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Protein

Tegument protein VP16

Gene

UL48

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei442Critical role in activation1

GO - Molecular functioni

GO - Biological processi

  • DNA-templated viral transcription Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tegument protein VP16
Alternative name(s):
Alpha trans-inducing protein
Alpha-TIF
ICP25
Vmw65
Gene namesi
ORF Names:UL48
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009294 Componenti: Genome

Subcellular locationi

  • Virion tegument By similarity
  • Host nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus, Virion, Virion tegument

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4218.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001157981 – 490Tegument protein VP16Add BLAST490

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei18Phosphoserine1 Publication1
Modified residuei353Phosphoserine1 Publication1
Modified residuei411Phosphoserine1 Publication1
Modified residuei452Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP06492.

PTM databases

iPTMnetiP06492.

Interactioni

Subunit structurei

Interacts with VP22. Interacts with gH (via C-terminus). Interacts with the virion host shutoff protein (vhs). Interacts with VP11/12. Associates with the VP16-induced complex; binding to host HCFC1 activates VP16 for association with the octamer motif-binding host protein POU2F1, to form a multiprotein-DNA complex responsible for activating transcription of the viral immediate early genes.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MED25Q7XYY22EBI-7489933,EBI-1386292From a different organism.
UL46P102302EBI-7489933,EBI-7694458
UL49P102332EBI-7489933,EBI-7490002

Protein-protein interaction databases

BioGridi971443. 13 interactors.
DIPiDIP-41776N.
IntActiP06492. 6 interactors.
MINTiMINT-275736.

Chemistry databases

BindingDBiP06492.

Structurei

Secondary structure

1490
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi58 – 69Combined sources12
Helixi74 – 83Combined sources10
Helixi96 – 99Combined sources4
Helixi103 – 105Combined sources3
Helixi109 – 118Combined sources10
Helixi143 – 145Combined sources3
Helixi146 – 196Combined sources51
Helixi203 – 247Combined sources45
Helixi250 – 253Combined sources4
Beta strandi256 – 261Combined sources6
Helixi264 – 267Combined sources4
Beta strandi278 – 282Combined sources5
Helixi289 – 301Combined sources13
Turni310 – 312Combined sources3
Helixi332 – 344Combined sources13
Beta strandi398 – 401Combined sources4
Turni466 – 469Combined sources4
Helixi470 – 473Combined sources4
Helixi475 – 479Combined sources5
Turni480 – 482Combined sources3
Beta strandi483 – 485Combined sources3
Helixi486 – 488Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
16VPX-ray2.10A47-412[»]
2PHENMR-C465-490[»]
2PHGNMR-B465-490[»]
ProteinModelPortaliP06492.
SMRiP06492.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06492.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni411 – 490Transcriptional activationAdd BLAST80

Domaini

The transcriptional activation region seems to target many proteins of the RNA polymerase II transcription machinery.

Sequence similaritiesi

Phylogenomic databases

KOiK19444.

Family and domain databases

Gene3Di1.10.1290.10. 1 hit.
InterProiIPR003174. Alpha_TIF.
IPR021051. HSV_VP16_C.
[Graphical view]
PfamiPF02232. Alpha_TIF. 1 hit.
PF12149. HSV_VP16_C. 1 hit.
[Graphical view]
SMARTiSM00814. Alpha_TIF. 1 hit.
[Graphical view]
SUPFAMiSSF56548. SSF56548. 1 hit.

Sequencei

Sequence statusi: Complete.

P06492-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLLVDELFA DMNADGASPP PPRPAGGPKN TPAAPPLYAT GRLSQAQLMP
60 70 80 90 100
SPPMPVPPAA LFNRLLDDLG FSAGPALCTM LDTWNEDLFS ALPTNADLYR
110 120 130 140 150
ECKFLSTLPS DVVEWGDAYV PERTQIDIRA HGDVAFPTLP ATRDGLGLYY
160 170 180 190 200
EALSRFFHAE LRAREESYRT VLANFCSALY RYLRASVRQL HRQAHMRGRD
210 220 230 240 250
RDLGEMLRAT IADRYYRETA RLARVLFLHL YLFLTREILW AAYAEQMMRP
260 270 280 290 300
DLFDCLCCDL ESWRQLAGLF QPFMFVNGAL TVRGVPIEAR RLRELNHIRE
310 320 330 340 350
HLNLPLVRSA ATEEPGAPLT TPPTLHGNQA RASGYFMVLI RAKLDSYSSF
360 370 380 390 400
TTSPSEAVMR EHAYSRARTK NNYGSTIEGL LDLPDDDAPE EAGLAAPRLS
410 420 430 440 450
FLPAGHTRRL STAPPTDVSL GDELHLDGED VAMAHADALD DFDLDMLGDG
460 470 480 490
DSPGPGFTPH DSAPYGALDM ADFEFEQMFT DALGIDEYGG
Length:490
Mass (Da):54,345
Last modified:January 1, 1988 - v1
Checksum:i8DDDEDEDB2A699D3
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti14A → S in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti124T → A in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti235T → A in strain: 17 syn+. 1
Natural varianti390E → K in strain: Nonneuroinvasive mutant HF10. 1
Natural varianti413A → P in strain: Nonneuroinvasive mutant HF10. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32298.1.
X03141 Genomic DNA. Translation: CAA26913.1.
DQ889502 Genomic DNA. Translation: ABI63509.1.
FJ593289 Genomic DNA. Translation: ACM62271.1.
PIRiA24118. IXBE17.
RefSeqiYP_009137123.1. NC_001806.2.

Genome annotation databases

GeneIDi24271473.
KEGGivg:24271473.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32298.1.
X03141 Genomic DNA. Translation: CAA26913.1.
DQ889502 Genomic DNA. Translation: ABI63509.1.
FJ593289 Genomic DNA. Translation: ACM62271.1.
PIRiA24118. IXBE17.
RefSeqiYP_009137123.1. NC_001806.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
16VPX-ray2.10A47-412[»]
2PHENMR-C465-490[»]
2PHGNMR-B465-490[»]
ProteinModelPortaliP06492.
SMRiP06492.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971443. 13 interactors.
DIPiDIP-41776N.
IntActiP06492. 6 interactors.
MINTiMINT-275736.

Chemistry databases

BindingDBiP06492.
ChEMBLiCHEMBL4218.

PTM databases

iPTMnetiP06492.

Proteomic databases

PRIDEiP06492.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24271473.
KEGGivg:24271473.

Phylogenomic databases

KOiK19444.

Miscellaneous databases

EvolutionaryTraceiP06492.
PROiP06492.

Family and domain databases

Gene3Di1.10.1290.10. 1 hit.
InterProiIPR003174. Alpha_TIF.
IPR021051. HSV_VP16_C.
[Graphical view]
PfamiPF02232. Alpha_TIF. 1 hit.
PF12149. HSV_VP16_C. 1 hit.
[Graphical view]
SMARTiSM00814. Alpha_TIF. 1 hit.
[Graphical view]
SUPFAMiSSF56548. SSF56548. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiVP16_HHV11
AccessioniPrimary (citable) accession number: P06492
Secondary accession number(s): B9VQH6, Q09I86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 2, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.