UniProt ID | VIF_HV1B1 | |
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UniProt AC | P69720 | |
Protein Name | Virion infectivity factor {ECO:0000255|HAMAP-Rule:MF_04081} | |
Gene Name | vif {ECO:0000255|HAMAP-Rule:MF_04081} | |
Organism | Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1). | |
Sequence Length | 192 | |
Subcellular Localization |
Host cytoplasm . Host cell membrane Peripheral membrane protein Cytoplasmic side . Virion . In the cytoplasm, seems to colocalize with intermediate filament vimentin. A fraction is associated with the cytoplasmic side of cellular membranes, presu |
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Protein Description | Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyubiquitination of APOBEC3G and APOBEC3F. In turn, they are directed to the 26S proteasome for degradation. Vif interaction with APOBEC3G also blocks its cytidine deaminase activity in a proteasome-independent manner, suggesting a dual inhibitory mechanism. May interact directly with APOBEC3G mRNA in order to inhibit its translation. Seems to play a role in viral morphology by affecting the stability of the viral nucleoprotein core. Finally, Vif also contributes to the G2 cell cycle arrest observed in HIV infected cells.. | |
Protein Sequence | MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
96 | Phosphorylation | WRKKRYSTQVDPELA EHHHHCCCCCCHHHH | 24.55 | - | |
144 | Phosphorylation | AGHNKVGSLQYLALA CCCCCCHHHHHHHHH | 18.45 | - | |
155 | Phosphorylation | LALAALITPKKIKPP HHHHHHHCCCCCCCC | 29.88 | - | |
165 | Phosphorylation | KIKPPLPSVTKLTED CCCCCCCCCCCCCCC | 50.53 | - | |
188 | Phosphorylation | KGHRGSHTMNGH--- CCCCCCCCCCCC--- | 17.65 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
96 | T | Phosphorylation | Kinase | MAP4K1 | - | Uniprot |
165 | S | Phosphorylation | Kinase | MAP4K1 | - | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of VIF_HV1B1 !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of VIF_HV1B1 !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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