ABC3B_HUMAN
ID ABC3B_HUMAN Reviewed; 382 AA.
AC Q9UH17; B0QYD2; O95618; Q20WL1; Q5IFJ4; Q7Z2N3; Q7Z6D6; Q9UE74;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3B;
DE Short=A3B;
DE EC=3.5.4.38;
DE AltName: Full=Phorbolin-1-related protein;
DE AltName: Full=Phorbolin-2/3;
GN Name=APOBEC3B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-146, AND INDUCTION.
RC TISSUE=Keratinocyte;
RX PubMed=10469298; DOI=10.1046/j.1523-1747.1999.00682.x;
RA Madsen P.P., Anant S., Rasmussen H.H., Gromov P., Vorum H., Dumanski J.P.,
RA Tommerup N., Collins J.E., Wright C.L., Dunham I., Macginnitie A.J.,
RA Davidson N.O., Celis J.E.;
RT "Psoriasis upregulated phorbolin-1 shares structural but not functional
RT similarity to the mRNA-editing protein apobec-1.";
RL J. Invest. Dermatol. 113:162-169(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=16060832; DOI=10.1089/aid.2005.21.611;
RA Rose K.M., Marin M., Kozak S.L., Kabat D.;
RT "Regulated production and anti-HIV type 1 activities of cytidine deaminases
RT APOBEC3B, 3F, and 3G.";
RL AIDS Res. Hum. Retroviruses 21:611-619(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS GLU-62 AND
RP LYS-146.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LYS-146.
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP GENE FAMILY ORGANIZATION, TISSUE SPECIFICITY, RNA-BINDING, ZINC-BINDING,
RP AND INTERACTION WITH APOBEC3G.
RX PubMed=11863358; DOI=10.1006/geno.2002.6718;
RA Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J.,
RA Navaratnam N.;
RT "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on
RT chromosome 22.";
RL Genomics 79:285-296(2002).
RN [7]
RP REVIEW ON APOBEC FAMILIES.
RX PubMed=12683974; DOI=10.1016/s0168-9525(03)00054-4;
RA Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.;
RT "Messenger RNA editing in mammals: new members of the APOBEC family seeking
RT roles in the family business.";
RL Trends Genet. 19:207-216(2003).
RN [8]
RP FUNCTION IN HIV-1 INFECTIVITY.
RX PubMed=12859895; DOI=10.1016/s0092-8674(03)00515-4;
RA Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., Bollman B.,
RA Muenk C., Nymark-McMahon H., Landau N.R.;
RT "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.";
RL Cell 114:21-31(2003).
RN [9]
RP FUNCTION IN SIV RESTRICTION.
RX PubMed=15466872; DOI=10.1074/jbc.m408802200;
RA Yu Q., Chen D., Koenig R., Mariani R., Unutmaz D., Landau N.R.;
RT "APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency
RT virus replication.";
RL J. Biol. Chem. 279:53379-53386(2004).
RN [10]
RP FUNCTION IN RETROTRANSPOSITION.
RX PubMed=16527742; DOI=10.1016/j.cub.2006.01.031;
RA Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., Landau N.R.,
RA Weitzman M.D.;
RT "APOBEC3A is a potent inhibitor of adeno-associated virus and
RT retrotransposons.";
RL Curr. Biol. 16:480-485(2006).
RN [11]
RP DOMAIN CMP/DCMP DEAMINASE.
RX PubMed=17020885; DOI=10.1074/jbc.m604980200;
RA Hakata Y., Landau N.R.;
RT "Reversed functional organization of mouse and human APOBEC3 cytidine
RT deaminase domains.";
RL J. Biol. Chem. 281:36624-36631(2006).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=16699599; DOI=10.1371/journal.ppat.0020041;
RA Wichroski M.J., Robb G.B., Rana T.M.;
RT "Human retroviral host restriction factors APOBEC3G and APOBEC3F localize
RT to mRNA processing bodies.";
RL PLoS Pathog. 2:E41-E41(2006).
RN [13]
RP REVIEW.
RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350;
RA Chiu Y.L., Greene W.C.;
RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing
RT exogenous retroviruses and endogenous retroelements.";
RL Annu. Rev. Immunol. 26:317-353(2008).
RN [14]
RP REVIEW ON FUNCTION IN HBV RESTRICTION.
RX PubMed=18448976; DOI=10.1097/qco.0b013e3282fe1bb2;
RA Bonvin M., Greeve J.;
RT "Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine deaminases
RT as effectors in innate immunity against the hepatitis B virus.";
RL Curr. Opin. Infect. Dis. 21:298-303(2008).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=18667511; DOI=10.1128/jvi.02471-07;
RA Stenglein M.D., Matsuo H., Harris R.S.;
RT "Two regions within the amino-terminal half of APOBEC3G cooperate to
RT determine cytoplasmic localization.";
RL J. Virol. 82:9591-9599(2008).
RN [16]
RP TISSUE SPECIFICITY.
RX PubMed=20308164; DOI=10.1093/nar/gkq174;
RA Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L.,
RA Harris R.S.;
RT "Quantitative profiling of the full APOBEC3 mRNA repertoire in lymphocytes
RT and tissues: implications for HIV-1 restriction.";
RL Nucleic Acids Res. 38:4274-4284(2010).
RN [17]
RP FUNCTION IN RETROTRANSPOSITION.
RX PubMed=20062055; DOI=10.1038/nsmb.1744;
RA Stenglein M.D., Burns M.B., Li M., Lengyel J., Harris R.S.;
RT "APOBEC3 proteins mediate the clearance of foreign DNA from human cells.";
RL Nat. Struct. Mol. Biol. 17:222-229(2010).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=21835787; DOI=10.1128/jvi.05238-11;
RA Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L.,
RA Brown W.L., Harris R.S.;
RT "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H demonstrate a
RT conserved capacity to restrict Vif-deficient HIV-1.";
RL J. Virol. 85:11220-11234(2011).
RN [19]
RP REVIEW.
RX PubMed=22912627; DOI=10.3389/fmicb.2012.00275;
RA Arias J.F., Koyama T., Kinomoto M., Tokunaga K.;
RT "Retroelements versus APOBEC3 family members: No great escape from the
RT magnificent seven.";
RL Front. Microbiol. 3:275-275(2012).
RN [20]
RP FUNCTION IN HTLV-1 RESTRICTION.
RX PubMed=22457529; DOI=10.1128/jvi.06570-11;
RA Ooms M., Krikoni A., Kress A.K., Simon V., Muenk C.;
RT "APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic
RT virus type 1.";
RL J. Virol. 86:6097-6108(2012).
RN [21]
RP SUBCELLULAR LOCATION.
RX PubMed=22915799; DOI=10.1128/jvi.00595-12;
RA Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.;
RT "HIV-1 replication and APOBEC3 antiviral activity are not regulated by P
RT bodies.";
RL J. Virol. 86:11712-11724(2012).
RN [22]
RP REVIEW.
RX PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004;
RA Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.;
RT "Functions and regulation of the APOBEC family of proteins.";
RL Semin. Cell Dev. Biol. 23:258-268(2012).
CC -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor
CC of retrovirus replication and retrotransposon mobility via deaminase-
CC dependent and -independent mechanisms. After the penetration of
CC retroviral nucleocapsids into target cells of infection and the
CC initiation of reverse transcription, it can induce the conversion of
CC cytosine to uracil in the minus-sense single-strand viral DNA, leading
CC to G-to-A hypermutations in the subsequent plus-strand viral DNA. The
CC resultant detrimental levels of mutations in the proviral genome, along
CC with a deamination-independent mechanism that works prior to the
CC proviral integration, together exert efficient antiretroviral effects
CC in infected target cells. Selectively targets single-stranded DNA and
CC does not deaminate double-stranded DNA or single- or double-stranded
CC RNA. Exhibits antiviral activity against simian immunodeficiency virus
CC (SIV), hepatitis B virus (HBV) and human T-cell leukemia virus type 1
CC (HTLV-1) and may inhibit the mobility of LTR and non-LTR
CC retrotransposons. {ECO:0000269|PubMed:12859895,
CC ECO:0000269|PubMed:15466872, ECO:0000269|PubMed:16060832,
CC ECO:0000269|PubMed:16527742, ECO:0000269|PubMed:20062055,
CC ECO:0000269|PubMed:22457529}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in single-stranded DNA + H(+) + H2O = a 2'-
CC deoxyuridine in single-stranded DNA + NH4(+); Xref=Rhea:RHEA:50948,
CC Rhea:RHEA-COMP:12846, Rhea:RHEA-COMP:12847, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:85452,
CC ChEBI:CHEBI:133902; EC=3.5.4.38;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC -!- SUBUNIT: Homodimer. Interacts with APOBEC3G. Does not interact with
CC APOBEC1. {ECO:0000269|PubMed:11863358}.
CC -!- INTERACTION:
CC Q9UH17; P11802: CDK4; NbExp=9; IntAct=EBI-2967317, EBI-295644;
CC Q9UH17-2; O95994: AGR2; NbExp=3; IntAct=EBI-17624977, EBI-712648;
CC Q9UH17-2; Q12982: BNIP2; NbExp=3; IntAct=EBI-17624977, EBI-752094;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16699599,
CC ECO:0000269|PubMed:18667511, ECO:0000269|PubMed:21835787,
CC ECO:0000269|PubMed:22915799}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UH17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UH17-2; Sequence=VSP_009802;
CC Name=3;
CC IsoId=Q9UH17-3; Sequence=VSP_044900;
CC -!- TISSUE SPECIFICITY: Expressed at high and moderate levels in peripheral
CC blood leukocytes, spleen, testes, heart, thymus, prostate and ovary.
CC Also expressed at low levels in several other tissues.
CC {ECO:0000269|PubMed:11863358, ECO:0000269|PubMed:20308164}.
CC -!- INDUCTION: Phorbol 12-myristate 13-acetate (PMA) induces overexpression
CC in keratinocytes. Up-regulated by IFN-alpha.
CC {ECO:0000269|PubMed:10469298}.
CC -!- DOMAIN: The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA-
CC dependent oligomerization and virion incorporation whereas the CMP/dCMP
CC deaminase domain 2 confers deoxycytidine deaminase activity and
CC substrate sequence specificity. {ECO:0000269|PubMed:17020885}.
CC -!- MISCELLANEOUS: It is one of seven related genes or pseudogenes found in
CC a cluster, thought to result from gene duplication, on chromosome 22.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD00089.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD00090.1; Type=Frameshift; Note=Frameshifts result in two separate ORFs termed phorbolins 2 and 3.; Evidence={ECO:0000305};
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DR EMBL; U61083; AAD00089.1; ALT_INIT; mRNA.
DR EMBL; U61084; AAD00090.1; ALT_FRAME; mRNA.
DR EMBL; AY743217; AAW31743.1; -; mRNA.
DR EMBL; CT841510; CAJ86440.1; -; mRNA.
DR EMBL; AL022318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053859; AAH53859.1; -; mRNA.
DR CCDS; CCDS13982.1; -. [Q9UH17-1]
DR CCDS; CCDS58807.1; -. [Q9UH17-3]
DR RefSeq; NP_001257340.1; NM_001270411.1. [Q9UH17-3]
DR RefSeq; NP_004891.4; NM_004900.4. [Q9UH17-1]
DR PDB; 2NBQ; NMR; -; A=187-382.
DR PDB; 5CQD; X-ray; 2.08 A; A/C=187-378.
DR PDB; 5CQH; X-ray; 1.73 A; A=187-378.
DR PDB; 5CQI; X-ray; 1.68 A; A=187-378.
DR PDB; 5CQK; X-ray; 1.88 A; A=187-378.
DR PDB; 5SXG; X-ray; 1.93 A; A/B=191-378.
DR PDB; 5SXH; X-ray; 1.78 A; A/B=191-378.
DR PDB; 5TD5; X-ray; 1.72 A; A=187-378.
DR PDB; 5TKM; X-ray; 1.90 A; A/B=1-191.
DR PDB; 6NFK; X-ray; 1.86 A; A=187-378.
DR PDB; 6NFL; X-ray; 1.73 A; A=187-378.
DR PDB; 6NFM; X-ray; 2.53 A; A=187-378.
DR PDBsum; 2NBQ; -.
DR PDBsum; 5CQD; -.
DR PDBsum; 5CQH; -.
DR PDBsum; 5CQI; -.
DR PDBsum; 5CQK; -.
DR PDBsum; 5SXG; -.
DR PDBsum; 5SXH; -.
DR PDBsum; 5TD5; -.
DR PDBsum; 5TKM; -.
DR PDBsum; 6NFK; -.
DR PDBsum; 6NFL; -.
DR PDBsum; 6NFM; -.
DR AlphaFoldDB; Q9UH17; -.
DR SMR; Q9UH17; -.
DR BioGRID; 114950; 140.
DR IntAct; Q9UH17; 29.
DR MINT; Q9UH17; -.
DR STRING; 9606.ENSP00000327459; -.
DR ChEMBL; CHEMBL4523487; -.
DR iPTMnet; Q9UH17; -.
DR PhosphoSitePlus; Q9UH17; -.
DR BioMuta; APOBEC3B; -.
DR DMDM; 12643884; -.
DR EPD; Q9UH17; -.
DR jPOST; Q9UH17; -.
DR MassIVE; Q9UH17; -.
DR MaxQB; Q9UH17; -.
DR PaxDb; Q9UH17; -.
DR PeptideAtlas; Q9UH17; -.
DR PRIDE; Q9UH17; -.
DR ProteomicsDB; 2630; -.
DR ProteomicsDB; 84274; -. [Q9UH17-1]
DR ProteomicsDB; 84275; -. [Q9UH17-2]
DR ABCD; Q9UH17; 1 sequenced antibody.
DR Antibodypedia; 35027; 171 antibodies from 29 providers.
DR DNASU; 9582; -.
DR Ensembl; ENST00000333467.4; ENSP00000327459.3; ENSG00000179750.16. [Q9UH17-1]
DR Ensembl; ENST00000335760.9; ENSP00000338897.5; ENSG00000179750.16. [Q9UH17-2]
DR Ensembl; ENST00000407298.7; ENSP00000385068.3; ENSG00000179750.16. [Q9UH17-3]
DR GeneID; 9582; -.
DR KEGG; hsa:9582; -.
DR MANE-Select; ENST00000333467.4; ENSP00000327459.3; NM_004900.5; NP_004891.5.
DR UCSC; uc003awo.3; human. [Q9UH17-1]
DR CTD; 9582; -.
DR DisGeNET; 9582; -.
DR GeneCards; APOBEC3B; -.
DR HGNC; HGNC:17352; APOBEC3B.
DR HPA; ENSG00000179750; Tissue enhanced (bone marrow, intestine).
DR MIM; 607110; gene.
DR neXtProt; NX_Q9UH17; -.
DR OpenTargets; ENSG00000179750; -.
DR PharmGKB; PA24892; -.
DR VEuPathDB; HostDB:ENSG00000179750; -.
DR eggNOG; KOG4075; Eukaryota.
DR GeneTree; ENSGT00940000164701; -.
DR HOGENOM; CLU_047918_0_0_1; -.
DR OMA; LCHKVEL; -.
DR OrthoDB; 586309at2759; -.
DR PhylomeDB; Q9UH17; -.
DR TreeFam; TF331356; -.
DR BRENDA; 3.5.4.38; 2681.
DR PathwayCommons; Q9UH17; -.
DR Reactome; R-HSA-72200; mRNA Editing: C to U Conversion.
DR Reactome; R-HSA-75094; Formation of the Editosome.
DR SignaLink; Q9UH17; -.
DR SIGNOR; Q9UH17; -.
DR BioGRID-ORCS; 9582; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; APOBEC3B; human.
DR GeneWiki; APOBEC3B; -.
DR GenomeRNAi; 9582; -.
DR Pharos; Q9UH17; Tbio.
DR PRO; PR:Q9UH17; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UH17; protein.
DR Bgee; ENSG00000179750; Expressed in mucosa of transverse colon and 90 other tissues.
DR ExpressionAtlas; Q9UH17; baseline and differential.
DR Genevisible; Q9UH17; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0004126; F:cytidine deaminase activity; IBA:GO_Central.
DR GO; GO:0047844; F:deoxycytidine deaminase activity; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016554; P:cytidine to uridine editing; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0070383; P:DNA cytosine deamination; IBA:GO_Central.
DR GO; GO:0080111; P:DNA demethylation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IBA:GO_Central.
DR GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR SUPFAM; SSF53927; SSF53927; 2.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 2.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense; Hydrolase; Immunity;
KW Innate immunity; Metal-binding; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Zinc.
FT CHAIN 1..382
FT /note="DNA dC->dU-editing enzyme APOBEC-3B"
FT /id="PRO_0000171753"
FT DOMAIN 29..138
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 210..326
FT /note="CMP/dCMP-type deaminase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 255
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT VAR_SEQ 191..382
FT /note="YLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLMDQHMGFLCNEA
FT KNLLCGFYGRHAELRFLDLVPSLQLDPAQIYRVTWFISWSPCFSWGCAGEVRAFLQENT
FT HVRLRIFAARIYDYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGCPFQPWD
FT GLEEHSQALSGRLRAILQNQGN -> LRIFSVAFTAAMRSCASWTWFLLCSWTRPRSTG
FT SLGSSPGAPASPGAVPGKCVRSFRRTHT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009802"
FT VAR_SEQ 242..266
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15461802"
FT /id="VSP_044900"
FT VARIANT 62
FT /note="K -> E (in dbSNP:rs2076109)"
FT /evidence="ECO:0000269|PubMed:15461802"
FT /id="VAR_018142"
FT VARIANT 98
FT /note="P -> L (in dbSNP:rs2076110)"
FT /id="VAR_018143"
FT VARIANT 109
FT /note="S -> A (in dbSNP:rs17000697)"
FT /id="VAR_033455"
FT VARIANT 146
FT /note="T -> K (in dbSNP:rs5995649)"
FT /evidence="ECO:0000269|PubMed:10469298,
FT ECO:0000269|PubMed:15461802, ECO:0000269|PubMed:15489334"
FT /id="VAR_018144"
FT VARIANT 351
FT /note="R -> H (in dbSNP:rs1053813)"
FT /id="VAR_048722"
FT CONFLICT 103..104
FT /note="KL -> NV (in Ref. 1; AAD00090)"
FT /evidence="ECO:0000305"
FT CONFLICT 227..228
FT /note="TW -> WM (in Ref. 1; AAD00089)"
FT /evidence="ECO:0000305"
FT CONFLICT 255..256
FT /note="EL -> DW (in Ref. 1; AAD00089)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="R -> P (in Ref. 1; AAD00089)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="F -> S (in Ref. 2; AAW31743)"
FT /evidence="ECO:0000305"
FT HELIX 14..21
FT /evidence="ECO:0007829|PDB:5TKM"
FT STRAND 32..43
FT /evidence="ECO:0007829|PDB:5TKM"
FT STRAND 46..61
FT /evidence="ECO:0007829|PDB:5TKM"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:5TKM"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:5TKM"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:5TKM"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:5TKM"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:5TKM"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:5TKM"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:5TKM"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:5TKM"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:5TKM"
FT HELIX 174..188
FT /evidence="ECO:0007829|PDB:5TKM"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:5CQI"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:5CQI"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:5CQI"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:5CQI"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:5CQI"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2NBQ"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:5CQI"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:5CQI"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2NBQ"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:5CQI"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:5CQI"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:2NBQ"
FT STRAND 303..311
FT /evidence="ECO:0007829|PDB:5CQI"
FT HELIX 319..328
FT /evidence="ECO:0007829|PDB:5CQI"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:5CQI"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:5CQI"
FT HELIX 362..377
FT /evidence="ECO:0007829|PDB:5CQI"
SQ SEQUENCE 382 AA; 45924 MW; DA6EDD23E8856240 CRC64;
MNPQIRNPME RMYRDTFYDN FENEPILYGR SYTWLCYEVK IKRGRSNLLW DTGVFRGQVY
FKPQYHAEMC FLSWFCGNQL PAYKCFQITW FVSWTPCPDC VAKLAEFLSE HPNVTLTISA
ARLYYYWERD YRRALCRLSQ AGARVTIMDY EEFAYCWENF VYNEGQQFMP WYKFDENYAF
LHRTLKEILR YLMDPDTFTF NFNNDPLVLR RRQTYLCYEV ERLDNGTWVL MDQHMGFLCN
EAKNLLCGFY GRHAELRFLD LVPSLQLDPA QIYRVTWFIS WSPCFSWGCA GEVRAFLQEN
THVRLRIFAA RIYDYDPLYK EALQMLRDAG AQVSIMTYDE FEYCWDTFVY RQGCPFQPWD
GLEEHSQALS GRLRAILQNQ GN
