APOBEC3F

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. 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.13 Publications

Miscellaneous

It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22.

Catalytic activityⁱ

Cytidine + H₂O = uridine + NH₃.

Cofactorⁱ

Zn²⁺By similarity

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 key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	65	ZincBy similarity	1
Metal bindingⁱ	96	ZincBy similarity	1
Metal bindingⁱ	99	ZincBy similarity	1
Active siteⁱ	251	Proton donorBy similarity	1

GO - Molecular functionⁱ

cytidine deaminase activity
Source: HGNC
Inferred from direct assayⁱ
- 17121840
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 23685212
RNA binding
Source: HGNC
Inferred from direct assayⁱ
- 11863358
zinc ion binding
Source: HGNC
Inferred from direct assayⁱ
- 11863358

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

base conversion or substitution editing
Source: HGNC
Inferred from direct assayⁱ
- 17121840
cytidine to uridine editing
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
defense response to virus
Source: UniProtKB
Inferred from direct assayⁱ
- 21835787
- 22915799
DNA cytosine deamination
Source: UniProtKB
Inferred from direct assayⁱ
- 21835787
DNA demethylation
Source: UniProtKB
Inferred from direct assayⁱ
- 21496894
innate immune response
Source: HGNC
Inferred from direct assayⁱ
- 17121840
negative regulation of single stranded viral RNA replication via double stranded DNA intermediate
Source: UniProtKB
Inferred from direct assayⁱ
- 21835787
negative regulation of transposition
Source: UniProtKB
Inferred from direct assayⁱ
- 16527742
- 20062055
negative regulation of viral genome replication
Source: UniProtKB
Inferred from direct assayⁱ
- 16378963
negative regulation of viral process
Source: HGNC
Inferred from direct assayⁱ
- 17121840
positive regulation of defense response to virus by host
Source: HGNC
Inferred from direct assayⁱ
- 17121840

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	Antiviral defense, Immunity, Innate immunity
Ligand	Metal-binding, Zinc

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: DNA dC->dU-editing enzyme APOBEC-3F (EC:3.5.4.-) Alternative name(s): Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F Short name: A3F
Gene namesⁱ	Name:APOBEC3F
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 22

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000128394.16
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:17356 APOBEC3F
MIMⁱ	608993 gene
neXtProtⁱ	NX_Q8IUX4

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	67	E → A: Decrease in cytidine deaminase and antiviral activity; when associated with A-251. 1 Publication	1
Mutagenesisⁱ	67	E → A: No effect on cytidine deaminase and antiviral activity. 1 Publication	1
Mutagenesisⁱ	251	E → A: Decrease in cytidine deaminase and antiviral activity. 1 Publication	1
Mutagenesisⁱ	251	E → A: Decrease in cytidine deaminase and antiviral activity; when associated with A-67. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	200316
Open Targets More...OpenTargetsⁱ	ENSG00000128394
PharmGKBⁱ	PA24896

Chemistry databases

ChEMBLⁱ	CHEMBL2007626

ChEMBLⁱ

CHEMBL2007626

Polymorphism and mutation databases

BioMutaⁱ	APOBEC3F
DMDMⁱ	161784334

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000171757	1 – 373	DNA dC->dU-editing enzyme APOBEC-3FAdd BLAST		373

Proteomic databases

EPDⁱ	Q8IUX4
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q8IUX4
PaxDbⁱ	Q8IUX4
PeptideAtlas More...PeptideAtlasⁱ	Q8IUX4
PRIDEⁱ	Q8IUX4
ProteomicsDBⁱ	70623 70624 [Q8IUX4-2] 70625 [Q8IUX4-3]

PTM databases

iPTMnetⁱ	Q8IUX4
PhosphoSitePlusⁱ	Q8IUX4

Expressionⁱ

Tissue specificityⁱ

Widely expressed. Highly expressed in ovary.3 Publications

Inductionⁱ

Up-regulated by IFN-alpha.

Gene expression databases

Bgeeⁱ	ENSG00000128394 Expressed in 130 organ(s), highest expression level in leukocyte
CleanExⁱ	HS_APOBEC3F
Genevisibleⁱ	Q8IUX4 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA073637

HPAⁱ

HPA073637

Interactionⁱ

Subunit structureⁱ

Binds HIV-1 Vif. In the absence of Vif protein, specifically packaged into HIV-1 virions. Interacts with APOBEC3G in an RNA-dependent manner. Interacts with AGO1, AGO2 and AGO3.2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-11306991,EBI-11306991

With

Entry

#Exp.

IntAct

Notes

itself

2

EBI-11306991,EBI-11306991

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 23685212

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	128319, 11 interactors
Database of interacting proteins More...DIPⁱ	DIP-59966N
IntActⁱ	Q8IUX4, 7 interactors
STRINGⁱ	9606.ENSP00000309749

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	197 – 204	Combined sources	8
Helixⁱ	208 – 212	Combined sources	5
Beta strandⁱ	217 – 226	Combined sources	10
Beta strandⁱ	232 – 239	Combined sources	8
Beta strandⁱ	243 – 245	Combined sources	3
Helixⁱ	250 – 261	Combined sources	12
Beta strandⁱ	267 – 277	Combined sources	11
Helixⁱ	281 – 293	Combined sources	13
Beta strandⁱ	297 – 305	Combined sources	9
Turnⁱ	307 – 310	Combined sources	4
Helixⁱ	312 – 323	Combined sources	12
Beta strandⁱ	327 – 330	Combined sources	4
Helixⁱ	333 – 343	Combined sources	11
Helixⁱ	357 – 372	Combined sources	16

Show more details

3D structure databases

ProteinModelPortalⁱ	Q8IUX4
SMRⁱ	Q8IUX4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	29 – 137	CMP/dCMP-type deaminase 1PROSITE-ProRule annotationAdd BLAST		109
Domainⁱ	174 – 321	CMP/dCMP-type deaminase 2PROSITE-ProRule annotationAdd BLAST		148

Domainⁱ

The CMP/dCMP deaminase domain 1 mediates RNA binding, RNA-dependent oligomerization and virion incorporation whereas the CMP/dCMP deaminase domain 2 confers deoxycytidine deaminase activity and substrate sequence specificity.1 Publication

Sequence similaritiesⁱ

Belongs to the cytidine and deoxycytidylate deaminase family.Curated

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	ENOG410JBA1 Eukaryota ENOG41119MS LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000062933
HOGENOMⁱ	HOG000033755
HOVERGENⁱ	HBG050434
KEGG Orthology (KO) More...KOⁱ	K18750
OMAⁱ	FEYCWDN
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G07EI
PhylomeDBⁱ	Q8IUX4
TreeFamⁱ	TF331356

Family and domain databases

InterProⁱ	View protein in InterPro IPR016192 APOBEC/CMP_deaminase_Zn-bd IPR013158 APOBEC_N IPR002125 CMP_dCMP_dom IPR016193 Cytidine_deaminase-like
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08210 APOBEC_N, 2 hits
SUPFAMⁱ	SSF53927 SSF53927, 2 hits
PROSITEⁱ	View protein in PROSITE PS00903 CYT_DCMP_DEAMINASES_1, 2 hits PS51747 CYT_DCMP_DEAMINASES_2, 2 hits

Sequences (3)ⁱ

Sequence statusⁱ: Complete.

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

Isoform 1 (identifier: Q8IUX4-1) [UniParc]FASTA Add 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 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

Checksum:ⁱAF1A0E13830695F4

GO

Isoform 2 (identifier: Q8IUX4-2) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPRLD 
        60         70 
AKIFRGQVPP GLQSLCRQEL SQLGKQTTH

Note: May be due to a competing donor splice site. No experimental confirmation available.

Show »

Length:79

Mass (Da):9,445

Checksum:ⁱ03ABEACA44AB0748

GO

Isoform 3 (identifier: Q8IUX4-3) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPRLD 
        60         70         80         90        100
AKIFRGQVPR SFIRAPFQVL SSPFGQCAPP HGTAQVQWPP QLTAGREQGR 

P

Show »

Length:101

Mass (Da):11,823

Checksum:ⁱ1659A5E223CB1EFE

GO

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_038355	48	R → P1 PublicationCorresponds to variant dbSNP:rs35053197Ensembl.	1
Natural variantⁱVAR_018145	61	Q → L. Corresponds to variant dbSNP:rs2076109Ensembl.	1
Natural variantⁱVAR_018146	97	P → L. Corresponds to variant dbSNP:rs2076110Ensembl.	1
Natural variantⁱVAR_018147	108	A → S1 PublicationCorresponds to variant dbSNP:rs2020390Ensembl.	1
Natural variantⁱVAR_025058	178	A → T1 PublicationCorresponds to variant dbSNP:rs34182094Ensembl.	1
Natural variantⁱVAR_018148	231	V → I1 PublicationCorresponds to variant dbSNP:rs2076101Ensembl.	1
Natural variantⁱVAR_025059	307	Y → C1 PublicationCorresponds to variant dbSNP:rs12157816Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_009803	58 – 79	VYSQP…CGNQL → VPPGLQSLCRQELSQLGKQT TH in isoform 2. 1 PublicationAdd BLAST	22
Alternative sequenceⁱVSP_042754	59 – 113	YSQPE…EHPNV → PRSFIRAPFQVLSSPFGQCA PPHGTAQVQWPPQLTAGREQ GRP in isoform 3. 1 PublicationAdd BLAST	55
Alternative sequenceⁱVSP_009804	80 – 373	Missing in isoform 2. 1 PublicationAdd BLAST	294
Alternative sequenceⁱVSP_042755	114 – 373	Missing in isoform 3. 1 PublicationAdd BLAST	260

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
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]
UniGeneⁱ	Hs.659809 Hs.660143

Genome annotation databases

Ensemblⁱ	ENST00000308521; ENSP00000309749; ENSG00000128394 [Q8IUX4-1] ENST00000381565; ENSP00000370977; ENSG00000128394 [Q8IUX4-3]
GeneIDⁱ	200316
KEGGⁱ	hsa:200316
UCSC genome browser More...UCSCⁱ	uc003awv.4 human [Q8IUX4-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q8IUX4	cDNA FLJ60505, highly similar to Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F		HUMAN		189	UniRef100_Q8IUX4

Protein	Similar proteins		Species	Score	Length	Source
Q8IUX4	cDNA FLJ60505, highly similar to Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F		HUMAN		189	UniRef90_Q8IUX4
Apolipoprotein B mRNA editing enzyme catalytic subunit 3C		PANTR		373
Apobec3F (Fragment)		western gorilla		373
Apolipoprotein B mRNA editing enzyme catalytic subunit 3F		GORGO		373
Apolipoprotein B editing enzyme catalytic polypeptide-like 3F		HUMAN		373
+2
Q8IUX4-3	APOBEC3F isoform 4		PANTR		101	UniRef90_Q8IUX4-3
Uncharacterized protein		PANPA		101
Apolipoprotein B mRNA editing enzyme catalytic subunit 3F		GORGO		101
UPI000CEF9A00		PONAB		101

Protein	Similar proteins		Species	Score	Length	Source
Q8IUX4	DNA dC->dU-editing enzyme APOBEC-3D		HUMAN		386	UniRef50_Q8IUX4
Apobec3F (Fragment)		western gorilla		373
Apolipoprotein B mRNA editing enzyme catalytic subunit 3F		GORGO		373
APOBEC3F isoform 1		PANTR		373
DNA dC->dU-editing enzyme APOBEC-3F-like		TARSY		459
+60
Q8IUX4-2	Isoform 3 of DNA dC->dU-editing enzyme APOBEC-3G		HUMAN		79	UniRef50_Q9HC16-3
Apobec3DE (Fragment)		NOMLE		64
Uncharacterized protein		CERAT		79
UPI00083FCE14		CALJA		73
Q8IUX4-3	Apolipoprotein B mRNA editing enzyme catalytic subunit 3F		GORGO		101	UniRef50_Q8IUX4-3
APOBEC3F isoform 4		PANTR		101
Uncharacterized protein		PANPA		101
Uncharacterized protein		NOMLE		87
Uncharacterized protein		RHIBE		94
+1

Cross-referencesⁱ

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
CCDSⁱ	CCDS33648.1 [Q8IUX4-1] CCDS33649.1 [Q8IUX4-3]
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]
UniGeneⁱ	Hs.659809 Hs.660143

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3WUS	X-ray	2.54	A/B	187-373	[»]
	4IOU	X-ray	2.75	A/B/C/D	185-373	[»]
	4J4J	X-ray	3.10	A/B	218-373	[»]
	5HX4	X-ray	1.92	A/B	185-373	[»]
	5HX5	X-ray	2.33	A/B	185-373	[»]
	5W2M	X-ray	3.70	A/B/C/D/J/K/L/M	190-373	[»]
ProteinModelPortalⁱ	Q8IUX4
SMRⁱ	Q8IUX4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	128319, 11 interactors
DIPⁱ	DIP-59966N
IntActⁱ	Q8IUX4, 7 interactors
STRINGⁱ	9606.ENSP00000309749

Chemistry databases

ChEMBLⁱ	CHEMBL2007626

ChEMBLⁱ

CHEMBL2007626

PTM databases

iPTMnetⁱ	Q8IUX4
PhosphoSitePlusⁱ	Q8IUX4

Polymorphism and mutation databases

BioMutaⁱ	APOBEC3F
DMDMⁱ	161784334

Proteomic databases

EPDⁱ	Q8IUX4
MaxQBⁱ	Q8IUX4
PaxDbⁱ	Q8IUX4
PeptideAtlasⁱ	Q8IUX4
PRIDEⁱ	Q8IUX4
ProteomicsDBⁱ	70623 70624 [Q8IUX4-2] 70625 [Q8IUX4-3]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	200316
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000308521; ENSP00000309749; ENSG00000128394 [Q8IUX4-1] ENST00000381565; ENSP00000370977; ENSG00000128394 [Q8IUX4-3]
GeneIDⁱ	200316
KEGGⁱ	hsa:200316
UCSCⁱ	uc003awv.4 human [Q8IUX4-1]

Organism-specific databases

CTDⁱ	200316
DisGeNETⁱ	200316
EuPathDBⁱ	HostDB:ENSG00000128394.16
GeneCardsⁱ	APOBEC3F
H-InvDBⁱ	HIX0213264
HGNCⁱ	HGNC:17356 APOBEC3F
HPAⁱ	HPA073637
MIMⁱ	608993 gene
neXtProtⁱ	NX_Q8IUX4
OpenTargetsⁱ	ENSG00000128394
PharmGKBⁱ	PA24896
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410JBA1 Eukaryota ENOG41119MS LUCA
GeneTreeⁱ	ENSGT00530000062933
HOGENOMⁱ	HOG000033755
HOVERGENⁱ	HBG050434
KOⁱ	K18750
OMAⁱ	FEYCWDN
OrthoDBⁱ	EOG091G07EI
PhylomeDBⁱ	Q8IUX4
TreeFamⁱ	TF331356

Miscellaneous databases

ChiTaRSⁱ	APOBEC3F human
GeneWikiⁱ	APOBEC3F
GenomeRNAiⁱ	200316
Protein Ontology More...PROⁱ	PR:Q8IUX4
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000128394 Expressed in 130 organ(s), highest expression level in leukocyte
CleanExⁱ	HS_APOBEC3F
Genevisibleⁱ	Q8IUX4 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR016192 APOBEC/CMP_deaminase_Zn-bd IPR013158 APOBEC_N IPR002125 CMP_dCMP_dom IPR016193 Cytidine_deaminase-like
Pfamⁱ	View protein in Pfam PF08210 APOBEC_N, 2 hits
SUPFAMⁱ	SSF53927 SSF53927, 2 hits
PROSITEⁱ	View protein in PROSITE PS00903 CYT_DCMP_DEAMINASES_1, 2 hits PS51747 CYT_DCMP_DEAMINASES_2, 2 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ABC3F_HUMAN
Accessionⁱ	Q8IUX4Primary (citable) accession number: Q8IUX4 Secondary accession number(s): B0QYD4 , Q45F03, Q6ICH3, Q7Z2N2, Q7Z2N5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 29, 2004
	Last sequence update:	October 23, 2007
	Last modified:	November 7, 2018
	This is version 145 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human chromosome 22
Human chromosome 22: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q8IUX4 (ABC3F_HUMAN)

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

Select a section on the left to see content.

<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

Miscellaneous

Sites

<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>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

Organism-specific databases

<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

Other locations

Nucleus

Other locations

Keywords - Cellular componenti

<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

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Proteomic databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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

GO - Molecular functioni

Protein-protein interaction databases

<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

3D structure databases

<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

<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

Phylogenomic databases

Family and domain databases

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ