UniProt ID | VP16_HHV11 | |
---|---|---|
UniProt AC | P06492 | |
Protein Name | Tegument protein VP16 | |
Gene Name | UL48 | |
Organism | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1). | |
Sequence Length | 490 | |
Subcellular Localization | Virion tegument . Host nucleus . | |
Protein Description | Transcriptional activator of immediate-early (IE) gene products (alpha genes). Acts as a key activator of lytic infection by initiating the lytic program through the assembly of the transcriptional regulatory VP16-induced complex composed of VP16 and two cellular factors, HCFC1 and POU2F 1. VP16-induced complex represents a regulatory switch: when it is on, it promotes IE-gene expression and thus lytic infection, and when it is off, it limits IE-gene transcription favoring latent infection.; May play a role in the aggregation of tegument proteins around nucleocapsids during virus morphogenesis.. | |
Protein Sequence | MDLLVDELFADMNADGASPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSALPTNADLYRECKFLSTLPSDVVEWGDAYVPERTQIDIRAHGDVAFPTLPATRDGLGLYYEALSRFFHAELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRDRDLGEMLRATIADRYYRETARLARVLFLHLYLFLTREILWAAYAEQMMRPDLFDCLCCDLESWRQLAGLFQPFMFVNGALTVRGVPIEARRLRELNHIREHLNLPLVRSAATEEPGAPLTTPPTLHGNQARASGYFMVLIRAKLDSYSSFTTSPSEAVMREHAYSRARTKNNYGSTIEGLLDLPDDDAPEEAGLAAPRLSFLPAGHTRRLSTAPPTDVSLGDELHLDGEDVAMAHADALDDFDLDMLGDGDSPGPGFTPHDSAPYGALDMADFEFEQMFTDALGIDEYGG | |
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 |
---|---|---|---|---|---|
18 | Phosphorylation | DMNADGASPPPPRPA CCCCCCCCCCCCCCC | 43.39 | 16297954 | |
353 | Phosphorylation | SYSSFTTSPSEAVMR CCCCCCCCHHHHHHH | 24.30 | 16297954 | |
411 | Phosphorylation | AGHTRRLSTAPPTDV CCCCCCCCCCCCCCC | 22.25 | 16297954 | |
452 | Phosphorylation | DMLGDGDSPGPGFTP HCCCCCCCCCCCCCC | 36.97 | 16297954 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of VP16_HHV11 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VP16_HHV11 !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of VP16_HHV11 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CSTF2_HUMAN | CSTF2 | physical | 17135252 | |
MED15_HUMAN | MED15 | physical | 17135252 | |
MED25_HUMAN | MED25 | physical | 17135252 | |
MED23_HUMAN | MED23 | physical | 10353252 | |
MED7_HUMAN | MED7 | physical | 10353252 | |
CCNC_HUMAN | CCNC | physical | 10353252 | |
IFRD1_HUMAN | IFRD1 | physical | 7809103 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Phosphorylation of the VP16 transcriptional activator protein duringherpes simplex virus infection and mutational analysis of putativephosphorylation sites."; Ottosen S., Herrera F.J., Doroghazi J.R., Hull A., Mittal S.,Lane W.S., Triezenberg S.J.; Virology 345:468-481(2006). Cited for: PHOSPHORYLATION AT SER-18; SER-353; SER-411 AND SER-452. |