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Protein

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

Gene

APOBEC3B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons.6 Publications

Catalytic activityi

Cytidine + H2O = uridine + NH3.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi66 – 661ZincBy similarity
Metal bindingi97 – 971ZincBy similarity
Metal bindingi100 – 1001ZincBy similarity
Metal bindingi253 – 2531ZincBy similarity
Active sitei255 – 2551Proton donorSequence analysis
Metal bindingi284 – 2841ZincBy similarity
Metal bindingi289 – 2891ZincBy similarity

GO - Molecular functioni

  • deoxycytidine deaminase activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • defense response to virus Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • negative regulation of transposition Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DNA dC->dU-editing enzyme APOBEC-3B (EC:3.5.4.-)
Short name:
A3B
Alternative name(s):
Phorbolin-1-related protein
Phorbolin-2/3
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:17352. APOBEC3B.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24892.

Polymorphism and mutation databases

BioMutaiAPOBEC3B.
DMDMi12643884.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382DNA dC->dU-editing enzyme APOBEC-3BPRO_0000171753Add
BLAST

Proteomic databases

EPDiQ9UH17.
MaxQBiQ9UH17.
PaxDbiQ9UH17.
PRIDEiQ9UH17.

PTM databases

iPTMnetiQ9UH17.
PhosphoSiteiQ9UH17.

Expressioni

Tissue specificityi

Expressed at high and moderate levels in peripheral blood leukocytes, spleen, testes, heart, thymus, prostate and ovary. Also expressed at low levels in several other tissues.2 Publications

Inductioni

Phorbol 12-myristate 13-acetate (PMA) induces overexpression in keratinocytes. Up-regulated by IFN-alpha.1 Publication

Gene expression databases

BgeeiQ9UH17.
CleanExiHS_APOBEC3B.
ExpressionAtlasiQ9UH17. baseline and differential.
GenevisibleiQ9UH17. HS.

Interactioni

Subunit structurei

Homodimer. Interacts with APOBEC3G. Does not interact with APOBEC1.1 Publication

Protein-protein interaction databases

BioGridi114950. 15 interactions.
IntActiQ9UH17. 15 interactions.
MINTiMINT-4992727.
STRINGi9606.ENSP00000327459.

Structurei

Secondary structure

1
382
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni188 – 1903Combined sources
Helixi195 – 2028Combined sources
Beta strandi215 – 22410Combined sources
Beta strandi227 – 2304Combined sources
Helixi232 – 2343Combined sources
Beta strandi236 – 2394Combined sources
Helixi254 – 2618Combined sources
Helixi262 – 2654Combined sources
Beta strandi273 – 2819Combined sources
Helixi289 – 29911Combined sources
Beta strandi303 – 3119Combined sources
Helixi319 – 32810Combined sources
Beta strandi332 – 3354Combined sources
Helixi338 – 34811Combined sources
Helixi362 – 37716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5CQDX-ray2.08A/C187-378[»]
5CQHX-ray1.73A187-378[»]
5CQIX-ray1.68A187-378[»]
5CQKX-ray1.88A187-378[»]
ProteinModelPortaliQ9UH17.
SMRiQ9UH17. Positions 5-378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 138110CMP/dCMP-type deaminase 1PROSITE-ProRule annotationAdd
BLAST
Domaini210 – 326117CMP/dCMP-type deaminase 2PROSITE-ProRule annotationAdd
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Contains 2 CMP/dCMP-type deaminase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410JBA1. Eukaryota.
ENOG41119MS. LUCA.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033755.
HOVERGENiHBG050434.
KOiK18750.
OrthoDBiEOG75QR3Z.
PhylomeDBiQ9UH17.
TreeFamiTF331356.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF08210. APOBEC_N. 2 hits.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 2 hits.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 2 hits.
PS51747. CYT_DCMP_DEAMINASES_2. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UH17-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNPQIRNPME RMYRDTFYDN FENEPILYGR SYTWLCYEVK IKRGRSNLLW
60 70 80 90 100
DTGVFRGQVY FKPQYHAEMC FLSWFCGNQL PAYKCFQITW FVSWTPCPDC
110 120 130 140 150
VAKLAEFLSE HPNVTLTISA ARLYYYWERD YRRALCRLSQ AGARVTIMDY
160 170 180 190 200
EEFAYCWENF VYNEGQQFMP WYKFDENYAF LHRTLKEILR YLMDPDTFTF
210 220 230 240 250
NFNNDPLVLR RRQTYLCYEV ERLDNGTWVL MDQHMGFLCN EAKNLLCGFY
260 270 280 290 300
GRHAELRFLD LVPSLQLDPA QIYRVTWFIS WSPCFSWGCA GEVRAFLQEN
310 320 330 340 350
THVRLRIFAA RIYDYDPLYK EALQMLRDAG AQVSIMTYDE FEYCWDTFVY
360 370 380
RQGCPFQPWD GLEEHSQALS GRLRAILQNQ GN
Length:382
Mass (Da):45,924
Last modified:May 1, 2000 - v1
Checksum:iDA6EDD23E8856240
GO
Isoform 2 (identifier: Q9UH17-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     191-382: YLMDPDTFTF...LRAILQNQGN → LRIFSVAFTA...CVRSFRRTHT

Note: May be due to a competing donor splice site.
Show »
Length:251
Mass (Da):29,798
Checksum:i9F2B8220F6689383
GO
Isoform 3 (identifier: Q9UH17-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     242-266: Missing.

Note: No experimental confirmation available.
Show »
Length:357
Mass (Da):43,081
Checksum:iC2666AD355F1D771
GO

Sequence cautioni

The sequence AAD00089.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAD00090.1 differs from that shown. Reason: Frameshift at positions 59 and 134. Frameshifts result in two separate ORFs termed phorbolins 2 and 3.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1042KL → NV in AAD00090 (PubMed:10469298).Curated
Sequence conflicti227 – 2282TW → WM in AAD00089 (PubMed:10469298).Curated
Sequence conflicti255 – 2562EL → DW in AAD00089 (PubMed:10469298).Curated
Sequence conflicti306 – 3061R → P in AAD00089 (PubMed:10469298).Curated
Sequence conflicti356 – 3561F → S in AAW31743 (PubMed:16060832).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti62 – 621K → E.1 Publication
Corresponds to variant rs2076109 [ dbSNP | Ensembl ].
VAR_018142
Natural varianti98 – 981P → L.
Corresponds to variant rs2076110 [ dbSNP | Ensembl ].
VAR_018143
Natural varianti109 – 1091S → A.
Corresponds to variant rs17000697 [ dbSNP | Ensembl ].
VAR_033455
Natural varianti146 – 1461T → K.3 Publications
Corresponds to variant rs5995649 [ dbSNP | Ensembl ].
VAR_018144
Natural varianti351 – 3511R → H.
Corresponds to variant rs1053813 [ dbSNP | Ensembl ].
VAR_048722

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei191 – 382192YLMDP…QNQGN → LRIFSVAFTAAMRSCASWTW FLLCSWTRPRSTGSLGSSPG APASPGAVPGKCVRSFRRTH T in isoform 2. 1 PublicationVSP_009802Add
BLAST
Alternative sequencei242 – 26625Missing in isoform 3. 1 PublicationVSP_044900Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61083 mRNA. Translation: AAD00089.1. Different initiation.
U61084 mRNA. Translation: AAD00090.1. Frameshift.
AY743217 mRNA. Translation: AAW31743.1.
CT841510 mRNA. Translation: CAJ86440.1.
AL022318 Genomic DNA. Translation: CAB45270.1.
AL022318 Genomic DNA. Translation: CAQ09851.1.
BC053859 mRNA. Translation: AAH53859.1.
CCDSiCCDS13982.1. [Q9UH17-1]
CCDS58807.1. [Q9UH17-3]
RefSeqiNP_001257340.1. NM_001270411.1.
NP_004891.4. NM_004900.4.
UniGeneiHs.226307.
Hs.658626.

Genome annotation databases

EnsembliENST00000333467; ENSP00000327459; ENSG00000179750. [Q9UH17-1]
ENST00000335760; ENSP00000338897; ENSG00000179750. [Q9UH17-2]
ENST00000407298; ENSP00000385068; ENSG00000179750. [Q9UH17-3]
GeneIDi9582.
KEGGihsa:9582.
UCSCiuc003awo.3. human. [Q9UH17-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U61083 mRNA. Translation: AAD00089.1. Different initiation.
U61084 mRNA. Translation: AAD00090.1. Frameshift.
AY743217 mRNA. Translation: AAW31743.1.
CT841510 mRNA. Translation: CAJ86440.1.
AL022318 Genomic DNA. Translation: CAB45270.1.
AL022318 Genomic DNA. Translation: CAQ09851.1.
BC053859 mRNA. Translation: AAH53859.1.
CCDSiCCDS13982.1. [Q9UH17-1]
CCDS58807.1. [Q9UH17-3]
RefSeqiNP_001257340.1. NM_001270411.1.
NP_004891.4. NM_004900.4.
UniGeneiHs.226307.
Hs.658626.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5CQDX-ray2.08A/C187-378[»]
5CQHX-ray1.73A187-378[»]
5CQIX-ray1.68A187-378[»]
5CQKX-ray1.88A187-378[»]
ProteinModelPortaliQ9UH17.
SMRiQ9UH17. Positions 5-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114950. 15 interactions.
IntActiQ9UH17. 15 interactions.
MINTiMINT-4992727.
STRINGi9606.ENSP00000327459.

PTM databases

iPTMnetiQ9UH17.
PhosphoSiteiQ9UH17.

Polymorphism and mutation databases

BioMutaiAPOBEC3B.
DMDMi12643884.

Proteomic databases

EPDiQ9UH17.
MaxQBiQ9UH17.
PaxDbiQ9UH17.
PRIDEiQ9UH17.

Protocols and materials databases

DNASUi9582.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333467; ENSP00000327459; ENSG00000179750. [Q9UH17-1]
ENST00000335760; ENSP00000338897; ENSG00000179750. [Q9UH17-2]
ENST00000407298; ENSP00000385068; ENSG00000179750. [Q9UH17-3]
GeneIDi9582.
KEGGihsa:9582.
UCSCiuc003awo.3. human. [Q9UH17-1]

Organism-specific databases

CTDi9582.
GeneCardsiAPOBEC3B.
HGNCiHGNC:17352. APOBEC3B.
MIMi607110. gene.
neXtProtiNX_Q9UH17.
PharmGKBiPA24892.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JBA1. Eukaryota.
ENOG41119MS. LUCA.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033755.
HOVERGENiHBG050434.
KOiK18750.
OrthoDBiEOG75QR3Z.
PhylomeDBiQ9UH17.
TreeFamiTF331356.

Miscellaneous databases

GeneWikiiAPOBEC3B.
GenomeRNAii9582.
NextBioi35465727.
PROiQ9UH17.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UH17.
CleanExiHS_APOBEC3B.
ExpressionAtlasiQ9UH17. baseline and differential.
GenevisibleiQ9UH17. HS.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR013158. APOBEC_N.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF08210. APOBEC_N. 2 hits.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 2 hits.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 2 hits.
PS51747. CYT_DCMP_DEAMINASES_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1."
    Madsen P.P., Anant S., Rasmussen H.H., Gromov P., Vorum H., Dumanski J.P., Tommerup N., Collins J.E., Wright C.L., Dunham I., Macginnitie A.J., Davidson N.O., Celis J.E.
    J. Invest. Dermatol. 113:162-169(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-146, INDUCTION.
    Tissue: Keratinocyte.
  2. "Regulated production and anti-HIV type 1 activities of cytidine deaminases APOBEC3B, 3F, and 3G."
    Rose K.M., Marin M., Kozak S.L., Kabat D.
    AIDS Res. Hum. Retroviruses 21:611-619(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANTS GLU-62 AND LYS-146.
  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. "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] (ISOFORM 2), VARIANT LYS-146.
    Tissue: Uterus.
  6. "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, RNA-BINDING, ZINC-BINDING, INTERACTION WITH APOBEC3G.
  7. "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 FAMILIES.
  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. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  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. "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.
  20. "APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T-lymphotropic virus type 1."
    Ooms M., Krikoni A., Kress A.K., Simon V., Muenk C.
    J. Virol. 86:6097-6108(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HTLV-1 RESTRICTION.
  21. "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: SUBCELLULAR LOCATION.
  22. Cited for: REVIEW.

Entry informationi

Entry nameiABC3B_HUMAN
AccessioniPrimary (citable) accession number: Q9UH17
Secondary accession number(s): B0QYD2
, O95618, Q20WL1, Q5IFJ4, Q7Z2N3, Q7Z6D6, Q9UE74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: April 13, 2016
This is version 134 of the entry and version 1 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.