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Protein

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

Gene

APOBEC3A

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

Functioni

DNA deaminase (cytidine deaminase) with restriction activity against viruses, foreign DNA and mobility of retrotransposons. Exhibits antiviral activity against adeno-associated virus (AAV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. Selectively targets single-stranded DNA and can deaminate both methylcytosine and cytosine in foreign DNA. Can induce somatic hypermutation in the nuclear and mitochondrial DNA. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.12 Publications

Catalytic activityi

Cytidine + H2O = uridine + NH3.4 Publications

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi70 – 701Zinc; catalyticBy similarity
Active sitei72 – 721Proton donorBy similarity
Metal bindingi101 – 1011Zinc; catalyticBy similarity
Metal bindingi106 – 1061Zinc; catalyticBy similarity

GO - Molecular functioni

  • cytidine deaminase activity Source: UniProtKB
  • deoxycytidine deaminase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to xenobiotic stimulus Source: UniProtKB
  • clearance of foreign intracellular DNA by conversion of DNA cytidine to uridine Source: UniProtKB
  • cytidine deamination Source: GOC
  • defense response to virus Source: UniProtKB
  • DNA cytosine deamination Source: UniProtKB
  • DNA demethylation Source: UniProtKB
  • innate immune response Source: UniProtKB
  • negative regulation of transposition Source: UniProtKB
  • negative regulation of viral genome replication Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DNA dC->dU-editing enzyme APOBEC-3A (EC:3.5.4.-)
Short name:
A3A
Alternative name(s):
Phorbolin-1
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:17343. APOBEC3A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi28 – 281R → E: No effect on deaminase activity despite an altered restriction activity towards genetic invaders. 1 Publication
Mutagenesisi29 – 291H → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication
Mutagenesisi30 – 301K → F: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication
Mutagenesisi57 – 571N → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication
Mutagenesisi60 – 601K → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication
Mutagenesisi69 – 691R → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication
Mutagenesisi70 – 701H → R: Altered deaminase activity. 1 Publication
Mutagenesisi72 – 721E → Q: Altered deaminase activity and restriction activity towards genetic invaders. 2 Publications
Mutagenesisi98 – 981W → L: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication
Mutagenesisi106 – 1061C → S: Altered deaminase activity. 1 Publication
Mutagenesisi128 – 1281R → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication
Mutagenesisi130 – 1301Y → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication
Mutagenesisi131 – 1311D → N: No effect on deaminase activity despite an altered restriction activity towards genetic invaders. 1 Publication
Mutagenesisi133 – 1331D → N: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication
Mutagenesisi136 – 1361Y → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication

Organism-specific databases

PharmGKBiPA24891.

Chemistry

ChEMBLiCHEMBL1741179.

Polymorphism and mutation databases

BioMutaiAPOBEC3A.
DMDMi12644206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 199199DNA dC->dU-editing enzyme APOBEC-3APRO_0000171752Add
BLAST

Proteomic databases

EPDiP31941.
PaxDbiP31941.
PRIDEiP31941.

PTM databases

iPTMnetiP31941.
PhosphoSiteiP31941.

Expressioni

Tissue specificityi

Expressed in peripheral leukocytes with higher expression in CD14-positive phagocytic cells. Highly expressed in keratinocytes and in periphery blood monocytes. Also detected in non-lymphoid tissues including lung and adipose tissues. Found at high levels in colorectal adenocarcinoma, Burkitt's lymphoma and chronic myelogenous leukemia.4 Publications

Inductioni

Up-regulated by interferon and CpG single-stranded DNA (at protein level).2 Publications

Gene expression databases

BgeeiP31941.
CleanExiHS_APOBEC3A.
ExpressionAtlasiP31941. baseline and differential.
GenevisibleiP31941. HS.

Organism-specific databases

HPAiHPA043237.

Interactioni

Subunit structurei

Interacts with AGO2. Interacts with TRIB3 (via N-terminus).2 Publications

Protein-protein interaction databases

BioGridi128318. 2 interactions.
DIPiDIP-61365N.
STRINGi9606.ENSP00000249116.

Chemistry

BindingDBiP31941.

Structurei

Secondary structure

1
199
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 217Combined sources
Beta strandi24 – 263Combined sources
Beta strandi27 – 293Combined sources
Beta strandi32 – 398Combined sources
Beta strandi44 – 474Combined sources
Beta strandi53 – 564Combined sources
Turni62 – 654Combined sources
Helixi71 – 8212Combined sources
Beta strandi90 – 989Combined sources
Turni103 – 1053Combined sources
Helixi106 – 11611Combined sources
Beta strandi120 – 1289Combined sources
Helixi136 – 1449Combined sources
Turni145 – 1473Combined sources
Beta strandi148 – 1525Combined sources
Helixi155 – 16410Combined sources
Helixi179 – 19517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M65NMR-A1-199[»]
4XXOX-ray2.84A/B1-199[»]
ProteinModelPortaliP31941.
SMRiP31941. Positions 1-199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 143117CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410JNPI. Eukaryota.
ENOG4111DZ4. LUCA.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033754.
HOVERGENiHBG050434.
KOiK18750.
OMAiSGPRHLM.
OrthoDBiEOG71CFNW.
PhylomeDBiP31941.
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. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P31941-1) [UniParc]FASTAAdd to basket

Also known as: Phorbolin-1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEASPASGPR HLMDPHIFTS NFNNGIGRHK TYLCYEVERL DNGTSVKMDQ
60 70 80 90 100
HRGFLHNQAK NLLCGFYGRH AELRFLDLVP SLQLDPAQIY RVTWFISWSP
110 120 130 140 150
CFSWGCAGEV RAFLQENTHV RLRIFAARIY DYDPLYKEAL QMLRDAGAQV
160 170 180 190
SIMTYDEFKH CWDTFVDHQG CPFQPWDGLD EHSQALSGRL RAILQNQGN
Note: Enzymatically active.
Length:199
Mass (Da):23,012
Last modified:January 11, 2001 - v3
Checksum:i42E99E0D7DF7AA14
GO
Isoform 2 (identifier: P31941-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: Missing.

Note: Enzymatically active.
Show »
Length:187
Mass (Da):21,778
Checksum:iC7901DFD6A693D9D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191T → A.
Corresponds to variant rs17000556 [ dbSNP | Ensembl ].
VAR_048721

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1212Missing in isoform 2. CuratedVSP_041723Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03891 mRNA. Translation: AAA03706.2.
CR456393 mRNA. Translation: CAG30279.1.
AL022318 Genomic DNA. Translation: CAI17897.1.
BC126416 mRNA. Translation: AAI26417.1.
CCDSiCCDS13981.1. [P31941-1]
PIRiG01233.
RefSeqiNP_001180218.1. NM_001193289.1. [P31941-1]
NP_663745.1. NM_145699.3. [P31941-1]
XP_011545347.1. XM_011547045.1. [P31941-1]
UniGeneiHs.226307.

Genome annotation databases

EnsembliENST00000249116; ENSP00000249116; ENSG00000128383. [P31941-1]
ENST00000402255; ENSP00000384359; ENSG00000128383. [P31941-1]
ENST00000570508; ENSP00000461288; ENSG00000262156. [P31941-1]
ENST00000618553; ENSP00000481904; ENSG00000128383. [P31941-1]
ENST00000623492; ENSP00000485234; ENSG00000262156. [P31941-1]
GeneIDi100913187.
200315.
KEGGihsa:100913187.
UCSCiuc003awn.2. human. [P31941-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03891 mRNA. Translation: AAA03706.2.
CR456393 mRNA. Translation: CAG30279.1.
AL022318 Genomic DNA. Translation: CAI17897.1.
BC126416 mRNA. Translation: AAI26417.1.
CCDSiCCDS13981.1. [P31941-1]
PIRiG01233.
RefSeqiNP_001180218.1. NM_001193289.1. [P31941-1]
NP_663745.1. NM_145699.3. [P31941-1]
XP_011545347.1. XM_011547045.1. [P31941-1]
UniGeneiHs.226307.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M65NMR-A1-199[»]
4XXOX-ray2.84A/B1-199[»]
ProteinModelPortaliP31941.
SMRiP31941. Positions 1-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128318. 2 interactions.
DIPiDIP-61365N.
STRINGi9606.ENSP00000249116.

Chemistry

BindingDBiP31941.
ChEMBLiCHEMBL1741179.

PTM databases

iPTMnetiP31941.
PhosphoSiteiP31941.

Polymorphism and mutation databases

BioMutaiAPOBEC3A.
DMDMi12644206.

Proteomic databases

EPDiP31941.
PaxDbiP31941.
PRIDEiP31941.

Protocols and materials databases

DNASUi200315.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249116; ENSP00000249116; ENSG00000128383. [P31941-1]
ENST00000402255; ENSP00000384359; ENSG00000128383. [P31941-1]
ENST00000570508; ENSP00000461288; ENSG00000262156. [P31941-1]
ENST00000618553; ENSP00000481904; ENSG00000128383. [P31941-1]
ENST00000623492; ENSP00000485234; ENSG00000262156. [P31941-1]
GeneIDi100913187.
200315.
KEGGihsa:100913187.
UCSCiuc003awn.2. human. [P31941-1]

Organism-specific databases

CTDi100913187.
200315.
GeneCardsiAPOBEC3A.
HGNCiHGNC:17343. APOBEC3A.
HPAiHPA043237.
MIMi607109. gene.
neXtProtiNX_P31941.
PharmGKBiPA24891.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JNPI. Eukaryota.
ENOG4111DZ4. LUCA.
GeneTreeiENSGT00530000062933.
HOGENOMiHOG000033754.
HOVERGENiHBG050434.
KOiK18750.
OMAiSGPRHLM.
OrthoDBiEOG71CFNW.
PhylomeDBiP31941.
TreeFamiTF331356.

Miscellaneous databases

NextBioi89887.
PROiP31941.
SOURCEiSearch...

Gene expression databases

BgeeiP31941.
CleanExiHS_APOBEC3A.
ExpressionAtlasiP31941. baseline and differential.
GenevisibleiP31941. 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. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[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], PROTEIN SEQUENCE OF 19-27; 31-35; 53-60; 112-123; 129-137 AND 192-198, FUNCTION.
    Tissue: Keratinocyte.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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].
  4. "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].
    Tissue: Brain.
  5. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 53-60; 112-121 AND 129-137.
    Tissue: Keratinocyte.
  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.
  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 HOST DEFENSE.
  9. "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 HOST DEFENSE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-70; GLU-72 AND CYS-106, TISSUE SPECIFICITY.
  10. "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.
  11. "Deaminase-independent inhibition of parvoviruses by the APOBEC3A cytidine deaminase."
    Narvaiza I., Linfesty D.C., Greener B.N., Hakata Y., Pintel D.J., Logue E., Landau N.R., Weitzman M.D.
    PLoS Pathog. 5:E1000439-E1000439(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AAV INHIBITION, SUBCELLULAR LOCATION.
  12. "Innate immune signaling induces high levels of TC-specific deaminase activity in primary monocyte-derived cells through expression of APOBEC3A isoforms."
    Thielen B.K., McNevin J.P., McElrath M.J., Hunt B.V., Klein K.C., Lingappa J.R.
    J. Biol. Chem. 285:27753-27766(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
  13. "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 FOREIGN DNA CLEARANCE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION.
  14. "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.
  15. "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.
  16. "APOBEC3A can activate the DNA damage response and cause cell-cycle arrest."
    Landry S., Narvaiza I., Linfesty D.C., Weitzman M.D.
    EMBO Rep. 12:444-450(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Structure-function analyses point to a polynucleotide-accommodating groove essential for APOBEC3A restriction activities."
    Bulliard Y., Narvaiza I., Bertero A., Peddi S., Roehrig U.F., Ortiz M., Zoete V., Castro-Diaz N., Turelli P., Telenti A., Michielin O., Weitzman M.D., Trono D.
    J. Virol. 85:1765-1776(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HOST DEFENSE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-28; HIS-29; LYS-30; ASN-57; LYS-60; ARG-69; GLU-72; TRP-98; ARG-128; TYR-130; ASP-131; ASP-133 AND TYR-136.
  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. "Somatic hypermutation of human mitochondrial and nuclear DNA by APOBEC3 cytidine deaminases, a pathway for DNA catabolism."
    Suspene R., Aynaud M.M., Guetard D., Henry M., Eckhoff G., Marchio A., Pineau P., Dejean A., Vartanian J.P., Wain-Hobson S.
    Proc. Natl. Acad. Sci. U.S.A. 108:4858-4863(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "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.
  21. "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.
  22. "Methylcytosine and normal cytosine deamination by the foreign DNA restriction enzyme APOBEC3A."
    Carpenter M.A., Li M., Rathore A., Lackey L., Law E.K., Land A.M., Leonard B., Shandilya S.M., Bohn M.F., Schiffer C.A., Brown W.L., Harris R.S.
    J. Biol. Chem. 287:34801-34808(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "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.
  24. "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.
  25. "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.
  26. Cited for: REVIEW.

Entry informationi

Entry nameiABC3A_HUMAN
AccessioniPrimary (citable) accession number: P31941
Secondary accession number(s): A0AVM1
, Q12807, Q5JZ93, Q9UH18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 11, 2001
Last modified: May 11, 2016
This is version 143 of the entry and version 3 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, Direct protein sequencing, 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.