APOBEC3H
entrez
164668
canonical
uniprot
Q6NTF7
canonical
ensembl
ENSG00000100298
resolver
ensp
ENSP00000216123
resolver
ensp
ENSP00000385741
resolver
ensp
ENSP00000393520
resolver
ensp
ENSP00000411754
resolver
ensp
ENSP00000482682
resolver
ensp
ENSP00000483689
resolver
enst
ENST00000421988
resolver
enst
ENST00000613996
resolver
genesymbol
APOBEC3H
resolver
hgnc
HGNC:24100
resolver
uniprot
A0A087WZI3
resolver
uniprot
B0QYP0
resolver
uniprot
B0QYP1
resolver
uniprot
B7TQM3
resolver
uniprot
B7TQM4
resolver
uniprot
B7TQM5
resolver
uniprot
B7TQM8
resolver
uniprot
B7TQM9
resolver
uniprot
E9PF38
resolver
uniprot
M4W6S4
resolver
uniprot
Q5JYL9
resolver
uniprot
Q6IC87
resolver
uniprot_entry
A0A087WZI3_HUMAN
resolver
uniprot_entry
ABC3H_HUMAN
resolver
uniprot_entry
B7TQM3_HUMAN
resolver
uniprot_entry
B7TQM4_HUMAN
resolver
uniprot_entry
B7TQM8_HUMAN
resolver
uniprot_entry
B7TQM9_HUMAN
resolver
uniprot_sec
B0QYP0
resolver
uniprot_sec
B0QYP1
resolver
uniprot_sec
B7TQM5
resolver
uniprot_sec
E9PF38
resolver
uniprot_sec
M4W6S4
resolver
uniprot_sec
Q5JYL9
resolver
uniprot_sec
Q6IC87
resolver
activity_regulation
ACTIVITY REGULATION: APOBEC3H activity is regulated by RNA (PubMed:29290613). While RNA-binding inhibits the DNA deaminase activity, double-stranded RNA is required for HIV-1 restriction by promoting APOBEC3H homodimerization and packaging into retroviral nucleocapsids (PubMed:29290613). {ECO:0000269|PubMed:29290613}.; ACTIVITY REGULATION: (Microbial infection) Antiviral activity is inhibited to some extent 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. {ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:37640699}.
uniprot
proteins
amino_acid_sequence
MALLTAETFRLQFNNKRRLRRPYYPRKALLCYQLTPQNGSTPTRGYFENKKKCHAEICFINEIKSMGLDETQCYQVTCYLTWSPCSSCAWELVDFIKAHDHLNLGIFASRLYYHWCKPQQKGLRLLCGSQVPVEVMGFPEFADCWENFVDHEKPLSFNPYKMLEELDKNSRAIKRRLERIKIPGVRAQGRYMDILCDAEV
uniprot
proteins
ec_number
3.5.4.38
uniprot
proteins
function
FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms (PubMed:16571802, PubMed:16920826, PubMed:18779051, PubMed:18827027, PubMed:20062055, PubMed:22915799, PubMed:29290613). The A3H-var/haplotype 2 exhibits antiviral activity against vif-deficient HIV-1 (PubMed:18299330, PubMed:21835787, PubMed:23097438, PubMed:29290613). 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 (PubMed:18299330). 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 (PubMed:18299330). Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (PubMed:20062055). Exhibits antiviral activity also against T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons (PubMed:20062055, PubMed:22457529). {ECO:0000269|PubMed:16571802, ECO:0000269|PubMed:16920826, ECO:0000269|PubMed:18299330, ECO:0000269|PubMed:18779051, ECO:0000269|PubMed:18827027, ECO:0000269|PubMed:20062055, ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:22457529, ECO:0000269|PubMed:22915799, ECO:0000269|PubMed:23097438, ECO:0000269|PubMed:29290613}.
uniprot
proteins
mass_dalton
23532
uniprot
proteins
mutagenesis
MUTAGEN 18; /note="R->E: Increased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 20; /note="R->E: Increased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 21; /note="R->E: Decreased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 22; /note="P->A: Decreased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 23; /note="Y->A: Decreased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 24; /note="Y->A: Decreased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 25; /note="P->A: Decreased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 26; /note="R->E: Does not affect the DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 50..51; /note="KK->RR: Does not affect ubiquitination by an ECS complex hijacked by HIV-1 Vif."; /evidence="ECO:0000269|PubMed:37640699"; MUTAGEN 50; /note="K->E: Does not affect the DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 51; /note="K->E: Does not affect the DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 52; /note="K->E: Does not affect the DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 56; /note="E->A: Abolished DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 56; /note="E->Q: Reduces the ability to inhibit the retrotransposition of LINE-1 elements."; /evidence="ECO:0000269|PubMed:18827027"; MUTAGEN 70; /note="E->R: Partial resistance to ubiquitination and degradation by an ECS complex hijacked by HIV-1 Vif."; /evidence="ECO:0000269|PubMed:37640699"; MUTAGEN 90; /note="W->A: Resistance to ubiquitination and degradation by an ECS complex hijacked by HIV-1 Vif."; /evidence="ECO:0000269|PubMed:37640699"; MUTAGEN 94; /note="D->A: Resistance to ubiquitination and degradation by an ECS complex hijacked by HIV-1 Vif."; /evidence="ECO:0000269|PubMed:37640699"; MUTAGEN 97; /note="K->Q: Increased ubiquitination and degradation by an ECS complex hijacked by HIV-1 Vif."; /evidence="ECO:0000269|PubMed:37640699"; MUTAGEN 110; /note="R->E: Decreased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 111; /note="L->A: Decreased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 112; /note="Y->A: Decreased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 113; /note="Y->A: Decreased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 114; /note="H->A: Increased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 115; /note="W->A: Increased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 125; /note="L->R: Resistance to ubiquitination and degradation by an ECS complex hijacked by HIV-1 Vif."; /evidence="ECO:0000269|PubMed:37640699"; MUTAGEN 129; /note="S->R: Resistance to ubiquitination and degradation by an ECS complex hijacked by HIV-1 Vif."; /evidence="ECO:0000269|PubMed:37640699"; MUTAGEN 171; /note="R->E: Increased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 172; /note="A->E: Increased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 173; /note="I->A,E: Increased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 175; /note="R->E: Increased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 176; /note="R->E: Increased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613"; MUTAGEN 179; /note="R->E: Increased DNA deaminase activity."; /evidence="ECO:0000269|PubMed:29290613
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Following infection by some HIV-1 strains, such as isolate BRU/LAI, can be ubiquitinated by a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, leading to its degradation (PubMed:37640699). Ubiquitination by the ECS complex is however less efficient compared to APOBEC3G or APOBEC3G (PubMed:37640699). {ECO:0000269|PubMed:37640699}.
uniprot
proteins
protein_family
Cytidine and deoxycytidylate deaminase family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
12683974
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16571802
uniprot
proteins
pubmed
16920826
uniprot
proteins
pubmed
18299330
uniprot
proteins
pubmed
18304004
uniprot
proteins
pubmed
18779051
uniprot
proteins
pubmed
18827027
uniprot
proteins
pubmed
18945781
uniprot
proteins
pubmed
20062055
uniprot
proteins
pubmed
20308164
uniprot
proteins
pubmed
21653666
uniprot
proteins
pubmed
21835787
uniprot
proteins
pubmed
22001110
uniprot
proteins
pubmed
22457529
uniprot
proteins
pubmed
22912627
uniprot
proteins
pubmed
22915799
uniprot
proteins
pubmed
23097438
uniprot
proteins
pubmed
29290613
uniprot
proteins
pubmed
37640699
uniprot
proteins
sequence_length
200
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21653666, ECO:0000269|PubMed:21835787, ECO:0000269|PubMed:29290613}. Nucleus {ECO:0000269|PubMed:18779051, ECO:0000269|PubMed:21653666}. Cytoplasm, P-body {ECO:0000269|PubMed:22915799}. Note=Haplotype 1 is distributed in both the nucleus and cytoplasm, whereas haplotype 2 is predominantly cytoplasmic. {ECO:0000269|PubMed:21653666}.
uniprot
proteins