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Entry version 179 (13 Nov 2019)
Sequence version 1 (01 Mar 2001)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi65ZincBy similarity1
Metal bindingi97ZincBy similarity1
Metal bindingi100ZincBy similarity1
Metal bindingi257Zinc; catalytic3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei259Proton donorCurated1
Metal bindingi288Zinc; catalytic3 Publications1
Metal bindingi291Zinc; catalytic3 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processAntiviral defense, Host-virus interaction, Immunity, Innate immunity
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.4.B9 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-180585 Vif-mediated degradation of APOBEC3G
R-HSA-180689 APOBEC3G mediated resistance to HIV-1 infection

SIGNOR Signaling Network Open Resource

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SIGNORi
Q9HC16

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
ORF Names:MDS019
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 22

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:17357 APOBEC3G

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
607113 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9HC16

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi67E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-259. 3 Publications1
Mutagenesisi67E → A: No effect on cytidine deaminase and antiviral activity. 3 Publications1
Mutagenesisi67E → Q: Decreases cytidine deaminase activity. 3 Publications1
Mutagenesisi81H → A: Decreases cytidine deaminase activity. 2 Publications1
Mutagenesisi85E → Q: Does not decrease cytidine deaminase activity. 1 Publication1
Mutagenesisi97C → A: Decreases cytidine deaminase activity. 2 Publications1
Mutagenesisi100C → A or S: Decreases cytidine deaminase activity. 3 Publications1
Mutagenesisi128D → K: Complete loss of VIF-induced degradation. 1 Publication1
Mutagenesisi213R → A: Slightly reduces enzyme activity. 2 Publications1
Mutagenesisi213R → E: Reduces enzyme activity. 2 Publications1
Mutagenesisi215R → A or E: Abolishes enzyme activity. 2 Publications1
Mutagenesisi217E → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-247. 1 Publication1
Mutagenesisi218T → A: Loss of phosphorylation. No effect on cytidine deaminase activity or HIV-1 restriction activity. 1 Publication1
Mutagenesisi218T → E: Phosphomimetic mutant which shows loss of cytidine deaminase activity and HIV-1 restriction activity. 1 Publication1
Mutagenesisi221C → S: Does not decrease cytidine deaminase activity. 1 Publication1
Mutagenesisi244N → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi247P → K: Modifies the spectrum of action against mobile genetic elements; when associated with K-217. 1 Publication1
Mutagenesisi256R → E: Strongly reduces enzyme activity. 1
Mutagenesisi257H → A: Decreases cytidine deaminase activity. 2 Publications1
Mutagenesisi259E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity. 4 Publications1
Mutagenesisi259E → A: Loss of cytidine deaminase activity and significant decrease in antiviral activity; when associated with A-67. 4 Publications1
Mutagenesisi259E → Q: Decreases cytidine deaminase activity and antiviral activity. 4 Publications1
Mutagenesisi285W → A: Abolishes enzyme activity. 2 Publications1
Mutagenesisi288C → A: Decreases cytidine deaminase activity. 2 Publications1
Mutagenesisi291C → A or S: Decreases cytidine deaminase activity. 3 Publications1
Mutagenesisi313R → A or E: Abolishes enzyme activity. 1 Publication1
Mutagenesisi315Y → A: Abolishes enzyme activity. 1 Publication1
Mutagenesisi320R → A: Slightly reduces enzyme activity. 1 Publication1
Mutagenesisi320R → E: Reduces enzyme activity. 1 Publication1
Mutagenesisi323E → Q: Does not decrease cytidine deaminase activity. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
60489

Open Targets

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OpenTargetsi
ENSG00000239713

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24897

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q9HC16

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1741217

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
APOBEC3G

Domain mapping of disease mutations (DMDM)

More...
DMDMi
44887683

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001717611 – 384DNA dC->dU-editing enzyme APOBEC-3GAdd BLAST384

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei32Phosphothreonine; by PKA2 Publications1
Modified residuei218Phosphothreonine; by PKA and CAMK21 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
Q9HC16

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9HC16

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9HC16

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q9HC16

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9HC16

PeptideAtlas

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PeptideAtlasi
Q9HC16

PRoteomics IDEntifications database

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PRIDEi
Q9HC16

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
81623 [Q9HC16-1]
81624 [Q9HC16-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9HC16

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9HC16

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by IFN-alpha.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000239713 Expressed in 209 organ(s), highest expression level in blood

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9HC16 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA001812
HPA073637

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

10 Publications

(Microbial infection) Interacts with HIV-1 Vif and reverse transcriptase/ribonuclease H.

4 Publications

(Microbial infection) Interacts with hepatitis B virus capsid protein.

1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei244Interaction with DNACurated1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
121920, 15 interactors

Database of interacting proteins

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DIPi
DIP-37519N

Protein interaction database and analysis system

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IntActi
Q9HC16, 9 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000385057

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q9HC16

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1384
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9HC16

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q9HC16

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini29 – 138CMP/dCMP-type deaminase 1PROSITE-ProRule annotationAdd BLAST110
Domaini214 – 328CMP/dCMP-type deaminase 2PROSITE-ProRule annotationAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 60Essential for cytoplasmic localizationAdd BLAST60
Regioni209 – 336Necessary for homooligomerizationAdd BLAST128
Regioni213 – 215Interaction with DNACurated3
Regioni313 – 320Interaction with DNACurated8

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410JBA1 Eukaryota
ENOG41119MS LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000161999

KEGG Orthology (KO)

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KOi
K18750

Identification of Orthologs from Complete Genome Data

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OMAi
GEPFQPW

Database of Orthologous Groups

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OrthoDBi
586309at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9HC16

TreeFam database of animal gene trees

More...
TreeFami
TF331356

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016192 APOBEC/CMP_deaminase_Zn-bd
IPR040551 APOBEC3G
IPR002125 CMP_dCMP_dom
IPR016193 Cytidine_deaminase-like

The PANTHER Classification System

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PANTHERi
PTHR13857:SF20 PTHR13857:SF20, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53927 SSF53927, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00903 CYT_DCMP_DEAMINASES_1, 1 hit
PS51747 CYT_DCMP_DEAMINASES_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q9HC16-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti162S → N no nucleotide entry (PubMed:14557625).Curated1
Sequence conflicti370D → Y no nucleotide entry (PubMed:14557625).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_017837186H → R1 PublicationCorresponds to variant dbSNP:rs8177832Ensembl.1
Natural variantiVAR_048723256R → H. Corresponds to variant dbSNP:rs17000736Ensembl.1
Natural variantiVAR_025060275Q → E1 PublicationCorresponds to variant dbSNP:rs17496046Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_00958858 – 79VYSEL…SKWRK → VPPGLQSLCRQELSQLGKQT TH in isoform 3. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_00958980 – 384Missing in isoform 3. 1 PublicationAdd BLAST305

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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 No translation available.
AL078641 Genomic DNA No translation available.
CH471095 Genomic DNA Translation: EAW60292.1
BC024268 mRNA Translation: AAH24268.1
BC061914 mRNA Translation: AAH61914.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS13984.1 [Q9HC16-1]

NCBI Reference Sequences

More...
RefSeqi
NP_068594.1, NM_021822.3 [Q9HC16-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000407997; ENSP00000385057; ENSG00000239713 [Q9HC16-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
60489

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:60489

UCSC genome browser

More...
UCSCi
uc003awx.3 human [Q9HC16-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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 No translation available.
AL078641 Genomic DNA No translation available.
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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]
5ZVAX-ray2.30A/B198-221[»]
5ZVBX-ray2.00A/B198-221[»]
6BUXX-ray1.86A189-384[»]
6BWYX-ray2.90A/B/E/G195-384[»]
6K3JNMR-A197-384[»]
6K3KNMR-A197-384[»]
SMRiQ9HC16
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi121920, 15 interactors
DIPiDIP-37519N
IntActiQ9HC16, 9 interactors
STRINGi9606.ENSP00000385057

Chemistry databases

BindingDBiQ9HC16
ChEMBLiCHEMBL1741217

PTM databases

iPTMnetiQ9HC16
PhosphoSitePlusiQ9HC16

Polymorphism and mutation databases

BioMutaiAPOBEC3G
DMDMi44887683

Proteomic databases

EPDiQ9HC16
jPOSTiQ9HC16
MassIVEiQ9HC16
MaxQBiQ9HC16
PaxDbiQ9HC16
PeptideAtlasiQ9HC16
PRIDEiQ9HC16
ProteomicsDBi81623 [Q9HC16-1]
81624 [Q9HC16-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
200316
60489

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
60489
DisGeNETi60489

GeneCards: human genes, protein and diseases

More...
GeneCardsi
APOBEC3G
HGNCiHGNC:17357 APOBEC3G
HPAiHPA001812
HPA073637
MIMi607113 gene
neXtProtiNX_Q9HC16
OpenTargetsiENSG00000239713
PharmGKBiPA24897

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410JBA1 Eukaryota
ENOG41119MS LUCA
GeneTreeiENSGT00940000161999
KOiK18750
OMAiGEPFQPW
OrthoDBi586309at2759
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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
APOBEC3G human
EvolutionaryTraceiQ9HC16

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
APOBEC3G

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
60489
PharosiQ9HC16

Protein Ontology

More...
PROi
PR:Q9HC16

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000239713 Expressed in 209 organ(s), highest expression level in blood
GenevisibleiQ9HC16 HS

Family and domain databases

InterProiView protein in InterPro
IPR016192 APOBEC/CMP_deaminase_Zn-bd
IPR040551 APOBEC3G
IPR002125 CMP_dCMP_dom
IPR016193 Cytidine_deaminase-like
PANTHERiPTHR13857:SF20 PTHR13857:SF20, 2 hits
SUPFAMiSSF53927 SSF53927, 1 hit
PROSITEiView protein in PROSITE
PS00903 CYT_DCMP_DEAMINASES_1, 1 hit
PS51747 CYT_DCMP_DEAMINASES_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiABC3G_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9HC16
Secondary accession number(s): B2RDR9
, Q45F02, Q5TF77, Q7Z2N1, Q7Z2N4, Q9H9H8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2001
Last modified: November 13, 2019
This is version 179 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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. SIMILARITY comments
    Index of protein domains and families
  4. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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