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P04289 (TEG2_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tegument protein UL11
Gene names
ORF Names:UL11
OrganismHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]
Taxonomic identifier10299 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length96 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tegument protein that may play a role in the nucleocapsid secondary envelopment at the trans-Golgi network during virus morphogenesis Potential.

Subunit structure

Interacts with UL16. Interacts with gE (via C-terminus). Interacts with gD (via C-terminus). Interacts with UL56 By similarity. Ref.6

Subcellular location

Virion tegument. Virion membrane; Lipid-anchor By similarity. Host cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Host Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side By similarity. Host nucleus membrane; Lipid-anchor; Cytoplasmic side. Note: Virion membrane-associated tegument protein (about 700 copies per virion). Associates with host membrane lipids rafts By similarity. During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) By similarity. Ref.5 Ref.7

Domain

The acidic region is required for efficient packaging. It is also involved in recycling the protein from the plasma membrane to the Golgi apparatus, and in the interaction with the capsid-binding protein UL16 By similarity.

Post-translational modification

Myristoylation and palmitoylation (probably on one or more of the nearby cysteines at the N-terminus) enable membrane-binding and Golgi apparatus-specific targeting and are essential for efficient packaging By similarity.

Phosphorylated. Phosphorylation does not seem to be needed for UL11 recycling to the Golgi apparatus. Packaging is selective for underphosphorylated forms By similarity.

Sequence similarities

Belongs to the herpesviridae HHV-1 UL11 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UL16P102003EBI-7044930,EBI-7044955

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host
Chain2 – 9695Tegument protein UL11
PRO_0000115925

Regions

Region37 – 437Asp/Glu-rich (acidic)
Motif18 – 192Di-leucine-like internalization motif Potential

Amino acid modifications

Modified residue401Phosphoserine By similarity
Lipidation21N-myristoyl glycine; by host Ref.5

Natural variations

Natural variant391E → K in strain: 17 syn+.
Natural variant541G → V in strain: Nonneuroinvasive mutant HF10.
Natural variant651R → C in strain: Nonneuroinvasive mutant HF10.

Sequences

Sequence LengthMass (Da)Tools
P04289 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5D09A5B1F2034B09

FASTA9610,487
        10         20         30         40         50         60 
MGLSFSGARP CCCRNNVLIT DDGEVVSLTA HDFDVVDIES EEEGNFYVPP DMRGVTRAPG 

        70         80         90 
RQRLRSSDPP SRHTHRRTPG GACPATQFPP PMSDSE 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence of the region in the genome of herpes simplex virus type 1 containing the exonuclease gene and neighbouring genes."
McGeoch D.J., Dolan A., Frame M.C.
Nucleic Acids Res. 14:3435-3448(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus."
Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.
Microbes Infect. 9:142-149(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nonneuroinvasive mutant HF10.
[4]"Herpes simplex virus type 1 bacterial artificial chromosome."
Cunningham C., Davison A.J.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 17 syn+.
[5]"The myristylated virion proteins of herpes simplex virus type 1: investigation of their role in the virus life cycle."
MacLean C.A., Dolan A., Jamieson F.E., McGeoch D.J.
J. Gen. Virol. 73:539-547(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION AT GLY-2, SUBCELLULAR LOCATION.
[6]"Cytoplasmic residues of herpes simplex virus glycoprotein gE required for secondary envelopment and binding of tegument proteins VP22 and UL11 to gE and gD."
Farnsworth A., Wisner T.W., Johnson D.C.
J. Virol. 81:319-331(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GLYCOPROTEIN D AND GLYCOPROTEIN E.
Strain: F.
[7]"Comprehensive characterization of extracellular herpes simplex virus type 1 virions."
Loret S., Guay G., Lippe R.
J. Virol. 82:8605-8618(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: F.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14112 Genomic DNA. Translation: CAA32347.1.
X03839 Genomic DNA. Translation: CAA27452.1.
DQ889502 Genomic DNA. Translation: ABI63473.1.
FJ593289 Genomic DNA. Translation: ACM62233.1.
PIRWMBE11. A03737.
RefSeqNP_044612.1. NC_001806.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP04289. 1 interaction.
MINTMINT-6732677.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703380.

Phylogenomic databases

ProtClustDBPHA3356.

Family and domain databases

InterProIPR024351. Tegument_UL11_Herpesvir.
IPR016395. UL11_simplexvir-type.
[Graphical view]
PfamPF11094. UL11. 1 hit.
[Graphical view]
PIRSFPIRSF003496. Myristoylat_tegument_UL11. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTEG2_HHV11
AccessionPrimary (citable) accession number: P04289
Secondary accession number(s): B9VQD8, Q09IC2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families