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Q9NRW3

- ABC3C_HUMAN

UniProt

Q9NRW3 - ABC3C_HUMAN

Protein

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

Gene

APOBEC3C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (29 Mar 2004)
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    Functioni

    DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. 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 against simian immunodeficiency virus (SIV), hepatitis B virus (HBV), herpes simplex virus 1 (HHV-1) and Epstein-Barr virus (EBV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.6 Publications

    Catalytic activityi

    Cytidine + H2O = uridine + NH3.

    Cofactori

    Zinc.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi66 – 661Zinc; catalyticBy similarity
    Active sitei68 – 681Proton donorBy similarity
    Metal bindingi97 – 971Zinc; catalyticBy similarity
    Metal bindingi100 – 1001Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cytidine deamination Source: UniProtKB
    2. defense response to virus Source: UniProtKB-KW
    3. DNA demethylation Source: UniProtKB
    4. innate immune response Source: UniProtKB-KW
    5. negative regulation of transposition Source: UniProtKB
    6. negative regulation of viral genome replication Source: UniProtKB
    7. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antiviral defense, Host-virus interaction, Immunity, Innate immunity

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA dC->dU-editing enzyme APOBEC-3C (EC:3.5.4.-)
    Short name:
    A3C
    Alternative name(s):
    APOBEC1-like
    Phorbolin I
    Gene namesi
    Name:APOBEC3C
    Synonyms:APOBEC1L, PBI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:17353. APOBEC3C.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24893.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 190190DNA dC->dU-editing enzyme APOBEC-3CPRO_0000171755Add
    BLAST

    Proteomic databases

    MaxQBiQ9NRW3.
    PaxDbiQ9NRW3.
    PRIDEiQ9NRW3.

    PTM databases

    PhosphoSiteiQ9NRW3.

    Expressioni

    Tissue specificityi

    Expressed in spleen, testes, peripherical blood lymphocytes, heart, thymus, prostate and ovary.2 Publications

    Inductioni

    Up-regulated by IFN-alpha.

    Gene expression databases

    ArrayExpressiQ9NRW3.
    BgeeiQ9NRW3.
    CleanExiHS_APOBEC3C.
    GenevestigatoriQ9NRW3.

    Organism-specific databases

    HPAiCAB033048.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with human foamy virus protein Bet; this interaction does not induce APOBEC3C degradation, but prevents dimerization and incorporation into virion of the latter. Interacts with TRIB3 and AGO2.3 Publications

    Protein-protein interaction databases

    BioGridi118162. 9 interactions.
    DIPiDIP-48919N.
    IntActiQ9NRW3. 4 interactions.
    MINTiMINT-6631470.
    STRINGi9606.ENSP00000355340.

    Structurei

    Secondary structure

    1
    190
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 207
    Turni27 – 293
    Beta strandi32 – 4312
    Beta strandi46 – 5813
    Helixi63 – 653
    Helixi67 – 759
    Beta strandi84 – 9411
    Helixi98 – 11013
    Beta strandi114 – 1229
    Turni124 – 1274
    Helixi129 – 14113
    Beta strandi144 – 1474
    Helixi150 – 16011
    Helixi174 – 18916

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VM8X-ray3.00A/B1-190[»]
    3VOWX-ray2.15A/B1-190[»]
    ProteinModelPortaliQ9NRW3.
    SMRiQ9NRW3. Positions 5-190.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini66 – 10035CMP/dCMP deaminase zinc-bindingAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG289247.
    HOGENOMiHOG000033754.
    HOVERGENiHBG050434.
    InParanoidiQ9NRW3.
    KOiK01500.
    OMAiSETHCHA.
    PhylomeDBiQ9NRW3.
    TreeFamiTF331356.

    Family and domain databases

    InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR007904. APOBEC_C.
    IPR016193. Cytidine_deaminase-like.
    [Graphical view]
    PfamiPF05240. APOBEC_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF53927. SSF53927. 1 hit.
    PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NRW3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNPQIRNPMK AMYPGTFYFQ FKNLWEANDR NETWLCFTVE GIKRRSVVSW    50
    KTGVFRNQVD SETHCHAERC FLSWFCDDIL SPNTKYQVTW YTSWSPCPDC 100
    AGEVAEFLAR HSNVNLTIFT ARLYYFQYPC YQEGLRSLSQ EGVAVEIMDY 150
    EDFKYCWENF VYNDNEPFKP WKGLKTNFRL LKRRLRESLQ 190
    Length:190
    Mass (Da):22,826
    Last modified:March 29, 2004 - v2
    Checksum:iBE49E80F95C71214
    GO

    Sequence cautioni

    The sequence AAF86650.1 differs from that shown. Reason: Frameshift at position 172.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311N → D in AAH11739. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF165520 mRNA. Translation: AAF86650.1. Frameshift.
    CR456394 mRNA. Translation: CAG30280.1.
    AK313272 mRNA. Translation: BAG36081.1.
    AL022318 Genomic DNA. Translation: CAI17898.1.
    CH471095 Genomic DNA. Translation: EAW60284.1.
    BC011739 mRNA. Translation: AAH11739.1.
    BC021080 mRNA. No translation available.
    CCDSiCCDS13983.1.
    RefSeqiNP_055323.2. NM_014508.2.
    UniGeneiHs.441124.

    Genome annotation databases

    EnsembliENST00000361441; ENSP00000355340; ENSG00000244509.
    GeneIDi27350.
    KEGGihsa:27350.
    UCSCiuc003awr.3. human.

    Polymorphism databases

    DMDMi48474983.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF165520 mRNA. Translation: AAF86650.1 . Frameshift.
    CR456394 mRNA. Translation: CAG30280.1 .
    AK313272 mRNA. Translation: BAG36081.1 .
    AL022318 Genomic DNA. Translation: CAI17898.1 .
    CH471095 Genomic DNA. Translation: EAW60284.1 .
    BC011739 mRNA. Translation: AAH11739.1 .
    BC021080 mRNA. No translation available.
    CCDSi CCDS13983.1.
    RefSeqi NP_055323.2. NM_014508.2.
    UniGenei Hs.441124.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VM8 X-ray 3.00 A/B 1-190 [» ]
    3VOW X-ray 2.15 A/B 1-190 [» ]
    ProteinModelPortali Q9NRW3.
    SMRi Q9NRW3. Positions 5-190.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118162. 9 interactions.
    DIPi DIP-48919N.
    IntActi Q9NRW3. 4 interactions.
    MINTi MINT-6631470.
    STRINGi 9606.ENSP00000355340.

    PTM databases

    PhosphoSitei Q9NRW3.

    Polymorphism databases

    DMDMi 48474983.

    Proteomic databases

    MaxQBi Q9NRW3.
    PaxDbi Q9NRW3.
    PRIDEi Q9NRW3.

    Protocols and materials databases

    DNASUi 27350.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361441 ; ENSP00000355340 ; ENSG00000244509 .
    GeneIDi 27350.
    KEGGi hsa:27350.
    UCSCi uc003awr.3. human.

    Organism-specific databases

    CTDi 27350.
    GeneCardsi GC22P039410.
    HGNCi HGNC:17353. APOBEC3C.
    HPAi CAB033048.
    MIMi 607750. gene.
    neXtProti NX_Q9NRW3.
    PharmGKBi PA24893.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289247.
    HOGENOMi HOG000033754.
    HOVERGENi HBG050434.
    InParanoidi Q9NRW3.
    KOi K01500.
    OMAi SETHCHA.
    PhylomeDBi Q9NRW3.
    TreeFami TF331356.

    Miscellaneous databases

    ChiTaRSi APOBEC3C. human.
    GeneWikii APOBEC3C.
    GenomeRNAii 27350.
    NextBioi 50452.
    PROi Q9NRW3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRW3.
    Bgeei Q9NRW3.
    CleanExi HS_APOBEC3C.
    Genevestigatori Q9NRW3.

    Family and domain databases

    InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
    IPR007904. APOBEC_C.
    IPR016193. Cytidine_deaminase-like.
    [Graphical view ]
    Pfami PF05240. APOBEC_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53927. SSF53927. 1 hit.
    PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
      Gu J., Huang Q., Yu Y., Xu S., Wang Y., Han Z., Chen Z., Zhou J., Tu Y., Gu W., Fu G., Huang C.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Hematopoietic stem cell.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
    7. "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.
    8. Cited for: FUNCTION IN HIV-1 INFECTIVITY.
    9. "APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication."
      Yu Q., Chen D., Koenig R., Mariani R., Unutmaz D., Landau N.R.
      J. Biol. Chem. 279:53379-53386(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SIV RESTRICTION.
    10. "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.
    11. "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.
    12. "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.
    13. Cited for: INTERACTION WITH HUMAN FOAMY VIRUS PROTEIN BET.
    14. "APOBEC3 proteins mediate the clearance of foreign DNA from human cells."
      Stenglein M.D., Burns M.B., Li M., Lengyel J., Harris R.S.
      Nat. Struct. Mol. Biol. 17:222-229(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RETROTRANSPOSITION.
    15. "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.
    16. "Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain."
      Guo J.U., Su Y., Zhong C., Ming G.L., Song H.
      Cell 145:423-434(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA DEMETHYLATION.
    17. "Genetic editing of herpes simplex virus 1 and Epstein-Barr herpesvirus genomes by human APOBEC3 cytidine deaminases in culture and in vivo."
      Suspene R., Aynaud M.M., Koch S., Pasdeloup D., Labetoulle M., Gaertner B., Vartanian J.P., Meyerhans A., Wain-Hobson S.
      J. Virol. 85:7594-7602(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EBV AND HHV-1 INHIBITION.
    18. "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: SUBCELLULAR LOCATION.
    19. "Cytosine deaminases APOBEC3A, APOBEC3C, and APOBEC3H: Current understanding of their functional roles."
      Love R.
      Student Perspec. Contemp. Virol. 0:0-0(2011)
      Cited for: REVIEW.
    20. "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.
    21. "Human Tribbles 3 protects nuclear DNA from cytidine deamination by APOBEC3A."
      Aynaud M.M., Suspene R., Vidalain P.O., Mussil B., Guetard D., Tangy F., Wain-Hobson S., Vartanian J.P.
      J. Biol. Chem. 287:39182-39192(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRIB3, SUBCELLULAR LOCATION, SUBUNIT.
    22. "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: INTERACTION WITH AGO2.
    23. Cited for: REVIEW.

    Entry informationi

    Entry nameiABC3C_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRW3
    Secondary accession number(s): B2R884
    , Q5JZ92, Q7Z2N7, Q96F12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2004
    Last sequence update: March 29, 2004
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

    It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

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