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Protein

Tegument protein UL11

Gene

UL11

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

Plays an important role in the cytoplasmic envelopment of tegument proteins and capsids during the assembly and egress processes. Participates also in viral entry at the fusion step probably by regulating the core fusion machinery.4 Publications

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Tegument protein UL11
Gene namesi
ORF Names:UL11
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]
ProteomesiUP000009294 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host Golgi apparatus, Host membrane, Membrane, Virion, Virion tegument

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by host
Chaini2 – 9695Tegument protein UL11PRO_0000115925Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by host1 Publication
Modified residuei40 – 401Phosphoserine1 Publication

Post-translational modificationi

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.2 Publications
Phosphorylated. Phosphorylation does not seem to be needed for UL11 recycling to the Golgi apparatus. Packaging is selective for underphosphorylated forms.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Interactioni

Subunit structurei

Interacts with UL16; this interaction is essential for the proper localization of each protein to the assembly complex and thus for the production of infectious virus. Interacts with gE (via C-terminus). Interacts with gD (via C-terminus). Interacts with UL56.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UL16P102003EBI-7044930,EBI-7044955

Protein-protein interaction databases

IntActiP04289. 1 interaction.
MINTiMINT-6732677.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 437Asp/Glu-rich (acidic)

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi18 – 192Di-leucine-like internalization motifSequence Analysis

Domaini

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 UL16.1 Publication

Sequence similaritiesi

Belongs to the herpesviridae HHV-1 UL11 family.Curated

Family and domain databases

InterProiIPR024351. Tegument_UL11_Herpesvir.
IPR016395. UL11_simplexvir-type.
[Graphical view]
PfamiPF11094. UL11. 1 hit.
[Graphical view]
PIRSFiPIRSF003496. Myristoylat_tegument_UL11. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04289-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLSFSGARP CCCRNNVLIT DDGEVVSLTA HDFDVVDIES EEEGNFYVPP
60 70 80 90
DMRGVTRAPG RQRLRSSDPP SRHTHRRTPG GACPATQFPP PMSDSE
Length:96
Mass (Da):10,487
Last modified:January 23, 2007 - v3
Checksum:i5D09A5B1F2034B09
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391E → K in strain: 17 syn+.
Natural varianti54 – 541G → V in strain: Nonneuroinvasive mutant HF10.
Natural varianti65 – 651R → C in strain: Nonneuroinvasive mutant HF10.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32347.1.
X03839 Genomic DNA. Translation: CAA27452.1.
DQ889502 Genomic DNA. Translation: ABI63473.1.
FJ593289 Genomic DNA. Translation: ACM62233.1.
PIRiA03737. WMBE11.
RefSeqiNP_044612.1. NC_001806.1.

Genome annotation databases

GeneIDi2703380.
KEGGivg:2703380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32347.1.
X03839 Genomic DNA. Translation: CAA27452.1.
DQ889502 Genomic DNA. Translation: ABI63473.1.
FJ593289 Genomic DNA. Translation: ACM62233.1.
PIRiA03737. WMBE11.
RefSeqiNP_044612.1. NC_001806.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04289. 1 interaction.
MINTiMINT-6732677.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703380.
KEGGivg:2703380.

Family and domain databases

InterProiIPR024351. Tegument_UL11_Herpesvir.
IPR016395. UL11_simplexvir-type.
[Graphical view]
PfamiPF11094. UL11. 1 hit.
[Graphical view]
PIRSFiPIRSF003496. Myristoylat_tegument_UL11. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "The UL11 gene of herpes simplex virus 1 encodes a function that facilitates nucleocapsid envelopment and egress from cells."
    Baines J.D., Roizman B.
    J. Virol. 66:5168-5174(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Membrane targeting properties of a herpesvirus tegument protein-retrovirus Gag chimera."
    Bowzard J.B., Visalli R.J., Wilson C.B., Loomis J.S., Callahan E.M., Courtney R.J., Wills J.W.
    J. Virol. 74:8692-8699(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Intracellular trafficking of the UL11 tegument protein of herpes simplex virus type 1."
    Loomis J.S., Bowzard J.B., Courtney R.J., Wills J.W.
    J. Virol. 75:12209-12219(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-40, DI-LEUCINE-LIKE INTERNALIZATION MOTIF, ACIDIC REGION.
  9. "Packaging determinants in the UL11 tegument protein of herpes simplex virus type 1."
    Loomis J.S., Courtney R.J., Wills J.W.
    J. Virol. 80:10534-10541(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
  10. "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.
  11. "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.
  12. "Function of glycoprotein E of herpes simplex virus requires coordinated assembly of three tegument proteins on its cytoplasmic tail."
    Han J., Chadha P., Starkey J.L., Wills J.W.
    Proc. Natl. Acad. Sci. U.S.A. 109:19798-19803(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Regulated interaction of tegument proteins UL16 and UL11 from herpes simplex virus."
    Chadha P., Han J., Starkey J.L., Wills J.W.
    J. Virol. 86:11886-11898(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UL16.
  14. "Herpes simplex virus 1 glycoprotein M and the membrane-associated protein UL11 are required for virus-induced cell fusion and efficient virus entry."
    Kim I.J., Chouljenko V.N., Walker J.D., Kousoulas K.G.
    J. Virol. 87:8029-8037(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiTEG2_HHV11
AccessioniPrimary (citable) accession number: P04289
Secondary accession number(s): B9VQD8, Q09IC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 83 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.