41(2006).
[28]
REVIEW.
PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350;
Chiu Y.L., Greene W.C.;
"The APOBEC3 cytidine deaminases: an innate defensive network opposing
exogenous retroviruses and endogenous retroelements.";
Annu. Rev. Immunol. 26:317-353(2008).
[29]
REVIEW ON FUNCTION IN HBV RESTRICTION.
PubMed=18448976; DOI=10.1097/QCO.0b013e3282fe1bb2;
Bonvin M., Greeve J.;
"Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine
deaminases as effectors in innate immunity against the hepatitis B
virus.";
Curr. Opin. Infect. Dis. 21:298-303(2008).
[30]
SUBUNIT.
PubMed=18842592; DOI=10.1074/jbc.M803726200;
Bennett R.P., Salter J.D., Liu X., Wedekind J.E., Smith H.C.;
"APOBEC3G subunits self-associate via the C-terminal deaminase
domain.";
J. Biol. Chem. 283:33329-33336(2008).
[31]
SUBCELLULAR LOCATION.
PubMed=18667511; DOI=10.1128/JVI.02471-07;
Stenglein M.D., Matsuo H., Harris R.S.;
"Two regions within the amino-terminal half of APOBEC3G cooperate to
determine cytoplasmic localization.";
J. Virol. 82:9591-9599(2008).
[32]
PHOSPHORYLATION AT THR-32, AND INTERACTION WITH PRKACA.
PubMed=18836454; DOI=10.1038/nsmb.1497;
Shirakawa K., Takaori-Kondo A., Yokoyama M., Izumi T., Matsui M.,
Io K., Sato T., Sato H., Uchiyama T.;
"Phosphorylation of APOBEC3G by protein kinase A regulates its
interaction with HIV-1 Vif.";
Nat. Struct. Mol. Biol. 15:1184-1191(2008).
[33]
FUNCTION IN EIAV RESTRICTION.
PubMed=19458006; DOI=10.1128/JVI.00015-09;
Zielonka J., Bravo I.G., Marino D., Conrad E., Perkovic M.,
Battenberg M., Cichutek K., Muenk C.;
"Restriction of equine infectious anemia virus by equine APOBEC3
cytidine deaminases.";
J. Virol. 83:7547-7559(2009).
[34]
REVIEW.
PubMed=19008196; DOI=10.1098/rstb.2008.0193;
Chiu Y.L., Greene W.C.;
"APOBEC3G: an intracellular centurion.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 364:689-703(2009).
[35]
FUNCTION IN HIV-1 RESTRICTION.
PubMed=20219927; DOI=10.1128/JVI.02358-09;
Mbisa J.L., Bu W., Pathak V.K.;
"APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different
mechanisms.";
J. Virol. 84:5250-5259(2010).
[36]
FUNCTION IN XMRV RESTRICTION.
PubMed=20335265; DOI=10.1128/JVI.00134-10;
Paprotka T., Venkatachari N.J., Chaipan C., Burdick R.,
Delviks-Frankenberry K.A., Hu W.S., Pathak V.K.;
"Inhibition of xenotropic murine leukemia virus-related virus by
APOBEC3 proteins and antiviral drugs.";
J. Virol. 84:5719-5729(2010).
[37]
TISSUE SPECIFICITY.
PubMed=20308164; DOI=10.1093/nar/gkq174;
Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L.,
Harris R.S.;
"Quantitative profiling of the full APOBEC3 mRNA repertoire in
lymphocytes and tissues: implications for HIV-1 restriction.";
Nucleic Acids Res. 38:4274-4284(2010).
[38]
INTERACTION WITH HEPATITIS B VIRUS CAPSID PROTEIN.
PubMed=20510315; DOI=10.1016/j.virusres.2010.05.009;
Zhao D., Wang X., Lou G., Peng G., Li J., Zhu H., Chen F., Li S.,
Liu D., Chen Z., Yang Z.;
"APOBEC3G directly binds Hepatitis B virus core protein in cell and
cell free systems.";
Virus Res. 151:213-219(2010).
[39]
PHOSPHORYLATION AT THR-32 AND THR-218, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF THR-218.
PubMed=21659520; DOI=10.1074/jbc.M111.235721;
Demorest Z.L., Li M., Harris R.S.;
"Phosphorylation directly regulates the intrinsic DNA cytidine
deaminase activity of activation-induced deaminase and APOBEC3G
protein.";
J. Biol. Chem. 286:26568-26575(2011).
[40]
FUNCTION IN HOST DEFENSE, AND MUTAGENESIS OF GLU-217 AND PRO-247.
PubMed=21123384; DOI=10.1128/JVI.01651-10;
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.;
"Structure-function analyses point to a polynucleotide-accommodating
groove essential for APOBEC3A restriction activities.";
J. Virol. 85:1765-1776(2011).
[41]
FUNCTION IN HIV-1 RESTRICTION, SUBCELLULAR LOCATION, AND ENZYME
REGULATION.
PubMed=21835787; DOI=10.1128/JVI.05238-11;
Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L.,
Brown W.L., Harris R.S.;
"Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H
demonstrate a conserved capacity to restrict Vif-deficient HIV-1.";
J. Virol. 85:11220-11234(2011).
[42]
REVIEW.
PubMed=21239176; DOI=10.1016/j.tibs.2010.12.003;
Smith H.C.;
"APOBEC3G: a double agent in defense.";
Trends Biochem. Sci. 36:239-244(2011).
[43]
DOMAIN CMP/DCMP DEAMINASE.
PubMed=21489586; DOI=10.1016/j.virol.2011.03.014;
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.;
"Functional analysis of the two cytidine deaminase domains in
APOBEC3G.";
Virology 414:130-136(2011).
[44]
REVIEW.
PubMed=22787460; DOI=10.3389/fmicb.2012.00250;
Imahashi M., Nakashima M., Iwatani Y.;
"Antiviral mechanism and biochemical basis of the human APOBEC3
family.";
Front. Microbiol. 3:250-250(2012).
[45]
REVIEW.
PubMed=22912627; DOI=10.3389/fmicb.2012.00275;
Arias J.F., Koyama T., Kinomoto M., Tokunaga K.;
"Retroelements versus APOBEC3 family members: No great escape from the
magnificent seven.";
Front. Microbiol. 3:275-275(2012).
[46]
FUNCTION, AND INTERACTION WITH MOV10.
PubMed=22791714; DOI=10.1074/jbc.M112.354001;
Liu C., Zhang X., Huang F., Yang B., Li J., Liu B., Luo H., Zhang P.,
Zhang H.;
"APOBEC3G inhibits microRNA-mediated repression of translation by
interfering with the interaction between Argonaute-2 and MOV10.";
J. Biol. Chem. 287:29373-29383(2012).
[47]
INTERACTION WITH HIV-1 REVERSE TRANSCRIPTASE/RIBONUCLEASE H.
PubMed=22301159; DOI=10.1128/JVI.06594-11;
Wang X., Ao Z., Chen L., Kobinger G., Peng J., Yao X.;
"The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse
transcriptase and inhibits its function during viral replication.";
J. Virol. 86:3777-3786(2012).
[48]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AGO1; AGO2 AND
AGO3.
PubMed=22915799; DOI=10.1128/JVI.00595-12;
Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.;
"HIV-1 replication and APOBEC3 antiviral activity are not regulated by
P bodies.";
J. Virol. 86:11712-11724(2012).
[49]
FUNCTION IN HIV-1 RESTRICTION.
PubMed=22807680; DOI=10.1371/journal.ppat.1002800;
Refsland E.W., Hultquist J.F., Harris R.S.;
"Endogenous origins of HIV-1 G-to-A hypermutation and restriction in
the nonpermissive T cell line CEM2n.";
PLoS Pathog. 8:E1002800-E1002800(2012).
[50]
REVIEW.
PubMed=22546055; DOI=10.1186/1742-4690-9-35;
Monajemi M., Woodworth C.F., Benkaroun J., Grant M., Larijani M.;
"Emerging complexities of APOBEC3G action on immunity and viral
fitness during HIV infection and treatment.";
Retrovirology 9:35-35(2012).
[51]
REVIEW.
PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004;
Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.;
"Functions and regulation of the APOBEC family of proteins.";
Semin. Cell Dev. Biol. 23:258-268(2012).
[52]
FUNCTION IN HIV-1 RESTRICTION.
PubMed=23097438; DOI=10.1128/JVI.00676-12;
Chaipan C., Smith J.L., Hu W.S., Pathak V.K.;
"APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and
APOBEC3DE in human primary CD4+ t cells and macrophages.";
J. Virol. 87:444-453(2013).
[53]
FUNCTION IN HIV-1 RESTRICTION.
PubMed=23152537; DOI=10.1128/JVI.02587-12;
Gillick K., Pollpeter D., Phalora P., Kim E.Y., Wolinsky S.M.,
Malim M.H.;
"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.";
J. Virol. 87:1508-1517(2013).
[54]
STRUCTURE BY NMR OF 198-384 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY,
FUNCTION, AND MUTAGENESIS OF ARG-213; ARG-215; GLU-259; TRP-285;
ARG-313 AND ARG-320.
PubMed=18288108; DOI=10.1038/nature06638;
Chen K.M., Harjes E., Gross P.J., Fahmy A., Lu Y., Shindo K.,
Harris R.S., Matsuo H.;
"Structure of the DNA deaminase domain of the HIV-1 restriction factor
APOBEC3G.";
Nature 452:116-119(2008).
[55]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 197-380 IN COMPLEX WITH
ZINC, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-213; ARG-215;
ASN-244; TRP-285 AND TYR-315.
PubMed=18849968; DOI=10.1038/nature07357;
Holden L.G., Prochnow C., Chang Y.P., Bransteitter R., Chelico L.,
Sen U., Stevens R.C., Goodman M.F., Chen X.S.;
"Crystal structure of the anti-viral APOBEC3G catalytic domain and
functional implications.";
Nature 456:121-124(2008).
[56]
STRUCTURE BY NMR OF 193-384 IN COMPLEX WITH ZINC, AND CATALYTIC
ACTIVITY.
PubMed=19153609; DOI=10.1038/emboj.2008.290;
Furukawa A., Nagata T., Matsugami A., Habu Y., Sugiyama R.,
Hayashi F., Kobayashi N., Yokoyama S., Takaku H., Katahira M.;
"Structure, interaction and real-time monitoring of the enzymatic
reaction of wild-type APOBEC3G.";
EMBO J. 28:440-451(2009).
[57]
X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 191-380.
PubMed=22181350; DOI=10.1021/cb200440y;
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.;
"First-in-class small molecule inhibitors of the single-strand DNA
cytosine deaminase APOBEC3G.";
ACS Chem. Biol. 7:506-517(2012).
-!- 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. {ECO:0000269|PubMed:12167863,
ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:12808466,
ECO:0000269|PubMed:12809610, ECO:0000269|PubMed:12859895,
ECO:0000269|PubMed:12970355, ECO:0000269|PubMed:14528300,
ECO:0000269|PubMed:14557625, ECO:0000269|PubMed:15031497,
ECO:0000269|PubMed:16378963, ECO:0000269|PubMed:16527742,
ECO:0000269|PubMed:18288108, ECO:0000269|PubMed:19458006,
ECO:0000269|PubMed:20219927, ECO:0000269|PubMed:20335265,
ECO:0000269|PubMed:21123384, ECO:0000269|PubMed:21835787,
ECO:0000269|PubMed:22791714, ECO:0000269|PubMed:22807680,
ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23097438,
ECO:0000269|PubMed:23152537}.
-!- CATALYTIC ACTIVITY: Deoxycytidine + H(2)O = deoxyuridine + NH(3).
{ECO:0000269|PubMed:12808465, ECO:0000269|PubMed:18288108,
ECO:0000269|PubMed:18849968, ECO:0000269|PubMed:19153609}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
-!- 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. {ECO:0000269|PubMed:21835787}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:11863358,
ECO:0000269|PubMed:12859895, ECO:0000269|PubMed:14527406,
ECO:0000269|PubMed:14528301, ECO:0000269|PubMed:16699599,
ECO:0000269|PubMed:17020885, ECO:0000269|PubMed:18288108,
ECO:0000269|PubMed:18836454, ECO:0000269|PubMed:18842592,
ECO:0000269|PubMed:18849968, ECO:0000269|PubMed:19153609,
ECO:0000269|PubMed:20510315, ECO:0000269|PubMed:22301159,
ECO:0000269|PubMed:22791714, ECO:0000269|PubMed:22915799}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-717839, EBI-717839;
P17612:PRKACA; NbExp=6; IntAct=EBI-717839, EBI-476586;
P69723:vif (xeno); NbExp=3; IntAct=EBI-717839, EBI-15528966;
Q77YG0:vif (xeno); NbExp=2; IntAct=EBI-717839, EBI-15731903;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9HC16-1; Sequence=Displayed;
Name=3;
IsoId=Q9HC16-3; Sequence=VSP_009588, VSP_009589;
Note=May be due to a competing donor splice site.;
-!- 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. {ECO:0000269|PubMed:11863358,
ECO:0000269|PubMed:12167863, ECO:0000269|PubMed:20308164}.
-!- INDUCTION: Up-regulated by IFN-alpha.
-!- DOMAIN: The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA-
dependent oligomerization and virion incorporation whereas the
CMP/dCMP deaminase domain 2 confers deoxycytidine deaminase
activity and substrate sequence specificity.
{ECO:0000269|PubMed:17020885, ECO:0000269|PubMed:21489586}.
-!- PTM: Ubiquitinated in the presence of HIV-1 VIF. Association with
VIF targets the protein for proteolysis by the ubiquitin-dependent
proteasome pathway.
-!- PTM: Phosphorylation at Thr-32 reduces its binding to HIV-1 VIF
and subsequent ubiquitination and degradation thus promoting its
antiviral activity. {ECO:0000269|PubMed:18836454,
ECO:0000269|PubMed:21659520}.
-!- 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. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB45274.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- 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="https://web.expasy.org/spotlight/back_issues/045";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK022802; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK315650; BAG38016.1; -; mRNA.
EMBL; AF182420; AAG14956.1; -; mRNA.
EMBL; CR456472; CAG30358.1; -; mRNA.
EMBL; DQ147772; AAZ38722.1; -; Genomic_DNA.
EMBL; AL022318; CAB45274.1; ALT_SEQ; Genomic_DNA.
EMBL; AL078641; CAI21556.1; -; Genomic_DNA.
EMBL; AL022318; CAI21556.1; JOINED; Genomic_DNA.
EMBL; AL022318; CAI17900.1; -; Genomic_DNA.
EMBL; AL078641; CAI17900.1; JOINED; Genomic_DNA.
EMBL; CH471095; EAW60292.1; -; Genomic_DNA.
EMBL; BC024268; AAH24268.1; -; mRNA.
EMBL; BC061914; AAH61914.1; -; mRNA.
CCDS; CCDS13984.1; -. [Q9HC16-1]
RefSeq; NP_068594.1; NM_021822.3. [Q9HC16-1]
UniGene; Hs.660143; -.
PDB; 2JYW; NMR; -; A=198-384.
PDB; 2KBO; NMR; -; A=193-384.
PDB; 2KEM; NMR; -; A=191-384.
PDB; 3E1U; X-ray; 2.30 A; A=197-380.
PDB; 3IQS; X-ray; 2.30 A; A=197-380.
PDB; 3IR2; X-ray; 2.25 A; A/B=191-384.
PDB; 3V4J; X-ray; 2.04 A; A/B=191-384.
PDB; 3V4K; X-ray; 1.38 A; A/B=191-380.
PDB; 4ROV; X-ray; 1.80 A; A/B=193-384.
PDB; 4ROW; X-ray; 1.70 A; A=193-384.
PDBsum; 2JYW; -.
PDBsum; 2KBO; -.
PDBsum; 2KEM; -.
PDBsum; 3E1U; -.
PDBsum; 3IQS; -.
PDBsum; 3IR2; -.
PDBsum; 3V4J; -.
PDBsum; 3V4K; -.
PDBsum; 4ROV; -.
PDBsum; 4ROW; -.
ProteinModelPortal; Q9HC16; -.
SMR; Q9HC16; -.
BioGrid; 121920; 12.
DIP; DIP-37519N; -.
IntAct; Q9HC16; 9.
MINT; MINT-1428867; -.
STRING; 9606.ENSP00000385057; -.
BindingDB; Q9HC16; -.
ChEMBL; CHEMBL1741217; -.
iPTMnet; Q9HC16; -.
PhosphoSitePlus; Q9HC16; -.
BioMuta; APOBEC3G; -.
DMDM; 44887683; -.
EPD; Q9HC16; -.
MaxQB; Q9HC16; -.
PaxDb; Q9HC16; -.
PeptideAtlas; Q9HC16; -.
PRIDE; Q9HC16; -.
DNASU; 200316; -.
DNASU; 60489; -.
Ensembl; ENST00000407997; ENSP00000385057; ENSG00000239713. [Q9HC16-1]
GeneID; 60489; -.
KEGG; hsa:60489; -.
UCSC; uc003awx.3; human. [Q9HC16-1]
CTD; 60489; -.
DisGeNET; 60489; -.
EuPathDB; HostDB:ENSG00000239713.7; -.
GeneCards; APOBEC3G; -.
HGNC; HGNC:17357; APOBEC3G.
HPA; HPA001812; -.
HPA; HPA073637; -.
MIM; 607113; gene.
neXtProt; NX_Q9HC16; -.
OpenTargets; ENSG00000239713; -.
PharmGKB; PA24897; -.
eggNOG; ENOG410JBA1; Eukaryota.
eggNOG; ENOG41119MS; LUCA.
GeneTree; ENSGT00530000062933; -.
HOVERGEN; HBG050434; -.
KO; K18750; -.
OMA; ISFWKLD; -.
OrthoDB; EOG091G07EI; -.
PhylomeDB; Q9HC16; -.
TreeFam; TF331356; -.
BRENDA; 3.5.4.B9; 2681.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
SIGNOR; Q9HC16; -.
ChiTaRS; APOBEC3G; human.
EvolutionaryTrace; Q9HC16; -.
GeneWiki; APOBEC3G; -.
GenomeRNAi; 60489; -.
PRO; PR:Q9HC16; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000239713; -.
CleanEx; HS_APOBEC3G; -.
Genevisible; Q9HC16; HS.
GO; GO:0030895; C:apolipoprotein B mRNA editing enzyme complex; TAS:HGNC.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IDA:UniProtKB.
GO; GO:0004126; F:cytidine deaminase activity; TAS:HGNC.
GO; GO:0008829; F:dCTP deaminase activity; TAS:Reactome.
GO; GO:0047844; F:deoxycytidine deaminase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; NAS:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0016553; P:base conversion or substitution editing; TAS:HGNC.
GO; GO:0009972; P:cytidine deamination; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0070383; P:DNA cytosine deamination; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IDA:HGNC.
GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB.
GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0048525; P:negative regulation of viral process; IDA:HGNC.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:HGNC.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
InterPro; IPR013158; APOBEC_N.
InterPro; IPR002125; CMP_dCMP_dom.
InterPro; IPR016193; Cytidine_deaminase-like.
Pfam; PF08210; APOBEC_N; 2.
SUPFAM; SSF53927; SSF53927; 1.
PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antiviral defense;
Complete proteome; Cytoplasm; Host-virus interaction; Hydrolase;
Immunity; Innate immunity; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Ubl conjugation; Zinc.
CHAIN 1 384 DNA dC->dU-editing enzyme APOBEC-3G.
/FTId=PRO_0000171761.
DOMAIN 29 138 CMP/dCMP-type deaminase 1.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
DOMAIN 214 328 CMP/dCMP-type deaminase 2.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
REGION 1 60 Essential for cytoplasmic localization.
REGION 209 336 Necessary for homooligomerization.
REGION 213 215 Interaction with DNA. {ECO:0000305}.
REGION 313 320 Interaction with DNA. {ECO:0000305}.
ACT_SITE 259 259 Proton donor. {ECO:0000305}.
METAL 65 65 Zinc. {ECO:0000250}.
METAL 97 97 Zinc. {ECO:0000250}.
METAL 100 100 Zinc. {ECO:0000250}.
METAL 257 257 Zinc; catalytic.
{ECO:0000269|PubMed:18288108,
ECO:0000269|PubMed:18849968,
ECO:0000269|PubMed:19153609}.
METAL 288 288 Zinc; catalytic.
{ECO:0000269|PubMed:18288108,
ECO:0000269|PubMed:18849968,
ECO:0000269|PubMed:19153609}.
METAL 291 291 Zinc; catalytic.
{ECO:0000269|PubMed:18288108,
ECO:0000269|PubMed:18849968,
ECO:0000269|PubMed:19153609}.
SITE 244 244 Interaction with DNA. {ECO:0000305}.
MOD_RES 32 32 Phosphothreonine; by PKA.
{ECO:0000269|PubMed:18836454,
ECO:0000269|PubMed:21659520}.
MOD_RES 218 218 Phosphothreonine; by PKA and CAMK2.
{ECO:0000269|PubMed:21659520}.
VAR_SEQ 58 79 VYSELKYHPEMRFFHWFSKWRK -> VPPGLQSLCRQELSQ
LGKQTTH (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009588.
VAR_SEQ 80 384 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_009589.
VARIANT 186 186 H -> R (in dbSNP:rs8177832).
{ECO:0000269|Ref.5}.
/FTId=VAR_017837.
VARIANT 256 256 R -> H (in dbSNP:rs17000736).
/FTId=VAR_048723.
VARIANT 275 275 Q -> E (in dbSNP:rs17496046).
{ECO:0000269|Ref.5}.
/FTId=VAR_025060.
MUTAGEN 67 67 E->A: Loss of cytidine deaminase activity
and significant decrease in antiviral
activity; when associated with A-259.
{ECO:0000269|PubMed:12808466,
ECO:0000269|PubMed:12970355,
ECO:0000269|PubMed:17020885}.
MUTAGEN 67 67 E->A: No effect on cytidine deaminase and
antiviral activity.
{ECO:0000269|PubMed:12808466,
ECO:0000269|PubMed:12970355,
ECO:0000269|PubMed:17020885}.
MUTAGEN 67 67 E->Q: Decreases cytidine deaminase
activity. {ECO:0000269|PubMed:12808466,
ECO:0000269|PubMed:12970355,
ECO:0000269|PubMed:17020885}.
MUTAGEN 81 81 H->A: Decreases cytidine deaminase
activity. {ECO:0000269|PubMed:12808465,
ECO:0000269|PubMed:12808466}.
MUTAGEN 85 85 E->Q: Does not decrease cytidine
deaminase activity.
{ECO:0000269|PubMed:12808466}.
MUTAGEN 97 97 C->A: Decreases cytidine deaminase
activity. {ECO:0000269|PubMed:12808465,
ECO:0000269|PubMed:12808466}.
MUTAGEN 100 100 C->A,S: Decreases cytidine deaminase
activity. {ECO:0000269|PubMed:12808465,
ECO:0000269|PubMed:12808466,
ECO:0000269|PubMed:12970355}.
MUTAGEN 128 128 D->K: Complete loss of VIF-induced
degradation.
{ECO:0000269|PubMed:15054139}.
MUTAGEN 213 213 R->A: Slightly reduces enzyme activity.
{ECO:0000269|PubMed:18288108,
ECO:0000269|PubMed:18849968}.
MUTAGEN 213 213 R->E: Reduces enzyme activity.
{ECO:0000269|PubMed:18288108,
ECO:0000269|PubMed:18849968}.
MUTAGEN 215 215 R->A,E: Abolishes enzyme activity.
{ECO:0000269|PubMed:18288108,
ECO:0000269|PubMed:18849968}.
MUTAGEN 217 217 E->K: Modifies the spectrum of action
against mobile genetic elements; when
associated with K-247.
{ECO:0000269|PubMed:21123384}.
MUTAGEN 218 218 T->A: Loss of phosphorylation. No effect
on cytidine deaminase activity or HIV-1
restriction activity.
{ECO:0000269|PubMed:21659520}.
MUTAGEN 218 218 T->E: Phosphomimetic mutant which shows
loss of cytidine deaminase activity and
HIV-1 restriction activity.
{ECO:0000269|PubMed:21659520}.
MUTAGEN 221 221 C->S: Does not decrease cytidine
deaminase activity.
{ECO:0000269|PubMed:12808466}.
MUTAGEN 244 244 N->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:18849968}.
MUTAGEN 247 247 P->K: Modifies the spectrum of action
against mobile genetic elements; when
associated with K-217.
{ECO:0000269|PubMed:21123384}.
MUTAGEN 256 256 R->E: Strongly reduces enzyme activity.
MUTAGEN 257 257 H->A: Decreases cytidine deaminase
activity. {ECO:0000269|PubMed:12808465,
ECO:0000269|PubMed:12808466}.
MUTAGEN 259 259 E->A: Loss of cytidine deaminase activity
and significant decrease in antiviral
activity. {ECO:0000269|PubMed:12808466,
ECO:0000269|PubMed:12970355,
ECO:0000269|PubMed:17020885,
ECO:0000269|PubMed:18288108}.
MUTAGEN 259 259 E->A: Loss of cytidine deaminase activity
and significant decrease in antiviral
activity; when associated with A-67.
{ECO:0000269|PubMed:12808466,
ECO:0000269|PubMed:12970355,
ECO:0000269|PubMed:17020885,
ECO:0000269|PubMed:18288108}.
MUTAGEN 259 259 E->Q: Decreases cytidine deaminase
activity and antiviral activity.
{ECO:0000269|PubMed:12808466,
ECO:0000269|PubMed:12970355,
ECO:0000269|PubMed:17020885,
ECO:0000269|PubMed:18288108}.
MUTAGEN 285 285 W->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:18288108,
ECO:0000269|PubMed:18849968}.
MUTAGEN 288 288 C->A: Decreases cytidine deaminase
activity. {ECO:0000269|PubMed:12808465,
ECO:0000269|PubMed:12808466}.
MUTAGEN 291 291 C->A,S: Decreases cytidine deaminase
activity. {ECO:0000269|PubMed:12808465,
ECO:0000269|PubMed:12808466,
ECO:0000269|PubMed:12970355}.
MUTAGEN 313 313 R->A,E: Abolishes enzyme activity.
{ECO:0000269|PubMed:18288108}.
MUTAGEN 315 315 Y->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:18849968}.
MUTAGEN 320 320 R->A: Slightly reduces enzyme activity.
{ECO:0000269|PubMed:18288108}.
MUTAGEN 320 320 R->E: Reduces enzyme activity.
{ECO:0000269|PubMed:18288108}.
MUTAGEN 323 323 E->Q: Does not decrease cytidine
deaminase activity.
{ECO:0000269|PubMed:12808466}.
CONFLICT 162 162 S -> N (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
CONFLICT 370 370 D -> Y (in Ref. 1; no nucleotide entry).
{ECO:0000305}.
STRAND 195 197 {ECO:0000244|PDB:2KBO}.
HELIX 199 206 {ECO:0000244|PDB:3V4K}.
STRAND 213 217 {ECO:0000244|PDB:2JYW}.
STRAND 219 228 {ECO:0000244|PDB:3V4K}.
STRAND 231 234 {ECO:0000244|PDB:3V4K}.
HELIX 236 238 {ECO:0000244|PDB:3V4K}.
STRAND 240 243 {ECO:0000244|PDB:3V4K}.
STRAND 247 250 {ECO:0000244|PDB:2JYW}.
HELIX 258 265 {ECO:0000244|PDB:3V4K}.
HELIX 266 269 {ECO:0000244|PDB:3V4K}.
STRAND 273 275 {ECO:0000244|PDB:3E1U}.
STRAND 277 285 {ECO:0000244|PDB:3V4K}.
HELIX 289 301 {ECO:0000244|PDB:3V4K}.
STRAND 305 313 {ECO:0000244|PDB:3V4K}.
STRAND 318 320 {ECO:0000244|PDB:3V4K}.
HELIX 321 330 {ECO:0000244|PDB:3V4K}.
STRAND 334 337 {ECO:0000244|PDB:3V4K}.
HELIX 340 350 {ECO:0000244|PDB:3V4K}.
HELIX 364 379 {ECO:0000244|PDB:3V4K}.
SEQUENCE 384 AA; 46408 MW; 60525DC3B7D903D6 CRC64;
MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPPLD AKIFRGQVYS
ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC TRDMATFLAE DPKVTLTIFV
ARLYYFWDPD YQEALRSLCQ KRDGPRATMK IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK
YYILLHIMLG EILRHSMDPP TFTFNFNNEP WVRGRHETYL CYEVERMHND TWVLLNQRRG
FLCNQAPHKH GFLEGRHAEL CFLDVIPFWK LDLDQDYRVT CFTSWSPCFS CAQEMAKFIS
KNKHVSLCIF TARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF VDHQGCPFQP
WDGLDEHSQD LSGRLRAILQ NQEN


Related products :

Catalog number Product name Quantity
18-661-15176 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.1 mg
18-003-42391 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.1 mg Protein A
18-003-42391 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.05 mg Aff Pur
18-003-42392 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.1 mg Protein A
18-003-42392 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.05 mg Aff Pur
E1116h Rat ELISA Kit FOR Putative C->U-editing enzyme APOBEC-4 96T
ABC3F_HUMAN Human ELISA Kit FOR DNA dC->dU-editing enzyme APOBEC-3F 96T
ABEC3_MOUSE Mouse ELISA Kit FOR DNA dC->dU-editing enzyme APOBEC-3 96T
E1078b Rabbit ELISA Kit FOR C->U-editing enzyme APOBEC-1 96T
CSB-EL001919RA Rat C->U-editing enzyme APOBEC-1(APOBEC1) ELISA kit 96T
G5244 Putative C->U-editing enzyme APOBEC-4 (APOBEC4), Rat, ELISA Kit 96T
CSB-EL001928RA Rat Putative C->U-editing enzyme APOBEC-4(APOBEC4) ELISA kit 96T
CSB-EL001919MO Mouse C->U-editing enzyme APOBEC-1(APOBEC1) ELISA kit 96T
CSB-EL001919RA Rat C->U-editing enzyme APOBEC-1(APOBEC1) ELISA kit SpeciesRat 96T
AE56033RB Rabbit C->U-editing enzyme APOBEC-1 (APOBEC1) ELISA Kit 48T
CSB-EL001927HU Human DNA dC->dU-editing enzyme APOBEC-3H(APOBEC3H) ELISA kit 96T
CSB-EL001926HU Human DNA dC->dU-editing enzyme APOBEC-3G(APOBEC3G) ELISA kit 96T
CSB-EL001925HU Human DNA dC->dU-editing enzyme APOBEC-3F(APOBEC3F) ELISA kit 96T
ABC3A_HUMAN Human ELISA Kit FOR Probable DNA dC->dU-editing enzyme APOBEC-3A 96T
CSB-EL001919HU Human C->U-editing enzyme APOBEC-1(APOBEC1) ELISA kit 96T
ABEC2_HUMAN Human ELISA Kit FOR Probable C->U-editing enzyme APOBEC-2 96T
ABC3D_HUMAN Human ELISA Kit FOR Probable DNA dC->dU-editing enzyme APOBEC-3D 96T
G1026 Probable C->U-editing enzyme APOBEC-2 (APOBEC2), Human, ELISA Kit 96T
G1060 Probable DNA dC->dU-editing enzyme APOBEC-3B (APOBEC3B), Human, ELISA Kit 96T
CSB-EL001919HU Human C->U-editing enzyme APOBEC-1(APOBEC1) ELISA kit SpeciesHuman 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur