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UniProtKB - Q8IUX4 (ABC3F_HUMAN)

Entry version 164 (02 Jun 2021)
Sequence version 3 (23 Oct 2007)
Previous versions | rss
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Protein

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

Gene

APOBEC3F

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 antiviral activity against Vif-deficient HIV-1 (PubMed:15152192, PubMed:23001005).

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 hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.

14 Publications

Miscellaneous

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%5Fsection">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+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Antiviral activity is neutralized by the HIV-1 virion infectivity factor (Vif), that prevents its incorporation into progeny virions by both inhibiting its translation and/or by inducing its ubiquitination and subsequent degradation by the 26S proteasome.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi65ZincPROSITE-ProRule annotation1
Metal bindingi96ZincPROSITE-ProRule annotation1
Metal bindingi99ZincPROSITE-ProRule annotation1
Metal bindingi249Zinc; catalyticPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei251Proton donorPROSITE-ProRule annotation1
Metal bindingi280Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi283Zinc; catalyticPROSITE-ProRule annotation1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Immunity, Innate immunity
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.5.4.38, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q8IUX4

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q8IUX4

<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%5Fand%5Ftaxonomy%5Fsection">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-3F (EC:3.5.4.38)
Alternative name(s):
Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F
Short name:
A3F
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
Name:APOBEC3F
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

More...HGNCi		HGNC:17356, APOBEC3F

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		608993, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q8IUX4

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000128394.16

<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

Keywords - Cellular componenti

Cytoplasm

<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%5Fand%5Fbiotech%5Fsection">'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: Decrease in cytidine deaminase and antiviral activity; when associated with A-251. 1 Publication1
Mutagenesisi67E → A: No effect on cytidine deaminase and antiviral activity. 1 Publication1
Mutagenesisi251E → A: Decrease in cytidine deaminase and antiviral activity. 1 Publication1
Mutagenesisi251E → A: Decrease in cytidine deaminase and antiviral activity; when associated with A-67. 1 Publication1
Mutagenesisi251E → Q: Remains able to bind Vif. 1 Publication1
Mutagenesisi255L → D: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication1
Mutagenesisi258F → A: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication1
Mutagenesisi259C → K: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication1
Mutagenesisi262 – 263IL → AA: Resistant to HIV-1 Vif and abolishes Vif binding but is still efficiently incorporated into the virion. 1 Publication2
Mutagenesisi264S → D: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication1
Mutagenesisi269Y → A: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication1
Mutagenesisi289E → K: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication1
Mutagenesisi290F → K: Resistant to HIV-1 Vif and reduces Vif binding but is still efficiently incorporated into the virion. 1 Publication1
Mutagenesisi294H → D: Resistant to HIV-1 Vif, reduces Vif binding and abolishes incorporation into the virion. 1 Publication1
Mutagenesisi324E → K or A: Resistant to HIV-1 Vif and reduces Vif binding. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		200316

Open Targets

More...OpenTargetsi		ENSG00000128394

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA24896

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q8IUX4, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2007626

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		APOBEC3F

Domain mapping of disease mutations (DMDM)

More...DMDMi		161784334

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001717571 – 373DNA dC->dU-editing enzyme APOBEC-3FAdd BLAST373

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q8IUX4

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q8IUX4

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q8IUX4

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q8IUX4

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

More...PaxDbi		Q8IUX4

PeptideAtlas

More...PeptideAtlasi		Q8IUX4

PRoteomics IDEntifications database

More...PRIDEi		Q8IUX4

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		70623 [Q8IUX4-1]
70624 [Q8IUX4-2]
70625 [Q8IUX4-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q8IUX4

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

More...PhosphoSitePlusi		Q8IUX4

<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

Widely expressed. Highly expressed in ovary.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		ENSG00000128394, Expressed in muscle tissue and 150 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q8IUX4, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000128394, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with APOBEC3G in an RNA-dependent manner (PubMed:16699599).

Interacts with AGO1, AGO2 and AGO3 (PubMed:22915799).

2 Publications

(Microbial infection) Interacts with HIV-1 Vif (PubMed:15152192, PubMed:23001005). In the absence of Vif protein, specifically packaged into HIV-1 virions (PubMed:15152192).

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Q8IUX4
With#Exp.IntAct
itself2EBI-11306991,EBI-11306991

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		128319, 19 interactors

Database of interacting proteins

More...DIPi		DIP-59966N

Protein interaction database and analysis system

More...IntActi		Q8IUX4, 12 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000309749

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q8IUX4, protein

<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

1373
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

More...SMRi		Q8IUX4

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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%5Fand%5Fdomains%5Fsection">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 – 137CMP/dCMP-type deaminase 1PROSITE-ProRule annotationAdd BLAST109
Domaini174 – 321CMP/dCMP-type deaminase 2PROSITE-ProRule annotationAdd BLAST148

<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.1 Publication

<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

Belongs to the cytidine and deoxycytidylate deaminase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4075, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000162695

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_047918_0_0_1

Identification of Orthologs from Complete Genome Data

More...OMAi		PWNGLNE

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q8IUX4

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
IPR002125, CMP_dCMP_dom
IPR016193, Cytidine_deaminase-like

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53927, SSF53927, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00903, CYT_DCMP_DEAMINASES_1, 2 hits
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%5Flength">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 (3)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 3 <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: Q8IUX4-1) [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 TKGPSRPRLD 
        60         70         80         90        100
AKIFRGQVYS QPEHHAEMCF LSWFCGNQLP AYKCFQITWF VSWTPCPDCV 
       110        120        130        140        150
AKLAEFLAEH PNVTLTISAA RLYYYWERDY RRALCRLSQA GARVKIMDDE 
       160        170        180        190        200
EFAYCWENFV YSEGQPFMPW YKFDDNYAFL HRTLKEILRN PMEAMYPHIF 
       210        220        230        240        250
YFHFKNLRKA YGRNESWLCF TMEVVKHHSP VSWKRGVFRN QVDPETHCHA 
       260        270        280        290        300
ERCFLSWFCD DILSPNTNYE VTWYTSWSPC PECAGEVAEF LARHSNVNLT 
       310        320        330        340        350
IFTARLYYFW DTDYQEGLRS LSQEGASVEI MGYKDFKYCW ENFVYNDDEP 
       360        370 
FKPWKGLKYN FLFLDSKLQE ILE
Length:373
Mass (Da):45,020
Last modified:October 23, 2007 - v3
<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:iAF1A0E13830695F4
GO
Isoform 2 (identifier: Q8IUX4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-79: VYSQPEHHAEMCFLSWFCGNQL → VPPGLQSLCRQELSQLGKQTTH
     80-373: Missing.

Note: May be due to a competing donor splice site.Curated
Show »
Length:79
Mass (Da):9,445
Checksum:i03ABEACA44AB0748
GO
Isoform 3 (identifier: Q8IUX4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-113: YSQPEHHAEM...AEFLAEHPNV → PRSFIRAPFQ...LTAGREQGRP
     114-373: Missing.

Show »
Length:101
Mass (Da):11,823
Checksum:i1659A5E223CB1EFE
GO

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_03835548R → P1 PublicationCorresponds to variant dbSNP:rs35053197Ensembl.1
Natural variantiVAR_01814561Q → L. Corresponds to variant dbSNP:rs2076109Ensembl.1
Natural variantiVAR_01814697P → L. Corresponds to variant dbSNP:rs201939303Ensembl.1
Natural variantiVAR_018147108A → S1 PublicationCorresponds to variant dbSNP:rs2020390Ensembl.1
Natural variantiVAR_025058178A → T1 PublicationCorresponds to variant dbSNP:rs34182094Ensembl.1
Natural variantiVAR_018148231V → I1 PublicationCorresponds to variant dbSNP:rs2076101Ensembl.1
Natural variantiVAR_025059307Y → C1 PublicationCorresponds to variant dbSNP:rs12157816EnsemblClinVar.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_00980358 – 79VYSQP…CGNQL → VPPGLQSLCRQELSQLGKQT TH in isoform 2. 1 PublicationAdd BLAST22
Alternative sequenceiVSP_04275459 – 113YSQPE…EHPNV → PRSFIRAPFQVLSSPFGQCA PPHGTAQVQWPPQLTAGREQ GRP in isoform 3. 1 PublicationAdd BLAST55
Alternative sequenceiVSP_00980480 – 373Missing in isoform 2. 1 PublicationAdd BLAST294
Alternative sequenceiVSP_042755114 – 373Missing in isoform 3. 1 PublicationAdd BLAST260

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
CR456395 mRNA Translation: CAG30281.1
DQ146365 Genomic DNA Translation: AAZ38720.1
AL022318 Genomic DNA No translation available.
CH471095 Genomic DNA Translation: EAW60288.1
CH471095 Genomic DNA Translation: EAW60289.1
BC038808 mRNA Translation: AAH38808.1
BC061914 mRNA Translation: AAH61914.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS33648.1 [Q8IUX4-1]
CCDS33649.1 [Q8IUX4-3]

NCBI Reference Sequences

More...RefSeqi		NP_001006667.1, NM_001006666.1 [Q8IUX4-3]
NP_660341.2, NM_145298.5 [Q8IUX4-1]
XP_016884132.1, XM_017028643.1 [Q8IUX4-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000308521; ENSP00000309749; ENSG00000128394 [Q8IUX4-1]
ENST00000381565; ENSP00000370977; ENSG00000128394 [Q8IUX4-3]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		200316

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:200316

UCSC genome browser

More...UCSCi		uc003awv.4, human [Q8IUX4-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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%5Freferences%5Fsection">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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR456395 mRNA Translation: CAG30281.1
DQ146365 Genomic DNA Translation: AAZ38720.1
AL022318 Genomic DNA No translation available.
CH471095 Genomic DNA Translation: EAW60288.1
CH471095 Genomic DNA Translation: EAW60289.1
BC038808 mRNA Translation: AAH38808.1
BC061914 mRNA Translation: AAH61914.1
CCDSiCCDS33648.1 [Q8IUX4-1]
CCDS33649.1 [Q8IUX4-3]
RefSeqiNP_001006667.1, NM_001006666.1 [Q8IUX4-3]
NP_660341.2, NM_145298.5 [Q8IUX4-1]
XP_016884132.1, XM_017028643.1 [Q8IUX4-3]

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
3WUSX-ray2.54A/B187-373[»]
4IOUX-ray2.75A/B/C/D185-373[»]
4J4JX-ray3.10A/B218-373[»]
5HX4X-ray1.92A/B185-373[»]
5HX5X-ray2.33A/B185-373[»]
5W2MX-ray3.70A/B/C/D/J/K/L/M190-373[»]
6NILelectron microscopy3.90A/D/G/J185-373[»]
SMRiQ8IUX4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi128319, 19 interactors
DIPiDIP-59966N
IntActiQ8IUX4, 12 interactors
STRINGi9606.ENSP00000309749

Chemistry databases

ChEMBLiCHEMBL2007626

PTM databases

iPTMnetiQ8IUX4
PhosphoSitePlusiQ8IUX4

Genetic variation databases

BioMutaiAPOBEC3F
DMDMi161784334

Proteomic databases

EPDiQ8IUX4
jPOSTiQ8IUX4
MassIVEiQ8IUX4
MaxQBiQ8IUX4
PaxDbiQ8IUX4
PeptideAtlasiQ8IUX4
PRIDEiQ8IUX4
ProteomicsDBi70623 [Q8IUX4-1]
70624 [Q8IUX4-2]
70625 [Q8IUX4-3]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		34783, 198 antibodies

The DNASU plasmid repository

More...DNASUi		200316

Genome annotation databases

EnsembliENST00000308521; ENSP00000309749; ENSG00000128394 [Q8IUX4-1]
ENST00000381565; ENSP00000370977; ENSG00000128394 [Q8IUX4-3]
GeneIDi200316
KEGGihsa:200316
UCSCiuc003awv.4, human [Q8IUX4-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		200316
DisGeNETi200316

GeneCards: human genes, protein and diseases

More...GeneCardsi		APOBEC3F
HGNCiHGNC:17356, APOBEC3F
HPAiENSG00000128394, Low tissue specificity
MIMi608993, gene
neXtProtiNX_Q8IUX4
OpenTargetsiENSG00000128394
PharmGKBiPA24896
VEuPathDBiHostDB:ENSG00000128394.16

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4075, Eukaryota
GeneTreeiENSGT00940000162695
HOGENOMiCLU_047918_0_0_1
OMAiPWNGLNE
PhylomeDBiQ8IUX4
TreeFamiTF331356

Enzyme and pathway databases

BRENDAi3.5.4.38, 2681
PathwayCommonsiQ8IUX4
SIGNORiQ8IUX4

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		200316, 4 hits in 934 CRISPR screens

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

More...ChiTaRSi		APOBEC3F, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		APOBEC3F

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

More...GenomeRNAii		200316
PharosiQ8IUX4, Tbio

Protein Ontology

More...PROi		PR:Q8IUX4
RNActiQ8IUX4, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000128394, Expressed in muscle tissue and 150 other tissues
GenevisibleiQ8IUX4, HS

Family and domain databases

InterProiView protein in InterPro
IPR016192, APOBEC/CMP_deaminase_Zn-bd
IPR002125, CMP_dCMP_dom
IPR016193, Cytidine_deaminase-like
SUPFAMiSSF53927, SSF53927, 2 hits
PROSITEiView protein in PROSITE
PS00903, CYT_DCMP_DEAMINASES_1, 2 hits
PS51747, CYT_DCMP_DEAMINASES_2, 2 hits

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 nameiABC3F_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: Q8IUX4
Secondary accession number(s): B0QYD4
, Q45F03, Q6ICH3, Q7Z2N2, Q7Z2N5
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: October 23, 2007
Last modified: June 2, 2021
This is version 164 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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
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