5D26ABF88B822AA77D0C10CF4B21BA4AD55ADC2ED45EF3B2BB2D9B79D69BE4DEAA255C085791B091C0A96C6F7609FCE6

Homomultimer; in vitro and presumably in vivo. Interacts with viral Pr55Gag precursor and host APOBEC3G. The interaction between Vif and APOBEC3G is species-specific, which may play a role in restricting the replication of SIV to their host. Forms an E3 ligase complex by interacting with host CUL5 and elongin BC complex (TCEB1 and TCEB2) (By similarity).

Source:http://purl.uniprot.org/SHA-384/5D26ABF88B822AA77D0C10CF4B21BA4AD55ADC2ED45EF3B2BB2D9B79D69BE4DEAA255C085791B091C0A96C6F7609FCE6

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Predicate	Object
rdf:type	uniprot:Subunit_Annotation
rdfs:comment	Homomultimer; in vitro and presumably in vivo. Interacts with viral Pr55Gag precursor and host APOBEC3G. The interaction between Vif and APOBEC3G is species-specific, which may play a role in restricting the replication of SIV to their host. Forms an E3 ligase complex by interacting with host CUL5 and elongin BC complex (TCEB1 and TCEB2) (By similarity).