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Protein

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

Gene

APOBEC3G

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. Exhibits potent antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double-stranded RNA. Exhibits antiviral activity also against simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV). May inhibit the mobility of LTR and non-LTR retrotransposons.22 Publications

Catalytic activityi

Deoxycytidine + H2O = deoxyuridine + NH3.4 Publications

Cofactori

Enzyme regulationi

Assembly into ribonucleoprotein complexes of high-molecular-mass (HMM) inhibits its enzymatic activity. Antiviral activity is neutralized by the HIV-1 virion infectivity factor (VIF), that prevents its incorporation into progeny HIV-1 virions by both inhibiting its translation and/or by inducing its ubiquitination and subsequent degradation by the 26S proteasome. Can also be neutralized by simian immunodeficiency virus sooty mangabey monkey virus (SIV-sm) and chimpanzee immunodeficiency virus (SIV-cpz) VIF.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi65 – 651ZincBy similarity
Metal bindingi97 – 971ZincBy similarity
Metal bindingi100 – 1001ZincBy similarity
Metal bindingi257 – 2571Zinc; catalytic3 Publications
Active sitei259 – 2591Proton donorCurated
Metal bindingi288 – 2881Zinc; catalytic3 Publications
Metal bindingi291 – 2911Zinc; catalytic3 Publications

GO - Molecular functioni

  • cytidine deaminase activity Source: HGNC
  • dCTP deaminase activity Source: Reactome
  • deoxycytidine deaminase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • base conversion or substitution editing Source: HGNC
  • cytidine deamination Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • DNA cytosine deamination Source: UniProtKB
  • innate immune response Source: HGNC
  • negative regulation of single stranded viral RNA replication via double stranded DNA intermediate Source: UniProtKB
  • negative regulation of transposition Source: UniProtKB
  • negative regulation of viral genome replication Source: UniProtKB
  • negative regulation of viral process Source: HGNC
  • positive regulation of defense response to virus by host Source: HGNC
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

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

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.B9. 2681.
ReactomeiR-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-180689. APOBEC3G mediated resistance to HIV-1 infection.
SIGNORiQ9HC16.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA dC->dU-editing enzyme APOBEC-3G (EC:3.5.4.-)
Alternative name(s):
APOBEC-related cytidine deaminase
Short name:
APOBEC-related protein
Short name:
ARCD
APOBEC-related protein 9
Short name:
ARP-9
CEM-15
Short name:
CEM15
Deoxycytidine deaminase
Short name:
A3G
Gene namesi
ORF Names:MDS019
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:17357. APOBEC3G.

Subcellular locationi

  • Cytoplasm
  • Nucleus
  • CytoplasmP-body

  • Note: Mainly cytoplasmic. Small amount are found in the nucleus. During HIV-1 infection, virion-encapsidated in absence of HIV-1 VIF.

GO - Cellular componenti

  • apolipoprotein B mRNA editing enzyme complex Source: HGNC
  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytosol Source: Reactome
  • intracellular ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-259. 3 Publications
Mutagenesisi67 – 671E → A: No effect on cytidine deaminase and antiviral activity. 3 Publications
Mutagenesisi67 – 671E → Q: Decreases cytidine deaminase activity. 3 Publications
Mutagenesisi81 – 811H → A: Decreases cytidine deaminase activity. 2 Publications
Mutagenesisi85 – 851E → Q: Does not decrease cytidine deaminase activity. 1 Publication
Mutagenesisi97 – 971C → A: Decreases cytidine deaminase activity. 2 Publications
Mutagenesisi100 – 1001C → A or S: Decreases cytidine deaminase activity. 3 Publications
Mutagenesisi128 – 1281D → K: Complete loss of VIF-induced degradation. 1 Publication
Mutagenesisi213 – 2131R → A: Slightly reduces enzyme activity. 2 Publications
Mutagenesisi213 – 2131R → E: Reduces enzyme activity. 2 Publications
Mutagenesisi215 – 2151R → A or E: Abolishes enzyme activity. 2 Publications
Mutagenesisi217 – 2171E → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-247. 1 Publication
Mutagenesisi218 – 2181T → A: Loss of phosphorylation. No effect on cytidine deaminase activity or HIV-1 restriction activity. 1 Publication
Mutagenesisi218 – 2181T → E: Phosphomimetic mutant which shows loss of cytidine deaminase activity and HIV-1 restriction activity. 1 Publication
Mutagenesisi221 – 2211C → S: Does not decrease cytidine deaminase activity. 1 Publication
Mutagenesisi244 – 2441N → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi247 – 2471P → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-217. 1 Publication
Mutagenesisi256 – 2561R → E: Strongly reduces enzyme activity.
Mutagenesisi257 – 2571H → A: Decreases cytidine deaminase activity. 2 Publications
Mutagenesisi259 – 2591E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity. 4 Publications
Mutagenesisi259 – 2591E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-67. 4 Publications
Mutagenesisi259 – 2591E → Q: Decreases cytidine deaminase activity and antiviral activity. 4 Publications
Mutagenesisi285 – 2851W → A: Abolishes enzyme activity. 2 Publications
Mutagenesisi288 – 2881C → A: Decreases cytidine deaminase activity. 2 Publications
Mutagenesisi291 – 2911C → A or S: Decreases cytidine deaminase activity. 3 Publications
Mutagenesisi313 – 3131R → A or E: Abolishes enzyme activity. 1 Publication
Mutagenesisi315 – 3151Y → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi320 – 3201R → A: Slightly reduces enzyme activity. 1 Publication
Mutagenesisi320 – 3201R → E: Reduces enzyme activity. 1 Publication
Mutagenesisi323 – 3231E → Q: Does not decrease cytidine deaminase activity. 1 Publication

Organism-specific databases

PharmGKBiPA24897.

Chemistry

ChEMBLiCHEMBL1741217.

Polymorphism and mutation databases

BioMutaiAPOBEC3G.
DMDMi44887683.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 384384DNA dC->dU-editing enzyme APOBEC-3GPRO_0000171761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphothreonine; by PKA2 Publications
Modified residuei218 – 2181Phosphothreonine; by PKA and CAMK21 Publication

Post-translational modificationi

Ubiquitinated in the presence of HIV-1 VIF. Association with VIF targets the protein for proteolysis by the ubiquitin-dependent proteasome pathway.
Phosphorylation at Thr-32 reduces its binding to HIV-1 VIF and subsequent ubiquitination and degradation thus promoting its antiviral activity.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9HC16.
MaxQBiQ9HC16.
PaxDbiQ9HC16.
PeptideAtlasiQ9HC16.
PRIDEiQ9HC16.

PTM databases

iPTMnetiQ9HC16.
PhosphoSiteiQ9HC16.

Expressioni

Tissue specificityi

Expressed in spleen, testes, ovary and peripheral blood leukocytes and CD4+ lymphocytes. Also expressed in non-permissive peripheral blood mononuclear cells, and several tumor cell lines; no expression detected in permissive lymphoid and non-lymphoid cell lines. Exists only in the LMM form in peripheral blood-derived resting CD4 T-cells and monocytes, both of which are refractory to HIV-1 infection. LMM is converted to a HMM complex when resting CD4 T-cells are activated or when monocytes are induced to differentiate into macrophages. This change correlates with increased susceptibility of these cells to HIV-1 infection.3 Publications

Inductioni

Up-regulated by IFN-alpha.

Gene expression databases

BgeeiENSG00000239713.
CleanExiHS_APOBEC3G.
GenevisibleiQ9HC16. HS.

Organism-specific databases

HPAiHPA001812.

Interactioni

Subunit structurei

Homodimer. Homooligomer. Can bind RNA to form ribonucleoprotein complexes of high-molecular-mass (HMM) or low-molecular-mass (LMM). HMM is inactive and heterogeneous in protein composition because of binding nonselectively to cellular RNAs, which in turn are associated with variety of cellular proteins. The LMM form which is enzymatically active has few or no RNAs associated. Its ability to form homooligomer is distinct from its ability to assemble into HMM. Interacts with APOBEC3B, APOBEC3F, MOV10, AGO2, EIF4E, EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent manner. Interacts with AGO1, AGO3 and PKA/PRKACA. Interacts with HIV-1 VIF and reverse transcriptase/ribonuclease H. Interacts with hepatitis B virus capsid protein.15 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei244 – 2441Interaction with DNACurated

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi121920. 12 interactions.
DIPiDIP-37519N.
IntActiQ9HC16. 3 interactions.
MINTiMINT-1428867.
STRINGi9606.ENSP00000385057.

Chemistry

BindingDBiQ9HC16.

Structurei

Secondary structure

1
384
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi195 – 1973Combined sources
Helixi199 – 2068Combined sources
Beta strandi213 – 2175Combined sources
Beta strandi219 – 22810Combined sources
Beta strandi231 – 2344Combined sources
Helixi236 – 2383Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi247 – 2504Combined sources
Helixi258 – 2658Combined sources
Helixi266 – 2694Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi277 – 2859Combined sources
Helixi289 – 30113Combined sources
Beta strandi305 – 3139Combined sources
Beta strandi318 – 3203Combined sources
Helixi321 – 33010Combined sources
Beta strandi334 – 3374Combined sources
Helixi340 – 35011Combined sources
Helixi364 – 37916Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JYWNMR-A198-384[»]
2KBONMR-A193-384[»]
2KEMNMR-A191-384[»]
3E1UX-ray2.30A197-380[»]
3IQSX-ray2.30A197-380[»]
3IR2X-ray2.25A/B191-384[»]
3V4JX-ray2.04A/B191-384[»]
3V4KX-ray1.38A/B191-380[»]
4ROVX-ray1.80A/B193-384[»]
4ROWX-ray1.70A193-384[»]
ProteinModelPortaliQ9HC16.
SMRiQ9HC16. Positions 12-381.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HC16.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 138110CMP/dCMP-type deaminase 1PROSITE-ProRule annotationAdd
BLAST
Domaini214 – 328115CMP/dCMP-type deaminase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6060Essential for cytoplasmic localizationAdd
BLAST
Regioni209 – 336128Necessary for homooligomerizationAdd
BLAST
Regioni213 – 2153Interaction with DNACurated
Regioni313 – 3208Interaction with DNACurated

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.2 Publications

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410JBA1. Eukaryota.
ENOG41119MS. LUCA.
GeneTreeiENSGT00530000062933.
HOVERGENiHBG050434.
KOiK18750.
OMAiWDPDYQE.
OrthoDBiEOG091G07EI.
PhylomeDBiQ9HC16.
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. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9HC16-1) [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
MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPPLD
60 70 80 90 100
AKIFRGQVYS ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC
110 120 130 140 150
TRDMATFLAE DPKVTLTIFV ARLYYFWDPD YQEALRSLCQ KRDGPRATMK
160 170 180 190 200
IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK YYILLHIMLG EILRHSMDPP
210 220 230 240 250
TFTFNFNNEP WVRGRHETYL CYEVERMHND TWVLLNQRRG FLCNQAPHKH
260 270 280 290 300
GFLEGRHAEL CFLDVIPFWK LDLDQDYRVT CFTSWSPCFS CAQEMAKFIS
310 320 330 340 350
KNKHVSLCIF TARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF
360 370 380
VDHQGCPFQP WDGLDEHSQD LSGRLRAILQ NQEN
Length:384
Mass (Da):46,408
Last modified:March 1, 2001 - v1
Checksum:i60525DC3B7D903D6
GO
Isoform 3 (identifier: Q9HC16-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-79: VYSELKYHPEMRFFHWFSKWRK → VPPGLQSLCRQELSQLGKQTTH
     80-384: Missing.

Note: May be due to a competing donor splice site.
Show »
Length:79
Mass (Da):9,386
Checksum:i359E8ACA44AB074A
GO

Sequence cautioni

The sequence CAB45274 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621S → N no nucleotide entry (PubMed:14557625).Curated
Sequence conflicti370 – 3701D → Y no nucleotide entry (PubMed:14557625).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti186 – 1861H → R.1 Publication
Corresponds to variant rs8177832 [ dbSNP | Ensembl ].
VAR_017837
Natural varianti256 – 2561R → H.
Corresponds to variant rs17000736 [ dbSNP | Ensembl ].
VAR_048723
Natural varianti275 – 2751Q → E.1 Publication
Corresponds to variant rs17496046 [ dbSNP | Ensembl ].
VAR_025060

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 7922VYSEL…SKWRK → VPPGLQSLCRQELSQLGKQT TH in isoform 3. 1 PublicationVSP_009588Add
BLAST
Alternative sequencei80 – 384305Missing in isoform 3. 1 PublicationVSP_009589Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022802 mRNA. No translation available.
AK315650 mRNA. Translation: BAG38016.1.
AF182420 mRNA. Translation: AAG14956.1.
CR456472 mRNA. Translation: CAG30358.1.
DQ147772 Genomic DNA. Translation: AAZ38722.1.
AL022318 Genomic DNA. Translation: CAB45274.1. Sequence problems.
AL078641, AL022318 Genomic DNA. Translation: CAI21556.1.
AL022318, AL078641 Genomic DNA. Translation: CAI17900.1.
CH471095 Genomic DNA. Translation: EAW60292.1.
BC024268 mRNA. Translation: AAH24268.1.
BC061914 mRNA. Translation: AAH61914.1.
CCDSiCCDS13984.1. [Q9HC16-1]
RefSeqiNP_068594.1. NM_021822.3. [Q9HC16-1]
UniGeneiHs.660143.

Genome annotation databases

EnsembliENST00000407997; ENSP00000385057; ENSG00000239713. [Q9HC16-1]
ENST00000452957; ENSP00000413376; ENSG00000239713. [Q9HC16-1]
GeneIDi60489.
KEGGihsa:60489.
UCSCiuc003awx.3. human. [Q9HC16-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs
Protein Spotlight

Protein wars - Issue 45 of April 2004

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK022802 mRNA. No translation available.
AK315650 mRNA. Translation: BAG38016.1.
AF182420 mRNA. Translation: AAG14956.1.
CR456472 mRNA. Translation: CAG30358.1.
DQ147772 Genomic DNA. Translation: AAZ38722.1.
AL022318 Genomic DNA. Translation: CAB45274.1. Sequence problems.
AL078641, AL022318 Genomic DNA. Translation: CAI21556.1.
AL022318, AL078641 Genomic DNA. Translation: CAI17900.1.
CH471095 Genomic DNA. Translation: EAW60292.1.
BC024268 mRNA. Translation: AAH24268.1.
BC061914 mRNA. Translation: AAH61914.1.
CCDSiCCDS13984.1. [Q9HC16-1]
RefSeqiNP_068594.1. NM_021822.3. [Q9HC16-1]
UniGeneiHs.660143.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JYWNMR-A198-384[»]
2KBONMR-A193-384[»]
2KEMNMR-A191-384[»]
3E1UX-ray2.30A197-380[»]
3IQSX-ray2.30A197-380[»]
3IR2X-ray2.25A/B191-384[»]
3V4JX-ray2.04A/B191-384[»]
3V4KX-ray1.38A/B191-380[»]
4ROVX-ray1.80A/B193-384[»]
4ROWX-ray1.70A193-384[»]
ProteinModelPortaliQ9HC16.
SMRiQ9HC16. Positions 12-381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121920. 12 interactions.
DIPiDIP-37519N.
IntActiQ9HC16. 3 interactions.
MINTiMINT-1428867.
STRINGi9606.ENSP00000385057.

Chemistry

BindingDBiQ9HC16.
ChEMBLiCHEMBL1741217.

PTM databases

iPTMnetiQ9HC16.
PhosphoSiteiQ9HC16.

Polymorphism and mutation databases

BioMutaiAPOBEC3G.
DMDMi44887683.

Proteomic databases

EPDiQ9HC16.
MaxQBiQ9HC16.
PaxDbiQ9HC16.
PeptideAtlasiQ9HC16.
PRIDEiQ9HC16.

Protocols and materials databases

DNASUi200316.
60489.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000407997; ENSP00000385057; ENSG00000239713. [Q9HC16-1]
ENST00000452957; ENSP00000413376; ENSG00000239713. [Q9HC16-1]
GeneIDi60489.
KEGGihsa:60489.
UCSCiuc003awx.3. human. [Q9HC16-1]

Organism-specific databases

CTDi60489.
GeneCardsiAPOBEC3G.
HGNCiHGNC:17357. APOBEC3G.
HPAiHPA001812.
MIMi607113. gene.
neXtProtiNX_Q9HC16.
PharmGKBiPA24897.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410JBA1. Eukaryota.
ENOG41119MS. LUCA.
GeneTreeiENSGT00530000062933.
HOVERGENiHBG050434.
KOiK18750.
OMAiWDPDYQE.
OrthoDBiEOG091G07EI.
PhylomeDBiQ9HC16.
TreeFamiTF331356.

Enzyme and pathway databases

BRENDAi3.5.4.B9. 2681.
ReactomeiR-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-180689. APOBEC3G mediated resistance to HIV-1 infection.
SIGNORiQ9HC16.

Miscellaneous databases

ChiTaRSiAPOBEC3G. human.
EvolutionaryTraceiQ9HC16.
GeneWikiiAPOBEC3G.
GenomeRNAii60489.
PROiQ9HC16.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000239713.
CleanExiHS_APOBEC3G.
GenevisibleiQ9HC16. 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. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiABC3G_HUMAN
AccessioniPrimary (citable) accession number: Q9HC16
Secondary accession number(s): B2RDR9
, Q45F02, Q5TF77, Q7Z2N1, Q7Z2N4, Q9H9H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2001
Last modified: September 7, 2016
This is version 151 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

Accumulation of APOBEC3G induced non-lethal hypermutation could contribute to the genetic variation of primate lentiviral populations.
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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  7. 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.