Recombinant Human DNA dC->dU-editing enzyme APOBEC-3H (APOBEC3H)

1. the results support a model in which structured RNA negatively regulates the potentially harmful DNA deamination activity of APOBEC3H while, at the same time, positively regulating its antiviral activity. PMID: 29290613
2. These studies combine to suggest that A3B and A3H-I haplotypes, together, explain the bulk of 'APOBEC signature' mutations in cancer. PMID: 27650891
3. APOBEC3H role in the spontaneous control of HIV infection. PMID: 29333092
4. we speculate that stably expressed human A3H protects humans against the cross-species transmission of zoonotic infection of SIV of chimpanzee PMID: 29267382
5. Stable variants of APOBEC3H impose selective pressure on HIV-1. PMID: 28475648
6. The deamination activity of these APOBEC3H variants correlates well with their reported anti-HIV activity for the different haplotypes, suggesting that deaminase activity may be an important factor in determining their respective anti-HIV activities. PMID: 27534815
7. There are 10 APOBEC3H residues required for the HIV-1 Vif susceptibility and Vif binding. PMID: 28336404
8. Haplotype analysis showed that the frequencies of 15del-105R was high (0.475 vs 0.400, OR=1.36, permutation P=0.037) in the HIV-1-infected subjects, confirming the association of A3H polymorphisms with the susceptibility to HIV-1 infection PMID: 26559750
9. The eQTL-missense polymorphisms of APOBEC3H are associated with lung cancer risk in a Han Chinese population PMID: 26459911
10. APOBEC3H haplotype II was able to processively deaminate multiple cytosines in a single enzyme-substrate encounter by using sliding, jumping, and intersegmental transfer movements. PMID: 26396192
11. The existence and persistence of both types of HIV-1 Vif variant suggests the importance of APOBEC3H suppression and cell cycle regulation for HIV-1's survival in vivo. PMID: 25590520
12. Importantly, APOBEC3H appears to use both deaminase-dependent and -independent mechanisms to target reverse transcription and restrict HIV-1 replication. PMID: 25614027
13. stable APOBEC3H haplotypes present as in vivo barriers to HIV-1 replication, that Vif is capable of adapting to these restrictive pressures, and that an evolutionary equilibrium has yet to be reached. PMID: 25411794
14. A3H with low anti-HIV-1 activity, APOBEC3H-hapC, is associated with the susceptibility to HIV-1 infection, whereas the A3H producing a stable protein, A3H-hapB, may confer a low risk of disease progression to AIDS. PMID: 25721876
15. Taken together, these data validate APOBEC3H expressed at endogenous levels as a bona fide HIV-1 restriction factor. PMID: 24139399
16. A3H-hapII is resistant to NL4-3 Vif while it is efficiently degraded by LAI Vif. PMID: 23469063
17. Amino acid changes within APOBEC3H can give rise to variants that are highly diverse in anti-viral activities and cellular localizations. PMID: 22859935
18. The authors show that APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 (A3H hapII) acted as potent inhibitors of HTLV-1. PMID: 22457529
19. A positively selected APOBEC3H haplotype is associated with natural resistance to HIV-1 infection. PMID: 22023594
20. APOBEC3H protein encoded by haplotype II is actively retained in the cytoplasm by interacting with speci fi c host factors, whereas the less active protein encoded by haplotype I is allowed to enter the nucleus by a passive mechanism PMID: 21653666
21. examined SNPs in APOBEC3 locus paired with sequences of proviral HIV-1 vif from HIV-1-infected adults; evidence for APOBEC3H linkage disequilibrium block associated with variation in GA --> AA, or APOBEC3F/H signature, sequence changes in proviral vif PMID: 21167246
22. The authors conclude that stably expressed APOBEC3H haplotypes may be more broadly distributed in humans than previously realized, and APOBEC3H protein is resistant to HIV-1 Vif. PMID: 21270145
23. These data show that the antiviral activity of APOBEC3H haplotypes is determined by its incorporation into the viral core, in proximity to the reverse transcription complex. PMID: 20519396
24. In contrast to APOBEC3H(A3H)_HapII, A3H_Haplotype I (HapI), which differs in only three amino acids from A3H_HapII, was resistant to HIV-1 Vif-mediated degradation. Residue 121 was critical for determining A3H sensitivity and binding to HIV-1 Vif. PMID: 19939923
25. APOBEC3H is not as strong of a selective force for current HIV-1 infections as human APOBEC3G. PMID: 19828612
26. A3H inhibits HIV-1 replication potently by a cytidine deamination-independent mechanism PMID: 18299330
27. study provides evidence of editing of human papillomavirus 1a and 16 DNA by APOBEC3 in plantar warts and precancerous cervix biopsies PMID: 18403710
28. APOBEC3H antiviral activity has been lost in the majority of humans may have important consequences for our susceptibility to retroviral infections as well as ongoing retroelement proliferation in the human genome. PMID: 18779051
29. These observations suggest that human Z2-type cytidine deaminase A3H variants have varying intrinsic abilities to restrict retroelements and that various APOBEC3 proteins may have evolved distinct inhibitory mechanisms against retroelements. PMID: 18827027
30. the anti-HIV activity of APOBEC3H seems to be regulated by a combination of genomic variation and alternative splicing. PMID: 18945781

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HGNC: 24100

OMIM: 610976

KEGG: hsa:164668

STRING: 9606.ENSP00000385741

UniGene: Hs.440515