APOBEC3F apolipoprotein B mRNA editing enzyme catalytic subunit 3F [Homo sapiens (human)] - Gene

Summary

Official Symbol: APOBEC3Fprovided by HGNC
Official Full Name: apolipoprotein B mRNA editing enzyme catalytic subunit 3Fprovided by HGNC
Primary source: HGNC:HGNC:17356
See related: Ensembl:ENSG00000128394 MIM:608993; AllianceGenome:HGNC:17356
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: A3F; KA6; ARP8; BK150C2.4.MRNA
Summary: This gene is a member of the cytidine deaminase gene family. It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1. It is thought that the proteins may be RNA editing enzymes and have roles in growth or cell cycle control. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]
Expression: Broad expression in lymph node (RPKM 2.8), ovary (RPKM 2.8) and 24 other tissues See more
Orthologs: all
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Genomic context

Location:: 22q13.1

Exon count:: 9

Annotation release	Status	Assembly	Chr	Location
RS_2023_10	current	GRCh38.p14 (GCF_000001405.40)	22	NC_000022.11 (39040864..39055972)
RS_2023_10	current	T2T-CHM13v2.0 (GCF_009914755.1)	22	NC_060946.1 (39511283..39526391)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	22	NC_000022.10 (39436869..39451977)

Chromosome 22 - NC_000022.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

APOBEC3F Is a Mutational Driver of the Human Monkeypox Virus Identified in the 2022 Outbreak.
Title: APOBEC3F Is a Mutational Driver of the Human Monkeypox Virus Identified in the 2022 Outbreak.
Stability of APOBEC3F in the Presence of the APOBEC3 Antagonist HIV-1 Vif Increases at the Expense of Co-Expressed APOBEC3H Haplotype I.
Title: Stability of APOBEC3F in the Presence of the APOBEC3 Antagonist HIV-1 Vif Increases at the Expense of Co-Expressed APOBEC3H Haplotype I.
Differential Activity of APOBEC3F, APOBEC3G, and APOBEC3H in the Restriction of HIV-2.
Title: Differential Activity of APOBEC3F, APOBEC3G, and APOBEC3H in the Restriction of HIV-2.
analysis of the dependence of the deamination rate of human APOBEC3F on the length of single-stranded DNA, which is affected by the concentrations of APOBEC3F and single-stranded DNA
Title: An insight into the dependence of the deamination rate of human APOBEC3F on the length of single-stranded DNA, which is affected by the concentrations of APOBEC3F and single-stranded DNA.
The cryo-EM structure of the Vif-targeted C-terminal domain of human A3F in complex with HIV-1 Vif and the cellular cofactor core-binding factor beta (CBFbeta) at 3.9-A resolution shows that Vif and CBFbeta form a platform to recruit A3F, revealing a direct A3F-recruiting role of CBFbeta beyond Vif stabilization, and it captures multiple independent A3F-Vif interfaces.
Title: Structural basis of antagonism of human APOBEC3F by HIV-1 Vif.
Apolipoprotein B mRNA editing enzyme catalytic subunit 3F (A3F) polymorphism A3F 231V restrict HIV-1 infection more efficiently than A3F 231 and is partially protected from Vif-mediated degradation. A3F 231V induces more mutations than A3F 231I in HIV-1 proviral DNA. A3F genotypes are commonly heterozygous. Hetero-oligomerization with A3F 231V results in partial stabilization of A3F 231I and A3G in the presence of Vif.
Title: Polymorphisms of the cytidine deaminase APOBEC3F have different HIV-1 restriction efficiencies.
APOBEC3DE binds to itself, APOBEC3F, and APOBEC3G and antagonizes APOBEC3F and, to a lesser extent, APOBEC3G restriction of hepatitis B virus replication.
Title: APOBEC3DE Antagonizes Hepatitis B Virus Restriction Factors APOBEC3F and APOBEC3G.
These results indicate that APOBEC3 proteins can be copackaged and can comutate the same genomes, and can cooperate to inhibit HIV replication.
Title: APOBEC3 proteins can copackage and comutate HIV-1 genomes.
an APOBEC3F/APOBEC3G hetero-oligomer can form that has unique properties compared to each APOBEC3 alone. This hetero-oligomer has increased efficiency of virus hypermutation, raising the idea that we still may not fully realize the antiviral mechanisms of endogenous APOBEC3 enzymes. Hetero-oligomerization may be a mechanism to increase their antiviral activity in the presence of Vif.
Title: Mechanism of Enhanced HIV Restriction by Virion Coencapsidated Cytidine Deaminases APOBEC3F and APOBEC3G.
virus adaptation and computational studies to interrogate the APOBEC3F-Vif interface and build a robust structural model; taken together with mutagenesis results, propose a wobble model to explain how HIV-1 Vif has evolved to bind different APOBEC3 enzymes
Title: The Binding Interface between Human APOBEC3F and HIV-1 Vif Elucidated by Genetic and Computational Approaches.

Submit: New GeneRIF Correction See all GeneRIFs (68)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
HIV/tuberculosis coinfection upregulates APOBEC3F expression in pleural fluid mononuclear cells (PFMC) isolated from antiretroviral-naive coinfected patients (relative to patients infected with only tuberculosis)	PubMed
Knockdown of APOBEC3F by siRNA enhances HIV-1 infection of immature dendritic cells (iDCs), indicating that APOBEC3F controls the sensitivity of iDCs to HIV-1 infection	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	HIV-1 Env gp120 variable loop 3 (V3) region mutation is increased by incomplete Vif neutralization (Vif K22E) of APOBEC3G/F activity and may contribute to genetic evolution from CCR5 to CXCR4 co-receptor usage	PubMed
Pol	gag-pol	Analyses of longitudinal HIV-1 pol sequences from patients without hypermutated viruses during chronic infection indicate that A3F may increase HIV-1 diversification and facilitate viral adaption and propagation in vivo	PubMed
Pr55(Gag)	gag	R7R10K11S, A30P, P31L, R32G, and RKK32-34SSS mutations in the NC domain of HIV-1 Gag result in a significant decrease in APOBEC3F incorporation into virus-like particles	PubMed
	gag	Amino acids 104-156, located between the two cytidine deaminase domains of APOBEC3F, are required for its incorporation into Gag virus-like particles	PubMed
	gag	The NC domain of HIV-1 Gag is required for 7SL RNA and APOBEC3F packaging	PubMed
	gag	APOBEC3F may be incorporated into virions by HIV-1 Gag polyprotein	PubMed
	gag	Single-virion fluorescence microscopy analysis demonstrates that the efficiency of A3G-YFP and A3F-YFP incorporation into HIV-1 Gag-CeFP virions is higher than that of A3C-YFP incorporation into HIV-1 Gag-CeFP virions	PubMed
	gag	The efficiency of incorporation of Mov10, A3G, and A3F into viral particles, which contains both HIV-1 Gag and genomic RNA, is much higher than that of the other P-body proteins AGO2, DCP1a, DCP2, and DDX6	PubMed
	gag	In HIV-1 virions, APOBEC3F interacts with HIV-1 IN and NC, which are known to be important for reverse transcription and integration	PubMed
Vif	vif	HIV-1 Vif binds APOBEC3F; the interaction is between amino acid residue R15 in Vif and E289 in APOBEC3F	PubMed
	vif	HIV-1 Vif degrades APOBEC3F; degradation is dependent on interactions between amino acid residue R15 in Vif and E289 in APOBEC3F	PubMed
	vif	HIV-1 Vif degrades APOBEC3F dependent upon L291, A292, R293, and E324 in APOBEC3F	PubMed
	vif	HIV-1 Vif binds amino acids L291, A292 and R293 in APOBEC3F	PubMed
	vif	HIV-1 Vif degrades APOBEC3C and APOBEC3F and is dependent on Vif F1, F2, and F3 box mutations involving residues D14, R15, M16, W79, D172, and W174	PubMed
	vif	HIV-1 Vif degrades APOBEC3F and APOBEC3C	PubMed
	vif	HIV-1 Vif internal amino acid salt bridge (E171-K167-D101) mediates human APOBEC3C and APOBEC3F degradation	PubMed
	vif	HIV-1 Vif specifically binds APOBEC3F, and Vif suppresses both the inhibition of virus infectivity caused by APOBEC3F and virion incorporation of APOBEC3F	PubMed
	vif	APOBEC3F levels are increased by compound N.41 treatment only in cells co-expressing HIV-1 Vif, and APOBEC3F levels in virus particles are also increased	PubMed
	vif	APOBEC3F, similar to APOBEC3G, induces G to A hypermutations in HIV-1 genomic DNA, and the HIV-1 Vif protein inhibits this activity	PubMed
	vif	Certain residues L125, G126, R127, E134, Y135, G138 in HCCH motif (residues 125-141) of HIV-1 Vif are required for inhibition of APOBEC3F	PubMed
	vif	Immunoblotting and crystal structure analyses reveal ten amino acids L225, F258, C259, I262, L263, S264, Y269, D289, F290, and H294 in APOBEC3F are involved in forming Vif-interaction interface	PubMed
	vif	A potent small molecular compound VEC-5 protects APOBEC3G, APOBEC3F, and APOBEC3C from HIV-1 Vif-induced degradation and enhances A3G incorporation into HIV-1 virions by inhibiting the interaction between Vif and elongin C	PubMed
	vif	HIV-1 Vif W21A, S32A, W38A, Y69A, E76A, W79A, H108A, C114S, C133S, and H139A mutants have no viral ability to neutralize APOBEC3F	PubMed
	vif	An extensive mutational analysis of HIV-1 Vif reveals that two distinct regions of Vif, amino acids Y(40)RHHY(44) and D(14)RMR(17), which are essential for binding to A3G and A3F, respectively	PubMed
	vif	CBF-beta-mediated increase of HIV-1 Vif steady-state levels results in decreased cellular levels of all Vif-sensitive APOBEC proteins (A3C, A3D, A3F, A3G, and A3H haplotype II)	PubMed
	vif	Endogenous APOBEC3 proteins, particularly APOBEC3D, APOBEC3F, and APOBEC3G, can potently inhibit HIV-1 propagation in a mouse model by mutating 14DRMR17 and/or 40YRHHY44 motifs in Vif	PubMed
	vif	Amino acids P281, E282, D313, E316, Q323, and E324 in APOBEC3F are required for the interface binding to HIV-1 Vif(IIIB)	PubMed
	vif	HIV-1 Vif mutants 84DVAAAA89, 88EW/AA89, G84A, G84D, W89A, D104A, L106S, and I107S result in upregulated APOBEC3F expression and show a reduced ability to neutralize the antiviral activity of APOBEC3F	PubMed
	vif	HIV-1 Vif mutant E88A/W89A fails to bind to CBF-beta, which impairs Vif-mediated degradation of both A3F and A3G proteins and HIV-1 replication in non-permissive CEM cells	PubMed
	vif	A novel conserved 69YXXL72 motif in HIV-1 Vif mediates binding to human A3F and its subsequent degradation. Tyr69 and Leu72 residues in the YXXL motif are important for degradation of A3F	PubMed
	vif	HIV-1 Vif, which suppresses both APOBEC3G and APOBEC3F antiviral function by inducing their degradation, may selectively remove these proteins from, and/or restrict their localization to, P-bodies	PubMed
	vif	HIV-1 Vif mutants W11R and R15G are restricted in permissive SupT11 and nonpermissive CEM2n cell lines that express A3F, while H43N and H43N/E117K Vif mutants are capable of spreading efficiently in the presence of A3F	PubMed
	vif	HIV-1 Vif mutants W5S, W21S, W38S, W89S, F112S, and F115S have a reduced ability to interact with CBF-beta and these Vif hydrophobic residues are important for Vif-mediated degradation of A3F	PubMed
	vif	The crystal structure provides a structural basis that L255A, L255D, F258A, C259K, C259S, I262A, Y269A, E286A, E289Q, F290A, F290K, H294A, H294D, E316Q, S320A, and E324Q mutations fail to bind to HIV-1 Vif	PubMed
	vif	The HIV-1 Vif N-terminal motif (residues 18-38) binds CUL5 in mammalian cells and is reguired for A3F and A3G degradation and HIV-1 infectivity	PubMed
	vif	Replacement of all lysines with arginines in A3F results in inhibition of HIV-1 Vif-mediated A3F degradation by polyubiquitination. Lysines at positions 40, 52, 209, 334, 337, 355, and 358 in A3F are important for its degradation by Vif	PubMed
	vif	A3F mutants C259K and IL262-263AA are resistant to HIV-1 Vif-mediated A3F degradation	PubMed
	vif	The amino acids 223-232 of A3F-CTD beta1-2 loop is conserved to the amino acids 23-32 of HIV-1 Vif, while the amino acids 305-313 of A3F-CTD beta4-alpha4 loop is conserved to the amino acids 108-113 of HIV-1 Vif	PubMed
	vif	Unusual substitutions V13I, V55T, and L81M in HIV-1 Vif from children infected perinatally without progression to AIDS are located in three distinct Vif motifs important for the interaction with A3G/A3F	PubMed
	vif	The antiviral activity of A3G to HIV-1 vif mutants NL4-3 40YRHHY44>A5 and NL4-3 14DRMR17>A4 with G-to-A hypermutations confers a greater restriction than the combined antiviral activity of A3F and A3DE in activated CD4+ T cells and macrophages	PubMed
	vif	HIV-1 Vif alleles from seven HIV-1 subtypes show their abilities to degrade and counteract A3F efficiently	PubMed
	vif	Highly conserved Tryptophan residues in the N-terminal region of HIV-1 Vif are required for the suppression of both APOBEC3G and APOBEC3F	PubMed
	vif	HIV-1 Vif motif TGERxW (amino acids 74-79) is important for A3F interaction and inhibition	PubMed
	vif	Stress causes A3A, A3B, A3C, and A3F to co-localize efficiently with Vif(IIIB) and mRNA-PABP1 complexes in stress granules	PubMed
	vif	Vif-deficient HIV-1 replicates as equally well as wild-type virus in CEM-T4 cells expressing high levels of A3G and A3F, indicating CEM-T4 cells lack a cellular co-factor for these endogenous antiretroviral proteins	PubMed
	vif	Small molecule RN-18 specifically inhibits HIV-1 Vif-mediated downregulation of APOBEC3C/F/G proteins by decreasing Vif protein levels when Vif interacts with these proteins	PubMed
	vif	Amino acids 283 to 300 of A3F are critical for binding to the DRMR region of HIV-1 Vif and for A3F degradation	PubMed
	vif	The SLV portion of the Vif SLV/Ix4Yx9Y motif is required for optimal suppression of A3F	PubMed
	vif	The carboxyl-terminal domain (residues 183-373) of A3F alone binds to HIV-1 Vif and behaves like the full-length A3F in terms of Vif sensitivity	PubMed
	vif	Human T cell line CEM.NKR clones display inhibition of HIV-1 replication although these clones retain low levels of A3DE, A3F, A3G, and A3H expression, suggesting that a novel restriction factor distinct from APOBEC3s exists in CEM.NKR cells	PubMed
	vif	Incorporation of Vif into virions is dependent on its interaction with A3G/A3F	PubMed
	vif	Long-term restriction by A3F selects HIV-1 clones with Vif Q26-Q27 or Y26-Q27 mutations, which are fully capable of overcoming A3F but susceptible to restriction by A3G	PubMed
	vif	Alternative splice removal of exon 2 of A3F produces a Vif-resistant protein that retains significant antiviral activity. Splice removal of exons 2-4 results in a Vif-sensitive A3F protein with weaker antiviral activity	PubMed
	vif	The T(Q/D/E)x(5)ADx(2)(I/L) motif, located at residues 96 to 107 in HIV-1 Vif, plays a critical role in neutralizing activity toward A3F. This motif regulates Vif interaction with Cul5	PubMed
	vif	All residues except N175 in the (171)EDRWN(175) domain of Vif are equally important for regulation of A3F neutralization	PubMed
	vif	Residues L81, G82, and G84, and, to a lesser extent, I87 and W89 within the (81)LGxGxxIxW(89) domain affect Vif binding to A3F and play very critical roles in A3F neutralizing activity	PubMed
	vif	Amino-acid residues QE323-324EK in A3F affect the differential susceptibility of human A3F and monkey A3F to HIV-1 Vif. Mutation of A3F E324 alone alters functional susceptibility of its binding to Vif	PubMed
	vif	Amino acid E289 in the EFLARH sequence of A3F is critical for HIV-1 Vif sensitivity	PubMed
Vpu	vpu	The expression of APOBEC3F is enhanced in Vpu-deficient HIV-1-infected cells as compared to that in wild-type-infected cells	PubMed
capsid	gag	HIV-1 CA mutations (K203A and E128A/R132A) that alter HIV-1 core stability decrease nuclear import of A3F-YFP-labeled preintegration complexes (PICs) in infected cells	PubMed
integrase	gag-pol	In HIV-1 virions, APOBEC3F interacts with HIV-1 IN and NC, which are known to be important for reverse transcription and integration	PubMed
nucleocapsid	gag	The NC domain of HIV-1 Gag is required for 7SL RNA and APOBEC3F packaging	PubMed
	gag	In HIV-1 virions, APOBEC3F interacts with HIV-1 IN and NC, which are known to be important for reverse transcription and integration	PubMed
reverse transcriptase	gag-pol	Vif-negative HIV-1 produced from 293T cells transiently expressing hA3F is impaired in early and late viral DNA production, and in viral infectivity, effects that are correlated with an inability of tRNA(3)(Lys) to prime reverse transcription	PubMed
	gag-pol	APOBEC3-driven mutagenesis contributes to the generation of both M184I and E138K mutations in HIV-1 RT in the absence of drug exposure	PubMed

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

L18506 (e-PCR)
- UniSTS:54024

L17688 (e-PCR)
- UniSTS:74509

GDB:434012 (e-PCR)
- UniSTS:157204

D8S2279 (e-PCR)
- UniSTS:473907

GDB:314949 (e-PCR)
- UniSTS:156503

L18426 (e-PCR)
- UniSTS:34648

G38154 (e-PCR)
- UniSTS:53341

D1S1423 (e-PCR)
- UniSTS:149619

G18167 (e-PCR)
- UniSTS:43142

D11S3316 (e-PCR)
- UniSTS:152558

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables RNA binding	HDA more info	PubMed
enables RNA binding	IBA Inferred from Biological aspect of Ancestor more info
enables RNA binding	IDA Inferred from Direct Assay more info	PubMed
enables cytidine deaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables cytidine deaminase activity	IDA Inferred from Direct Assay more info	PubMed
enables deoxycytidine deaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables zinc ion binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA cytosine deamination	IBA Inferred from Biological aspect of Ancestor more info
involved_in DNA cytosine deamination	IDA Inferred from Direct Assay more info	PubMed
involved_in DNA demethylation	IBA Inferred from Biological aspect of Ancestor more info
involved_in base conversion or substitution editing	IDA Inferred from Direct Assay more info	PubMed
involved_in clearance of foreign intracellular DNA	IDA Inferred from Direct Assay more info	PubMed
involved_in cytidine deamination	IEA Inferred from Electronic Annotation more info
involved_in cytidine to uridine editing	IBA Inferred from Biological aspect of Ancestor more info
involved_in defense response to virus	IBA Inferred from Biological aspect of Ancestor more info
involved_in defense response to virus	IDA Inferred from Direct Assay more info	PubMed
involved_in innate immune response	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of single stranded viral RNA replication via double stranded DNA intermediate	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of single stranded viral RNA replication via double stranded DNA intermediate	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of viral genome replication	IDA Inferred from Direct Assay more info	PubMed
involved_in negative regulation of viral process	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of defense response to virus by host	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of gene expression via chromosomal CpG island demethylation	IDA Inferred from Direct Assay more info	PubMed
involved_in retrotransposon silencing	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
is_active_in P-body	IBA Inferred from Biological aspect of Ancestor more info
located_in P-body	IDA Inferred from Direct Assay more info	PubMed
part_of apolipoprotein B mRNA editing enzyme complex	TAS Traceable Author Statement more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
part_of ribonucleoprotein complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: DNA dC->dU-editing enzyme APOBEC-3F

Names: apolipoprotein B editing enzyme catalytic polypeptide-like 3F; apolipoprotein B mRNA editing enzyme cytidine deaminase; apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F; induced upon T-cell activation

NP_001006667.1

EC 3.5.4.38

NP_660341.2

EC 3.5.4.38

XP_016884131.1

EC 3.5.4.38

XP_047297140.1

EC 3.5.4.38

XP_047297141.1

EC 3.5.4.38

XP_054181200.1

EC 3.5.4.38

XP_054181201.1

EC 3.5.4.38

XP_054181202.1

EC 3.5.4.38

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001006666.2 → NP_001006667.1 DNA dC->dU-editing enzyme APOBEC-3F isoform b

See identical proteins and their annotated locations for NP_001006667.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) contains a distinct 3' UTR and 3' coding region, compared to variant 1. The resulting isoform (b) is shorter and has a distinct C-terminus when compared to isoform a.

Source sequence(s)

BM681311, CR456395

Consensus CDS

CCDS33649.1

UniProtKB/Swiss-Prot

Q8IUX4

Related

ENSP00000370977.2, ENST00000381565.2

Conserved Domains (1) summary

pfam08210
Location:17 → 88

APOBEC_N; APOBEC-like N-terminal domain
NM_145298.6 → NP_660341.2 DNA dC->dU-editing enzyme APOBEC-3F isoform a

See identical proteins and their annotated locations for NP_660341.2

Status: REVIEWED

Description

Transcript Variant: This variant (1) represents the longer transcript, and encodes the longer isoform (a).

Source sequence(s)

AL022318, BC038808, BQ182066, CX165430, DA221480

Consensus CDS

CCDS33648.1

UniProtKB/Swiss-Prot

B0QYD4, Q45F03, Q6ICH3, Q8IUX4

UniProtKB/TrEMBL

M4VR43

Related

ENSP00000309749.5, ENST00000308521.10

Conserved Domains (2) summary

pfam18772
Location:195 → 373

APOBEC2

pfam18782
Location:10 → 188

NAD2; Novel AID APOBEC clade 2

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2023_10

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000022.11 Reference GRCh38.p14 Primary Assembly

Range

39040864..39055972

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_047441184.1 → XP_047297140.1 DNA dC->dU-editing enzyme APOBEC-3F isoform X1
XM_047441185.1 → XP_047297141.1 DNA dC->dU-editing enzyme APOBEC-3F isoform X2
XM_017028642.3 → XP_016884131.1 DNA dC->dU-editing enzyme APOBEC-3F isoform X3

UniProtKB/TrEMBL

B4DGW8