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APOBEC3H apolipoprotein B mRNA editing enzyme catalytic subunit 3H [ Homo sapiens (human) ]

Gene ID: 164668, updated on 12-Aug-2022

Summary

Official Symbol
APOBEC3Hprovided by HGNC
Official Full Name
apolipoprotein B mRNA editing enzyme catalytic subunit 3Hprovided by HGNC
Primary source
HGNC:HGNC:24100
See related
Ensembl:ENSG00000100298 MIM:610976; AllianceGenome:HGNC:24100
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
A3H; ARP10; ARP-10
Summary
This gene encodes a member of the apolipoprotein B mRNA-editing enzyme catalytic polypeptide 3 family of proteins. The encoded protein is a cytidine deaminase that has antiretroviral activity by generating lethal hypermutations in viral genomes. Polymorphisms and alternative splicing in this gene influence its antiretroviral activity and are associated with increased resistence to human immunodeficiency virus type 1 infection in certain populations. Alternative splicing results in multiple transcript variants.[provided by RefSeq, Oct 2009]
Expression
Broad expression in lymph node (RPKM 1.2), colon (RPKM 1.0) and 22 other tissues See more
Orthologs
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Genomic context

See APOBEC3H in Genome Data Viewer
Location:
22q13.1
Exon count:
6
Annotation release Status Assembly Chr Location
110 current GRCh38.p14 (GCF_000001405.40) 22 NC_000022.11 (39097244..39104067)
110 current T2T-CHM13v2.0 (GCF_009914755.1) 22 NC_060946.1 (39567663..39574409)
105.20220307 previous assembly GRCh37.p13 (GCF_000001405.25) 22 NC_000022.10 (39493249..39500072)

Chromosome 22 - NC_000022.11Genomic Context describing neighboring genes Neighboring gene apolipoprotein B mRNA editing enzyme catalytic subunit 3G Neighboring gene uncharacterized LOC101927202 Neighboring gene cytochrome c oxidase subunit 5B pseudogene 7 Neighboring gene chromobox 7 Neighboring gene Sharpr-MPRA regulatory region 533

Genomic regions, transcripts, and products

Expression

  • 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

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

HIV-1 interactions

Replication interactions

Interaction Pubs
HIV-1 (delta Vif) replication is restricted by APOBEC3H haplotypes II and V with similar efficiences, but by different mechanisms PubMed

Protein interactions

Protein Gene Interaction Pubs
Pr55(Gag) gag A3H hapI-GKE and hapII-RDD variants are packaged into virions through an association with the matrix-capsid region (amino acids 10-277) and with the NC region (amino acids 378-432) of Gag in an RNA-dependent manner, respectively PubMed
Vif vif The combination of N48H and GDAK60-63EKGE results in a hyperfunctional Vif protein capable of fully inhibiting stable APOBEC3H-hapII PubMed
vif Single mutations I31V, R33G, K36R, and K50R in HIV-1 Vif from NL4-3 sufficiently reduce or abolish their ability to cause G2 arrest, but induce APOBEC3H degradation PubMed
vif HIV-1 Vif proteins from NL4-3, SG3, and C2 have the ability to induce G2 arrest in HEK293T cells, but are defective in inducing APOBEC3H degradation when compared to HIV-1 Vif from HXB2 PubMed
vif A3H interacts with both HIV-1 Vif(IIIB) and Vif(HXB2) in cells and in vitro, but Vif(IIIB) fails to degrade A3H and Vif(HXB2) H48N mutant reduces its ability to degrade A3H in cells PubMed
vif A histidine at position 48 (48H) in HIV-1 Vif confers activity against A3H-hapII, while an asparagine (48N) abolishes its anti-A3H activity PubMed
vif A glutamic acid at position 121 (121E) renders A3H-hapII sensitivity to both LAI and NL4-3 Vif proteins, while a lysine (121K) results in resistance of A3H-hapII to both Vif alleles 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 APOBEC3H variants encoding a SNP cluster (G105R, K121D and E178D, hapII-RDD) restrict human immunodeficiency virus type 1 (HIV-1) more efficiently than wild-type APOBEC3H (hapI-GKE). All APOBEC3H variants are resistant to HIV-1 Vif PubMed
vif Once expression is optimized and stabilized, human A3H can significantly reduce HIV-1 infectivity. HIV-1 Vif fails to suppress A3H activity PubMed
vif The interaction of HIV-1 Vif(HXB2) with A3H induces polyubiquitination of A3H at K63 position PubMed
vif HIV-1 Vif variants from subtype F are highly effective in counteracting A3H hapII. Two residues in the amino-terminal region of Vif (positions 39F and 48H) from HIV-1 subtype F are necessary for association of Vif with A3H hapII PubMed
vif HIV-1 Vif 39F efficiently inhibits A3H-hapII, but Vif 39V is defective in counteracting A3H-hapII. Mutation at position 39F to the different residues (C, E, G, H, I, K, L, S, T, and V) is inactive against A3H-hapII, but only 39Y can counteract A3H-hapII 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 G105R and K121E residues are important for A3H (HapI) stability and increased antiviral activity and for the resistance of A3H (HapI) to Vif, respectively PubMed
vif HIV-1 Vif targets A3H (HapII) for proteasome-mediated degradation. L64, I66, Y69, and L72 residues in Vif are required for Vif-mediated A3H degradation PubMed
nucleocapsid gag A3H (HapVII) virion packaging is dependent on a (112)YYXW(115) motif, which binds HIV-1 nucleocapsid in an RNA-dependent manner. A single Y112A mutation completely disrupts A3H virion incorporation PubMed

Go to the HIV-1, Human Interaction Database

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
enables RNA binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
enables cytidine deaminase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
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
PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
 
Process Evidence Code Pubs
involved_in DNA cytosine deamination IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
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
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
PubMed 
involved_in defense response to virus IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
involved_in defense response to virus IDA
Inferred from Direct Assay
more info
PubMed 
involved_in innate immune response IEA
Inferred from Electronic Annotation
more info
 
involved_in negative regulation of single stranded viral RNA replication via double stranded DNA intermediate IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
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 transposition IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
involved_in negative regulation of transposition IDA
Inferred from Direct Assay
more info
PubMed 
involved_in negative regulation of transposition IMP
Inferred from Mutant Phenotype
more info
PubMed 
involved_in negative regulation of viral process IMP
Inferred from Mutant Phenotype
more info
PubMed 
Component Evidence Code Pubs
is_active_in P-body IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
located_in P-body IDA
Inferred from Direct Assay
more info
PubMed 
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
located_in cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
located_in cytosol IDA
Inferred from Direct Assay
more info
 
located_in nucleoplasm IDA
Inferred from Direct Assay
more info
 
is_active_in nucleus IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
located_in nucleus IDA
Inferred from Direct Assay
more info
PubMed 

General protein information

Preferred Names
DNA dC->dU-editing enzyme APOBEC-3H
Names
APOBEC-related protein 10
apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3H
NP_001159474.2
NP_001159475.2
NP_001159476.2
NP_861438.3
XP_011528292.1
XP_011528293.1
XP_011528294.1

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)

  1. NM_001166002.3NP_001159474.2  DNA dC->dU-editing enzyme APOBEC-3H isoform SV-182

    See identical proteins and their annotated locations for NP_001159474.2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (SV-182) lacks an alternate exon and uses an alternate splice site, resulting in an alternate 3' coding region and 3' UTR, compared to variant SV-200. The encoded isoform (SV-182) has a distinct C-terminus and is shorter than isoform SV-200.
    Source sequence(s)
    BC069023
    Consensus CDS
    CCDS54531.1
    UniProtKB/Swiss-Prot
    Q6NTF7
    UniProtKB/TrEMBL
    B7TQM4
    Related
    ENSP00000216123.5, ENST00000348946.8
    Conserved Domains (1) summary
    pfam08210
    Location:27179
    APOBEC_N; APOBEC-like N-terminal domain
  2. NM_001166003.3NP_001159475.2  DNA dC->dU-editing enzyme APOBEC-3H isoform SV-200

    See identical proteins and their annotated locations for NP_001159475.2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (SV-200) represents the longest transcript and encodes the longest isoform (SV-200).
    Source sequence(s)
    BC069023, BQ054330
    Consensus CDS
    CCDS54530.1
    UniProtKB/Swiss-Prot
    Q6IC87, Q6NTF7
    UniProtKB/TrEMBL
    M4W6S4
    Related
    ENSP00000385741.1, ENST00000401756.5
    Conserved Domains (1) summary
    pfam08210
    Location:27179
    APOBEC_N; APOBEC-like N-terminal domain
  3. NM_001166004.3NP_001159476.2  DNA dC->dU-editing enzyme APOBEC-3H isoform SV-154

    Status: REVIEWED

    Description
    Transcript Variant: This variant (SV-154) lacks an alternate exon, resulting in a frameshift in the 3' coding region, compared to variant SV-200. The encoded isoform (SV-154) has a distinct C-terminus and is shorter than isoform SV-200. The 3' UTR of this variant is incomplete due to lack of a 3'-complete supporting transcript and splice site ambiguity in the terminal non-coding exon.
    Source sequence(s)
    BC069023, BQ054330, FJ376617
    Consensus CDS
    CCDS54532.1
    UniProtKB/Swiss-Prot
    Q6NTF7
    UniProtKB/TrEMBL
    A0A087WZI3, B7TQM9
    Related
    ENSP00000393520.2, ENST00000421988.6
    Conserved Domains (2) summary
    cd01283
    Location:30121
    cytidine_deaminase; Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on ...
    pfam05240
    Location:120140
    APOBEC_C; APOBEC-like C-terminal domain
  4. NM_181773.5NP_861438.3  DNA dC->dU-editing enzyme APOBEC-3H isoform SV-183

    See identical proteins and their annotated locations for NP_861438.3

    Status: REVIEWED

    Description
    Transcript Variant: This variant (SV-183) lacks an alternate exon, resulting in an alternate 3' coding region and 3' UTR, compared to variant SV-200. The encoded isoform (SV-183) has a distinct C-terminus and is shorter than isoform SV-200
    Source sequence(s)
    BC069023, BQ052182, BU585251
    Consensus CDS
    CCDS13985.1
    UniProtKB/Swiss-Prot
    Q6NTF7
    UniProtKB/TrEMBL
    B7TQM3
    Related
    ENSP00000411754.3, ENST00000442487.8
    Conserved Domains (3) summary
    cd01283
    Location:30121
    cytidine_deaminase; Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on ...
    pfam05240
    Location:120163
    APOBEC_C; APOBEC-like C-terminal domain
    pfam08210
    Location:27179
    APOBEC_N; APOBEC-like N-terminal domain

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 110 details...Open this link in a new tab

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

Reference GRCh38.p14 Primary Assembly

Genomic

  1. NC_000022.11 Reference GRCh38.p14 Primary Assembly

    Range
    39097244..39104067
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_011529990.3XP_011528292.1  DNA dC->dU-editing enzyme APOBEC-3H isoform X1

    See identical proteins and their annotated locations for XP_011528292.1

    Conserved Domains (3) summary
    cd01283
    Location:30121
    cytidine_deaminase; Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on ...
    pfam05240
    Location:120163
    APOBEC_C; APOBEC-like C-terminal domain
    pfam08210
    Location:27179
    APOBEC_N; APOBEC-like N-terminal domain
  2. XM_011529991.4XP_011528293.1  DNA dC->dU-editing enzyme APOBEC-3H isoform X1

    See identical proteins and their annotated locations for XP_011528293.1

    Conserved Domains (3) summary
    cd01283
    Location:30121
    cytidine_deaminase; Cytidine deaminase zinc-binding domain. These enzymes are Zn dependent. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on ...
    pfam05240
    Location:120163
    APOBEC_C; APOBEC-like C-terminal domain
    pfam08210
    Location:27179
    APOBEC_N; APOBEC-like N-terminal domain
  3. XM_011529992.4XP_011528294.1  DNA dC->dU-editing enzyme APOBEC-3H isoform X2

    See identical proteins and their annotated locations for XP_011528294.1

    UniProtKB/Swiss-Prot
    Q6IC87, Q6NTF7
    UniProtKB/TrEMBL
    M4W6S4
    Related
    ENSP00000483689.1, ENST00000613677.4
    Conserved Domains (1) summary
    pfam08210
    Location:27179
    APOBEC_N; APOBEC-like N-terminal domain

Alternate T2T-CHM13v2.0

Genomic

  1. NC_060946.1 Alternate T2T-CHM13v2.0

    Range
    39567663..39574409
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)