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Literature summary for 3.5.4.5 extracted from

  • Li, X.; Ma, J.; Zhang, Q.; Zhou, J.; Yin, X.; Zhai, C.; You, X.; Yu, L.; Guo, F.; Zhao, L.; Li, Z.; Zeng, Y.; Cen, S.
    Functional analysis of the two cytidine deaminase domains in APOBEC3G (2011), Virology, 414, 130-136.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining

General Information

General Information Comment Organism
evolution APOBEC3G belongs to an APOBEC superfamily containing at least 11 members Homo sapiens
malfunction CD domain switch or replacement greatly affect the sensitivity to Vif induced degradation, editing and antiviral activity of hA3G, but the replacement or switch of CDs has no effect on hA3G viral incorporation, overview. The mutants show a nucleotide sequence preference pattern Homo sapiens
additional information HIV-1 Vif protein interacts with hA3G as a part of a Vif-Cul5-SCF complex, resulting in polyubiquitination and proteosomal degradation of hA3G. The hA3G/Vif interaction is a prerequisite for the degradation of hA3G Homo sapiens
physiological function the two cytidine deaminase domains of the cytidine deaminase act as an anti-HIV-1 host factor. The two CD domains of A3G are functionally equivalent in virion encapsidation and the interaction with HIV-1 Vif off A3G, overview Homo sapiens