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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei442 – 4421Critical role in activation

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

ChEMBLiCHEMBL4218.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490Tegument protein VP16PRO_0000115798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Phosphoserine1 Publication
Modified residuei353 – 3531Phosphoserine1 Publication
Modified residuei411 – 4111Phosphoserine1 Publication
Modified residuei452 – 4521Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

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 interactions.
DIPiDIP-41776N.
IntActiP06492. 6 interactions.
MINTiMINT-275736.

Chemistry

BindingDBiP06492.

Structurei

Secondary structure

1
490
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi58 – 6912Combined sources
Helixi74 – 8310Combined sources
Helixi96 – 994Combined sources
Helixi103 – 1053Combined sources
Helixi109 – 11810Combined sources
Helixi143 – 1453Combined sources
Helixi146 – 19651Combined sources
Helixi203 – 24745Combined sources
Helixi250 – 2534Combined sources
Beta strandi256 – 2616Combined sources
Helixi264 – 2674Combined sources
Beta strandi278 – 2825Combined sources
Helixi289 – 30113Combined sources
Turni310 – 3123Combined sources
Helixi332 – 34413Combined sources
Beta strandi398 – 4014Combined sources
Turni466 – 4694Combined sources
Helixi470 – 4734Combined sources
Helixi475 – 4795Combined sources
Turni480 – 4823Combined sources
Beta strandi483 – 4853Combined sources
Helixi486 – 4883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
16VPX-ray2.10A47-412[»]
2PHENMR-C465-490[»]
2PHGNMR-B465-490[»]
ProteinModelPortaliP06492.
SMRiP06492. Positions 59-349, 456-490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06492.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni411 – 49080Transcriptional activationAdd
BLAST

Domaini

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

Sequence similaritiesi

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141A → S in strain: Nonneuroinvasive mutant HF10.
Natural varianti124 – 1241T → A in strain: Nonneuroinvasive mutant HF10.
Natural varianti235 – 2351T → A in strain: 17 syn+.
Natural varianti390 – 3901E → K in strain: Nonneuroinvasive mutant HF10.
Natural varianti413 – 4131A → P in strain: Nonneuroinvasive mutant HF10.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
16VPX-ray2.10A47-412[»]
2PHENMR-C465-490[»]
2PHGNMR-B465-490[»]
ProteinModelPortaliP06492.
SMRiP06492. Positions 59-349, 456-490.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiP06492.
ChEMBLiCHEMBL4218.

PTM databases

iPTMnetiP06492.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24271473.
KEGGivg:24271473.

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: September 7, 2016
This is version 110 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.